Tools for Understanding Nanoscale Lipid Regulation of Ion Channels
Anionic phospholipids are minor but prominent components of the plasma membrane that are necessary for ion channel function. Their persistence in bulk membranes, in particular phosphatidylinositol 4,5-bisphosphate (PIP2), initially suggested they act as channel cofactors. However, recent technologie...
Saved in:
Published in | Trends in biochemical sciences (Amsterdam. Regular ed.) Vol. 44; no. 9; pp. 795 - 806 |
---|---|
Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier Ltd
01.09.2019
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Anionic phospholipids are minor but prominent components of the plasma membrane that are necessary for ion channel function. Their persistence in bulk membranes, in particular phosphatidylinositol 4,5-bisphosphate (PIP2), initially suggested they act as channel cofactors. However, recent technologies have established an emerging system of nanoscale signaling to ion channels based on lipid compartmentalization (clustering), direct lipid binding, and local lipid dynamics that allow cells to harness lipid heterogeneity to gate ion channels. The new tools to study lipid binding are set to transform our view of the membrane and answer important questions surrounding ion channel-delimited processes such as mechanosensation.
Mass spectrometry, cryo-EM, and super-resolution microscopy are advanced tools set to evolve the role of phosphatidylinositol 4,5 bisphosphate (PIP2) and other anionic lipids in the regulation of ion channel function.Cells harness lipid heterogeneity to gate a channel.Phosphatidic acid (PA)-regulated channels are an emerging class of lipid-regulated channels.Nanoscale lipid gradients open up the possibility for membrane-resident anionic lipids to centrally coordinate biological processes by locally regulating ion channel function. |
---|---|
AbstractList | Anionic phospholipids are minor but prominent components of the plasma membrane that are necessary for ion channel function. Their persistence in bulk membranes, in particular phosphatidylinositol 4,5-bisphosphate (PIP2), initially suggested they act as channel cofactors. However, recent technologies have established an emerging system of nanoscale signaling to ion channels based on lipid compartmentalization (clustering), direct lipid binding, and local lipid dynamics that allow cells to harness lipid heterogeneity to gate ion channels. The new tools to study lipid binding are set to transform our view of the membrane and answer important questions surrounding ion channel-delimited processes such as mechanosensation.Anionic phospholipids are minor but prominent components of the plasma membrane that are necessary for ion channel function. Their persistence in bulk membranes, in particular phosphatidylinositol 4,5-bisphosphate (PIP2), initially suggested they act as channel cofactors. However, recent technologies have established an emerging system of nanoscale signaling to ion channels based on lipid compartmentalization (clustering), direct lipid binding, and local lipid dynamics that allow cells to harness lipid heterogeneity to gate ion channels. The new tools to study lipid binding are set to transform our view of the membrane and answer important questions surrounding ion channel-delimited processes such as mechanosensation. Anionic phospholipids are minor but prominent components of the plasma membrane and necessary for ion channel function. Their persistence in bulk membranes, in particular phosphatidylinositol 4,5-bisphosphate (PIP 2 ), initially suggested they act as channel cofactors. However, recent technologies have established an emerging system of nanoscale signaling to ion channels based on lipid compartmentalization (clustering), direct lipid binding, and local lipid dynamics that allow cells to harness lipid heterogeneity to gate ion channels. The new tools to study lipid binding are set to transform our view of the membrane and answer important questions surrounding ion channel delimited processes, such as mechanosensation. Anionic phospholipids are minor but prominent components of the plasma membrane that are necessary for ion channel function. Their persistence in bulk membranes, in particular phosphatidylinositol 4,5-bisphosphate (PIP ), initially suggested they act as channel cofactors. However, recent technologies have established an emerging system of nanoscale signaling to ion channels based on lipid compartmentalization (clustering), direct lipid binding, and local lipid dynamics that allow cells to harness lipid heterogeneity to gate ion channels. The new tools to study lipid binding are set to transform our view of the membrane and answer important questions surrounding ion channel-delimited processes such as mechanosensation. Anionic phospholipids are minor but prominent components of the plasma membrane that are necessary for ion channel function. Their persistence in bulk membranes, in particular phosphatidylinositol 4,5-bisphosphate (PIP2), initially suggested they act as channel cofactors. However, recent technologies have established an emerging system of nanoscale signaling to ion channels based on lipid compartmentalization (clustering), direct lipid binding, and local lipid dynamics that allow cells to harness lipid heterogeneity to gate ion channels. The new tools to study lipid binding are set to transform our view of the membrane and answer important questions surrounding ion channel-delimited processes such as mechanosensation. Anionic phospholipids are minor but prominent components of the plasma membrane that are necessary for ion channel function. Their persistence in bulk membranes, in particular phosphatidylinositol 4,5-bisphosphate (PIP2), initially suggested they act as channel cofactors. However, recent technologies have established an emerging system of nanoscale signaling to ion channels based on lipid compartmentalization (clustering), direct lipid binding, and local lipid dynamics that allow cells to harness lipid heterogeneity to gate ion channels. The new tools to study lipid binding are set to transform our view of the membrane and answer important questions surrounding ion channel-delimited processes such as mechanosensation. Mass spectrometry, cryo-EM, and super-resolution microscopy are advanced tools set to evolve the role of phosphatidylinositol 4,5 bisphosphate (PIP2) and other anionic lipids in the regulation of ion channel function.Cells harness lipid heterogeneity to gate a channel.Phosphatidic acid (PA)-regulated channels are an emerging class of lipid-regulated channels.Nanoscale lipid gradients open up the possibility for membrane-resident anionic lipids to centrally coordinate biological processes by locally regulating ion channel function. |
Author | Rohacs, Tibor Robinson, Carol V. Hansen, Scott B. |
AuthorAffiliation | 4 Department of Neuroscience, The Scripps Research Institute, Jupiter, Florida 33458, USA 3 Department of Molecular Medicine, The Scripps Research Institute, Jupiter, Florida 33458, USA 2 Department of Pharmacology, Physiology and Neuroscience, Rutgers - New Jersey Medical School, Newark, NJ 07103, USA 1 Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK |
AuthorAffiliation_xml | – name: 1 Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK – name: 2 Department of Pharmacology, Physiology and Neuroscience, Rutgers - New Jersey Medical School, Newark, NJ 07103, USA – name: 4 Department of Neuroscience, The Scripps Research Institute, Jupiter, Florida 33458, USA – name: 3 Department of Molecular Medicine, The Scripps Research Institute, Jupiter, Florida 33458, USA |
