Ca2+ signaling in mammalian spermatozoa
Calcium is an essential ion which regulates sperm motility, capacitation and the acrosome reaction (AR), three processes necessary for successful fertilization. The AR enables the spermatozoon to penetrate into the egg. In order to undergo the AR, the spermatozoon must reside in the female reproduct...
Saved in:
Published in | Molecular and cellular endocrinology Vol. 516; p. 110953 |
---|---|
Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Elsevier B.V
01.10.2020
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Calcium is an essential ion which regulates sperm motility, capacitation and the acrosome reaction (AR), three processes necessary for successful fertilization. The AR enables the spermatozoon to penetrate into the egg. In order to undergo the AR, the spermatozoon must reside in the female reproductive tract for several hours, during which a series of biochemical transformations takes place, collectively called capacitation. An early event in capacitation is relatively small elevation of intracellular Ca2+ (in the nM range) and bicarbonate, which collectively activate the soluble adenylyl cyclase to produce cyclic-AMP; c-AMP activates protein kinase A (PKA), leading to indirect tyrosine phosphorylation of proteins. During capacitation, there is an increase in the membrane-bound phospholipase C (PLC) which is activated prior to the AR by relatively high increase in intracellular Ca2+ (in the μM range). PLC catalyzes the hydrolysis of phosphatidyl-inositol-4,5-bisphosphate (PIP2) to diacylglycerol and inositol-trisphosphate (IP3), leading to activation of protein kinase C (PKC) and the IP3-receptor. PKC activates a Ca2+- channel in the plasma membrane, and IP3 activates the Ca2+- channel in the outer acrosomal membrane, leading to Ca2+ depletion from the acrosome. As a result, the plasma-membrane store-operated Ca2+ channel (SOCC) is activated to increase cytosolic Ca2+ concentration, enabling completion of the acrosome reaction. The hydrolysis of PIP2 by PLC results in the release and activation of PIP2-bound gelsolin, leading to F-actin dispersion, an essential step prior to the AR. Ca2+ is also involved in the regulation of sperm motility. During capacitation, the sperm develops a unique motility pattern called hyper-activated motility (HAM) which is essential for successful fertilization. The main Ca2+-channel that mediates HAM is the sperm-specific CatSper located in the sperm tail.
•Ca2+ is essential ion in spermatozoa for successful fertilization.•Intracellular [Ca2+] in sperm is precisely regulated by various systems.•Sperm motility is regulated by intracellular [Ca2+].•Sperm capacitation occurs in the female reproductive tract, is regulated by [Ca2+] including the development of hyperactivated motility and actin polymerization.• 2+The occurrence of the acrosome reaction depends upon high increase in intracellular [Ca]. |
---|---|
AbstractList | Calcium is an essential ion which regulates sperm motility, capacitation and the acrosome reaction (AR), three processes necessary for successful fertilization. The AR enables the spermatozoon to penetrate into the egg. In order to undergo the AR, the spermatozoon must reside in the female reproductive tract for several hours, during which a series of biochemical transformations takes place, collectively called capacitation. An early event in capacitation is relatively small elevation of intracellular Ca²⁺ (in the nM range) and bicarbonate, which collectively activate the soluble adenylyl cyclase to produce cyclic-AMP; c-AMP activates protein kinase A (PKA), leading to indirect tyrosine phosphorylation of proteins. During capacitation, there is an increase in the membrane-bound phospholipase C (PLC) which is activated prior to the AR by relatively high increase in intracellular Ca²⁺ (in the μM range). PLC catalyzes the hydrolysis of phosphatidyl-inositol-4,5-bisphosphate (PIP₂) to diacylglycerol and inositol-trisphosphate (IP₃), leading to activation of protein kinase C (PKC) and the IP₃-receptor. PKC activates a Ca²⁺- channel in the plasma membrane, and IP₃ activates the Ca²⁺- channel in the outer acrosomal membrane, leading to Ca²⁺ depletion from the acrosome. As a result, the plasma-membrane store-operated Ca²⁺ channel (SOCC) is activated to increase cytosolic Ca²⁺ concentration, enabling completion of the acrosome reaction. The hydrolysis of PIP₂ by PLC results in the release and activation of PIP₂-bound gelsolin, leading to F-actin dispersion, an essential step prior to the AR. Ca²⁺ is also involved in the regulation of sperm motility. During capacitation, the sperm develops a unique motility pattern called hyper-activated motility (HAM) which is essential for successful fertilization. The main Ca²⁺-channel that mediates HAM is the sperm-specific CatSper located in the sperm tail. Calcium is an essential ion which regulates sperm motility, capacitation and the acrosome reaction (AR), three processes necessary for successful fertilization. The AR enables the spermatozoon to penetrate into the egg. In order to undergo the AR, the spermatozoon must reside in the female reproductive tract for several hours, during which a series of biochemical transformations takes place, collectively called capacitation. An early event in capacitation is relatively small elevation of intracellular Ca2+ (in the nM range) and bicarbonate, which collectively activate the soluble adenylyl cyclase to produce cyclic-AMP; c-AMP activates protein kinase A (PKA), leading to indirect tyrosine phosphorylation of proteins. During capacitation, there is an increase in the membrane-bound phospholipase C (PLC) which is activated prior to the AR by relatively high increase in intracellular Ca2+ (in the μM range). PLC catalyzes the hydrolysis of phosphatidyl-inositol-4,5-bisphosphate (PIP2) to diacylglycerol and inositol-trisphosphate (IP3), leading to activation of protein kinase C (PKC) and the IP3-receptor. PKC activates a Ca2+- channel in the plasma membrane, and IP3 activates the Ca2+- channel in the outer acrosomal membrane, leading to Ca2+ depletion from the acrosome. As a result, the plasma-membrane store-operated Ca2+ channel (SOCC) is activated to increase cytosolic Ca2+ concentration, enabling completion of the acrosome reaction. The hydrolysis of PIP2 by PLC results in the release and activation of PIP2-bound gelsolin, leading to F-actin dispersion, an essential step prior to the AR. Ca2+ is also involved in the regulation of sperm motility. During capacitation, the sperm develops a unique motility pattern called hyper-activated motility (HAM) which is essential for successful fertilization. The main Ca2+-channel that mediates HAM is the sperm-specific CatSper located in the sperm tail. •Ca2+ is essential ion in spermatozoa for successful fertilization.•Intracellular [Ca2+] in sperm is precisely regulated by various systems.•Sperm motility is regulated by intracellular [Ca2+].•Sperm capacitation occurs in the female reproductive tract, is regulated by [Ca2+] including the development of hyperactivated motility and actin polymerization.• 2+The occurrence of the acrosome reaction depends upon high increase in intracellular [Ca]. Calcium is an essential ion which regulates sperm motility, capacitation and the acrosome reaction (AR), three processes necessary for successful fertilization. The AR enables the spermatozoon to penetrate into the egg. In order to undergo the AR, the spermatozoon must reside in the female reproductive tract for several hours, during which a series of biochemical transformations takes place, collectively called capacitation. An early event in capacitation is relatively small elevation of intracellular Ca2+ (in the nM range) and bicarbonate, which collectively activate the soluble adenylyl cyclase to produce cyclic-AMP; c-AMP activates protein kinase A (PKA), leading to indirect tyrosine phosphorylation of proteins. During capacitation, there is an increase in the membrane-bound phospholipase C (PLC) which is activated prior to the AR by relatively high increase in intracellular Ca2+ (in the μM range). PLC catalyzes the hydrolysis of phosphatidyl-inositol-4,5-bisphosphate (PIP2) to diacylglycerol and inositol-trisphosphate (IP3), leading to activation of protein kinase C (PKC) and the IP3-receptor. PKC activates a Ca2+- channel in the plasma membrane, and IP3 activates the Ca2+- channel in the outer acrosomal membrane, leading to Ca2+ depletion from the acrosome. As a result, the plasma-membrane store-operated Ca2+ channel (SOCC) is activated to increase cytosolic Ca2+ concentration, enabling completion of the acrosome reaction. The hydrolysis of PIP2 by PLC results in the release and activation of PIP2-bound gelsolin, leading to F-actin dispersion, an essential step prior to the AR. Ca2+ is also involved in the regulation of sperm motility. During capacitation, the sperm develops a unique motility pattern called hyper-activated motility (HAM) which is essential for successful fertilization. The main Ca2+-channel that mediates HAM is the sperm-specific CatSper located in the sperm tail.Calcium is an essential ion which regulates sperm motility, capacitation and the acrosome reaction (AR), three processes necessary for successful fertilization. The AR enables the spermatozoon to penetrate into the egg. In order to undergo the AR, the spermatozoon must reside in the female reproductive tract for several hours, during which a series of biochemical transformations takes place, collectively called capacitation. An early event in capacitation is relatively small elevation of intracellular Ca2+ (in the nM range) and bicarbonate, which collectively activate the soluble adenylyl cyclase to produce cyclic-AMP; c-AMP activates protein kinase A (PKA), leading to indirect tyrosine phosphorylation of proteins. During capacitation, there is an increase in the membrane-bound phospholipase C (PLC) which is activated prior to the AR by relatively high increase in intracellular Ca2+ (in the μM range). PLC catalyzes the hydrolysis of phosphatidyl-inositol-4,5-bisphosphate (PIP2) to diacylglycerol and inositol-trisphosphate (IP3), leading to activation of protein kinase C (PKC) and the IP3-receptor. PKC activates a Ca2+- channel in the plasma membrane, and IP3 activates the Ca2+- channel in the outer acrosomal membrane, leading to Ca2+ depletion from the acrosome. As a result, the plasma-membrane store-operated Ca2+ channel (SOCC) is activated to increase cytosolic Ca2+ concentration, enabling completion of the acrosome reaction. The hydrolysis of PIP2 by PLC results in the release and activation of PIP2-bound gelsolin, leading to F-actin dispersion, an essential step prior to the AR. Ca2+ is also involved in the regulation of sperm motility. During capacitation, the sperm develops a unique motility pattern called hyper-activated motility (HAM) which is essential for successful fertilization. The main Ca2+-channel that mediates HAM is the sperm-specific CatSper located in the sperm tail. |
ArticleNumber | 110953 |
Author | Breitbart, Haim Etkovitz, Nir Finkelstein, Maya |
Author_xml | – sequence: 1 givenname: Maya surname: Finkelstein fullname: Finkelstein, Maya organization: IVF Unit, The Edith Wolfson Medical Center, Tel-Aviv, Israel – sequence: 2 givenname: Nir surname: Etkovitz fullname: Etkovitz, Nir organization: Sperm Bank, Sheba Hospital, Tel-Hashomer, Israel – sequence: 3 givenname: Haim surname: Breitbart fullname: Breitbart, Haim email: Haim.Breitbart@biu.ac.il organization: The Mina & Everard Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan, 5290002, Israel |
BookMark | eNqFkE1LAzEURYNUsK3-AHezU5CpL8lkMoMrKX5BwY2uQyZ5U1JmkppMBf31TqkrF3X1uHDPhXdmZOKDR0IuKSwo0PJ2s-gNLhiwMVOoBT8hU1pJllcg5IRMgQPPJQN5RmYpbQBAClZNydVSs5ssubXXnfPrzPms130_Bu2ztMXY6yF8B31OTlvdJbz4vXPy_vjwtnzOV69PL8v7VW5YzYdcCGlZZVlpQDeIbVvQtixFZQorStGUtGlYw620tW3qGiS2TVHUsqyRUcMl8jm5PuxuY_jYYRpU75LBrtMewy4pJgSDglJJ_68WbPyR82pflYeqiSGliK0ybtCDC36I2nWKgtpbVBs1WlR7i-pgcSTpH3IbXa_j11Hm7sDgKOrTYVTJOPQGrYtoBmWDO0L_AFtwie0 |