Author_xml | – sequence: 1 givenname: Carol V. surname: Robinson fullname: Robinson, Carol V. organization: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK – sequence: 2 givenname: Tibor surname: Rohacs fullname: Rohacs, Tibor organization: Department of Pharmacology, Physiology and Neuroscience, Rutgers New Jersey Medical School, Newark, NJ 07103, USA – sequence: 3 givenname: Scott B. surname: Hansen fullname: Hansen, Scott B. email: shansen@scripps.edu organization: Department of Molecular Medicine, The Scripps Research Institute, Jupiter, FL 33458, USA |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31060927$$D View this record in MEDLINE/PubMed |
BookMark | eNqNkVFLHDEUhUOx1FX7B3yQefRlpjfJTGYGpFCXaoWlBdHnkEnurFmyyZrMCv33zXa1tH0QX3ID9zuHyzlH5MAHj4ScUqgoUPFpVU12SBUD2ldQVwD0HZlRLlhZcyYOyAx60ZUAUB-So5RWGWjatvlADjkFAT1rZ-TyLgSXijHE4t4bjGlS3li_LL4rH5JWDouF3VhT3OJy69Rkgy_CWNzkMX9Q3qNLJ-T9qFzCj8_zmNxffb2bfysXP65v5l8WpW6omErGuwHF0HZDDT2IRgjDdDMoZOOgW97XY_72qsuPoaJBqKnhqMzIle6NFvyYfN77brbDGo1GP0Xl5CbatYo_ZVBW_rvx9kEuw5MULesp2xmcPxvE8LjFNMm1TRqdUx7DNknGGp7D7Ch_A5pJyFE3GT37-6w_97xknIFuD-gYUoo4Sm2n30nmK62TFOSuTrmSuzrlrk4JtcxtZSn7T_ri_qroYi_K3eCTxSiTtug1GhtRT9IE-5r8FxS_uXU |
CitedBy_id | crossref_primary_10_1073_pnas_2102191118 crossref_primary_10_1016_j_jbc_2023_105484 crossref_primary_10_3389_fphys_2021_798102 crossref_primary_10_1007_s43440_023_00544_7 crossref_primary_10_3390_membranes13020250 crossref_primary_10_3390_ijms23158457 crossref_primary_10_1016_j_jmb_2021_167105 crossref_primary_10_1085_jgp_202112888 crossref_primary_10_1016_j_mcn_2022_103706 crossref_primary_10_1111_febs_15281 crossref_primary_10_1016_j_cellsig_2022_110396 crossref_primary_10_7554_eLife_89465_3 crossref_primary_10_1021_acsomega_0c03047 crossref_primary_10_3390_ijms23169357 crossref_primary_10_1016_j_bbalip_2023_159443 crossref_primary_10_1016_j_pharmthera_2023_108486 crossref_primary_10_1042_BST20190149 crossref_primary_10_1016_j_ceb_2019_12_007 crossref_primary_10_1038_s42003_022_03841_8 crossref_primary_10_1073_pnas_2315011120 crossref_primary_10_1016_j_sbi_2021_03_010 crossref_primary_10_1038_s41467_023_42363_7 crossref_primary_10_3390_ijms22169062 crossref_primary_10_1073_pnas_2301121120 crossref_primary_10_1016_j_plipres_2020_101065 crossref_primary_10_1016_j_jbc_2023_104763 crossref_primary_10_3389_fnmol_2022_915570 crossref_primary_10_31857_S0026898423040122 crossref_primary_10_1073_pnas_2004259117 crossref_primary_10_1213_ANE_0000000000006738 crossref_primary_10_1016_j_bioactmat_2023_10_008 crossref_primary_10_3390_biom12030352 crossref_primary_10_1021_acs_jctc_1c00708 crossref_primary_10_1194_jlr_TR119000468 crossref_primary_10_1016_j_plipres_2022_101198 crossref_primary_10_1016_j_bbamem_2019_183091 crossref_primary_10_7554_eLife_89465 crossref_primary_10_1073_pnas_2006737117 crossref_primary_10_1016_j_jprot_2020_103799 crossref_primary_10_1016_j_jbc_2021_100899 crossref_primary_10_3389_fcell_2020_00063 crossref_primary_10_3390_insects13100926 crossref_primary_10_1042_EBC20200041 crossref_primary_10_1016_j_ceca_2020_102287 crossref_primary_10_1016_j_semcdb_2020_07_017 crossref_primary_10_1038_s41594_022_00851_2 crossref_primary_10_1111_nph_20329 crossref_primary_10_3390_biology10111119 crossref_primary_10_3390_ijms21155531 crossref_primary_10_1080_15592324_2020_1789818 crossref_primary_10_1038_s41589_020_00659_5 crossref_primary_10_1038_s41467_024_54053_z crossref_primary_10_1098_rsob_200252 crossref_primary_10_1016_j_abb_2024_110045 crossref_primary_10_1016_j_phrs_2023_106729 crossref_primary_10_1002_jcb_30693 |
Cites_doi | 10.1038/nature10370 10.1085/jgp.201210806 10.1523/JNEUROSCI.0586-18.2018 10.1113/jphysiol.2004.081935 10.1021/bi052281z 10.1038/s41467-018-06493-7 10.1038/nprot.2013.005 10.1523/JNEUROSCI.3038-08.2008 10.1093/jb/mvi135 10.1111/bph.12778 10.1126/science.aav9334 10.1152/advan.00046.2004 10.1038/nature10545 10.1038/ncomms13873 10.1038/ncomms3786 10.1073/pnas.1407160111 10.1016/j.bpj.2018.07.012 10.1074/jbc.M109.071993 10.1085/jgp.201711875 10.3389/fphar.2012.00170 10.1038/35882 10.1038/s41586-018-0325-6 10.1016/0092-8674(90)90294-O 10.1038/nmeth.3771 10.1152/physrev.00028.2012 10.1038/nature12823 10.1016/j.pbiomolbio.2006.04.001 10.1074/jbc.R110.210005 10.1038/s41586-018-0833-4 10.1096/fj.15-281576 10.1016/j.bbamem.2013.10.019 10.1073/pnas.1721152115 10.1038/nature13419 10.1074/jbc.M113.520288 10.1021/bi702409t 10.1085/jgp.201411336 10.1038/35082088 10.1038/nature10812 10.1016/j.febslet.2007.11.039 10.1038/nn1411 10.1016/j.neuron.2012.12.016 10.1038/nature05185 10.1007/s00424-007-0250-2 10.1074/jbc.273.21.12846 10.1085/jgp.201511395 10.1083/jcb.200610151 10.1242/bio.20122071 10.1146/annurev.biophys.37.032807.125859 10.1007/s00424-007-0295-2 10.1016/S0021-9258(18)96298-8 10.1126/science.aat4346 10.2174/138161209788186326 10.1007/s00424-007-0280-9 10.7554/eLife.04366 10.1007/978-3-319-05161-1_18 10.1021/bi801352a 10.1016/j.tins.2013.12.002 10.2139/ssrn.3155650 10.7554/eLife.19891 10.1016/j.bbalip.2015.01.011 10.1038/nmeth.f.234 10.1126/science.1174621 10.1529/biophysj.105.070755 10.1038/s41467-018-06753-6 10.1016/j.bbamem.2016.10.023 10.1161/CIRCEP.108.789081 10.1085/jgp.201411309 10.1016/j.bpj.2010.06.013 10.1016/j.celrep.2017.07.034 10.1113/jphysiol.2007.132787 10.1016/j.cell.2011.07.046 10.1038/nature20820 10.1007/s12035-018-1244-0 10.1016/j.bpj.2010.12.3724 10.1083/jcb.200607116 10.1126/science.1068539 10.1126/science.1094113 10.1038/nature17964 10.1523/JNEUROSCI.3189-10.2010 10.1016/j.jmb.2018.11.028 10.1007/s12551-012-0078-7 10.1111/j.2042-7158.2010.01131.x |
ContentType | Journal Article |
Copyright | 2019 Elsevier Ltd Copyright © 2019 Elsevier Ltd. All rights reserved. |
Copyright_xml | – notice: 2019 Elsevier Ltd – notice: Copyright © 2019 Elsevier Ltd. All rights reserved. |
DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 7S9 L.6 5PM |
DOI | 10.1016/j.tibs.2019.04.001 |
DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic AGRICOLA AGRICOLA - Academic PubMed Central (Full Participant titles) |
DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
DatabaseTitleList | MEDLINE - Academic MEDLINE AGRICOLA |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Biology |
EISSN | 1362-4326 |
EndPage | 806 |
ExternalDocumentID | PMC6729126 31060927 10_1016_j_tibs_2019_04_001 S0968000419300817 |
Genre | Journal Article Review Research Support, N.I.H., Extramural |
GrantInformation_xml | – fundername: NINDS NIH HHS grantid: R01 NS055159 – fundername: NIGMS NIH HHS grantid: R01 GM093290 – fundername: NIGMS NIH HHS grantid: R01 GM131048 – fundername: NINDS NIH HHS grantid: DP2 NS087943 |
GroupedDBID | --- --K --M -DZ -~X .55 .GJ .~1 0R~ 123 1B1 1CY 1RT 1~. 1~5 29Q 3EH 3O- 4.4 457 4G. 53G 5VS 7-5 71M 85S 8P~ 9JM 9M8 AABNK AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAXUO ABFNM ABFRF ABGSF ABJNI ABLJU ABMAC ABOCM ABUDA ABXDB ABYKQ ACDAQ ACGFO ACGFS ACGOD ACKIV ACNCT ACPRK ACRLP ADBBV ADEZE ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFKWA AFRAH AFTJW AFXIZ AGHFR AGRDE AGUBO AGYEJ AHHHB AHPSJ AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CS3 D0L DOVZS DU5 EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 F5P FA8 FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q GBLVA HLW HVGLF HZ~ H~9 IH2 IHE J1W KOM LX3 M41 MO0 MVM N9A O-L O9- OAUVE OHT OZT P-8 P-9 P2P PC. PQQKQ Q38 R2- RIG RNS ROL RPZ RXW SBG SCC SDF SDG SDP SES SEW SPCBC SSU SSZ T5K TAE UQL WUQ X7M XFK XPP Y6R ZCA ZMT ~G- AAHBH AAMRU AATTM AAXKI AAYWO AAYXX ACVFH ADCNI ADVLN ADXHL AEIPS AEUPX AFPUW AGCQF AGRNS AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP BNPGV CITATION SSH CGR CUY CVF ECM EFKBS EIF NPM 7X8 7S9 L.6 5PM |
ID | FETCH-LOGICAL-c516t-238be6b78b40906566d2c5bae2fbc7394fae29a8e29d165e041d3eadf3ac9dc63 |
IEDL.DBID | .~1 |
ISSN | 0968-0004 |