CitedBy_id | crossref_primary_10_3389_fvets_2022_948074 crossref_primary_10_3389_fendo_2022_896193 crossref_primary_10_3389_fendo_2024_1377780 crossref_primary_10_1134_S1990747824700132 crossref_primary_10_2147_IJN_S408623 crossref_primary_10_3390_ijms23073718 crossref_primary_10_3390_cimb45090442 crossref_primary_10_1002_jat_4290 crossref_primary_10_3390_antiox13080885 crossref_primary_10_3390_ijms24043118 crossref_primary_10_3389_fendo_2022_896558 crossref_primary_10_3390_ani15030305 crossref_primary_10_3390_cells11060993 crossref_primary_10_3390_ijms232314646 crossref_primary_10_1002_mrd_70010 crossref_primary_10_1007_s43032_024_01782_7 crossref_primary_10_3390_ani11061788 crossref_primary_10_3390_cells11010102 crossref_primary_10_3390_biology11020213 crossref_primary_10_1016_j_reprotox_2024_108559 crossref_primary_10_1103_PhysRevLett_130_248401 crossref_primary_10_3390_ijms21239179 crossref_primary_10_3390_nu16111781 crossref_primary_10_1021_acsami_0c10957 crossref_primary_10_3390_ani13142300 crossref_primary_10_1186_s40659_024_00580_4 crossref_primary_10_47026_2413_4864_2024_1_74_81 crossref_primary_10_1002_rmb2_12614 crossref_primary_10_1093_biolre_ioac136 crossref_primary_10_3390_ijms22115693 crossref_primary_10_1590_1984_3143_ar2024_0033 crossref_primary_10_2217_epi_2022_0122 crossref_primary_10_3390_cells10123501 crossref_primary_10_1042_BSR20230057 crossref_primary_10_1083_jcb_202102146 crossref_primary_10_1177_0300060521999527 crossref_primary_10_1152_physrev_00009_2020 crossref_primary_10_1016_j_theriogenology_2022_08_017 crossref_primary_10_14202_vetworld_2025_122_132 crossref_primary_10_3390_ijms23095128 crossref_primary_10_5534_wjmh_220262 crossref_primary_10_1002_cbin_11848 crossref_primary_10_1016_j_biosystems_2021_104524 crossref_primary_10_4103_aja202329 crossref_primary_10_1016_j_biopha_2024_117367 crossref_primary_10_1097_RD9_0000000000000017 crossref_primary_10_71336_jabs_1080 crossref_primary_10_3390_ijms24054788 crossref_primary_10_1016_j_psj_2024_103959 crossref_primary_10_1038_s41598_023_49155_5 crossref_primary_10_1002_jcp_30951 crossref_primary_10_1002_jat_4650 crossref_primary_10_1016_j_fct_2022_113407 crossref_primary_10_1016_j_repbio_2024_100971 crossref_primary_10_1016_j_theriogenology_2024_05_042 crossref_primary_10_31857_S0233475524030086 crossref_primary_10_1016_j_cbpc_2024_109860 crossref_primary_10_1016_j_theriogenology_2023_11_017 crossref_primary_10_3389_fmicb_2022_977574 crossref_primary_10_1111_asj_13552 |
Cites_doi | 10.1186/1477-7827-1-53 10.1016/S0074-7696(05)43002-8 10.1046/j.1439-0272.2001.00410.x 10.1095/biolreprod.105.042184 10.1387/ijdb.082696hf 10.1091/mbc.11.5.1571 10.1242/jcs.108.6.2525 10.1083/jcb.142.2.473 10.1095/biolreprod.102.009233 10.1111/j.1600-0854.2008.00758.x 10.1038/emboj.2011.337 10.1074/jbc.M110.170951 10.1371/journal.pone.0008211 10.1006/dbio.2001.0527 10.1095/biolreprod65.5.1606 10.1093/molehr/gau073 10.1016/j.cell.2014.02.056 10.1073/pnas.93.23.13004 10.1095/biolreprod.110.088989 10.1016/0005-2736(83)90505-9 10.1093/molehr/7.2.119 10.1242/dev.136499 10.1095/biolreprod.116.140632 10.7554/eLife.35853 10.1152/physrev.00028.2010 10.1002/(SICI)1098-2795(199809)51:1<84::AID-MRD10>3.0.CO;2-U 10.1111/andr.12706 10.1083/jcb.130.4.857 10.1186/s13630-015-0015-z 10.1095/biolreprod55.1.207 10.1074/jbc.M114.607556 10.1186/1477-7827-7-11 10.1038/srep33589 10.1038/nature09767 10.1007/s00424-012-1122-y 10.1242/jcs.058263 10.1016/j.ydbio.2009.08.002 10.1002/jcp.24873 10.1016/j.ydbio.2006.11.007 10.1101/gad.367606 10.1074/jbc.M111.292292 10.1016/S0014-5793(04)00257-1 10.1038/sj.ejhg.5200991 10.1016/S0092-8674(00)81404-X 10.1002/jcp.27337 10.1016/S0014-5793(02)02529-2 10.1530/rep.1.00478 10.4103/aja.aja_99_18 10.1095/biolreprod.102.011163 10.1111/and.12068 10.1016/0143-4160(80)90040-8 10.1093/biolre/ioy132 10.1007/978-3-540-74805-2_5 10.1095/biolreprod66.2.429 10.1006/dbio.2002.0797 10.1074/jbc.M508854200 10.1016/0167-4889(96)00022-5 10.1006/dbio.1994.1229 10.1074/jbc.M401194200 10.1083/jcb.34.3.C1 10.1016/j.ydbio.2014.10.009 10.1530/REP-13-0560 10.1016/0014-5793(80)81255-5 10.1016/j.cell.2009.12.053 10.1073/pnas.1217018109 10.1095/biolreprod.102.004580 10.1074/jbc.M112.439356 10.1083/jcb.200210057 10.1042/bj2810473 10.1016/j.ydbio.2016.05.008 10.1073/pnas.1216588110 10.1210/endo.131.5.1425422 10.1371/journal.pone.0167622 10.1095/biolreprod.106.055038 10.1002/cm.20149 10.15252/embj.2019102363 10.1038/nature04417 10.1007/s00441-015-2229-1 10.1016/j.bbrc.2016.03.071 10.1046/j.1365-2605.2002.03521.x 10.1073/pnas.0610286104 10.1038/nrm2002 10.1186/1752-0509-2-19 10.1111/j.1365-2605.2008.00874.x 10.1016/S0166-2236(03)00195-4 10.1017/S0967199498000094 10.1016/j.devcel.2014.01.005 10.1111/febs.13710 10.1126/science.289.5479.625 10.1006/dbio.2001.0323 10.1016/j.ajhg.2009.03.004 10.1095/biolreprod.102.011320 10.1038/ncb0307-235 10.1016/S0021-9258(17)43388-6 10.1073/pnas.96.12.6757 10.1002/mrd.22996 10.1016/0014-5793(96)00515-7 10.1017/S096719941400029X 10.1016/0014-5793(94)80422-2 10.1074/jbc.M113.510073 10.1074/jbc.RA117.001566 10.1038/nature09769 10.1016/j.ydbio.2011.12.002 10.1242/dev.121.4.1139 10.1073/pnas.1018202108 10.1242/jcs.109.7.1947 10.1126/science.aad0836 10.1095/biolreprod61.5.1226 10.1126/science.1161748 10.1038/35074570 10.1016/j.bbrc.2018.02.042 10.1038/s41598-018-19898-7 10.1074/jbc.M501430200 10.1006/dbio.1996.0301 10.1073/pnas.1700367114 10.1095/biolreprod.105.040733 10.1002/jcp.26883 10.1095/biolreprod.114.119768 10.1016/S0021-9258(17)33330-6 10.1038/ncomms1153 10.1016/S0014-5793(03)00305-3 10.1074/jbc.M105345200 10.1016/S0021-9258(18)48135-5 10.1371/journal.pone.0006095 10.1093/molehr/gar044 10.1095/biolreprod67.1.301 10.1530/rep.0.1220519 10.1093/molehr/gam012 10.1002/jez.1402670312 10.1095/biolreprod.109.077107 10.1016/0092-8674(95)90239-2 10.1111/andr.12234 10.1074/jbc.M701083200 10.1093/humrep/dey377 10.1073/pnas.90.10.4660 10.1095/biolreprod.112.107078 10.1002/mrd.22782 10.1038/35098027 10.1016/S0015-0282(03)00267-X 10.1002/mrd.22921 10.1126/science.aad6887 10.1093/humrep/den314 10.1073/pnas.1816189115 10.1016/j.celrep.2018.08.016 |
ContentType | Journal Article |
Copyright | 2020 Elsevier B.V. Copyright © 2020 Elsevier B.V. All rights reserved. |
Copyright_xml | – notice: 2020 Elsevier B.V. – notice: Copyright © 2020 Elsevier B.V. All rights reserved. |
DBID | AAYXX CITATION 7X8 7S9 L.6 |
DOI | 10.1016/j.mce.2020.110953 |
DatabaseName | CrossRef MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
DatabaseTitle | CrossRef MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
DatabaseTitleList | AGRICOLA MEDLINE - Academic |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Medicine Anatomy & Physiology |
EISSN | 1872-8057 |
ExternalDocumentID | 10_1016_j_mce_2020_110953 S0303720720302537 |
GroupedDBID | --- --K --M -~X .~1 0R~ 123 1B1 1RT 1~. 1~5 4.4 457 4G. 5RE 5VS 7-5 71M 8P~ 9JM AABNK AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAXUO ABBQC ABFRF ABGSF ABJNI ABLVK ABMAC ABMZM ABUDA ABYKQ ACDAQ ACGFO ACGFS ACIUM ACRLP ADBBV ADEZE ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFKWA AFTJW AFXIZ AGHFR AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJOXV AJRQY ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ANZVX AXJTR BKOJK BLXMC BNPGV CS3 DOVZS DU5 EBS EFJIC EFLBG EO8 EO9 EP2 EP3 F5P FDB FIRID FNPLU FYGXN G-Q GBLVA IHE J1W KOM LCYCR LX3 LZ1 M29 M41 MO0 N9A O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 ROL RPZ SCC SCU SDF SDG SDP SES SPCBC SSH SSU SSZ T5K WH7 ~G- .55 .GJ 29M 3O- 53G AAHBH AAQXK AATTM AAXKI AAYWO AAYXX ABFNM ABWVN ABXDB ACIEU ACRPL ACVFH ADCNI ADMUD ADNMO AEIPS AEUPX AFJKZ AFPUW AGCQF AGQPQ AGRDE AGRNS AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP ASPBG AVWKF AZFZN CITATION EJD FEDTE FGOYB G-2 HDZ HLW HMK HMO HVGLF HZ~ J5H MVM R2- RIG SAE SBG SEW WUQ X7M ZGI ZXP 7X8 7S9 EFKBS L.6 |
ID | FETCH-LOGICAL-c293t-557d28d26c0abeeff41f6658c4d565b61bb2b3d7d9db9907efb449769e21c37e3 |
IEDL.DBID | .~1 |
ISSN | 0303-7207 1872-8057 |
IngestDate | Tue Aug 05 11:13:06 EDT 2025 Thu Jul 10 17:07:30 EDT 2025 Tue Jul 01 03:48:47 EDT 2025 Thu Apr 24 22:56:40 EDT 2025 Fri Feb 23 02:49:33 EST 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Keywords | Capacitation Acrosome reaction Spermatozoa Motility Calcium Fertilization |
Language | English |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c293t-557d28d26c0abeeff41f6658c4d565b61bb2b3d7d9db9907efb449769e21c37e3 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
PQID | 2427523381 |
PQPubID | 23479 |
ParticipantIDs | proquest_miscellaneous_2552041171 proquest_miscellaneous_2427523381 crossref_citationtrail_10_1016_j_mce_2020_110953 crossref_primary_10_1016_j_mce_2020_110953 elsevier_sciencedirect_doi_10_1016_j_mce_2020_110953 |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 2000 |
PublicationDate | 2020-10-01 2020-10-00 20201001 |
PublicationDateYYYYMMDD | 2020-10-01 |
PublicationDate_xml | – month: 10 year: 2020 text: 2020-10-01 day: 01 |
PublicationDecade | 2020 |
PublicationTitle | Molecular and cellular endocrinology |
PublicationYear | 2020 |
Publisher | Elsevier B.V |
Publisher_xml | – name: Elsevier B.V |
References | Pizzo, Drago, Filadi, Pozzan (bib112) 2012; 464 Bray, Son, Kumar, Meizel (bib19) 2005; 73 Megnagi, Finkelstein, Shabtay, Breitbart (bib96) 2015; 362 Avenarius, Hildebrand, Zhang, Meyer, Smith, Kahrizi (bib9) 2009; 84 Babcock, First, Lardy (bib11) 1976; 251 Bradley, Forrester (bib16) 1980; 1 Suarez, Varosi, Dai (bib133) 1993; 90 Castellano, Trevino, Rodriguez, Serrano, Pacheco, Tsutsumi (bib30) 2003; 541 Avidan, Tamary, Dgany, Cattan, Pariente, Thulliez (bib10) 2003; 11 Ho, Suarez (bib56) 2001; 122 Battistone, Alvau, Salicioni, Visconti, Da Ros, Cuasnicu (bib15) 2014; 20 De Blas, Darszon, Ocampo, Serrano, Castellano, Hernandez-Gonzalez (bib39) 2009; 4 Chung, Navarro, Krapivinsky, Krapivinsky, Clapham (bib33) 2011; 2 Alasmari, Costello, Correia, Oxenham, Morris, Fernandes (bib3) 2013; 288 Lievano, Santi, Serrano, Trevino, Bellve, Hernandez-Cruz, Darszon (bib79) 1996; 388 Otsuka, Harayama (bib110) 2017; 84 Sanchez-Cardenas, Servin-Vences, Jose, Trevino, Hernandez-Cruz, Darszon (bib123) 2014; 91 Buffone, Doncel, Calamera, Verstraeten (bib27) 2009; 32 Miller, Mannowetz, Iavarone, Safavi, Gracheva, Smith (bib100) 2016; 352 Luconi, Krausz, Forti, Baldi (bib85) 1996; 55 Breitbart, Lax, Rotem, Naor (bib21) 1992; 281 Shabtay, Breitbart (bib125) 2016; 415 Jaldety, Breitbart (bib65) 2015; 23 Arnoult, Cardullo, Lemos, Florman (bib7) 1996; 93 Navarrete, Garcia-Vazquez, Alvau, Escoffier, Krapf, Sanchez-Cardenas (bib106) 2015; 230 Sanchez-Cardenas, Montoya, Navarrete, Hernandez-Cruz, Corkidi, Visconti, Darszon (bib122) 2018; 99 Aitken, Baker (bib2) 2002; 25 Trevino, Felix, Castellano, Gutierrez, Rodriguez, Pacheco (bib136) 2004; 563 Baron, Fara, Zapata-Carmona, Zuniga, Kong, Signorelli (bib13) 2016; 4 Gur, Breitbart (bib53) 2006; 20 Peddinti, Nanduri, Kaya, Feugang, Burgess, Memili (bib111) 2008; 2 Breitbart, Stern, Rubinstein (bib23) 1983; 728 Chung, Shim, Everley, Gygi, Zhuang, Clapham (bib34) 2014; 157 Cohen, Buttke, Asano, Mukai, Nelson, Ren (bib35) 2014; 28 Jungnickel, Marrero, Birnbaumer, Lemos, Florman (bib68) 2001; 3 Spungin, Breitbart (bib130) 1996; 109 Ackermann, Zitranski, Borth, Buech, Gudermann, Boekhoff (bib1) 2009; 122 Bray, Son, Meizel (bib20) 2002; 67 Mundt, Spehr, Lishko (bib103) 2018; 7 Smith, Syritsyna, Fellous, Serres, Mannowetz, Kirichok, Lishko (bib128) 2013; 110 Son, Meizel (bib129) 2003; 68 Brose (bib25) 2008; 9 Visconti, Moore, Bailey, Laclerc, Connors, Pan (bib139) 1995; 121 Sakata, Saegusa, Zong, Osanai, Murakoshi, Shimizu (bib121) 2002; 516 Ignotz, Suarez (bib59) 2005; 73 Shojima, Hou, Takahashi, Matsumura, Okai, Nakamura (bib127) 2018; 8 Teves, Guidobaldi, Unates, Sanchez, Miska, Publicover (bib135) 2009; 4 Zhao, Kennedy, De Blas, Orta, Pavarotti, Arias (bib146) 2018; 115 Kirichok, Navarro, Clapham (bib70) 2006; 439 Carrera, Moos, Ning, Gerton, Tesarik, Kopf, Moss (bib29) 1996; 180 Marquez, Ignotz, Suarez (bib91) 2007; 303 Cook, Brokaw, Muller, Babcock (bib36) 1994; 165 Kumar, Majhi, Swain, Giri, Kar, Samanta, Goswami (bib73) 2016; 473 Lishko, Botchkina, Fedorenko, Kirichok (bib80) 2010; 140 De Toni, Garolla, Menegazzo, Magagna, Di Nisio, Sabovic (bib40) 2016; 11 O'Toole, Arnoult, Darszon, Steinhardt, Florman (bib108) 2000; 11 Nguyen, Duittoz, Praud, Combarnous, Blesbois (bib107) 2016; 283 Walensky, Snyder (bib140) 1995; 130 Mata-Martinez, Darszon, Trevino (bib93) 2018; 497 Li, Hung, Suarez (bib78) 2015; 10 Llanos (bib83) 1998; 51 Wang, Liu, Cho, Ren (bib141) 2009; 81 Jahn, Scheller (bib64) 2006; 7 Kirichok, Lishko (bib69) 2011; 17 Darszon, Nishigaki, Beltran, Trevino (bib37) 2011; 91 Drago, Pizzo, Pozzan (bib42) 2011; 30 Allouche-Fitoussi, Bakhshi, Breitbart (bib4) 2018; 85 Brener, Rubinstein, Cohen, Shternall, Rivlin, Breitbart (bib24) 2003; 68 Marquez, Suarez (bib92) 2007; 76 Qi, Moran, Navarro, Chong, Krapivinsky, Krapivinsky (bib114) 2007; 104 Babcock, Pfeiffer (bib12) 1987; 262 Jagannathan, Punt, Gu, Arnoult, Sakkas, Barratt, Publicover (bib63) 2002; 277 Carlson, Quill, Westenbroek, Schuh, Hille, Babcock (bib28) 2005; 280 Sudhof, Rothman (bib134) 2009; 323 Chen, Cann, Litvin, Iourgenko, Sinclair, Levin, Buck (bib32) 2000; 289 Brukman, Nunez, Puga Molina, Buffone, Darszon, Cuasnicu, Da Ros (bib26) 2019; 234 Shiba, Marian, Krasznai, Baba, Morisawa, Yoshida (bib126) 2006; 63 Alvau, Battistone, Gervasi, Navarrete, Xu, Sanchez-Cardenas (bib5) 2016; 143 Michailov, Ickowicz, Breitbart (bib98) 2014; 396 Gonzalez-Fernandez, Macias-Garcia, Loux, Varner, Hinrichs (bib49) 2013; 88 Lishko, Botchkina, Kirichok (bib81) 2011; 471 Dragileva, Rubinstein, Breitbart (bib41) 1999; 61 Lax, Rubinstein, Breitbart (bib76) 1994; 339 Varano, Lombardi, Cantini, Forti, Baldi, Luconi (bib138) 2008; 23 Itach, Finklestein, Etkovitz, Breitbart (bib61) 2012; 362 Bradley, Forrester (bib17) 1980; 121 Mannowetz, Miller, Lishko (bib89) 2017; 114 Goodson, Zhang, Tsuruta, Wang, O'Brien (bib51) 2011; 84 Rotem, Paz, Homonnai, Kalina, Lax, Breitbart, Naor (bib117) 1992; 131 Mizuno, Shiba, Okai, Takahashi, Shitaka, Oiwa (bib102) 2012; 109 Lang, Jahn (bib74) 2008 Espino, Mediero, Lozano, Bejarano, Ortiz, Garcia (bib43) 2009; 7 Ho, Suarez (bib58) 2003; 68 Spungin, Margalit, Breitbart (bib131) 1995; 108 Leclerc, Goupil (bib77) 2002; 67 Naaby-Hansen, Mandal, Wolkowicz, Sen, Westbrook, Shetty (bib104) 2002; 242 Felix (bib45) 2005; 129 Rossato, Di Virgilio, Rizzuto, Galeazzi, Foresta (bib116) 2001; 7 Itzhakov, Nitzan, Breitbart (bib62) 2019; 21 Ren, Navarro, Perez, Jackson, Hsu, Shi (bib115) 2001; 413 Breitbart, Rubinstein, Gruberger (bib22) 1996; 1312 Branham, Mayorga, Tomes (bib18) 2006; 281 Finkelstein, Etkovitz, Breitbart (bib46) 2010; 285 Inaba (bib60) 2015; 4 Weber, Zemelman, McNew, Westermann, Gmachl, Parlati (bib143) 1998; 92 Koh, Bellen (bib71) 2003; 26 Meizel, Turner (bib97) 1993; 267 Wang, Young, Tüttelmann, Röpke, Krallmann, Kliesch (bib142) 2020 Liu, Xia, Cho, Clapham, Ren (bib82) 2007; 282 Rufo, Schoff, Lardy (bib120) 1984; 259 Wiser, Sachar, Ghetler, Shulman, Breitbart (bib145) 2014; 46 Ho, Granish, Suarez (bib55) 2002; 250 Wiesner, Weiner, Middendorff, Hagen, Kaupp, Weyand (bib144) 1998; 142 Guidobaldi, Hirohashi, Cubilla, Buffone, Giojalas (bib52) 2017; 84 Miller, Kenny, Mannowetz, Mansell, Wojcik, Mendoza (bib99) 2018; 24 Orta, de la Vega-Beltran, Martin-Hidalgo, Santi, Visconti, Darszon (bib109) 2018; 293 Arnoult, Kazam, Visconti, Kopf, Villaz, Florman (bib8) 1999; 96 Kulan, Shivaji (bib72) 2001; 33 McMahon, Missler, Li, Sudhof (bib95) 1995; 83 Zippin, Chen, Straub, Hess, Diaz, Lee (bib147) 2013; 288 Fukami, Yoshida, Inoue, Kurokawa, Fissore, Yoshida (bib48) 2003; 161 Luria, Rubinstein, Lax, Breitbart (bib88) 2002; 66 Chavez, Ferreira, Butler, De La Vega Beltran, Trevino, Darszon (bib31) 2014; 289 Navarrete, Alvau, Lee, Levin, Buck, Leon (bib105) 2016; 6 Ruete, Lucchesi, Bustos, Tomes (bib119) 2014; 12 Lobley, Pierron, Reynolds, Allen, Michalovich (bib84) 2003; 1 Schiffer, Rieger, Brenker, Young, Hamzeh, Wachten (bib124) 2020 Luo, Chen, Zou, Wang, Cheng, Wang (bib86) 2019; 34 Luque, Dalotto-Moreno, Martin-Hidalgo, Ritagliati, Puga Molina, Romarowski (bib87) 2018; 233 Marin-Briggiler, Gonzalez-Echeverria, Buffone, Calamera, Tezon, Vazquez-Levin (bib90) 2003; 79 Ardon, Markello, Hu, Deutsch, Tung, Wu, Suarez (bib6) 2016; 95 Darszon, Nishigaki, Wood, Trevino, Felix, Beltran (bib38) 2005; 243 Gonzalez-Martinez, Galindo, de De La Torre, Zapata, Rodriguez, Florman, Darszon (bib50) 2001; 236 Strunker, Goodwin, Brenker, Kashikar, Weyand, Seifert, Kaupp (bib132) 2011; 471 Jin, Fujiwara, Kakiuchi, Okabe, Satouh, Baba (bib67) 2011; 108 Mayorga, Altamirano, Zanni Ruiz, Pavarotti (bib94) 2020; 8 Rotfeld, Hillman, Ickowicz, Breitbart (bib118) 2014; 147 Harper, Barratt, Publicover (bib54) 2004; 279 Publicover, Harper, Barratt (bib113) 2007; 9 Ho, Suarez (bib57) 2001; 65 Jaldety, Glick, Orr-Urtreger, Ickowicz, Gerber, Breitbart (bib66) 2012; 287 Miyata, Satouh, Mashiko, Muto, Nozawa, Shiba (bib101) 2015; 350 Trevino, Santi, Beltran, Hernandez-Cruz, Darszon, Lomeli (bib137) 1998; 6 Barros, Bedford, Franklin, Austin (bib14) 1967; 34 Etkovitz, Tirosh, Chazan, Jaldety, Daniel, Rubinstein, Breitbart (bib44) 2009; 334 Lawson, Dorval, Goupil, Leclerc (bib75) 2007; 13 Florman, Jungnickel, Sutton (bib47) 2008; 52 Avidan (10.1016/j.mce.2020.110953_bib10) 2003; 11 Mayorga (10.1016/j.mce.2020.110953_bib94) 2020; 8 Bradley (10.1016/j.mce.2020.110953_bib16) 1980; 1 Sanchez-Cardenas (10.1016/j.mce.2020.110953_bib122) 2018; 99 Sanchez-Cardenas (10.1016/j.mce.2020.110953_bib123) 2014; 91 Chung (10.1016/j.mce.2020.110953_bib33) 2011; 2 Mizuno (10.1016/j.mce.2020.110953_bib102) 2012; 109 Pizzo (10.1016/j.mce.2020.110953_bib112) 2012; 464 Spungin (10.1016/j.mce.2020.110953_bib130) 1996; 109 Drago (10.1016/j.mce.2020.110953_bib42) 2011; 30 Bray (10.1016/j.mce.2020.110953_bib20) 2002; 67 Lawson (10.1016/j.mce.2020.110953_bib75) 2007; 13 Felix (10.1016/j.mce.2020.110953_bib45) 2005; 129 Gonzalez-Fernandez (10.1016/j.mce.2020.110953_bib49) 2013; 88 Miller (10.1016/j.mce.2020.110953_bib99) 2018; 24 Zhao (10.1016/j.mce.2020.110953_bib146) 2018; 115 Mannowetz (10.1016/j.mce.2020.110953_bib89) 2017; 114 O'Toole (10.1016/j.mce.2020.110953_bib108) 2000; 11 Ruete (10.1016/j.mce.2020.110953_bib119) 2014; 12 Sudhof (10.1016/j.mce.2020.110953_bib134) 2009; 323 Alvau (10.1016/j.mce.2020.110953_bib5) 2016; 143 Cook (10.1016/j.mce.2020.110953_bib36) 1994; 165 Kulan (10.1016/j.mce.2020.110953_bib72) 2001; 33 Ackermann (10.1016/j.mce.2020.110953_bib1) 2009; 122 Arnoult (10.1016/j.mce.2020.110953_bib7) 1996; 93 Ho (10.1016/j.mce.2020.110953_bib58) 2003; 68 Chen (10.1016/j.mce.2020.110953_bib32) 2000; 289 Babcock (10.1016/j.mce.2020.110953_bib11) 1976; 251 Fukami (10.1016/j.mce.2020.110953_bib48) 2003; 161 Mundt (10.1016/j.mce.2020.110953_bib103) 2018; 7 Babcock (10.1016/j.mce.2020.110953_bib12) 1987; 262 Shabtay (10.1016/j.mce.2020.110953_bib125) 2016; 415 Etkovitz (10.1016/j.mce.2020.110953_bib44) 2009; 334 Breitbart (10.1016/j.mce.2020.110953_bib21) 1992; 281 Wiser (10.1016/j.mce.2020.110953_bib145) 2014; 46 Breitbart (10.1016/j.mce.2020.110953_bib23) 1983; 728 Kirichok (10.1016/j.mce.2020.110953_bib69) 2011; 17 Luo (10.1016/j.mce.2020.110953_bib86) 2019; 34 Arnoult (10.1016/j.mce.2020.110953_bib8) 1999; 96 Ardon (10.1016/j.mce.2020.110953_bib6) 2016; 95 Otsuka (10.1016/j.mce.2020.110953_bib110) 2017; 84 Leclerc (10.1016/j.mce.2020.110953_bib77) 2002; 67 Jin (10.1016/j.mce.2020.110953_bib67) 2011; 108 Ignotz (10.1016/j.mce.2020.110953_bib59) 2005; 73 Nguyen (10.1016/j.mce.2020.110953_bib107) 2016; 283 Meizel (10.1016/j.mce.2020.110953_bib97) 1993; 267 Weber (10.1016/j.mce.2020.110953_bib143) 1998; 92 Bradley (10.1016/j.mce.2020.110953_bib17) 1980; 121 Darszon (10.1016/j.mce.2020.110953_bib38) 2005; 243 Shojima (10.1016/j.mce.2020.110953_bib127) 2018; 8 Finkelstein (10.1016/j.mce.2020.110953_bib46) 2010; 285 Brener (10.1016/j.mce.2020.110953_bib24) 2003; 68 Kirichok (10.1016/j.mce.2020.110953_bib70) 2006; 439 Llanos (10.1016/j.mce.2020.110953_bib83) 1998; 51 Navarrete (10.1016/j.mce.2020.110953_bib105) 2016; 6 Navarrete (10.1016/j.mce.2020.110953_bib106) 2015; 230 Lievano (10.1016/j.mce.2020.110953_bib79) 1996; 388 Marin-Briggiler (10.1016/j.mce.2020.110953_bib90) 2003; 79 Miller (10.1016/j.mce.2020.110953_bib100) 2016; 352 Shiba (10.1016/j.mce.2020.110953_bib126) 2006; 63 Trevino (10.1016/j.mce.2020.110953_bib136) 2004; 563 Itach (10.1016/j.mce.2020.110953_bib61) 2012; 362 De Toni (10.1016/j.mce.2020.110953_bib40) 2016; 11 Jungnickel (10.1016/j.mce.2020.110953_bib68) 2001; 3 Darszon (10.1016/j.mce.2020.110953_bib37) 2011; 91 Teves (10.1016/j.mce.2020.110953_bib135) 2009; 4 Luria (10.1016/j.mce.2020.110953_bib88) 2002; 66 Battistone (10.1016/j.mce.2020.110953_bib15) 2014; 20 Smith (10.1016/j.mce.2020.110953_bib128) 2013; 110 Ho (10.1016/j.mce.2020.110953_bib56) 2001; 122 Florman (10.1016/j.mce.2020.110953_bib47) 2008; 52 De Blas (10.1016/j.mce.2020.110953_bib39) 2009; 4 Aitken (10.1016/j.mce.2020.110953_bib2) 2002; 25 Marquez (10.1016/j.mce.2020.110953_bib91) 2007; 303 Koh (10.1016/j.mce.2020.110953_bib71) 2003; 26 Megnagi (10.1016/j.mce.2020.110953_bib96) 2015; 362 Qi (10.1016/j.mce.2020.110953_bib114) 2007; 104 Jaldety (10.1016/j.mce.2020.110953_bib66) 2012; 287 Harper (10.1016/j.mce.2020.110953_bib54) 2004; 279 Kumar (10.1016/j.mce.2020.110953_bib73) 2016; 473 Luconi (10.1016/j.mce.2020.110953_bib85) 1996; 55 Naaby-Hansen (10.1016/j.mce.2020.110953_bib104) 2002; 242 Li (10.1016/j.mce.2020.110953_bib78) 2015; 10 Baron (10.1016/j.mce.2020.110953_bib13) 2016; 4 Michailov (10.1016/j.mce.2020.110953_bib98) 2014; 396 Rotem (10.1016/j.mce.2020.110953_bib117) 1992; 131 Alasmari (10.1016/j.mce.2020.110953_bib3) 2013; 288 Miyata (10.1016/j.mce.2020.110953_bib101) 2015; 350 Zippin (10.1016/j.mce.2020.110953_bib147) 2013; 288 Dragileva (10.1016/j.mce.2020.110953_bib41) 1999; 61 Bray (10.1016/j.mce.2020.110953_bib19) 2005; 73 McMahon (10.1016/j.mce.2020.110953_bib95) 1995; 83 Jaldety (10.1016/j.mce.2020.110953_bib65) 2015; 23 Jahn (10.1016/j.mce.2020.110953_bib64) 2006; 7 Allouche-Fitoussi (10.1016/j.mce.2020.110953_bib4) 2018; 85 Wiesner (10.1016/j.mce.2020.110953_bib144) 1998; 142 Publicover (10.1016/j.mce.2020.110953_bib113) 2007; 9 Walensky (10.1016/j.mce.2020.110953_bib140) 1995; 130 Lang (10.1016/j.mce.2020.110953_bib74) 2008 Son (10.1016/j.mce.2020.110953_bib129) 2003; 68 Gur (10.1016/j.mce.2020.110953_bib53) 2006; 20 Cohen (10.1016/j.mce.2020.110953_bib35) 2014; 28 Itzhakov (10.1016/j.mce.2020.110953_bib62) 2019; 21 Varano (10.1016/j.mce.2020.110953_bib138) 2008; 23 Carrera (10.1016/j.mce.2020.110953_bib29) 1996; 180 Sakata (10.1016/j.mce.2020.110953_bib121) 2002; 516 Rotfeld (10.1016/j.mce.2020.110953_bib118) 2014; 147 Rossato (10.1016/j.mce.2020.110953_bib116) 2001; 7 Chung (10.1016/j.mce.2020.110953_bib34) 2014; 157 Rufo (10.1016/j.mce.2020.110953_bib120) 1984; 259 Avenarius (10.1016/j.mce.2020.110953_bib9) 2009; 84 Trevino (10.1016/j.mce.2020.110953_bib137) 1998; 6 Chavez (10.1016/j.mce.2020.110953_bib31) 2014; 289 Wang (10.1016/j.mce.2020.110953_bib142) 2020 Spungin (10.1016/j.mce.2020.110953_bib131) 1995; 108 Visconti (10.1016/j.mce.2020.110953_bib139) 1995; 121 Lobley (10.1016/j.mce.2020.110953_bib84) 2003; 1 Inaba (10.1016/j.mce.2020.110953_bib60) 2015; 4 Castellano (10.1016/j.mce.2020.110953_bib30) 2003; 541 Ho (10.1016/j.mce.2020.110953_bib55) 2002; 250 Wang (10.1016/j.mce.2020.110953_bib141) 2009; 81 Brukman (10.1016/j.mce.2020.110953_bib26) 2019; 234 Peddinti (10.1016/j.mce.2020.110953_bib111) 2008; 2 Marquez (10.1016/j.mce.2020.110953_bib92) 2007; 76 Luque (10.1016/j.mce.2020.110953_bib87) 2018; 233 Schiffer (10.1016/j.mce.2020.110953_bib124) 2020 Jagannathan (10.1016/j.mce.2020.110953_bib63) 2002; 277 Strunker (10.1016/j.mce.2020.110953_bib132) 2011; 471 Guidobaldi (10.1016/j.mce.2020.110953_bib52) 2017; 84 Barros (10.1016/j.mce.2020.110953_bib14) 1967; 34 Orta (10.1016/j.mce.2020.110953_bib109) 2018; 293 Mata-Martinez (10.1016/j.mce.2020.110953_bib93) 2018; 497 Suarez (10.1016/j.mce.2020.110953_bib133) 1993; 90 Buffone (10.1016/j.mce.2020.110953_bib27) 2009; 32 Goodson (10.1016/j.mce.2020.110953_bib51) 2011; 84 Branham (10.1016/j.mce.2020.110953_bib18) 2006; 281 Ho (10.1016/j.mce.2020.110953_bib57) 2001; 65 Lishko (10.1016/j.mce.2020.110953_bib80) 2010; 140 Brose (10.1016/j.mce.2020.110953_bib25) 2008; 9 Ren (10.1016/j.mce.2020.110953_bib115) 2001; 413 Gonzalez-Martinez (10.1016/j.mce.2020.110953_bib50) 2001; 236 Breitbart (10.1016/j.mce.2020.110953_bib22) 1996; 1312 Carlson (10.1016/j.mce.2020.110953_bib28) 2005; 280 Espino (10.1016/j.mce.2020.110953_bib43) 2009; 7 Lishko (10.1016/j.mce.2020.110953_bib81) 2011; 471 Liu (10.1016/j.mce.2020.110953_bib82) 2007; 282 Lax (10.1016/j.mce.2020.110953_bib76) 1994; 339 |
References_xml | – volume: 728 start-page: 349 year: 1983 end-page: 355 ident: bib23 article-title: Calcium transport and Ca 2+ -ATPase activity in ram spermatozoa plasma membrane vesicles publication-title: Biochim. Biophys. Acta – volume: 140 start-page: 327 year: 2010 end-page: 337 ident: bib80 article-title: Acid extrusion from human spermatozoa is mediated by flagellar voltage-gated proton channel publication-title: Cell – volume: 68 start-page: 1348 year: 2003 end-page: 1353 ident: bib129 article-title: Evidence suggesting that the mouse sperm acrosome reaction initiated by the zona pellucida involves an alpha7 nicotinic acetylcholine receptor publication-title: Biol. Reprod. – volume: 323 start-page: 474 year: 2009 end-page: 477 ident: bib134 article-title: Membrane fusion: grappling with SNARE and SM proteins publication-title: Science – volume: 230 start-page: 1758 year: 2015 end-page: 1769 ident: bib106 article-title: Biphasic role of calcium in mouse sperm capacitation signaling pathways publication-title: J. Cell. Physiol. – volume: 334 start-page: 447 year: 2009 end-page: 457 ident: bib44 article-title: Bovine sperm acrosome reaction induced by G-protein-coupled receptor agonists is mediated by epidermal growth factor receptor transactivation publication-title: Dev. Biol. – volume: 85 start-page: 543 year: 2018 end-page: 556 ident: bib4 article-title: Signaling pathways involved in human sperm hyperactivated motility stimulated by Zn(2) publication-title: Mol. Reprod. Dev. – volume: 3 start-page: 499 year: 2001 end-page: 502 ident: bib68 article-title: Trp2 regulates entry of Ca2+ into mouse sperm triggered by egg ZP3 publication-title: Nat. Cell Biol. – volume: 157 start-page: 808 year: 2014 end-page: 822 ident: bib34 article-title: Structurally distinct Ca publication-title: Cell – volume: 165 start-page: 10 year: 1994 end-page: 19 ident: bib36 article-title: Sperm chemotaxis: Egg peptides control cytosolic calcium to regulate flagellar responses publication-title: Dev. Biol. – volume: 84 start-page: 310 year: 2017 end-page: 315 ident: bib52 article-title: An intact acrosome is required for the chemotactic response to progesterone in mouse spermatozoa publication-title: Mol. Reprod. Dev. – volume: 516 start-page: 229 year: 2002 end-page: 233 ident: bib121 article-title: Ca(v)2.3 (alpha1E) Ca publication-title: FEBS Lett. – volume: 66 start-page: 429 year: 2002 end-page: 437 ident: bib88 article-title: Extracellular adenosine triphosphate