IngestDate | Thu Aug 21 18:19:06 EDT 2025 Fri Jul 11 08:23:46 EDT 2025 Tue Aug 05 10:31:11 EDT 2025 Mon Jul 21 06:06:35 EDT 2025 Tue Jul 01 01:05:04 EDT 2025 Thu Apr 24 23:02:01 EDT 2025 Fri Feb 23 02:16:38 EST 2024 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 9 |
Keywords | lipid rafts mass spectrometry super-resolution imaging signaling lipids cryo-electron microscopy |
Language | English |
License | Copyright © 2019 Elsevier Ltd. All rights reserved. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c516t-238be6b78b40906566d2c5bae2fbc7394fae29a8e29d165e041d3eadf3ac9dc63 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
OpenAccessLink | https://www.ncbi.nlm.nih.gov/pmc/articles/6729126 |
PMID | 31060927 |
PQID | 2232003625 |
PQPubID | 23479 |
PageCount | 12 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_6729126 proquest_miscellaneous_2253201813 proquest_miscellaneous_2232003625 pubmed_primary_31060927 crossref_citationtrail_10_1016_j_tibs_2019_04_001 crossref_primary_10_1016_j_tibs_2019_04_001 elsevier_sciencedirect_doi_10_1016_j_tibs_2019_04_001 |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 2000 |
PublicationDate | 2019-09-01 |
PublicationDateYYYYMMDD | 2019-09-01 |
PublicationDate_xml | – month: 09 year: 2019 text: 2019-09-01 day: 01 |
PublicationDecade | 2010 |
PublicationPlace | England |
PublicationPlace_xml | – name: England |
PublicationTitle | Trends in biochemical sciences (Amsterdam. Regular ed.) |
PublicationTitleAlternate | Trends Biochem Sci |
PublicationYear | 2019 |
Publisher | Elsevier Ltd |
Publisher_xml | – name: Elsevier Ltd |
References | Yen (bb0075) 2018; 559 Laverty (bb0140) 2019; 565 Taylor, Sanders (bb0375) 2017; 1859 Cao (bb0115) 2013; 504 Stone (bb0195) 2017; 6 Balla (bb0305) 2013; 93 Coste (bb0325) 2012; 483 Rodriguez (bb0385) 2010; 99 Shipston (bb0010) 2011; 286 Dubyak (bb0300) 2004; 28 Berthier (bb0235) 2015; 145 Yang (bb0315) 1967; 242 Hille (bb0005) 2001 Powl (bb0335) 2008; 47 Flucher (bb0230) 2015; 145 Rodríguez-Menchaca (bb0265) 2012; 3 Wang, Richards (bb0165) 2012; 1 Yin (bb0125) 2019; 363 Chuang (bb0280) 2001; 411 Cheng (bb0120) 2018; 361 Pavel (bb0185) 2018 Wickenden, McNaughton-Smith (bb0380) 2009; 15 Gault (bb0065) 2016; 13 Pian (bb0260) 2007; 455 Badheka (bb0400) 2015; 146 Gao (bb0110) 2016; 534 Gamper, Shapiro (bb0040) 2007; 582 Pritchard (bb0240) 2014; 171 Cabanos (bb0090) 2017; 20 Zacharias (bb0190) 2002; 296 Varnai (bb0045) 2006; 175 Baenziger, DaCosta (bb0330) 2012; 5 Laganowsky (bb0070) 2014; 510 Di Paolo, De Camilli (bb0050) 2006; 443 Gupta (bb0080) 2017; 541 Kruse (bb0370) 2012; 140 Hughes (bb0130) 2018; 9 Sengupta (bb0170) 2013; 8 Hancock (bb0205) 1990; 63 Hansen (bb0100) 2011; 477 Uchida (bb0395) 2016; 30 Sturgeon, Magoski (bb0295) 2018; 38 Labriola (bb0290) 2010; 285 Liko (bb0085) 2018; 115 Greaves, Chamberlain (bb0210) 2007; 176 Hansen (bb0025) 2015; 1851 Lopes (bb0320) 2005; 564 Comoglio (bb0200) 2014; 111 Lukacs (bb0245) 2013; 288 Cheng (bb0055) 2011; 100 Whorton, MacKinnon (bb0105) 2011; 147 Nayebosadri (bb0215) 2018 Grant (bb0410) 2009; 2 Cao (bb0250) 2013; 77 Oliver (bb0255) 2004; 304 Marius (bb0345) 2005; 89 Lee (bb0360) 2013; 4 Zakharian (bb0405) 2010; 30 Tsantoulas, McMahon (bb0420) 2014; 37 van den Bogaart (bb0145) 2011; 479 Nicolson (bb0180) 2014; 1838 Lyman (bb0175) 2018; 115 Raja (bb0350) 2007; 581 Suh, Hille (bb0015) 2008; 37 Lingwood, Simons (bb0155) 2010; 327 Chung (bb0225) 2019; 431 Powl (bb0340) 2008; 47 Hilgemann (bb0020) 2007; 455 Fine (bb0135) 2018; 9 Pegan (bb0095) 2005; 8 Hite (bb0220) 2014; 3 Hilgemann (bb0035) 2018; 150 Huang (bb0030) 1998; 391 Chi (bb0150) 2009; 6 Xie (bb0365) 2007; 94 Lopez (bb0310) 1998; 273 Giblin (bb0355) 2018; 56 Petersen (bb0160) 2016; 7 Chemin (bb0275) 2007; 455 Hamouda (bb0060) 2006; 45 Irino (bb0285) 2005; 138 Bernier (bb0390) 2008; 28 Rohacs (bb0270) 2014; 223 Mathie (bb0415) 2010; 62 Hansen (10.1016/j.tibs.2019.04.001_bb0100) 2011; 477 Flucher (10.1016/j.tibs.2019.04.001_bb0230) 2015; 145 Gault (10.1016/j.tibs.2019.04.001_bb0065) 2016; 13 Whorton (10.1016/j.tibs.2019.04.001_bb0105) 2011; 147 Hughes (10.1016/j.tibs.2019.04.001_bb0130) 2018; 9 Rodríguez-Menchaca (10.1016/j.tibs.2019.04.001_bb0265) 2012; 3 Cao (10.1016/j.tibs.2019.04.001_bb0115) 2013; 504 Chuang (10.1016/j.tibs.2019.04.001_bb0280) 2001; 411 Yang (10.1016/j.tibs.2019.04.001_bb0315) 1967; 242 Irino (10.1016/j.tibs.2019.04.001_bb0285) 2005; 138 Oliver (10.1016/j.tibs.2019.04.001_bb0255) 2004; 304 Lopez (10.1016/j.tibs.2019.04.001_bb0310) 1998; 273 Suh (10.1016/j.tibs.2019.04.001_bb0015) 2008; 37 Zacharias (10.1016/j.tibs.2019.04.001_bb0190) 2002; 296 Gao (10.1016/j.tibs.2019.04.001_bb0110) 2016; 534 Berthier (10.1016/j.tibs.2019.04.001_bb0235) 2015; 145 Rodriguez (10.1016/j.tibs.2019.04.001_bb0385) 2010; 99 Balla (10.1016/j.tibs.2019.04.001_bb0305) 2013; 93 Lopes (10.1016/j.tibs.2019.04.001_bb0320) 2005; 564 Hite (10.1016/j.tibs.2019.04.001_bb0220) 2014; 3 Pian (10.1016/j.tibs.2019.04.001_bb0260) 2007; 455 Uchida (10.1016/j.tibs.2019.04.001_bb0395) 2016; 30 Sturgeon (10.1016/j.tibs.2019.04.001_bb0295) 2018; 38 Hilgemann (10.1016/j.tibs.2019.04.001_bb0035) 2018; 150 Huang (10.1016/j.tibs.2019.04.001_bb0030) 1998; 391 Gamper (10.1016/j.tibs.2019.04.001_bb0040) 2007; 582 Rohacs (10.1016/j.tibs.2019.04.001_bb0270) 2014; 223 Pegan (10.1016/j.tibs.2019.04.001_bb0095) 2005; 8 Powl (10.1016/j.tibs.2019.04.001_bb0340) 2008; 47 Lyman (10.1016/j.tibs.2019.04.001_bb0175) 2018; 115 Shipston (10.1016/j.tibs.2019.04.001_bb0010) 2011; 286 Zakharian (10.1016/j.tibs.2019.04.001_bb0405) 2010; 30 Labriola (10.1016/j.tibs.2019.04.001_bb0290) 2010; 285 Laverty (10.1016/j.tibs.2019.04.001_bb0140) 2019; 565 Chung (10.1016/j.tibs.2019.04.001_bb0225) 2019; 431 Hancock (10.1016/j.tibs.2019.04.001_bb0205) 1990; 63 Marius (10.1016/j.tibs.2019.04.001_bb0345) 2005; 89 Mathie (10.1016/j.tibs.2019.04.001_bb0415) 2010; 62 Hilgemann (10.1016/j.tibs.2019.04.001_bb0020) 2007; 455 Giblin (10.1016/j.tibs.2019.04.001_bb0355) 2018; 56 Hansen (10.1016/j.tibs.2019.04.001_bb0025) 2015; 1851 Laganowsky (10.1016/j.tibs.2019.04.001_bb0070) 2014; 510 Nicolson (10.1016/j.tibs.2019.04.001_bb0180) 2014; 1838 Dubyak (10.1016/j.tibs.2019.04.001_bb0300) 2004; 28 Badheka (10.1016/j.tibs.2019.04.001_bb0400) 2015; 146 Liko (10.1016/j.tibs.2019.04.001_bb0085) 2018; 115 Xie (10.1016/j.tibs.2019.04.001_bb0365) 2007; 94 Lukacs (10.1016/j.tibs.2019.04.001_bb0245) 2013; 288 Powl (10.1016/j.tibs.2019.04.001_bb0335) 2008; 47 Varnai (10.1016/j.tibs.2019.04.001_bb0045) 2006; 175 Stone (10.1016/j.tibs.2019.04.001_bb0195) 2017; 6 Greaves (10.1016/j.tibs.2019.04.001_bb0210) 2007; 176 Nayebosadri (10.1016/j.tibs.2019.04.001_bb0215) 2018 Baenziger (10.1016/j.tibs.2019.04.001_bb0330) 2012; 5 Pritchard (10.1016/j.tibs.2019.04.001_bb0240) 2014; 171 Sengupta (10.1016/j.tibs.2019.04.001_bb0170) 2013; 8 Yin (10.1016/j.tibs.2019.04.001_bb0125) 2019; 363 Cao (10.1016/j.tibs.2019.04.001_bb0250) 2013; 77 Di Paolo (10.1016/j.tibs.2019.04.001_bb0050) 2006; 443 Lee (10.1016/j.tibs.2019.04.001_bb0360) 2013; 4 Kruse (10.1016/j.tibs.2019.04.001_bb0370) 2012; 140 Bernier (10.1016/j.tibs.2019.04.001_bb0390) 2008; 28 Petersen (10.1016/j.tibs.2019.04.001_bb0160) 2016; 7 Yen (10.1016/j.tibs.2019.04.001_bb0075) 2018; 559 Comoglio (10.1016/j.tibs.2019.04.001_bb0200) 2014; 111 Tsantoulas (10.1016/j.tibs.2019.04.001_bb0420) 2014; 37 Fine (10.1016/j.tibs.2019.04.001_bb0135) 2018; 9 Wickenden (10.1016/j.tibs.2019.04.001_bb0380) 2009; 15 Taylor (10.1016/j.tibs.2019.04.001_bb0375) 2017; 1859 Wang (10.1016/j.tibs.2019.04.001_bb0165) 2012; 1 Gupta (10.1016/j.tibs.2019.04.001_bb0080) 2017; 541 Cheng (10.1016/j.tibs.2019.04.001_bb0055) 2011; 100 Cheng (10.1016/j.tibs.2019.04.001_bb0120) 2018; 361 Pavel (10.1016/j.tibs.2019.04.001_bb0185) 2018 Coste (10.1016/j.tibs.2019.04.001_bb0325) 2012; 483 Lingwood (10.1016/j.tibs.2019.04.001_bb0155) 2010; 327 Chemin (10.1016/j.tibs.2019.04.001_bb0275) 2007; 455 Hamouda (10.1016/j.tibs.2019.04.001_bb0060) 2006; 45 van den Bogaart (10.1016/j.tibs.2019.04.001_bb0145) 2011; 479 Cabanos (10.1016/j.tibs.2019.04.001_bb0090) 2017; 20 Grant (10.1016/j.tibs.2019.04.001_bb0410) 2009; 2 Raja (10.1016/j.tibs.2019.04.001_bb0350) 2007; 581 Chi (10.1016/j.tibs.2019.04.001_bb0150) 2009; 6 Hille (10.1016/j.tibs.2019.04.001_bb0005) 2001 |