stimulates acrosomal exocytosis in bovine spermatozoa via P2 purinoceptor publication-title: Biol. Reprod. – volume: 285 start-page: 39702 year: 2010 end-page: 39709 ident: bib46 article-title: Role and regulation of sperm gelsolin prior to fertilization publication-title: J. Biol. Chem. – volume: 471 start-page: 387 year: 2011 end-page: 391 ident: bib81 article-title: Progesterone activates the principal Ca publication-title: Nature – volume: 81 start-page: 539 year: 2009 end-page: 544 ident: bib141 article-title: A novel, single, transmembrane protein CATSPERG is associated with CATSPER1 channel protein publication-title: Biol. Reprod. – volume: 24 start-page: 2606 year: 2018 end-page: 2613 ident: bib99 article-title: Asymmetrically positioned flagellar control units regulate human sperm rotation publication-title: Cell Rep. – volume: 34 start-page: C1 year: 1967 end-page: C5 ident: bib14 article-title: Membrane vesiculation as a feature of the mammalian acrosome reaction publication-title: J. Cell Biol. – volume: 4 start-page: 1073 year: 2016 end-page: 1083 ident: bib13 article-title: Participation of protein kinases and phosphatases in the progesterone-induced acrosome reaction and calcium influx in human spermatozoa publication-title: Andrology – volume: 55 start-page: 207 year: 1996 end-page: 216 ident: bib85 article-title: Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa publication-title: Biol. Reprod. – volume: 541 start-page: 69 year: 2003 end-page: 74 ident: bib30 article-title: Transient receptor potential (TRPC) channels in human sperm: expression, cellular localization and involvement in the regulation of flagellar motility publication-title: FEBS Lett. – volume: 7 year: 2018 ident: bib103 article-title: TRPV4 is the temperature-sensitive ion channel of human sperm publication-title: Elife – volume: 114 start-page: 5743 year: 2017 end-page: 5748 ident: bib89 article-title: Regulation of the sperm calcium channel CatSper by endogenous steroids and plant triterpenoids publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 84 start-page: 1203 year: 2017 end-page: 1217 ident: bib110 article-title: Characterization of extracellular Ca publication-title: Mol. Reprod. Dev. – volume: 10 year: 2015 ident: bib78 article-title: Ejaculated mouse sperm enter cumulus-oocyte complexes more efficiently publication-title: PLoS One – volume: 33 start-page: 95 year: 2001 end-page: 104 ident: bib72 article-title: Capacitation-associated changes in protein tyrosine phosphorylation, hyperactivation and acrosome reaction in hamster spermatozoa publication-title: Andrologia – volume: 92 start-page: 759 year: 1998 end-page: 772 ident: bib143 article-title: SNAREpins: minimal machinery for membrane fusion publication-title: Cell – volume: 20 start-page: 1054 year: 2014 end-page: 1066 ident: bib15 article-title: Evidence for the involvement of proline-rich tyrosine kinase 2 in tyrosine phosphorylation downstream of protein kinase A activation during human sperm capacitation publication-title: Mol. Hum. Reprod. – volume: 288 start-page: 33283 year: 2013 end-page: 33291 ident: bib147 article-title: CO publication-title: J. Biol. Chem. – volume: 143 start-page: 2325 year: 2016 end-page: 2333 ident: bib5 article-title: The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm publication-title: Development – volume: 293 start-page: 16830 year: 2018 end-page: 16841 ident: bib109 article-title: CatSper channels are regulated by protein kinase A publication-title: J. Biol. Chem. – volume: 413 start-page: 603 year: 2001 end-page: 609 ident: bib115 article-title: A sperm ion channel required for sperm motility and male fertility publication-title: Nature – volume: 1312 start-page: 79 year: 1996 end-page: 84 ident: bib22 article-title: Calcium efflux mechanism in sperm mitochondria publication-title: Biochim. Biophys. Acta – volume: 65 start-page: 1606 year: 2001 end-page: 1615 ident: bib57 article-title: An inositol 1,4,5-trisphosphate receptor-gated intracellular Ca2+ store is involved in regulating sperm hyperactivated motility publication-title: Biol. Reprod. – volume: 30 start-page: 4119 year: 2011 end-page: 4125 ident: bib42 article-title: After half a century mitochondrial calcium in- and efflux machineries reveal themselves publication-title: EMBO J. – volume: 32 start-page: 360 year: 2009 end-page: 375 ident: bib27 article-title: Capacitation-associated changes in membrane fluidity in asthenozoospermic human spermatozoa publication-title: Int. J. Androl. – volume: 233 start-page: 9685 year: 2018 end-page: 9700 ident: bib87 article-title: Only a subpopulation of mouse sperm displays a rapid increase in intracellular calcium during capacitation publication-title: J. Cell. Physiol. – volume: 4 year: 2009 ident: bib135 article-title: Molecular mechanism for human sperm chemotaxis mediated by progesterone publication-title: PLoS One – volume: 11 year: 2016 ident: bib40 article-title: Heat sensing receptor TRPV1 is a mediator of thermotaxis in human spermatozoa publication-title: PLoS One – volume: 281 start-page: 8656 year: 2006 end-page: 8666 ident: bib18 article-title: Calcium-induced acrosomal exocytosis requires cAMP acting through a protein kinase A-independent, Epac-mediated pathway publication-title: J. Biol. Chem. – volume: 34 start-page: 414 year: 2019 end-page: 423 ident: bib86 article-title: A novel copy number variation in CATSPER2 causes idiopathic male infertility with normal semen parameters publication-title: Hum. Reprod. – volume: 471 start-page: 382 year: 2011 end-page: 386 ident: bib132 article-title: The CatSper channel mediates progesterone-induced Ca publication-title: Nature – year: 2020 ident: bib124 article-title: Rotational motion and rheotaxis of human sperm do not require functional CatSper channels and transmembrane Ca publication-title: EMBO J. – volume: 121 start-page: 1139 year: 1995 end-page: 1150 ident: bib139 article-title: Capacitation in mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway publication-title: Development – volume: 236 start-page: 220 year: 2001 end-page: 229 ident: bib50 article-title: A sustained increase in intracellular Ca publication-title: Dev. Biol. – volume: 1 start-page: 53 year: 2003 ident: bib84 article-title: Identification of human and mouse CatSper3 and CatSper4 genes: characterisation of a common interaction domain and evidence for expression in testis publication-title: Reprod. Biol. Endocrinol. – volume: 11 start-page: 1571 year: 2000 end-page: 1584 ident: bib108 article-title: Ca(2+) entry through store-operated channels in mouse sperm is initiated by egg ZP3 and drives the acrosome reaction publication-title: Mol. Biol. Cell – volume: 7 start-page: 119 year: 2001 end-page: 128 ident: bib116 article-title: Intracellular calcium store depletion and acrosome reaction in human spermatozoa: Role of calcium and plasma membrane potential publication-title: Mol. Hum. Reprod. – volume: 7 start-page: 11 year: 2009 ident: bib43 article-title: Reduced levels of intracellular calcium releasing in spermatozoa from asthenozoospermic patients publication-title: Reprod. Biol. Endocrinol. – volume: 289 start-page: 32266 year: 2014 end-page: 32275 ident: bib31 article-title: SLO publication-title: J. Biol. Chem. – volume: 161 start-page: 79 year: 2003 end-page: 88 ident: bib48 article-title: Phospholipase Cdelta4 is required for Ca2+ mobilization essential for acrosome reaction in sperm publication-title: J. Cell Biol. – volume: 68 start-page: 1590 year: 2003 end-page: 1596 ident: bib58 article-title: Characterization of the intracellular calcium store at the base of the sperm flagellum that regulates hyperactivated motility publication-title: Biol. Reprod. – volume: 84 start-page: 505 year: 2009 end-page: 510 ident: bib9 article-title: Human male infertility caused by mutations in the CATSPER1 channel protein publication-title: Am. J. Hum. Genet. – volume: 280 start-page: 32238 year: 2005 end-page: 32244 ident: bib28 article-title: Identical phenotypes of CatSper1 and CatSper2 null sperm publication-title: J. Biol. Chem. – volume: 122 start-page: 519 year: 2001 end-page: 526 ident: bib56 article-title: Hyperactivation of mammalian spermatozoa: Function and regulation publication-title: Reproduction – volume: 13 start-page: 307 year: 2007 end-page: 316 ident: bib75 article-title: Identification and localisation of SERCA 2 isoforms in mammalian sperm publication-title: Mol. Hum. Reprod. – volume: 21 start-page: 337 year: 2019 end-page: 344 ident: bib62 article-title: Protein kinase A inhibition induces EPAC-dependent acrosomal exocytosis in human sperm publication-title: Asian J. Androl. – volume: 180 start-page: 284 year: 1996 end-page: 296 ident: bib29 article-title: Regulation of protein tyrosine phosphorylation in human sperm by a calcium/calmodulin-dependent mechanism: identification of A kinase anchor proteins as major substrates for tyrosine phosphorylation publication-title: Dev. Biol. – volume: 129 start-page: 251 year: 2005 end-page: 262 ident: bib45 article-title: Molecular physiology and pathology of Ca publication-title: Reproduction – volume: 108 start-page: 2525 year: 1995 end-page: 2535 ident: bib131 article-title: Sperm exocytosis reconstructed in a cell-free system. Evidence for the involvement of phospholipase C and actin filaments in membrane fusion publication-title: J. Cell Sci. – volume: 95 start-page: 90 year: 2016 ident: bib6 article-title: Dynamics of bovine sperm interaction with epithelium differ between publication-title: Biol. Reprod. – volume: 25 start-page: 191 year: 2002 end-page: 194 ident: bib2 article-title: Reactive oxygen species generation by human spermatozoa: A continuing enigma publication-title: Int. J. Androl. – volume: 52 start-page: 503 year: 2008 end-page: 510 ident: bib47 article-title: Regulating the acrosome reaction publication-title: Int. J. Dev. Biol. – volume: 12 start-page: 43 year: 2014 ident: bib119 article-title: Epac, Rap and Rab3 act in concert to mobilize calcium from sperm's acrosome during exocytosis publication-title: Cell Commun. Signal. – volume: 91 start-page: 67 year: 2014 ident: bib123 article-title: Acrosome reaction and Ca publication-title: Biol. Reprod. – volume: 251 start-page: 3881 year: 1976 end-page: 3886 ident: bib11 article-title: Action of ionophore A23187 at the cellular level. Separation of effects at the plasma and mitochondrial membranes publication-title: J. Biol. Chem. – volume: 2 start-page: 19 year: 2008 ident: bib111 article-title: Comprehensive proteomic analysis of bovine spermatozoa of varying fertility rates and identification of biomarkers associated with fertility publication-title: BMC Syst. Biol. – volume: 46 start-page: 313 year: 2014 end-page: 315 ident: bib145 article-title: Assessment of sperm hyperactivated motility and acrosome reaction can discriminate the use of spermatozoa for conventional in vitro fertilisation or intracytoplasmic sperm injection: preliminary results publication-title: Andrologia – volume: 362 start-page: 665 year: 2015 end-page: 675 ident: bib96 article-title: The role and importance of cofilin in human sperm capacitation and the acrosome reaction publication-title: Cell Tissue Res. – volume: 283 start-page: 1902 year: 2016 end-page: 1920 ident: bib107 article-title: Calcium channels in chicken sperm regulate motility and the acrosome reaction publication-title: FEBS J. – volume: 76 start-page: 660 year: 2007 end-page: 665 ident: bib92 article-title: Bovine sperm hyperactivation is promoted by alkaline-stimulated Ca publication-title: Biol. Reprod. – volume: 396 start-page: 246 year: 2014 end-page: 255 ident: bib98 article-title: Zn publication-title: Dev. Biol. – volume: 109 start-page: 20497 year: 2012 end-page: 20502 ident: bib102 article-title: Calaxin drives sperm chemotaxis by Ca publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 2 start-page: 153 year: 2011 ident: bib33 article-title: A novel gene required for male fertility and functional CATSPER channel formation in spermatozoa publication-title: Nat. Commun. – volume: 28 start-page: 310 year: 2014 end-page: 321 ident: bib35 article-title: Lipid modulation of calcium flux through CaV2.3 regulates acrosome exocytosis and fertilization publication-title: Dev. Cell – volume: 142 start-page: 473 year: 1998 end-page: 484 ident: bib144 article-title: Cyclic nucleotide-gated channels on the flagellum control Ca publication-title: J. Cell Biol. – volume: 1 start-page: 381 year: 1980 end-page: 390 ident: bib16 article-title: A Ca2+ + Mg2+ -ATPase and active Ca2+ transport in the plasma membranes isolated from ram sperm flagella publication-title: Cell Calcium – volume: 108 start-page: 4892 year: 2011 end-page: 4896 ident: bib67 article-title: Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 267 start-page: 350 year: 1993 end-page: 355 ident: bib97 article-title: Initiation of the human sperm acrosome reaction by thapsigargin publication-title: J. Exp. Zool. – volume: 6 start-page: 33589 year: 2016 ident: bib105 article-title: Transient exposure to calcium ionophore enables in vitro fertilization in sterile mouse models publication-title: Sci. Rep. – volume: 110 start-page: 6823 year: 2013 end-page: 6828 ident: bib128 article-title: Disruption of the principal, progesterone-activated sperm Ca publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 303 start-page: 214 year: 2007 end-page: 221 ident: bib91 article-title: Contributions of extracellular and intracellular Ca publication-title: Dev. Biol. – volume: 464 start-page: 3 year: 2012 end-page: 17 ident: bib112 article-title: Mitochondrial Ca publication-title: Pflugers Arch. – volume: 17 start-page: 478 year: 2011 end-page: 499 ident: bib69 article-title: Rediscovering sperm ion channels with the patch-clamp technique publication-title: Mol. Hum. Reprod. – volume: 281 start-page: 473 year: 1992 end-page: 476 ident: bib21 article-title: Role of protein kinase C in the acrosome reaction of mammalian spermatozoa publication-title: Biochem. J. – volume: 88 start-page: 138 year: 2013 ident: bib49 article-title: Focal adhesion kinases and calcium/calmodulin-dependent protein kinases regulate protein tyrosine phosphorylation in stallion sperm publication-title: Biol. Reprod. – start-page: 107 year: 2008 end-page: 127 ident: bib74 article-title: Core proteins of the secretory machinery publication-title: Handb. Exp. Pharmacol. – volume: 90 start-page: 4660 year: 1993 end-page: 4664 ident: bib133 article-title: Intracellular calcium increases with hyperactivation in intact, moving hamster sperm and oscillates with the flagellar beat cycle publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 73 start-page: 519 year: 2005 end-page: 526 ident: bib59 article-title: Calcium/calmodulin and calmodulin kinase II stimulate hyperactivation in demembranated bovine sperm publication-title: Biol. Reprod. – volume: 23 start-page: 652 year: 2015 end-page: 661 ident: bib65 article-title: ERK1/2 mediates sperm acrosome reaction through elevation of intracellular calcium concentration publication-title: Zygote – volume: 104 start-page: 1219 year: 2007 end-page: 1223 ident: bib114 article-title: All four CatSper ion channel proteins are required for male fertility and sperm cell hyperactivated motility publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 121 start-page: 15 year: 1980 end-page: 18 ident: bib17 article-title: A sodium calcium exchange mechanism in plasma membrane vesicles isolated from ram flagella publication-title: FEBS (Fed. Eur. Biochem. Soc.) Lett. – volume: 20 start-page: 411 year: 2006 end-page: 416 ident: bib53 article-title: Mammalian sperm translate nuclear-encoded proteins by mitochondrial-type ribosomes publication-title: Genes Dev. – volume: 79 start-page: 1396 year: 2003 end-page: 1403 ident: bib90 article-title: Calcium requirements for human sperm function publication-title: Fertil. Steril. – volume: 147 start-page: 347 year: 2014 end-page: 356 ident: bib118 article-title: PKA and CaMKII mediate PI3K activation in bovine sperm by inhibition of the PKC/PP1 cascade publication-title: Reproduction – volume: 68 start-page: 837 year: 2003 end-page: 845 ident: bib24 article-title: Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction publication-title: Biol. Reprod. – volume: 250 start-page: 208 year: 2002 end-page: 217 ident: bib55 article-title: Hyperactivated motility of bull sperm is triggered at the axoneme by Ca publication-title: Dev. Biol. – volume: 67 start-page: 301 year: 2002 end-page: 307 ident: bib77 article-title: Regulation of the human sperm tyrosine kinase c-yes. Activation by cyclic adenosine 3',5'-monophosphate and inhibition by Ca 2+ publication-title: Biol. Reprod. – volume: 83 start-page: 111 year: 1995 end-page: 119 ident: bib95 article-title: Complexins: Cytosolic proteins that regulate SNAP receptor function publication-title: Cell – volume: 473 start-page: 781 year: 2016 end-page: 788 ident: bib73 article-title: TRPV4 is endogenously expressed in vertebrate spermatozoa and regulates intracellular calcium in human sperm publication-title: Biochem. Biophys. Res. Commun. – volume: 7 start-page: 631 year: 2006 end-page: 643 ident: bib64 article-title: SNAREs--engines for membrane fusion publication-title: Nat. Rev. Mol. Cell Biol. – volume: 23 start-page: 2652 year: 2008 end-page: 2662 ident: bib138 article-title: Src activation triggers capacitation and acrosome reaction but not motility in human spermatozoa publication-title: Hum. Reprod. – volume: 362 start-page: 154 year: 2012 end-page: 161 ident: bib61 article-title: Hyper-activated motility in sperm capacitation is mediated by phospholipase D-dependent actin polymerization publication-title: Dev. Biol. – volume: 288 start-page: 6248 year: 2013 end-page: 6258 ident: bib3 article-title: Ca publication-title: J. Biol. Chem. – volume: 259 start-page: 2547 year: 1984 end-page: 2552 ident: bib120 article-title: Regulation of calcium content in bovine spermatozoa publication-title: J. Biol. Chem. – volume: 277 start-page: 8449 year: 2002 end-page: 8456 ident: bib63 article-title: Identification and localization of T-type voltage-operated calcium channel subunits in human male germ cells. Expression of multiple isoforms publication-title: J. Biol. Chem. – volume: 131 start-page: 2235 year: 1992 end-page: 2243 ident: bib117 article-title: Ca 2+ -independent induction of acrosome reaction by protein kinase C in human sperm publication-title: Endocrinology – volume: 99 start-page: 1010 year: 2018 end-page: 1021 ident: bib122 article-title: Intracellular Ca publication-title: Biol. Reprod. – volume: 122 start-page: 4547 year: 2009 end-page: 4557 ident: bib1 article-title: CaMKIIalpha interacts with multi-PDZ domain protein MUPP1 in spermatozoa and prevents spontaneous acrosomal exocytosis publication-title: J. Cell Sci. – year: 2020 ident: bib142 article-title: Shedding Light on the Control of CatSper Ca – volume: 234 start-page: 5276 year: 2019 end-page: 5288 ident: bib26 article-title: Tyrosine phosphorylation signaling regulates Ca publication-title: J. Cell. Physiol. – volume: 6 start-page: 159 year: 1998 end-page: 172 ident: bib137 article-title: Localisation of inositol trisphosphate and ryanodine receptors during mouse spermatogenesis: Possible functional implications publication-title: Zygote – volume: 9 start-page: 1403 year: 2008 end-page: 1413 ident: bib25 article-title: For better or for worse: complexins regulate SNARE function and vesicle fusion publication-title: Traffic – volume: 339 start-page: 234 year: 1994 end-page: 238 ident: bib76 article-title: Epidermal growth factor induces acrosomal exocytosis in bovine sperm publication-title: FEBS (Fed. Eur. Biochem. Soc.) Lett. – volume: 130 start-page: 857 year: 1995 end-page: 869 ident: bib140 article-title: Inositol 1,4,5-trisphosphate receptors selectively localized to the acrosomes of mammalian sperm publication-title: J. Cell Biol. – volume: 282 start-page: 18945 year: 2007 end-page: 18952 ident: bib82 article-title: CatSperb, a novel transmembrane protein in the CatSper channel complex publication-title: J. Biol. Chem. – volume: 11 start-page: 497 year: 2003 end-page: 502 ident: bib10 article-title: CATSPER2, a human autosomal nonsyndromic male infertility gene publication-title: Eur. J. Hum. Genet. – volume: 8 start-page: 442 year: 2020 end-page: 449 ident: bib94 article-title: Human sperm capacitation is necessary for SNARE assembly in neurotoxin-resistant complexes publication-title: Andrology – volume: 350 start-page: 442 year: 2015 end-page: 445 ident: bib101 article-title: Sperm calcineurin inhibition prevents mouse fertility with implications for male contraceptive publication-title: Science – volume: 242 start-page: 236 year: 2002 end-page: 254 ident: bib104 article-title: CABYR, a novel calcium-binding tyrosine phosphorylation-regulated fibrous sheath protein involved in capacitation publication-title: Dev. Biol. – volume: 497 start-page: 146 year: 2018 end-page: 152 ident: bib93 article-title: pH-dependent Ca publication-title: Biochem. Biophys. Res. Commun. – volume: 63 start-page: 623 year: 2006 end-page: 632 ident: bib126 article-title: Na+/Ca publication-title: Cell Motil Cytoskeleton – volume: 262 start-page: 15041 year: 1987 end-page: 15047 ident: bib12 article-title: Independent elevation of cytosolic Ca2+ and pH of mammalian sperm by voltage dependent and pH sensitive mechanisms publication-title: J. Biol. Chem. – volume: 243 start-page: 79 year: 2005 end-page: 172 ident: bib38 article-title: Calcium channels and Ca publication-title: Int. Rev. Cytol. – volume: 96 start-page: 6757 year: 1999 end-page: 6762 ident: bib8 article-title: Control of the low voltage-activated calcium channel of mouse sperm by egg ZP3 and by membrane hyperpolarization during capacitation publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 279 start-page: 46315 year: 2004 end-page: 46325 ident: bib54 article-title: Stimulation of human spermatozoa with progesterone gradients to simulate approach to the oocyte. Induction of [Ca publication-title: J. Biol. Chem. – volume: 26 start-page: 413 year: 2003 end-page: 422 ident: bib71 article-title: Synaptotagmin I, a Ca publication-title: Trends Neurosci. – volume: 115 start-page: E11847 year: 2018 end-page: E11856 ident: bib146 article-title: Role of human Hv1 channels in sperm capacitation and white blood cell respiratory burst established by a designed peptide inhibitor publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 287 start-page: 22328 year: 2012 end-page: 22340 ident: bib66 article-title: Sperm epidermal growth factor receptor (EGFR) mediates alpha7 acetylcholine receptor (AChR) activation to promote fertilization publication-title: J. Biol. Chem. – volume: 73 start-page: 807 year: 2005 end-page: 814 ident: bib19 article-title: Mice deficient in CHRNA7, a subunit of the nicotinic acetylcholine receptor, produce sperm with impaired motility publication-title: Biol. Reprod. – volume: 109 start-page: 1947 year: 1996 end-page: 1955 ident: bib130 article-title: Calcium mobilization and influx during sperm exocytosis publication-title: J. Cell Sci. – volume: 289 start-page: 625 year: 2000 end-page: 628 ident: bib32 article-title: Soluble adenylyl cyclase as an evolutionarily conserved bicarbonate sensor publication-title: Science – volume: 4 year: 2009 ident: bib39 article-title: TRPM8, a versatile channel in human sperm publication-title: PLoS One – volume: 84 start-page: 1207 year: 2011 end-page: 1215 ident: bib51 article-title: Classification of mouse sperm motility patterns using an automated multiclass support vector machines model publication-title: Biol. Reprod. – volume: 388 start-page: 150 year: 1996 end-page: 154 ident: bib79 article-title: T-type Ca publication-title: FEBS Lett. – volume: 93 start-page: 13004 year: 1996 end-page: 13009 ident: bib7 article-title: Activation of mouse sperm T-type Ca publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 51 start-page: 84 year: 1998 end-page: 91 ident: bib83 article-title: Thapsigargin stimulates acrosomal exocytosis in hamster spermatozoa publication-title: Mol. Reprod. Dev. – volume: 9 start-page: 235 year: 2007 end-page: 242 ident: bib113 article-title: [Ca publication-title: Nat. Cell Biol. – volume: 439 start-page: 737 year: 2006 end-page: 740 ident: bib70 article-title: Whole-cell patch-clamp measurements of spermatozoa reveal an alkaline-activated Ca2+ channel publication-title: Nature – volume: 415 start-page: 64 year: 2016 end-page: 74 ident: bib125 article-title: CaMKII prevents spontaneous acrosomal exocytosis in sperm through induction of actin polymerization publication-title: Dev. Biol. – volume: 4 start-page: 6 year: 2015 ident: bib60 article-title: Calcium sensors of ciliary outer arm dynein: Functions and phylogenetic considerations for eukaryotic evolution publication-title: Cilia – volume: 67 start-page: 782 year: 2002 end-page: 788 ident: bib20 article-title: A nicotinic acetylcholine receptor is involved in the arosome reaction of human sperm initiated by recombinant human ZP3 publication-title: Biol. Reprod. – volume: 91 start-page: 1305 year: 2011 end-page: 1355 ident: bib37 article-title: Calcium channels in the development, maturation, and function of spermatozoa publication-title: Physiol. Rev. – volume: 61 start-page: 1226 year: 1999 end-page: 1234 ident: bib41 article-title: Intracellular Ca publication-title: Biol. Reprod. – volume: 8 start-page: 2014 year: 2018 ident: bib127 article-title: Crystal structure of a Ca publication-title: Sci. Rep. – volume: 563 start-page: 87 year: 2004 end-page: 92 ident: bib136 article-title: Expression and differential cell distribution of low-threshold Ca(2+) channels in mammalian male germ cells and sperm publication-title: FEBS Lett. – volume: 352 start-page: 555 year: 2016 end-page: 559 ident: bib100 article-title: Unconventional endocannabinoid signaling governs sperm activation via the sex hormone progesterone publication-title: Science – volume: 1 start-page: 53 year: 2003 ident: 10.1016/j.mce.2020.110953_bib84 article-title: Identification of human and mouse CatSper3 and CatSper4 genes: characterisation of a common interaction domain and evidence