References_xml | – volume: 89 start-page: 4081 year: 2005 end-page: 4089 ident: bb0345 article-title: The interfacial lipid binding site on the potassium channel KcsA is specific for anionic phospholipids publication-title: Biophys. J. – volume: 541 start-page: 421 year: 2017 end-page: 424 ident: bb0080 article-title: The role of interfacial lipids in stabilizing membrane protein oligomers publication-title: Nature – volume: 9 start-page: 4192 year: 2018 ident: bb0135 article-title: Structural basis for PIP publication-title: Nat. Commun. – volume: 93 start-page: 1019 year: 2013 end-page: 1137 ident: bb0305 article-title: Phosphoinositides: tiny lipids with giant impact on cell regulation publication-title: Physiol. Rev. – volume: 62 start-page: 1089 year: 2010 end-page: 1095 ident: bb0415 article-title: Ion channels as novel therapeutic targets in the treatment of pain publication-title: J. Pharm. Pharmacol. – volume: 28 start-page: 143 year: 2004 end-page: 154 ident: bb0300 article-title: Ion homeostasis, channels, and transporters: an update on cellular mechanisms publication-title: Adv. Physiol. Educ. – volume: 483 start-page: 176 year: 2012 end-page: 181 ident: bb0325 article-title: Piezo proteins are pore-forming subunits of mechanically activated channels publication-title: Nature – volume: 361 start-page: 876 year: 2018 end-page: 880 ident: bb0120 article-title: Single-particle cryo-EM – how did it get here and where will it go publication-title: Science – volume: 3 start-page: 170 year: 2012 ident: bb0265 article-title: Dual regulation of voltage-sensitive ion channels by PIP2 publication-title: Front. Pharmacol. – volume: 477 start-page: 495 year: 2011 end-page: 498 ident: bb0100 article-title: Structural basis of PIP publication-title: Nature – volume: 140 start-page: 189 year: 2012 end-page: 205 ident: bb0370 article-title: Regulation of voltage-gated potassium channels by PI(4,5)P publication-title: J. Gen. Physiol. – volume: 145 start-page: 361 year: 2015 end-page: 364 ident: bb0230 article-title: How is SR calcium release in muscle modulated by PIP(4,5) publication-title: J. Gen. Physiol. – volume: 564 start-page: 117 year: 2005 end-page: 129 ident: bb0320 article-title: PIP2 hydrolysis underlies agonist-induced inhibition and regulates voltage gating of two-pore domain K publication-title: J. Physiol. – volume: 30 start-page: 12526 year: 2010 end-page: 12534 ident: bb0405 article-title: Gating of transient receptor potential melastatin 8 (TRPM8) channels activated by cold and chemical agonists in planar lipid bilayers publication-title: J. Neurosci. – year: 2001 ident: bb0005 article-title: Ion Channels of Excitable Membranes – volume: 77 start-page: 667 year: 2013 end-page: 679 ident: bb0250 article-title: TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids publication-title: Neuron – volume: 223 start-page: 1143 year: 2014 end-page: 1176 ident: bb0270 article-title: Phosphoinositide regulation of TRP channels publication-title: Handb. Exp. Pharmacol. – volume: 9 start-page: 4198 year: 2018 ident: bb0130 article-title: Structural insights on TRPV5 gating by endogenous modulators publication-title: Nat. Commun. – volume: 443 start-page: 651 year: 2006 end-page: 657 ident: bb0050 article-title: Phosphoinositides in cell regulation and membrane dynamics publication-title: Nature – volume: 304 start-page: 265 year: 2004 end-page: 270 ident: bb0255 article-title: Functional conversion between A-type and delayed rectifier K publication-title: Science – volume: 111 start-page: 13547 year: 2014 end-page: 13552 ident: bb0200 article-title: Phospholipase D2 specifically regulates TREK potassium channels via direct interaction and local production of phosphatidic acid publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 13 start-page: 333 year: 2016 end-page: 336 ident: bb0065 article-title: High-resolution mass spectrometry of small molecules bound to membrane proteins publication-title: Nat. Methods – volume: 6 start-page: 15 year: 2009 end-page: 18 ident: bb0150 article-title: Super-resolution microscopy: breaking the limits publication-title: Nat. Methods – volume: 3 start-page: 1 year: 2014 end-page: 13 ident: bb0220 article-title: Phosphatidic acid modulation of K publication-title: Elife – volume: 38 year: 2018 ident: bb0295 article-title: A closely-associated phospholipase C regulates cation channel function through phosphoinositide hydrolysis publication-title: J. Neurosci. – volume: 20 start-page: 1287 year: 2017 end-page: 1294 ident: bb0090 article-title: A soluble fluorescent binding assay reveals PIP publication-title: Cell Rep. – volume: 559 start-page: 423 year: 2018 end-page: 427 ident: bb0075 article-title: PtdIns(4,5)P publication-title: Nature – volume: 37 start-page: 175 year: 2008 end-page: 195 ident: bb0015 article-title: PIP publication-title: Annu. Rev. Biophys. – volume: 288 start-page: 35003 year: 2013 end-page: 35013 ident: bb0245 article-title: Promiscuous activation of transient receptor potential vanilloid 1 (TRPV1) channels by negatively charged intracellular lipids: the key role of endogenous phosphoinositides in maintaining channel activity publication-title: J. Biol. Chem. – year: 2018 ident: bb0215 article-title: A membrane thickness sensor in TREK-1 channels transduces mechanical force publication-title: SSRN – volume: 1859 start-page: 586 year: 2017 end-page: 597 ident: bb0375 article-title: Regulation of KCNQ/Kv7 family voltage-gated K publication-title: Biochim. Biophys. Acta Biomembr. – volume: 6 year: 2017 ident: bb0195 article-title: Protein sorting by lipid phase-like domains supports emergent signaling function in B lymphocyte plasma membranes publication-title: Elife – volume: 30 start-page: 1306 year: 2016 end-page: 1316 ident: bb0395 article-title: Stimulation-dependent gating of TRPM3 channel in planar lipid bilayers publication-title: FASEB J. – volume: 285 start-page: 10337 year: 2010 end-page: 10343 ident: bb0290 article-title: Phospholipase C activity affinity purifies with the publication-title: J. Biol. Chem. – volume: 145 start-page: 315 year: 2015 end-page: 330 ident: bb0235 article-title: Depression of voltage-activated Ca publication-title: J. Gen. Physiol. – volume: 582 start-page: 967 year: 2007 end-page: 975 ident: bb0040 article-title: Target-specific PIP publication-title: J. Physiol. – volume: 63 start-page: 133 year: 1990 end-page: 139 ident: bb0205 article-title: A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane publication-title: Cell – volume: 455 start-page: 125 year: 2007 end-page: 145 ident: bb0260 article-title: Modulation of cyclic nucleotide-regulated HCN channels by PIP publication-title: Pflugers Arch. – volume: 391 start-page: 803 year: 1998 end-page: 806 ident: bb0030 article-title: Direct activation of inward rectifier potassium channels by PIP publication-title: Nature – volume: 455 start-page: 97 year: 2007 end-page: 103 ident: bb0275 article-title: Up- and down-regulation of the mechano-gated K2P channel TREK-1 by PIP publication-title: Pflugers Arch. Eur. J. Physiol. – volume: 8 start-page: 345 year: 2013 end-page: 354 ident: bb0170 article-title: Quantifying spatial organization in point-localization superresolution images using pair correlation analysis publication-title: Nat. Protoc. – volume: 286 start-page: 8709 year: 2011 end-page: 8716 ident: bb0010 article-title: Ion channel regulation by protein palmitoylation publication-title: J. Biol. Chem. – volume: 1 start-page: 857 year: 2012 end-page: 862 ident: bb0165 article-title: Segregation of PIP publication-title: Biol. Open – volume: 5 start-page: 1 year: 2012 end-page: 9 ident: bb0330 article-title: Molecular mechanisms of acetylcholine receptor–lipid interactions: from model membranes to human biology publication-title: Biophys. Rev. – volume: 455 start-page: 55 year: 2007 end-page: 67 ident: bb0020 article-title: Local PIP publication-title: Pflugers Arch. – volume: 175 start-page: 377 year: 2006 end-page: 382 ident: bb0045 article-title: Rapidly inducible changes in phosphatidylinositol 4,5-bisphosphate levels influence multiple regulatory functions of the lipid in intact living cells publication-title: J. Cell Biol. – volume: 479 start-page: 552 year: 2011 end-page: 555 ident: bb0145 article-title: Membrane protein sequestering by ionic protein-lipid interactions publication-title: Nature – volume: 56 start-page: 2524 year: 2018 end-page: 2541 ident: bb0355 article-title: Anionic phospholipids bind to and modulate the activity of human TRESK background K publication-title: Mol. Neurobiol. – volume: 45 start-page: 4327 year: 2006 end-page: 4337 ident: bb0060 article-title: Assessing the lipid requirements of the publication-title: Biochemistry – volume: 565 start-page: 516 year: 2019 end-page: 520 ident: bb0140 article-title: Cryo-EM structure of the human α1β3γ2 GABA publication-title: Nature – volume: 47 start-page: 12175 year: 2008 end-page: 12184 ident: bb0340 article-title: Importance of direct interactions with lipids for the function of the mechanosensitive channel MscL publication-title: Biochemistry – volume: 47 start-page: 4317 year: 2008 end-page: 4328 ident: bb0335 article-title: Anionic phospholipids affect the rate and extent of flux through the mechanosensitive channel of large conductance MscL publication-title: Biochemistry – volume: 28 start-page: 12938 year: 2008 end-page: 12945 ident: bb0390 article-title: Phosphoinositides regulate P2X4 ATP-gated channels through direct interactions publication-title: J. Neurosci. – volume: 8 start-page: 279 year: 2005 end-page: 287 ident: bb0095 article-title: Cytoplasmic domain structures of K publication-title: Nat. Neurosci. – volume: 534 start-page: 347 year: 2016 end-page: 351 ident: bb0110 article-title: TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action publication-title: Nature – volume: 7 year: 2016 ident: bb0160 article-title: Kinetic disruption of lipid rafts is a mechanosensor for phospholipase D publication-title: Nat. Commun. – volume: 115 start-page: 595 year: 2018 end-page: 604 ident: bb0175 article-title: From dynamics to membrane organization: experimental breakthroughs occasion a 'modeling manifesto' publication-title: Biophys. J. – volume: 176 start-page: 249 year: 2007 end-page: 254 ident: bb0210 article-title: Palmitoylation-dependent protein sorting publication-title: J. Cell Biol. – volume: 150 start-page: 211 year: 2018 end-page: 224 ident: bb0035 article-title: Lipid signaling to membrane proteins: from second messengers to membrane domains and adapter-free endocytosis publication-title: J. Gen. Physiol. – year: 2018 ident: bb0185 article-title: Studies on the mechanism of general anesthesia publication-title: bioRxiv – volume: 510 start-page: 172 year: 2014 end-page: 175 ident: bb0070 article-title: Membrane proteins bind lipids selectively to modulate their structure and function publication-title: Nature – volume: 363 year: 2019 ident: bb0125 article-title: Structural basis of cooling agent and lipid sensing by the cold-activated TRPM8 channel publication-title: Science – volume: 242 start-page: 477 year: 1967 end-page: 484 ident: bb0315 article-title: Transphosphatidylation by phospholipase D publication-title: J. Biol. Chem. – volume: 504 start-page: 113 year: 2013 end-page: 118 ident: bb0115 article-title: TRPV1 structures in distinct conformations reveal activation mechanisms publication-title: Nature – volume: 411 start-page: 957 year: 2001 end-page: 962 ident: bb0280 article-title: Bradykinin and nerve growth factor release the capsaicin receptor from PtdIns(4, 5)P2-mediated inhibition publication-title: Nature – volume: 581 start-page: 5715 year: 2007 end-page: 5722 ident: bb0350 article-title: Phosphatidic acid plays a special role in stabilizing and folding of the tetrameric potassium channel KcsA publication-title: FEBS Lett. – volume: 100 start-page: 620 year: 2011 end-page: 628 ident: bb0055 article-title: Dual-mode phospholipid regulation of human inward rectifying potassium channels publication-title: Biophys. J. – volume: 1838 start-page: 1451 year: 2014 end-page: 1466 ident: bb0180 article-title: The fluid-mosaic model of membrane structure: still relevant to understanding the structure, function and dynamics of biological membranes after more than 40 years publication-title: Biochim. Biophys. Acta – volume: 431 start-page: 196 year: 2019 end-page: 209 ident: bb0225 article-title: A molecular target for an alcohol chain length cutoff publication-title: J. Mol. Biol. – volume: 4 start-page: 2786 year: 2013 ident: bb0360 article-title: Secondary anionic phospholipid binding site and gating mechanism in K publication-title: Nat. Commun. – volume: 94 start-page: 320 year: 2007 end-page: 335 ident: bb0365 article-title: Activation of inwardly rectifying potassium (K publication-title: Prog. Biophys. Mol. Biol. – volume: 115 start-page: 6691 year: 2018 end-page: 6696 ident: bb0085 article-title: Lipid binding attenuates channel closure of the outer membrane protein OmpF publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 327 start-page: 46 year: 2010 end-page: 50 ident: bb0155 article-title: Lipid rafts as a membrane-organizing principle publication-title: Science – volume: 147 start-page: 199 year: 2011 end-page: 208 ident: bb0105 article-title: Crystal structure of the mammalian GIRK2 K publication-title: Cell – volume: 1851 start-page: 620 year: 2015 end-page: 628 ident: bb0025 article-title: Lipid agonism: the PIP publication-title: Biochim. Biophys. Acta – volume: 37 start-page: 146 year: 2014 end-page: 158 ident: bb0420 article-title: Opening paths to novel analgesics: the role of potassium channels in chronic pain publication-title: Trends Neurosci. – volume: 15 start-page: 1773 year: 2009 end-page: 1798 ident: bb0380 article-title: K publication-title: Curr. Pharm. Des. – volume: 138 start-page: 451 year: 2005 end-page: 456 ident: bb0285 article-title: Phospholipase Cδ4 associates with glutamate receptor interacting protein 1 in testis publication-title: J. Biochem. – volume: 273 start-page: 12846 year: 1998 end-page: 12852 ident: bb0310 article-title: Cloning and initial characterization of a human phospholipase D2 (hPLD2): ADP-ribosylation factor regulates hPLD2 publication-title: J. Biol. Chem. – volume: 99 start-page: 1110 year: 2010 end-page: 1118 ident: bb0385 article-title: Phosphatidylinositol-4,5-bisphosphate (PIP publication-title: Biophys. J. – volume: 146 start-page: 65 year: 2015 end-page: 77 ident: bb0400 article-title: Transient receptor potential melastatin 3 is a phosphoinositide-dependent ion channel publication-title: J. Gen. Physiol. – volume: 2 start-page: 185 year: 2009 end-page: 194 ident: bb0410 article-title: Cardiac ion channels publication-title: Circ. Arrhythm. Electrophysiol. – volume: 296 start-page: 913 year: 2002 end-page: 916 ident: bb0190 article-title: Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells publication-title: Science – volume: 171 start-page: 4311 