for expression in testis publication-title: Reprod. Biol. Endocrinol. doi: 10.1186/1477-7827-1-53 – volume: 243 start-page: 79 year: 2005 ident: 10.1016/j.mce.2020.110953_bib38 article-title: Calcium channels and Ca2+ fluctuations in sperm physiology publication-title: Int. Rev. Cytol. doi: 10.1016/S0074-7696(05)43002-8 – volume: 33 start-page: 95 year: 2001 ident: 10.1016/j.mce.2020.110953_bib72 article-title: Capacitation-associated changes in protein tyrosine phosphorylation, hyperactivation and acrosome reaction in hamster spermatozoa publication-title: Andrologia doi: 10.1046/j.1439-0272.2001.00410.x – volume: 73 start-page: 807 year: 2005 ident: 10.1016/j.mce.2020.110953_bib19 article-title: Mice deficient in CHRNA7, a subunit of the nicotinic acetylcholine receptor, produce sperm with impaired motility publication-title: Biol. Reprod. doi: 10.1095/biolreprod.105.042184 – volume: 52 start-page: 503 year: 2008 ident: 10.1016/j.mce.2020.110953_bib47 article-title: Regulating the acrosome reaction publication-title: Int. J. Dev. Biol. doi: 10.1387/ijdb.082696hf – volume: 11 start-page: 1571 year: 2000 ident: 10.1016/j.mce.2020.110953_bib108 article-title: Ca(2+) entry through store-operated channels in mouse sperm is initiated by egg ZP3 and drives the acrosome reaction publication-title: Mol. Biol. Cell doi: 10.1091/mbc.11.5.1571 – volume: 108 start-page: 2525 year: 1995 ident: 10.1016/j.mce.2020.110953_bib131 article-title: Sperm exocytosis reconstructed in a cell-free system. Evidence for the involvement of phospholipase C and actin filaments in membrane fusion publication-title: J. Cell Sci. doi: 10.1242/jcs.108.6.2525 – volume: 142 start-page: 473 year: 1998 ident: 10.1016/j.mce.2020.110953_bib144 article-title: Cyclic nucleotide-gated channels on the flagellum control Ca2+ entry into sperm publication-title: J. Cell Biol. doi: 10.1083/jcb.142.2.473 – volume: 68 start-page: 837 year: 2003 ident: 10.1016/j.mce.2020.110953_bib24 article-title: Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction publication-title: Biol. Reprod. doi: 10.1095/biolreprod.102.009233 – volume: 9 start-page: 1403 year: 2008 ident: 10.1016/j.mce.2020.110953_bib25 article-title: For better or for worse: complexins regulate SNARE function and vesicle fusion publication-title: Traffic doi: 10.1111/j.1600-0854.2008.00758.x – volume: 30 start-page: 4119 year: 2011 ident: 10.1016/j.mce.2020.110953_bib42 article-title: After half a century mitochondrial calcium in- and efflux machineries reveal themselves publication-title: EMBO J. doi: 10.1038/emboj.2011.337 – volume: 285 start-page: 39702 year: 2010 ident: 10.1016/j.mce.2020.110953_bib46 article-title: Role and regulation of sperm gelsolin prior to fertilization publication-title: J. Biol. Chem. doi: 10.1074/jbc.M110.170951 – volume: 4 year: 2009 ident: 10.1016/j.mce.2020.110953_bib135 article-title: Molecular mechanism for human sperm chemotaxis mediated by progesterone publication-title: PLoS One doi: 10.1371/journal.pone.0008211 – volume: 242 start-page: 236 year: 2002 ident: 10.1016/j.mce.2020.110953_bib104 article-title: CABYR, a novel calcium-binding tyrosine phosphorylation-regulated fibrous sheath protein involved in capacitation publication-title: Dev. Biol. doi: 10.1006/dbio.2001.0527 – volume: 65 start-page: 1606 year: 2001 ident: 10.1016/j.mce.2020.110953_bib57 article-title: An inositol 1,4,5-trisphosphate receptor-gated intracellular Ca2+ store is involved in regulating sperm hyperactivated motility publication-title: Biol. Reprod. doi: 10.1095/biolreprod65.5.1606 – volume: 20 start-page: 1054 year: 2014 ident: 10.1016/j.mce.2020.110953_bib15 article-title: Evidence for the involvement of proline-rich tyrosine kinase 2 in tyrosine phosphorylation downstream of protein kinase A activation during human sperm capacitation publication-title: Mol. Hum. Reprod. doi: 10.1093/molehr/gau073 – volume: 157 start-page: 808 year: 2014 ident: 10.1016/j.mce.2020.110953_bib34 article-title: Structurally distinct Ca2+ signaling domains of sperm flagella orchestrate tyrosine phosphorylation and motility publication-title: Cell doi: 10.1016/j.cell.2014.02.056 – volume: 93 start-page: 13004 year: 1996 ident: 10.1016/j.mce.2020.110953_bib7 article-title: Activation of mouse sperm T-type Ca2+ channels by adhesion to the egg zona pellucida publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.93.23.13004 – volume: 84 start-page: 1207 year: 2011 ident: 10.1016/j.mce.2020.110953_bib51 article-title: Classification of mouse sperm motility patterns using an automated multiclass support vector machines model publication-title: Biol. Reprod. doi: 10.1095/biolreprod.110.088989 – volume: 728 start-page: 349 year: 1983 ident: 10.1016/j.mce.2020.110953_bib23 article-title: Calcium transport and Ca 2+ -ATPase activity in ram spermatozoa plasma membrane vesicles publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2736(83)90505-9 – volume: 7 start-page: 119 year: 2001 ident: 10.1016/j.mce.2020.110953_bib116 article-title: Intracellular calcium store depletion and acrosome reaction in human spermatozoa: Role of calcium and plasma membrane potential publication-title: Mol. Hum. Reprod. doi: 10.1093/molehr/7.2.119 – volume: 143 start-page: 2325 year: 2016 ident: 10.1016/j.mce.2020.110953_bib5 article-title: The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm publication-title: Development doi: 10.1242/dev.136499 – volume: 95 start-page: 90 year: 2016 ident: 10.1016/j.mce.2020.110953_bib6 article-title: Dynamics of bovine sperm interaction with epithelium differ between Oviductal isthmus and Ampulla publication-title: Biol. Reprod. doi: 10.1095/biolreprod.116.140632 – volume: 7 year: 2018 ident: 10.1016/j.mce.2020.110953_bib103 article-title: TRPV4 is the temperature-sensitive ion channel of human sperm publication-title: Elife doi: 10.7554/eLife.35853 – volume: 91 start-page: 1305 year: 2011 ident: 10.1016/j.mce.2020.110953_bib37 article-title: Calcium channels in the development, maturation, and function of spermatozoa publication-title: Physiol. Rev. doi: 10.1152/physrev.00028.2010 – volume: 51 start-page: 84 year: 1998 ident: 10.1016/j.mce.2020.110953_bib83 article-title: Thapsigargin stimulates acrosomal exocytosis in hamster spermatozoa publication-title: Mol. Reprod. Dev. doi: 10.1002/(SICI)1098-2795(199809)51:1<84::AID-MRD10>3.0.CO;2-U – volume: 8 start-page: 442 year: 2020 ident: 10.1016/j.mce.2020.110953_bib94 article-title: Human sperm capacitation is necessary for SNARE assembly in neurotoxin-resistant complexes publication-title: Andrology doi: 10.1111/andr.12706 – volume: 130 start-page: 857 year: 1995 ident: 10.1016/j.mce.2020.110953_bib140 article-title: Inositol 1,4,5-trisphosphate receptors selectively localized to the acrosomes of mammalian sperm publication-title: J. Cell Biol. doi: 10.1083/jcb.130.4.857 – volume: 4 start-page: 6 year: 2015 ident: 10.1016/j.mce.2020.110953_bib60 article-title: Calcium sensors of ciliary outer arm dynein: Functions and phylogenetic considerations for eukaryotic evolution publication-title: Cilia doi: 10.1186/s13630-015-0015-z – volume: 55 start-page: 207 year: 1996 ident: 10.1016/j.mce.2020.110953_bib85 article-title: Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa publication-title: Biol. Reprod. doi: 10.1095/biolreprod55.1.207 – volume: 289 start-page: 32266 year: 2014 ident: 10.1016/j.mce.2020.110953_bib31 article-title: SLO3 K+ channels control calcium entry through CATSPER channels in sperm publication-title: J. Biol. Chem. doi: 10.1074/jbc.M114.607556 – volume: 7 start-page: 11 year: 2009 ident: 10.1016/j.mce.2020.110953_bib43 article-title: Reduced levels of intracellular calcium releasing in spermatozoa from asthenozoospermic patients publication-title: Reprod. Biol. Endocrinol. doi: 10.1186/1477-7827-7-11 – volume: 6 start-page: 33589 year: 2016 ident: 10.1016/j.mce.2020.110953_bib105 article-title: Transient exposure to calcium ionophore enables in vitro fertilization in sterile mouse models publication-title: Sci. Rep. doi: 10.1038/srep33589 – volume: 471 start-page: 387 year: 2011 ident: 10.1016/j.mce.2020.110953_bib81 article-title: Progesterone activates the principal Ca2+ channel of human sperm publication-title: Nature doi: 10.1038/nature09767 – volume: 464 start-page: 3 year: 2012 ident: 10.1016/j.mce.2020.110953_bib112 article-title: Mitochondrial Ca2+ homeostasis: Mechanism, role, and tissue specificities publication-title: Pflugers Arch. doi: 10.1007/s00424-012-1122-y – volume: 122 start-page: 4547 year: 2009 ident: 10.1016/j.mce.2020.110953_bib1 article-title: CaMKIIalpha interacts with multi-PDZ domain protein MUPP1 in spermatozoa and prevents spontaneous acrosomal exocytosis publication-title: J. Cell Sci. doi: 10.1242/jcs.058263 – volume: 334 start-page: 447 year: 2009 ident: 10.1016/j.mce.2020.110953_bib44 article-title: Bovine sperm acrosome reaction induced by G-protein-coupled receptor agonists is mediated by epidermal growth factor receptor transactivation publication-title: Dev. Biol. doi: 10.1016/j.ydbio.2009.08.002 – volume: 230 start-page: 1758 year: 2015 ident: 10.1016/j.mce.2020.110953_bib106 article-title: Biphasic role of calcium in mouse sperm capacitation signaling pathways publication-title: J. Cell. Physiol. doi: 10.1002/jcp.24873 – volume: 303 start-page: 214 year: 2007 ident: 10.1016/j.mce.2020.110953_bib91 article-title: Contributions of extracellular and intracellular Ca2+ to regulation of sperm motility: Release of intracellular stores can hyperactivate CatSper1 and CatSper2 null sperm publication-title: Dev. Biol. doi: 10.1016/j.ydbio.2006.11.007 – volume: 20 start-page: 411 year: 2006 ident: 10.1016/j.mce.2020.110953_bib53 article-title: Mammalian sperm translate nuclear-encoded proteins by mitochondrial-type ribosomes publication-title: Genes Dev. doi: 10.1101/gad.367606 – volume: 287 start-page: 22328 year: 2012 ident: 10.1016/j.mce.2020.110953_bib66 article-title: Sperm epidermal growth factor receptor (EGFR) mediates alpha7 acetylcholine receptor (AChR) activation to promote fertilization publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111.292292 – volume: 563 start-page: 87 year: 2004 ident: 10.1016/j.mce.2020.110953_bib136 article-title: Expression and differential cell distribution of low-threshold Ca(2+) channels in mammalian male germ cells and sperm publication-title: FEBS Lett. doi: 10.1016/S0014-5793(04)00257-1 – volume: 11 start-page: 497 year: 2003 ident: 10.1016/j.mce.2020.110953_bib10 article-title: CATSPER2, a human autosomal nonsyndromic male infertility gene publication-title: Eur. J. Hum. Genet. doi: 10.1038/sj.ejhg.5200991 – volume: 92 start-page: 759 year: 1998 ident: 10.1016/j.mce.2020.110953_bib143 article-title: SNAREpins: minimal machinery for membrane fusion publication-title: Cell doi: 10.1016/S0092-8674(00)81404-X – volume: 234 start-page: 5276 year: 2019 ident: 10.1016/j.mce.2020.110953_bib26 article-title: Tyrosine phosphorylation signaling regulates Ca2+ entry by affecting intracellular pH during human sperm capacitation publication-title: J. Cell. Physiol. doi: 10.1002/jcp.27337 – volume: 516 start-page: 229 year: 2002 ident: 10.1016/j.mce.2020.110953_bib121 article-title: Ca(v)2.3 (alpha1E) Ca2+ channel participates in the control of sperm function publication-title: FEBS Lett. doi: 10.1016/S0014-5793(02)02529-2 – volume: 129 start-page: 251 year: 2005 ident: 10.1016/j.mce.2020.110953_bib45 article-title: Molecular physiology and pathology of Ca2+-conducting channels in the plasma membrane of mammalian sperm publication-title: Reproduction doi: 10.1530/rep.1.00478 – volume: 21 start-page: 337 year: 2019 ident: 10.1016/j.mce.2020.110953_bib62 article-title: Protein kinase A inhibition induces EPAC-dependent acrosomal exocytosis in human sperm publication-title: Asian J. Androl. doi: 10.4103/aja.aja_99_18 – volume: 68 start-page: 1348 year: 2003 ident: 10.1016/j.mce.2020.110953_bib129 article-title: Evidence suggesting that the mouse sperm acrosome reaction initiated by the zona pellucida involves an alpha7 nicotinic acetylcholine receptor publication-title: Biol. Reprod. doi: 10.1095/biolreprod.102.011163 – volume: 46 start-page: 313 year: 2014 ident: 10.1016/j.mce.2020.110953_bib145 article-title: Assessment of sperm hyperactivated motility and acrosome reaction can discriminate the use of spermatozoa for conventional in vitro fertilisation or intracytoplasmic sperm injection: preliminary results publication-title: Andrologia doi: 10.1111/and.12068 – volume: 1 start-page: 381 year: 1980 ident: 10.1016/j.mce.2020.110953_bib16 article-title: A Ca2+ + Mg2+ -ATPase and active Ca2+ transport in the plasma membranes isolated from ram sperm flagella publication-title: Cell Calcium doi: 10.1016/0143-4160(80)90040-8 – volume: 99 start-page: 1010 year: 2018 ident: 10.1016/j.mce.2020.110953_bib122 article-title: Intracellular Ca2+ threshold reversibly switches flagellar beat off and on publication-title: Biol. Reprod. doi: 10.1093/biolre/ioy132 – start-page: 107 year: 2008 ident: 10.1016/j.mce.2020.110953_bib74 article-title: Core proteins of the secretory machinery publication-title: Handb. Exp. Pharmacol. doi: 10.1007/978-3-540-74805-2_5 – volume: 66 start-page: 429 year: 2002 ident: 10.1016/j.mce.2020.110953_bib88 article-title: Extracellular adenosine triphosphate stimulates acrosomal exocytosis in bovine spermatozoa via P2 purinoceptor publication-title: Biol. Reprod. doi: 10.1095/biolreprod66.2.429 – volume: 250 start-page: 208 year: 2002 ident: 10.1016/j.mce.2020.110953_bib55 article-title: Hyperactivated motility of bull sperm is triggered at the axoneme by Ca2+ and not cAMP publication-title: Dev. Biol. doi: 10.1006/dbio.2002.0797 – volume: 281 start-page: 8656 year: 2006 ident: 10.1016/j.mce.2020.110953_bib18 article-title: Calcium-induced acrosomal exocytosis requires cAMP acting through a protein kinase A-independent, Epac-mediated pathway publication-title: J. Biol. Chem. doi: 10.1074/jbc.M508854200 – volume: 1312 start-page: 79 year: 1996 ident: 10.1016/j.mce.2020.110953_bib22 article-title: Calcium efflux mechanism in sperm mitochondria publication-title: Biochim. Biophys. Acta doi: 10.1016/0167-4889(96)00022-5 – volume: 10 year: 2015 ident: 10.1016/j.mce.2020.110953_bib78 article-title: Ejaculated mouse sperm enter cumulus-oocyte complexes more efficiently in vitro than epididymal sperm publication-title: PLoS One – volume: 165 start-page: 10 year: 1994 ident: 10.1016/j.mce.2020.110953_bib36 article-title: Sperm chemotaxis: Egg peptides control cytosolic calcium to regulate flagellar responses publication-title: Dev. Biol. doi: 10.1006/dbio.1994.1229 – volume: 279 start-page: 46315 year: 2004 ident: 10.1016/j.mce.2020.110953_bib54 article-title: Stimulation of human spermatozoa with progesterone gradients to simulate approach to the oocyte. Induction of [Ca2+]i oscillations and cyclical transitions in flagellar beating publication-title: J. Biol. Chem. doi: 10.1074/jbc.M401194200 – volume: 34 start-page: C1 year: 1967 ident: 10.1016/j.mce.2020.110953_bib14 article-title: Membrane vesiculation as a feature of the mammalian acrosome reaction publication-title: J. Cell Biol. doi: 10.1083/jcb.34.3.C1 – volume: 396 start-page: 246 year: 2014 ident: 10.1016/j.mce.2020.110953_bib98 article-title: Zn2+-stimulation of sperm capacitation and of the acrosome reaction is mediated by EGFR activation publication-title: Dev. Biol. doi: 10.1016/j.ydbio.2014.10.009 – volume: 147 start-page: 347 year: 2014 ident: 10.1016/j.mce.2020.110953_bib118 article-title: PKA and CaMKII mediate PI3K activation in bovine sperm by inhibition of the PKC/PP1 cascade publication-title: Reproduction doi: 10.1530/REP-13-0560 – volume: 121 start-page: 15 year: 1980 ident: 10.1016/j.mce.2020.110953_bib17 article-title: A sodium calcium exchange mechanism in plasma membrane vesicles isolated from ram flagella publication-title: FEBS (Fed. Eur. Biochem. Soc.) Lett. doi: 10.1016/0014-5793(80)81255-5 – volume: 140 start-page: 327 year: 2010 ident: 10.1016/j.mce.2020.110953_bib80 article-title: Acid extrusion from human spermatozoa is mediated by flagellar voltage-gated proton channel publication-title: Cell doi: 10.1016/j.cell.2009.12.053 – volume: 109 start-page: 20497 year: 2012 ident: 10.1016/j.mce.2020.110953_bib102 article-title: Calaxin drives sperm chemotaxis by Ca2+-mediated direct modulation of a dynein motor publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1217018109 – volume: 67 start-page: 782 year: 2002 ident: 10.1016/j.mce.2020.110953_bib20 article-title: A nicotinic acetylcholine receptor is involved in the arosome reaction of human sperm initiated by recombinant human ZP3 publication-title: Biol. Reprod. doi: 10.1095/biolreprod.102.004580 – volume: 288 start-page: 6248 year: 2013 ident: 10.1016/j.mce.2020.110953_bib3 article-title: Ca2+ signals generated by CatSper and Ca2+ stores regulate different behaviors in human sperm publication-title: J. Biol. Chem. doi: 10.1074/jbc.M112.439356 – volume: 161 start-page: 79 year: 2003 ident: 10.1016/j.mce.2020.110953_bib48 article-title: Phospholipase Cdelta4 is required for Ca2+ mobilization essential for acrosome reaction in sperm publication-title: J. Cell Biol. doi: 10.1083/jcb.200210057 – volume: 281 start-page: 473 year: 1992 ident: 10.1016/j.mce.2020.110953_bib21 article-title: Role of protein kinase C in the acrosome reaction of mammalian spermatozoa publication-title: Biochem. J. doi: 10.1042/bj2810473 – volume: 415 start-page: 64 year: 2016 ident: 10.1016/j.mce.2020.110953_bib125 article-title: CaMKII prevents spontaneous acrosomal exocytosis in sperm through induction of actin polymerization publication-title: Dev. Biol. doi: 10.1016/j.ydbio.2016.05.008 – volume: 110 start-page: 6823 year: 2013 ident: 10.1016/j.mce.2020.110953_bib128 article-title: Disruption of the principal, progesterone-activated sperm Ca2+ channel in a CatSper2-deficient infertile patient publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1216588110 – volume: 131 start-page: 2235 year: 1992 ident: 10.1016/j.mce.2020.110953_bib117 article-title: Ca 2+ -independent induction of acrosome reaction by protein kinase C in human sperm publication-title: Endocrinology doi: 10.1210/endo.131.5.1425422 – volume: 11 year: 2016 ident: 10.1016/j.mce.2020.110953_bib40 article-title: Heat sensing receptor TRPV1 is a mediator of thermotaxis in human spermatozoa publication-title: PLoS One doi: 10.1371/journal.pone.0167622 – volume: 76 start-page: 660 year: 2007 ident: 10.1016/j.mce.2020.110953_bib92 article-title: Bovine sperm hyperactivation is promoted by alkaline-stimulated Ca2+ influx publication-title: Biol. Reprod. doi: 10.1095/biolreprod.106.055038 – volume: 63 start-page: 623 year: 2006 ident: 10.1016/j.mce.2020.110953_bib126 article-title: Na+/Ca2+ exchanger modulates the flagellar wave pattern for the regulation of motility activation and chemotaxis in the ascidian spermatozoa publication-title: Cell Motil Cytoskeleton doi: 10.1002/cm.20149 – year: 2020 ident: 10.1016/j.mce.2020.110953_bib124 article-title: Rotational motion and rheotaxis of human sperm do not require functional CatSper channels and transmembrane Ca2+ signaling publication-title: EMBO J. doi: 10.15252/embj.2019102363 – volume: 439 start-page: 737 year: 2006 ident: 10.1016/j.mce.2020.110953_bib70 article-title: Whole-cell patch-clamp measurements of spermatozoa reveal an alkaline-activated Ca2+ channel publication-title: Nature doi: 10.1038/nature04417 – volume: 362 start-page: 665 year: 2015 ident: 10.1016/j.mce.2020.110953_bib96 article-title: The role and importance of cofilin in human sperm capacitation and the acrosome reaction publication-title: Cell Tissue Res. doi: 10.1007/s00441-015-2229-1 – volume: 473 start-page: 781 year: 2016 ident: 10.1016/j.mce.2020.110953_bib73 article-title: TRPV4 is endogenously expressed in vertebrate spermatozoa and regulates intracellular calcium in human sperm publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2016.03.071 – volume: 25 start-page: 191 year: 2002 ident: 10.1016/j.mce.2020.110953_bib2 article-title: Reactive oxygen species generation by human spermatozoa: A continuing enigma publication-title: Int. J. Androl. doi: 10.1046/j.1365-2605.2002.03521.x – volume: 104 start-page: 1219 year: 2007 ident: 10.1016/j.mce.2020.110953_bib114 article-title: All four CatSper ion channel proteins are required for male fertility and sperm cell hyperactivated motility publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0610286104 – volume: 7 start-page: 631 year: 2006 ident: 10.1016/j.mce.2020.110953_bib64 article-title: SNAREs--engines for membrane fusion publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm2002 – volume: 2 start-page: 19 year: 2008 ident: 10.1016/j.mce.2020.110953_bib111 article-title: Comprehensive proteomic analysis of bovine spermatozoa of varying fertility rates and identification of biomarkers associated with fertility publication-title: BMC Syst. Biol. doi: 10.1186/1752-0509-2-19 – volume: 32 start-page: 360 year: 2009 ident: 10.1016/j.mce.2020.110953_bib27 article-title: Capacitation-associated changes in membrane fluidity in asthenozoospermic human spermatozoa publication-title: Int. J. Androl. doi: 10.1111/j.1365-2605.2008.00874.x – volume: 26 start-page: 413 year: 2003 ident: 10.1016/j.mce.2020.110953_bib71 article-title: Synaptotagmin I, a Ca2+ sensor for neurotransmitter release publication-title: Trends Neurosci. doi: 10.1016/S0166-2236(03)00195-4 – volume: 6 start-page: 159 year: 1998 ident: 10.1016/j.mce.2020.110953_bib137 article-title: Localisation of inositol trisphosphate and ryanodine receptors during mouse spermatogenesis: Possible functional implications publication-title: Zygote doi: 10.1017/S0967199498000094 – volume: 28 start-page: 310 year: 2014 ident: 10.1016/j.mce.2020.110953_bib35 article-title: Lipid modulation of calcium flux through CaV2.3 regulates acrosome exocytosis and fertilization publication-title: Dev. Cell doi: 10.1016/j.devcel.2014.01.005 – volume: 283 start-page: 1902 year: 2016 ident: 10.1016/j.mce.2020.110953_bib107 article-title: Calcium channels in chicken sperm regulate motility and the acrosome reaction publication-title: FEBS J. doi: 10.1111/febs.13710 – volume: 289 start-page: 625 year: 2000 ident: 10.1016/j.mce.2020.110953_bib32 article-title: Soluble adenylyl cyclase as an evolutionarily conserved bicarbonate sensor publication-title: Science doi: 10.1126/science.289.5479.625 – volume: 236 start-page: 220 year: 2001 ident: 10.1016/j.mce.2020.110953_bib50 article-title: A sustained increase in intracellular Ca2+ is required for the acrosome reaction in sea urchin sperm publication-title: Dev. Biol. doi: 10.1006/dbio.2001.0323 – volume: 84 start-page: 505 year: 2009 ident: 10.1016/j.mce.2020.110953_bib9 article-title: Human male infertility caused by mutations in the CATSPER1 channel protein publication-title: Am. J. Hum. Genet. doi: 10.1016/j.ajhg.2009.03.004 – volume: 68 start-page: 1590 year: 2003 ident: 10.1016/j.mce.2020.110953_bib58 article-title: Characterization of the intracellular calcium store at the base of the sperm flagellum that regulates hyperactivated motility publication-title: Biol. Reprod. doi: 10.1095/biolreprod.102.011320 – volume: 9 start-page: 235 year: 2007 ident: 10.1016/j.mce.2020.110953_bib113 article-title: [Ca2+]i signalling in sperm - making the most of what you've got publication-title: Nat. Cell Biol. doi: 10.1038/ncb0307-235 – volume: 12 start-page: 43 year: 2014 ident: 10.1016/j.mce.2020.110953_bib119 article-title: Epac, Rap and Rab3 act in concert to mobilize calcium from sperm's acrosome during exocytosis publication-title: Cell Commun. Signal. – volume: 259 start-page: 2547 year: 1984 ident: 10.1016/j.mce.2020.110953_bib120 article-title: Regulation of calcium content in bovine spermatozoa publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)43388-6 – volume: 96 start-page: 6757 year: 1999 ident: 10.1016/j.mce.2020.110953_bib8 article-title: Control of the low voltage-activated calcium channel of mouse sperm by egg ZP3 and by membrane hyperpolarization during capacitation publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.96.12.6757 – volume: 85 start-page: 543 year: 2018 ident: 10.1016/j.mce.2020.110953_bib4 article-title: Signaling pathways involved in human sperm hyperactivated motility stimulated by Zn(2) publication-title: Mol. Reprod. Dev. doi: 10.1002/mrd.22996 – volume: 388 start-page: 150 year: 1996 ident: 10.1016/j.mce.2020.110953_bib79 article-title: T-type Ca2+ channels and alpha1E expression in spermatogenic cells, and their possible relevance to the sperm acrosome reaction publication-title: FEBS Lett. doi: 10.1016/0014-5793(96)00515-7 – volume: 23 start-page: 652 year: 2015 ident: 10.1016/j.mce.2020.110953_bib65 article-title: ERK1/2 mediates sperm acrosome reaction through elevation of intracellular calcium concentration publication-title: Zygote doi: 10.1017/S096719941400029X – year: 2020 ident: 10.1016/j.mce.2020.110953_bib142 – volume: 339 start-page: 234 year: 1994 ident: 10.1016/j.mce.2020.110953_bib76 article-title: Epidermal growth factor induces acrosomal exocytosis in bovine sperm publication-title: FEBS (Fed. Eur. Biochem. Soc.) Lett. doi: 10.1016/0014-5793(94)80422-2 – volume: 288 start-page: 33283 year: 2013 ident: 10.1016/j.mce.2020.110953_bib147 article-title: CO2/HCO3- and calcium-regulated soluble adenylyl cyclase as a physiological ATP sensor publication-title: J. Biol. Chem. doi: 10.1074/jbc.M113.510073 – volume: 293 start-page: 16830 year: 2018 ident: 10.1016/j.mce.2020.110953_bib109 article-title: CatSper channels are regulated by protein kinase A publication-title: J. Biol. Chem. doi: 10.1074/jbc.RA117.001566 – volume: 471 start-page: 382 year: 2011 ident: 10.1016/j.mce.2020.110953_bib132 article-title: The CatSper channel mediates progesterone-induced Ca2+ influx in human sperm publication-title: Nature doi: 10.1038/nature09769 – volume: 362 start-page: 154 year: 2012 ident: 10.1016/j.mce.2020.110953_bib61 article-title: Hyper-activated motility in sperm capacitation is mediated by phospholipase D-dependent actin polymerization publication-title: Dev. Biol. doi: 10.1016/j.ydbio.2011.12.002 – volume: 121 start-page: 