year: 2014 end-page: 4321 ident: bb0240 article-title: Inhibitory role of phosphatidylinositol 4,5-bisphosphate on TMEM16A-encoded calcium-activated chloride channels in rat pulmonary artery publication-title: Br. J. Pharmacol. – volume: 477 start-page: 495 year: 2011 ident: 10.1016/j.tibs.2019.04.001_bb0100 article-title: Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2 publication-title: Nature doi: 10.1038/nature10370 – volume: 140 start-page: 189 year: 2012 ident: 10.1016/j.tibs.2019.04.001_bb0370 article-title: Regulation of voltage-gated potassium channels by PI(4,5)P2 publication-title: J. Gen. Physiol. doi: 10.1085/jgp.201210806 – volume: 38 year: 2018 ident: 10.1016/j.tibs.2019.04.001_bb0295 article-title: A closely-associated phospholipase C regulates cation channel function through phosphoinositide hydrolysis publication-title: J. Neurosci. doi: 10.1523/JNEUROSCI.0586-18.2018 – volume: 564 start-page: 117 year: 2005 ident: 10.1016/j.tibs.2019.04.001_bb0320 article-title: PIP2 hydrolysis underlies agonist-induced inhibition and regulates voltage gating of two-pore domain K+ channels publication-title: J. Physiol. doi: 10.1113/jphysiol.2004.081935 – volume: 45 start-page: 4327 year: 2006 ident: 10.1016/j.tibs.2019.04.001_bb0060 article-title: Assessing the lipid requirements of the Torpedo californica nicotinic acetylcholine receptor publication-title: Biochemistry doi: 10.1021/bi052281z – volume: 9 start-page: 4192 year: 2018 ident: 10.1016/j.tibs.2019.04.001_bb0135 article-title: Structural basis for PIP2-mediated human TRPML1 regulation publication-title: Nat. Commun. doi: 10.1038/s41467-018-06493-7 – volume: 8 start-page: 345 year: 2013 ident: 10.1016/j.tibs.2019.04.001_bb0170 article-title: Quantifying spatial organization in point-localization superresolution images using pair correlation analysis publication-title: Nat. Protoc. doi: 10.1038/nprot.2013.005 – volume: 28 start-page: 12938 year: 2008 ident: 10.1016/j.tibs.2019.04.001_bb0390 article-title: Phosphoinositides regulate P2X4 ATP-gated channels through direct interactions publication-title: J. Neurosci. doi: 10.1523/JNEUROSCI.3038-08.2008 – volume: 138 start-page: 451 year: 2005 ident: 10.1016/j.tibs.2019.04.001_bb0285 article-title: Phospholipase Cδ4 associates with glutamate receptor interacting protein 1 in testis publication-title: J. Biochem. doi: 10.1093/jb/mvi135 – volume: 171 start-page: 4311 year: 2014 ident: 10.1016/j.tibs.2019.04.001_bb0240 article-title: Inhibitory role of phosphatidylinositol 4,5-bisphosphate on TMEM16A-encoded calcium-activated chloride channels in rat pulmonary artery publication-title: Br. J. Pharmacol. doi: 10.1111/bph.12778 – volume: 363 year: 2019 ident: 10.1016/j.tibs.2019.04.001_bb0125 article-title: Structural basis of cooling agent and lipid sensing by the cold-activated TRPM8 channel publication-title: Science doi: 10.1126/science.aav9334 – volume: 28 start-page: 143 year: 2004 ident: 10.1016/j.tibs.2019.04.001_bb0300 article-title: Ion homeostasis, channels, and transporters: an update on cellular mechanisms publication-title: Adv. Physiol. Educ. doi: 10.1152/advan.00046.2004 – volume: 479 start-page: 552 year: 2011 ident: 10.1016/j.tibs.2019.04.001_bb0145 article-title: Membrane protein sequestering by ionic protein-lipid interactions publication-title: Nature doi: 10.1038/nature10545 – volume: 7 year: 2016 ident: 10.1016/j.tibs.2019.04.001_bb0160 article-title: Kinetic disruption of lipid rafts is a mechanosensor for phospholipase D publication-title: Nat. Commun. doi: 10.1038/ncomms13873 – volume: 4 start-page: 2786 year: 2013 ident: 10.1016/j.tibs.2019.04.001_bb0360 article-title: Secondary anionic phospholipid binding site and gating mechanism in Kir2.1 inward rectifier channels publication-title: Nat. Commun. doi: 10.1038/ncomms3786 – volume: 111 start-page: 13547 year: 2014 ident: 10.1016/j.tibs.2019.04.001_bb0200 article-title: Phospholipase D2 specifically regulates TREK potassium channels via direct interaction and local production of phosphatidic acid publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1407160111 – volume: 115 start-page: 595 year: 2018 ident: 10.1016/j.tibs.2019.04.001_bb0175 article-title: From dynamics to membrane organization: experimental breakthroughs occasion a 'modeling manifesto' publication-title: Biophys. J. doi: 10.1016/j.bpj.2018.07.012 – volume: 285 start-page: 10337 year: 2010 ident: 10.1016/j.tibs.2019.04.001_bb0290 article-title: Phospholipase C activity affinity purifies with the Torpedo nicotinic acetylcholine receptor publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.071993 – volume: 150 start-page: 211 year: 2018 ident: 10.1016/j.tibs.2019.04.001_bb0035 article-title: Lipid signaling to membrane proteins: from second messengers to membrane domains and adapter-free endocytosis publication-title: J. Gen. Physiol. doi: 10.1085/jgp.201711875 – volume: 3 start-page: 170 year: 2012 ident: 10.1016/j.tibs.2019.04.001_bb0265 article-title: Dual regulation of voltage-sensitive ion channels by PIP2 publication-title: Front. Pharmacol. doi: 10.3389/fphar.2012.00170 – volume: 391 start-page: 803 year: 1998 ident: 10.1016/j.tibs.2019.04.001_bb0030 article-title: Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gβγ publication-title: Nature doi: 10.1038/35882 – volume: 559 start-page: 423 year: 2018 ident: 10.1016/j.tibs.2019.04.001_bb0075 article-title: PtdIns(4,5)P2 stabilizes active states of GPCRs and enhances selectivity of G-protein coupling publication-title: Nature doi: 10.1038/s41586-018-0325-6 – volume: 63 start-page: 133 year: 1990 ident: 10.1016/j.tibs.2019.04.001_bb0205 article-title: A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane publication-title: Cell doi: 10.1016/0092-8674(90)90294-O – volume: 13 start-page: 333 year: 2016 ident: 10.1016/j.tibs.2019.04.001_bb0065 article-title: High-resolution mass spectrometry of small molecules bound to membrane proteins publication-title: Nat. Methods doi: 10.1038/nmeth.3771 – volume: 93 start-page: 1019 year: 2013 ident: 10.1016/j.tibs.2019.04.001_bb0305 article-title: Phosphoinositides: tiny lipids with giant impact on cell regulation publication-title: Physiol. Rev. doi: 10.1152/physrev.00028.2012 – volume: 504 start-page: 113 year: 2013 ident: 10.1016/j.tibs.2019.04.001_bb0115 article-title: TRPV1 structures in distinct conformations reveal activation mechanisms publication-title: Nature doi: 10.1038/nature12823 – volume: 94 start-page: 320 year: 2007 ident: 10.1016/j.tibs.2019.04.001_bb0365 article-title: Activation of inwardly rectifying potassium (Kir) channels by phosphatidylinositol-4,5-bisphosphate (PIP2): interaction with other regulatory ligands publication-title: Prog. Biophys. Mol. Biol. doi: 10.1016/j.pbiomolbio.2006.04.001 – volume: 286 start-page: 8709 year: 2011 ident: 10.1016/j.tibs.2019.04.001_bb0010 article-title: Ion channel regulation by protein palmitoylation publication-title: J. Biol. Chem. doi: 10.1074/jbc.R110.210005 – volume: 565 start-page: 516 year: 2019 ident: 10.1016/j.tibs.2019.04.001_bb0140 article-title: Cryo-EM structure of the human α1β3γ2 GABAA receptor in a lipid bilayer publication-title: Nature doi: 10.1038/s41586-018-0833-4 – volume: 30 start-page: 1306 year: 2016 ident: 10.1016/j.tibs.2019.04.001_bb0395 article-title: Stimulation-dependent gating of TRPM3 channel in planar lipid bilayers publication-title: FASEB J. doi: 10.1096/fj.15-281576 – volume: 1838 start-page: 1451 year: 2014 ident: 10.1016/j.tibs.2019.04.001_bb0180 article-title: The fluid-mosaic model of membrane structure: still relevant to understanding the structure, function and dynamics of biological membranes after more than 40 years publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamem.2013.10.019 – volume: 115 start-page: 6691 year: 2018 ident: 10.1016/j.tibs.2019.04.001_bb0085 article-title: Lipid binding attenuates channel closure of the outer membrane protein OmpF publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1721152115 – volume: 510 start-page: 172 year: 2014 ident: 10.1016/j.tibs.2019.04.001_bb0070 article-title: Membrane proteins bind lipids selectively to modulate their structure and function publication-title: Nature doi: 10.1038/nature13419 – volume: 288 start-page: 35003 year: 2013 ident: 10.1016/j.tibs.2019.04.001_bb0245 article-title: Promiscuous activation of transient receptor potential vanilloid 1 (TRPV1) channels by negatively charged intracellular lipids: the key role of endogenous phosphoinositides in maintaining channel activity publication-title: J. Biol. Chem. doi: 10.1074/jbc.M113.520288 – volume: 47 start-page: 4317 year: 2008 ident: 10.1016/j.tibs.2019.04.001_bb0335 article-title: Anionic phospholipids affect the rate and extent of flux through the mechanosensitive channel of large conductance MscL publication-title: Biochemistry doi: 10.1021/bi702409t – volume: 146 start-page: 65 year: 2015 ident: 10.1016/j.tibs.2019.04.001_bb0400 article-title: Transient receptor potential melastatin 3 is a phosphoinositide-dependent ion channel publication-title: J. Gen. Physiol. doi: 10.1085/jgp.201411336 – volume: 411 start-page: 957 year: 2001 ident: 10.1016/j.tibs.2019.04.001_bb0280 article-title: Bradykinin and nerve growth factor release the capsaicin receptor from PtdIns(4, 5)P2-mediated inhibition publication-title: Nature doi: 10.1038/35082088 – volume: 483 start-page: 176 year: 2012 ident: 10.1016/j.tibs.2019.04.001_bb0325 article-title: Piezo proteins are pore-forming subunits of mechanically activated channels publication-title: Nature doi: 10.1038/nature10812 – volume: 581 start-page: 5715 year: 2007 ident: 10.1016/j.tibs.2019.04.001_bb0350 article-title: Phosphatidic acid plays a special role in stabilizing and folding of the tetrameric potassium channel KcsA publication-title: FEBS Lett. doi: 10.1016/j.febslet.2007.11.039 – volume: 8 start-page: 279 year: 2005 ident: 10.1016/j.tibs.2019.04.001_bb0095 article-title: Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification publication-title: Nat. Neurosci. doi: 10.1038/nn1411 – volume: 77 start-page: 667 year: 2013 ident: 10.1016/j.tibs.2019.04.001_bb0250 article-title: TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids publication-title: Neuron doi: 10.1016/j.neuron.2012.12.016 – year: 2001 ident: 10.1016/j.tibs.2019.04.001_bb0005 – volume: 443 start-page: 651 year: 2006 ident: 10.1016/j.tibs.2019.04.001_bb0050 article-title: Phosphoinositides in cell regulation and membrane dynamics publication-title: Nature doi: 10.1038/nature05185 – volume: 455 start-page: 97 year: 2007 ident: 10.1016/j.tibs.2019.04.001_bb0275 article-title: Up- and down-regulation of the mechano-gated K2P channel TREK-1 by PIP2 and other membrane phospholipids publication-title: Pflugers Arch. Eur. J. Physiol. doi: 10.1007/s00424-007-0250-2 – volume: 273 start-page: 12846 year: 1998 ident: 10.1016/j.tibs.2019.04.001_bb0310 article-title: Cloning and initial characterization of a human phospholipase D2 (hPLD2): ADP-ribosylation factor regulates hPLD2 publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.21.12846 – volume: 145 start-page: 361 year: 2015 ident: 10.1016/j.tibs.2019.04.001_bb0230 article-title: How is SR calcium release in muscle modulated by PIP(4,5)2? publication-title: J. Gen. Physiol. doi: 10.1085/jgp.201511395 – volume: 176 start-page: 249 year: 2007 ident: 10.1016/j.tibs.2019.04.001_bb0210 article-title: Palmitoylation-dependent protein sorting publication-title: J. Cell Biol. doi: 10.1083/jcb.200610151 – volume: 1 start-page: 857 year: 2012 ident: 10.1016/j.tibs.2019.04.001_bb0165 article-title: Segregation of PIP2 and PIP3 into distinct nanoscale regions within the plasma membrane publication-title: Biol. Open doi: 10.1242/bio.20122071 – volume: 37 start-page: 175 year: 2008 ident: 10.1016/j.tibs.2019.04.001_bb0015 article-title: PIP2 is a necessary cofactor for ion channel function: how and why? publication-title: Annu. Rev. Biophys. doi: 10.1146/annurev.biophys.37.032807.125859 – volume: 455 start-page: 125 year: 2007 ident: 10.1016/j.tibs.2019.04.001_bb0260 article-title: Modulation of cyclic nucleotide-regulated HCN channels by PIP2 and receptors coupled to phospholipase C publication-title: Pflugers Arch. doi: 10.1007/s00424-007-0295-2 – volume: 242 start-page: 477 year: 1967 ident: 10.1016/j.tibs.2019.04.001_bb0315 article-title: Transphosphatidylation by phospholipase D publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)96298-8 – volume: 361 start-page: 876 year: 2018 ident: 10.1016/j.tibs.2019.04.001_bb0120 article-title: Single-particle cryo-EM – how did it get here and where will it go publication-title: Science doi: 10.1126/science.aat4346 – volume: 15 start-page: 1773 year: 2009 ident: 10.1016/j.tibs.2019.04.001_bb0380 article-title: Kv7 channels as targets for the treatment of pain publication-title: Curr. Pharm. Des. doi: 10.2174/138161209788186326 – volume: 455 start-page: 55 year: 2007 ident: 10.1016/j.tibs.2019.04.001_bb0020 article-title: Local PIP2 signals: when, where, and how? publication-title: Pflugers Arch. doi: 10.1007/s00424-007-0280-9 – volume: 3 start-page: 1 year: 2014 ident: 10.1016/j.tibs.2019.04.001_bb0220 article-title: Phosphatidic acid modulation of Kv channel voltage sensor function publication-title: Elife doi: 10.7554/eLife.04366 – volume: 223 start-page: 1143 year: 2014 ident: 10.1016/j.tibs.2019.04.001_bb0270 article-title: Phosphoinositide regulation of TRP channels publication-title: Handb. Exp. Pharmacol. doi: 10.1007/978-3-319-05161-1_18 – volume: 47 start-page: 12175 year: 2008 ident: 10.1016/j.tibs.2019.04.001_bb0340 article-title: Importance of direct interactions with lipids for the function of the mechanosensitive channel MscL publication-title: Biochemistry doi: 10.1021/bi801352a – volume: 37 start-page: 146 year: 2014 ident: 10.1016/j.tibs.2019.04.001_bb0420 article-title: Opening paths to novel analgesics: the role of potassium channels in chronic pain publication-title: Trends Neurosci. doi: 10.1016/j.tins.2013.12.002 – year: 2018 ident: 10.1016/j.tibs.2019.04.001_bb0215 article-title: A membrane thickness sensor in TREK-1 channels transduces mechanical force publication-title: SSRN doi: 10.2139/ssrn.3155650 – volume: 6 year: 2017 ident: 10.1016/j.tibs.2019.04.001_bb0195 article-title: Protein sorting by lipid phase-like domains supports emergent signaling function in B lymphocyte plasma membranes publication-title: Elife doi: 10.7554/eLife.19891 – volume: 1851 start-page: 620 year: 2015 ident: 10.1016/j.tibs.2019.04.001_bb0025 article-title: Lipid agonism: the PIP2 paradigm of ligand-gated ion channels publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbalip.2015.01.011 – volume: 6 start-page: 15 year: 2009 ident: 10.1016/j.tibs.2019.04.001_bb0150 article-title: Super-resolution microscopy: breaking the limits publication-title: Nat. Methods doi: 10.1038/nmeth.f.234 – volume: 327 start-page: 46 year: 2010 ident: 10.1016/j.tibs.2019.04.001_bb0155 article-title: Lipid rafts as a membrane-organizing principle publication-title: Science doi: 10.1126/science.1174621 – volume: 89 start-page: 4081 year: 2005 ident: 10.1016/j.tibs.2019.04.001_bb0345 article-title: The interfacial lipid binding site on the potassium channel KcsA is specific for anionic phospholipids publication-title: Biophys. J. doi: 10.1529/biophysj.105.070755 – volume: 9 start-page: 4198 year: 2018 ident: 10.1016/j.tibs.2019.04.001_bb0130 article-title: Structural insights on TRPV5 