1139 year: 1995 ident: 10.1016/j.mce.2020.110953_bib139 article-title: Capacitation in mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway publication-title: Development doi: 10.1242/dev.121.4.1139 – volume: 108 start-page: 4892 year: 2011 ident: 10.1016/j.mce.2020.110953_bib67 article-title: Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during in vitro fertilization publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1018202108 – volume: 109 start-page: 1947 year: 1996 ident: 10.1016/j.mce.2020.110953_bib130 article-title: Calcium mobilization and influx during sperm exocytosis publication-title: J. Cell Sci. doi: 10.1242/jcs.109.7.1947 – volume: 350 start-page: 442 year: 2015 ident: 10.1016/j.mce.2020.110953_bib101 article-title: Sperm calcineurin inhibition prevents mouse fertility with implications for male contraceptive publication-title: Science doi: 10.1126/science.aad0836 – volume: 61 start-page: 1226 year: 1999 ident: 10.1016/j.mce.2020.110953_bib41 article-title: Intracellular Ca2+ -Mg2+ -ATPase regulates calcium influx and acrosomal exocytosis in bull and ram spermatozoa publication-title: Biol. Reprod. doi: 10.1095/biolreprod61.5.1226 – volume: 323 start-page: 474 year: 2009 ident: 10.1016/j.mce.2020.110953_bib134 article-title: Membrane fusion: grappling with SNARE and SM proteins publication-title: Science doi: 10.1126/science.1161748 – volume: 3 start-page: 499 year: 2001 ident: 10.1016/j.mce.2020.110953_bib68 article-title: Trp2 regulates entry of Ca2+ into mouse sperm triggered by egg ZP3 publication-title: Nat. Cell Biol. doi: 10.1038/35074570 – volume: 497 start-page: 146 year: 2018 ident: 10.1016/j.mce.2020.110953_bib93 article-title: pH-dependent Ca2+ oscillations prevent untimely acrosome reaction in human sperm publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2018.02.042 – volume: 8 start-page: 2014 year: 2018 ident: 10.1016/j.mce.2020.110953_bib127 article-title: Crystal structure of a Ca2+-dependent regulator of flagellar motility reveals the open-closed structural transition publication-title: Sci. Rep. doi: 10.1038/s41598-018-19898-7 – volume: 280 start-page: 32238 year: 2005 ident: 10.1016/j.mce.2020.110953_bib28 article-title: Identical phenotypes of CatSper1 and CatSper2 null sperm publication-title: J. Biol. Chem. doi: 10.1074/jbc.M501430200 – volume: 180 start-page: 284 year: 1996 ident: 10.1016/j.mce.2020.110953_bib29 article-title: Regulation of protein tyrosine phosphorylation in human sperm by a calcium/calmodulin-dependent mechanism: identification of A kinase anchor proteins as major substrates for tyrosine phosphorylation publication-title: Dev. Biol. doi: 10.1006/dbio.1996.0301 – volume: 114 start-page: 5743 year: 2017 ident: 10.1016/j.mce.2020.110953_bib89 article-title: Regulation of the sperm calcium channel CatSper by endogenous steroids and plant triterpenoids publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1700367114 – volume: 73 start-page: 519 year: 2005 ident: 10.1016/j.mce.2020.110953_bib59 article-title: Calcium/calmodulin and calmodulin kinase II stimulate hyperactivation in demembranated bovine sperm publication-title: Biol. Reprod. doi: 10.1095/biolreprod.105.040733 – volume: 233 start-page: 9685 year: 2018 ident: 10.1016/j.mce.2020.110953_bib87 article-title: Only a subpopulation of mouse sperm displays a rapid increase in intracellular calcium during capacitation publication-title: J. Cell. Physiol. doi: 10.1002/jcp.26883 – volume: 91 start-page: 67 year: 2014 ident: 10.1016/j.mce.2020.110953_bib123 article-title: Acrosome reaction and Ca2+ imaging in single human spermatozoa: new regulatory roles of [Ca2+]i publication-title: Biol. Reprod. doi: 10.1095/biolreprod.114.119768 – volume: 251 start-page: 3881 year: 1976 ident: 10.1016/j.mce.2020.110953_bib11 article-title: Action of ionophore A23187 at the cellular level. Separation of effects at the plasma and mitochondrial membranes publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)33330-6 – volume: 2 start-page: 153 year: 2011 ident: 10.1016/j.mce.2020.110953_bib33 article-title: A novel gene required for male fertility and functional CATSPER channel formation in spermatozoa publication-title: Nat. Commun. doi: 10.1038/ncomms1153 – volume: 541 start-page: 69 year: 2003 ident: 10.1016/j.mce.2020.110953_bib30 article-title: Transient receptor potential (TRPC) channels in human sperm: expression, cellular localization and involvement in the regulation of flagellar motility publication-title: FEBS Lett. doi: 10.1016/S0014-5793(03)00305-3 – volume: 277 start-page: 8449 year: 2002 ident: 10.1016/j.mce.2020.110953_bib63 article-title: Identification and localization of T-type voltage-operated calcium channel subunits in human male germ cells. Expression of multiple isoforms publication-title: J. Biol. Chem. doi: 10.1074/jbc.M105345200 – volume: 262 start-page: 15041 year: 1987 ident: 10.1016/j.mce.2020.110953_bib12 article-title: Independent elevation of cytosolic Ca2+ and pH of mammalian sperm by voltage dependent and pH sensitive mechanisms publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)48135-5 – volume: 4 year: 2009 ident: 10.1016/j.mce.2020.110953_bib39 article-title: TRPM8, a versatile channel in human sperm publication-title: PLoS One doi: 10.1371/journal.pone.0006095 – volume: 17 start-page: 478 year: 2011 ident: 10.1016/j.mce.2020.110953_bib69 article-title: Rediscovering sperm ion channels with the patch-clamp technique publication-title: Mol. Hum. Reprod. doi: 10.1093/molehr/gar044 – volume: 67 start-page: 301 year: 2002 ident: 10.1016/j.mce.2020.110953_bib77 article-title: Regulation of the human sperm tyrosine kinase c-yes. Activation by cyclic adenosine 3',5'-monophosphate and inhibition by Ca 2+ publication-title: Biol. Reprod. doi: 10.1095/biolreprod67.1.301 – volume: 122 start-page: 519 year: 2001 ident: 10.1016/j.mce.2020.110953_bib56 article-title: Hyperactivation of mammalian spermatozoa: Function and regulation publication-title: Reproduction doi: 10.1530/rep.0.1220519 – volume: 13 start-page: 307 year: 2007 ident: 10.1016/j.mce.2020.110953_bib75 article-title: Identification and localisation of SERCA 2 isoforms in mammalian sperm publication-title: Mol. Hum. Reprod. doi: 10.1093/molehr/gam012 – volume: 267 start-page: 350 year: 1993 ident: 10.1016/j.mce.2020.110953_bib97 article-title: Initiation of the human sperm acrosome reaction by thapsigargin publication-title: J. Exp. Zool. doi: 10.1002/jez.1402670312 – volume: 81 start-page: 539 year: 2009 ident: 10.1016/j.mce.2020.110953_bib141 article-title: A novel, single, transmembrane protein CATSPERG is associated with CATSPER1 channel protein publication-title: Biol. Reprod. doi: 10.1095/biolreprod.109.077107 – volume: 83 start-page: 111 year: 1995 ident: 10.1016/j.mce.2020.110953_bib95 article-title: Complexins: Cytosolic proteins that regulate SNAP receptor function publication-title: Cell doi: 10.1016/0092-8674(95)90239-2 – volume: 4 start-page: 1073 year: 2016 ident: 10.1016/j.mce.2020.110953_bib13 article-title: Participation of protein kinases and phosphatases in the progesterone-induced acrosome reaction and calcium influx in human spermatozoa publication-title: Andrology doi: 10.1111/andr.12234 – volume: 282 start-page: 18945 year: 2007 ident: 10.1016/j.mce.2020.110953_bib82 article-title: CatSperb, a novel transmembrane protein in the CatSper channel complex publication-title: J. Biol. Chem. doi: 10.1074/jbc.M701083200 – volume: 34 start-page: 414 year: 2019 ident: 10.1016/j.mce.2020.110953_bib86 article-title: A novel copy number variation in CATSPER2 causes idiopathic male infertility with normal semen parameters publication-title: Hum. Reprod. doi: 10.1093/humrep/dey377 – volume: 90 start-page: 4660 year: 1993 ident: 10.1016/j.mce.2020.110953_bib133 article-title: Intracellular calcium increases with hyperactivation in intact, moving hamster sperm and oscillates with the flagellar beat cycle publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.90.10.4660 – volume: 88 start-page: 138 year: 2013 ident: 10.1016/j.mce.2020.110953_bib49 article-title: Focal adhesion kinases and calcium/calmodulin-dependent protein kinases regulate protein tyrosine phosphorylation in stallion sperm publication-title: Biol. Reprod. doi: 10.1095/biolreprod.112.107078 – volume: 84 start-page: 310 year: 2017 ident: 10.1016/j.mce.2020.110953_bib52 article-title: An intact acrosome is required for the chemotactic response to progesterone in mouse spermatozoa publication-title: Mol. Reprod. Dev. doi: 10.1002/mrd.22782 – volume: 413 start-page: 603 year: 2001 ident: 10.1016/j.mce.2020.110953_bib115 article-title: A sperm ion channel required for sperm motility and male fertility publication-title: Nature doi: 10.1038/35098027 – volume: 79 start-page: 1396 year: 2003 ident: 10.1016/j.mce.2020.110953_bib90 article-title: Calcium requirements for human sperm function in vitro publication-title: Fertil. Steril. doi: 10.1016/S0015-0282(03)00267-X – volume: 84 start-page: 1203 year: 2017 ident: 10.1016/j.mce.2020.110953_bib110 article-title: Characterization of extracellular Ca2+-dependent full-type hyperactivation in ejaculated boar spermatozoa preincubated with a cAMP analog publication-title: Mol. Reprod. Dev. doi: 10.1002/mrd.22921 – volume: 352 start-page: 555 year: 2016 ident: 10.1016/j.mce.2020.110953_bib100 article-title: Unconventional endocannabinoid signaling governs sperm activation via the sex hormone progesterone publication-title: Science doi: 10.1126/science.aad6887 – volume: 23 start-page: 2652 year: 2008 ident: 10.1016/j.mce.2020.110953_bib138 article-title: Src activation triggers capacitation and acrosome reaction but not motility in human spermatozoa publication-title: Hum. Reprod. doi: 10.1093/humrep/den314 – volume: 115 start-page: E11847 year: 2018 ident: 10.1016/j.mce.2020.110953_bib146 article-title: Role of human Hv1 channels in sperm capacitation and white blood cell respiratory burst established by a designed peptide inhibitor publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1816189115 – volume: 24 start-page: 2606 year: 2018 ident: 10.1016/j.mce.2020.110953_bib99 article-title: Asymmetrically positioned flagellar control units regulate human sperm rotation publication-title: Cell Rep. doi: 10.1016/j.celrep.2018.08.016 |
SSID | ssj0007528 |
Score | 2.5404146 |
SecondaryResourceType | review_article |
Snippet | Calcium is an essential ion which regulates sperm motility, capacitation and the acrosome reaction (AR), three processes necessary for successful... |
SourceID | proquest crossref elsevier |
SourceType | Aggregation Database Enrichment Source Index Database Publisher |
StartPage | 110953 |
SubjectTerms | acrosome Acrosome reaction actin adenylate cyclase bicarbonates Calcium cAMP-dependent protein kinase Capacitation cyclic AMP diacylglycerols eggs endocrinology female reproductive system Fertilization hydrolysis mammals Motility phospholipase C phosphorylation plasma membrane protein kinase C sperm motility Spermatozoa tyrosine |
Title | Ca2+ signaling in mammalian spermatozoa |
URI | https://dx.doi.org/10.1016/j.mce.2020.110953 https://www.proquest.com/docview/2427523381 https://www.proquest.com/docview/2552041171 |
Volume | 516 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LS8NAEF5EQbyIT3yWCKKgxOaxm22OpViqohcVelsy-4CKSYu2Bz34253JQ1GwB48JsyR8u5n5svPtDGPHYSIDa5zzbQCJT4zYB3DaN0mHaw3GpI62Bm7vksEjvx6K4QLrNWdhSFZZ-_7Kp5feur7TrtFsT0aj9j0uT2qxQnlEDNwxnSjnXNIqv_j4lnlIUfZXJWOfrJvMZqnxyjVVyoyqupsi_is2_fLSZejpr7HVmjN63eq11tmCLTbYZrfA_-X8zTvxShVnuT2-wZZv62T5JjvtZdG5RwKNjM6ce6PCy7M8Lzc2PCoQjmR1_D7Otthj__KhN_Drvgi-xuA89YWQJuqYKNFBBtY6x0OXIJPQ3CA9gyQEiCA20qQGMNhI64BzpB2pjUIdSxtvs8ViXNgd5gFPwXFhnQaN2PGOk1oipchSDiBi2GVBg4jSddFw6l3xrBp12JNCEBWBqCoQd9nZ15BJVTFjnjFvYFY_pl2hR5837KiZEoWfA-U4ssKOZ68KGQfOOP53h3NshIgCHoYy3Pvf4_fZCl1Vmr4Dtjh9mdlD5CZTaJWLr8WWulc3g7tPMCPhKA |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LS8RADA66gnoRn_i2gigoZfuY6WyPy6Ksj92LCt6GZh6wYruLrgf99Wb6EBTcg9c2oSWZSb5JMgnASZiIwGhrfRNg4jtE7CNa5eukw5RCrVPrQgODYdJ_ZDdP_GkOes1dGFdWWdv-yqaX1rp-0q6l2Z6MRu17Wp5uxIrLI5LjjsU8LLjuVLwFC93r2_7w2yALXo5YdfS-Y2iSm2WZV65cs8yoar3J47_c0y9DXXqfq1VYqWGj163-bA3mTLEOG92Cjsz5h3fqlYWcZYR8HRYHdb58A856WXThuRqNzF0790aFl2d5XsY2PNcjnPDq-HOcbcLj1eVDr-_XoxF8Rf556nMudNTRUaKCDI2xloU2ITChmCaEhkmIGGGshU41kr8RxiJjhDxSE4UqFibeglYxLsw2eMhStIwbq1AxkbCOFUoQqshShshj3IGgkYhUdd9wN77iRTYFYs-ShCidEGUlxB04_2aZVE0zZhGzRszyh-YlGfVZbMeNSiTtCJfmyAozfn-TBDpI43T0DmfQcB4FLAxFuPu_zx_BUv9hcCfvroe3e7Ds3lQlfvvQmr6-mwOCKlM8rJfiF_jz49k |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Ca2%2B+signaling+in+mammalian+spermatozoa&rft.jtitle=Molecular+and+cellular+endocrinology&rft.au=Finkelstein%2C+Maya&rft.au=Etkovitz%2C+Nir&rft.au=Breitbart%2C+Haim&rft.date=2020-10-01&rft.issn=0303-7207&rft.volume=516&rft.spage=110953&rft_id=info:doi/10.1016%2Fj.mce.2020.110953&rft.externalDBID=n%2Fa&rft.externalDocID=10_1016_j_mce_2020_110953 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0303-7207&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0303-7207&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0303-7207&client=summon |