gating by endogenous modulators publication-title: Nat. Commun. doi: 10.1038/s41467-018-06753-6 – volume: 1859 start-page: 586 year: 2017 ident: 10.1016/j.tibs.2019.04.001_bb0375 article-title: Regulation of KCNQ/Kv7 family voltage-gated K+ channels by lipids publication-title: Biochim. Biophys. Acta Biomembr. doi: 10.1016/j.bbamem.2016.10.023 – volume: 2 start-page: 185 year: 2009 ident: 10.1016/j.tibs.2019.04.001_bb0410 article-title: Cardiac ion channels publication-title: Circ. Arrhythm. Electrophysiol. doi: 10.1161/CIRCEP.108.789081 – volume: 145 start-page: 315 year: 2015 ident: 10.1016/j.tibs.2019.04.001_bb0235 article-title: Depression of voltage-activated Ca2+ release in skeletal muscle by activation of a voltage-sensing phosphatase publication-title: J. Gen. Physiol. doi: 10.1085/jgp.201411309 – volume: 99 start-page: 1110 year: 2010 ident: 10.1016/j.tibs.2019.04.001_bb0385 article-title: Phosphatidylinositol-4,5-bisphosphate (PIP2) stabilizes the open pore conformation of the Kv11.1 (hERG) channel publication-title: Biophys. J. doi: 10.1016/j.bpj.2010.06.013 – volume: 20 start-page: 1287 year: 2017 ident: 10.1016/j.tibs.2019.04.001_bb0090 article-title: A soluble fluorescent binding assay reveals PIP2 antagonism of TREK-1 channels publication-title: Cell Rep. doi: 10.1016/j.celrep.2017.07.034 – volume: 582 start-page: 967 year: 2007 ident: 10.1016/j.tibs.2019.04.001_bb0040 article-title: Target-specific PIP2 signalling: how might it work? publication-title: J. Physiol. doi: 10.1113/jphysiol.2007.132787 – volume: 147 start-page: 199 year: 2011 ident: 10.1016/j.tibs.2019.04.001_bb0105 article-title: Crystal structure of the mammalian GIRK2 K+ channel and gating regulation by G proteins, PIP2, and sodium publication-title: Cell doi: 10.1016/j.cell.2011.07.046 – year: 2018 ident: 10.1016/j.tibs.2019.04.001_bb0185 article-title: Studies on the mechanism of general anesthesia – volume: 541 start-page: 421 year: 2017 ident: 10.1016/j.tibs.2019.04.001_bb0080 article-title: The role of interfacial lipids in stabilizing membrane protein oligomers publication-title: Nature doi: 10.1038/nature20820 – volume: 56 start-page: 2524 year: 2018 ident: 10.1016/j.tibs.2019.04.001_bb0355 article-title: Anionic phospholipids bind to and modulate the activity of human TRESK background K+ channel publication-title: Mol. Neurobiol. doi: 10.1007/s12035-018-1244-0 – volume: 100 start-page: 620 year: 2011 ident: 10.1016/j.tibs.2019.04.001_bb0055 article-title: Dual-mode phospholipid regulation of human inward rectifying potassium channels publication-title: Biophys. J. doi: 10.1016/j.bpj.2010.12.3724 – volume: 175 start-page: 377 year: 2006 ident: 10.1016/j.tibs.2019.04.001_bb0045 article-title: Rapidly inducible changes in phosphatidylinositol 4,5-bisphosphate levels influence multiple regulatory functions of the lipid in intact living cells publication-title: J. Cell Biol. doi: 10.1083/jcb.200607116 – volume: 296 start-page: 913 year: 2002 ident: 10.1016/j.tibs.2019.04.001_bb0190 article-title: Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells publication-title: Science doi: 10.1126/science.1068539 – volume: 304 start-page: 265 year: 2004 ident: 10.1016/j.tibs.2019.04.001_bb0255 article-title: Functional conversion between A-type and delayed rectifier K+ channels by membrane lipids publication-title: Science doi: 10.1126/science.1094113 – volume: 534 start-page: 347 year: 2016 ident: 10.1016/j.tibs.2019.04.001_bb0110 article-title: TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action publication-title: Nature doi: 10.1038/nature17964 – volume: 30 start-page: 12526 year: 2010 ident: 10.1016/j.tibs.2019.04.001_bb0405 article-title: Gating of transient receptor potential melastatin 8 (TRPM8) channels activated by cold and chemical agonists in planar lipid bilayers publication-title: J. Neurosci. doi: 10.1523/JNEUROSCI.3189-10.2010 – volume: 431 start-page: 196 year: 2019 ident: 10.1016/j.tibs.2019.04.001_bb0225 article-title: A molecular target for an alcohol chain length cutoff publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2018.11.028 – volume: 5 start-page: 1 year: 2012 ident: 10.1016/j.tibs.2019.04.001_bb0330 article-title: Molecular mechanisms of acetylcholine receptor–lipid interactions: from model membranes to human biology publication-title: Biophys. Rev. doi: 10.1007/s12551-012-0078-7 – volume: 62 start-page: 1089 year: 2010 ident: 10.1016/j.tibs.2019.04.001_bb0415 article-title: Ion channels as novel therapeutic targets in the treatment of pain publication-title: J. Pharm. Pharmacol. doi: 10.1111/j.2042-7158.2010.01131.x |
SSID | ssj0015775 |
Score | 2.5215116 |
SecondaryResourceType | review_article |
Snippet | Anionic phospholipids are minor but prominent components of the plasma membrane that are necessary for ion channel function. Their persistence in bulk... Anionic phospholipids are minor but prominent components of the plasma membrane and necessary for ion channel function. Their persistence in bulk membranes, in... |
SourceID | pubmedcentral proquest pubmed crossref elsevier |
SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
StartPage | 795 |
SubjectTerms | cryo-electron microscopy Humans ion channels Ion Channels - metabolism lipid rafts mass spectrometry Nanotechnology phospholipids Phospholipids - metabolism plasma membrane signaling lipids super-resolution imaging |
Title | Tools for Understanding Nanoscale Lipid Regulation of Ion Channels |
URI | https://dx.doi.org/10.1016/j.tibs.2019.04.001 https://www.ncbi.nlm.nih.gov/pubmed/31060927 https://www.proquest.com/docview/2232003625 https://www.proquest.com/docview/2253201813 https://pubmed.ncbi.nlm.nih.gov/PMC6729126 |
Volume | 44 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT8JAEJ4QjIkX41t8kDXxZip97rZHJBLQhINCwq3pdrcRQ1oicPDib3emDwJqOHjhOU2WmWXm2_SbbwBu_SiJsLApw-GBY7iWEIYMiAlAYlKWayc8ylm-A94buU9jb1yDTtULQ7TKMvcXOT3P1uUnrdKbrdlk0npF8O0TJEEIQoWNOspdV9Auv_9a0TwsT-Riu2Scd1CXjTMFx2sxkSTZbQW53Gk5GOaP4vQbfP7kUK4Vpe4B7JdokrWLBR9CTadHsFvMl_w8hodhlk3nDHEpG603sTDMqdkco6MZza5W7KWYSI8xYlnC-vhEXQcpLu0ERt3HYadnlEMTjNiz-MLAEiw1l8KXeHIzCa0pO_ZkpO1ExsIJ3ARfBpGPD8rinkb_KQe3U-JEcaBi7pxCPc1SfQ7MjmSitRCmqRNXmVS4fMQbeCKLbSV91QCr8lYYl4riNNhiGlbUsfeQPBySh0PTJf5cA-5W18wKPY2t1l4VhHBjV4SY8Lded1NFLMS_C90DiVKdLdEIEWSuweNts6FpGQh9nAacFVFerRXRMDcDWzRAbMR_ZUBy3ZvfpJO3XLab4znGsvnFP3_TJezRu4LfdgX1xcdSXyMgWshmvuObsNPuP_cG3yCRCiU |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LS8NAEB58IHoR39bnCt4kNs_d5Khiqc-DttDbks1usFKSYuvBi7_dmTyKVenBS1uaCWxnNjPf0m--ATgN4zTGwqYtj0ee5TtCWCoiJgCJSTm-m_K4YPk-8nbXv-0FvTm4qnthiFZZ5f4ypxfZuvqmWXmzOez3m88IvkOCJAhBqLCJeVj08fGlMQbnnxOehxOIQm2XrIsW6qpzpiR5jfuKNLudqNA7rSbD_FGdfqPPnyTKb1WptQarFZxkF-WK12HOZBuwVA6Y_NiEy06eD0YMgSnrfu9iYZhU8xGGxzAaXq3ZUzmSHoPE8pTd4Bu1HWS4tC3otq47V22rmppgJYHDxxbWYGW4EqHCo5tNcE27SaBi46YqEV7kp_gxikN80Q4PDDpQe7ifUi9OIp1wbxsWsjwzu8DcWKXGCGHbJvW1TZUrRMCBR7LE1SrUDXBqb8mkkhSnyRYDWXPHXiV5WJKHpe0Tga4BZ5N7hqWgxkzroA6CnNoWEjP-zPtO6ohJfF7oT5A4M_k7GiGELER4glk2NC4DsY_XgJ0yypO1IhzmduSKBoip-E8MSK97-krWfyl0uzkeZByX7_3zNx3DcrvzcC_vbx7v9mGFrpRktwNYGL-9m0NER2N1VOz-LxhWC7M |
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=Tools+for+understanding+nanoscale+lipid+regulation+of+ion+channels&rft.jtitle=Trends+in+biochemical+sciences+%28Amsterdam.+Regular+ed.%29&rft.au=Robinson%2C+Carol+V.&rft.au=Rohacs%2C+Tibor&rft.au=Hansen%2C+Scott+B.&rft.date=2019-09-01&rft.issn=0968-0004&rft.volume=44&rft.issue=9&rft.spage=795&rft.epage=806&rft_id=info:doi/10.1016%2Fj.tibs.2019.04.001&rft_id=info%3Apmid%2F31060927&rft.externalDocID=PMC6729126 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0968-0004&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0968-0004&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0968-0004&client=summon |