Multidimensional significance of crystallin protein–protein interactions and their implications in various human diseases
Crystallins are the important structural and functional proteins in the eye lens responsible for refractive index. Post-translational modifications (PTMs) and mutations are major causative factors that affect crystallin structural conformation and functional characteristics thus playing a vital role...
Saved in:
| Published in | Biochimica et biophysica acta Vol. 1860; no. 1; pp. 222 - 233 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.01.2016
|
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | Crystallins are the important structural and functional proteins in the eye lens responsible for refractive index. Post-translational modifications (PTMs) and mutations are major causative factors that affect crystallin structural conformation and functional characteristics thus playing a vital role in the etiology of cataractogenesis.
The significance of crystallin protein–protein interactions (PPIs) in the lens and non-lenticular tissues is summarized.
Aberrancy of PPIs between crystallin, its associated protein and metal ions has been accomplished in various human diseases including cataract. A detailed account on multidimensional structural and functional significance of crystallin PPI in humans must be brought into limelight, in order to understand the biochemical and molecular basis augmenting the aberrancies of such interaction. In this scenario, the present review is focused to shed light on studies which will aid to expand our present understanding on disease pathogenesis related to loss of PPI thereby paving the way for putative future therapeutic targets to curb such diseases.
The interactions with α-crystallins always aid to protect their structural and functional characteristics. The up-regulation of αB-crystallin in the non-lenticular tissues always decodes as biomarker for various stress related disorders. For better understanding and treatment of various diseases, PPI studies provide overall outline about the structural and functional characteristics of the proteins. This information not only helps to find out the route of cataractogenesis but also aid to identify potential molecules to inhibit/prevent the further development of such complicated phenomenon. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease.
•Structural and functional significance of α-crystallin Protein-protein interaction (PPI) with lens associated proteins are narrated•Merits and demerits of PPI techniques are discussed•Significance of α-crystallin PPI with non-lenticular proteins are illustrated•Future scope of crystallin studies are specified |
|---|---|
| AbstractList | Crystallins are the important structural and functional proteins in the eye lens responsible for refractive index. Post-translational modifications (PTMs) and mutations are major causative factors that affect crystallin structural conformation and functional characteristics thus playing a vital role in the etiology of cataractogenesis.
The significance of crystallin protein-protein interactions (PPIs) in the lens and non-lenticular tissues is summarized.
Aberrancy of PPIs between crystallin, its associated protein and metal ions has been accomplished in various human diseases including cataract. A detailed account on multidimensional structural and functional significance of crystallin PPI in humans must be brought into limelight, in order to understand the biochemical and molecular basis augmenting the aberrancies of such interaction. In this scenario, the present review is focused to shed light on studies which will aid to expand our present understanding on disease pathogenesis related to loss of PPI thereby paving the way for putative future therapeutic targets to curb such diseases.
The interactions with α-crystallins always aid to protect their structural and functional characteristics. The up-regulation of αB-crystallin in the non-lenticular tissues always decodes as biomarker for various stress related disorders. For better understanding and treatment of various diseases, PPI studies provide overall outline about the structural and functional characteristics of the proteins. This information not only helps to find out the route of cataractogenesis but also aid to identify potential molecules to inhibit/prevent the further development of such complicated phenomenon. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease. BACKGROUNDCrystallins are the important structural and functional proteins in the eye lens responsible for refractive index. Post-translational modifications (PTMs) and mutations are major causative factors that affect crystallin structural conformation and functional characteristics thus playing a vital role in the etiology of cataractogenesis.SCOPE OF REVIEWThe significance of crystallin protein-protein interactions (PPIs) in the lens and non-lenticular tissues is summarized.MAJOR CONCLUSIONSAberrancy of PPIs between crystallin, its associated protein and metal ions has been accomplished in various human diseases including cataract. A detailed account on multidimensional structural and functional significance of crystallin PPI in humans must be brought into limelight, in order to understand the biochemical and molecular basis augmenting the aberrancies of such interaction. In this scenario, the present review is focused to shed light on studies which will aid to expand our present understanding on disease pathogenesis related to loss of PPI thereby paving the way for putative future therapeutic targets to curb such diseases.GENERAL SIGNIFICANCEThe interactions with α-crystallins always aid to protect their structural and functional characteristics. The up-regulation of αB-crystallin in the non-lenticular tissues always decodes as biomarker for various stress related disorders. For better understanding and treatment of various diseases, PPI studies provide overall outline about the structural and functional characteristics of the proteins. This information not only helps to find out the route of cataractogenesis but also aid to identify potential molecules to inhibit/prevent the further development of such complicated phenomenon. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease. Crystallins are the important structural and functional proteins in the eye lens responsible for refractive index. Post-translational modifications (PTMs) and mutations are major causative factors that affect crystallin structural conformation and functional characteristics thus playing a vital role in the etiology of cataractogenesis.The significance of crystallin protein–protein interactions (PPIs) in the lens and non-lenticular tissues is summarized.Aberrancy of PPIs between crystallin, its associated protein and metal ions has been accomplished in various human diseases including cataract. A detailed account on multidimensional structural and functional significance of crystallin PPI in humans must be brought into limelight, in order to understand the biochemical and molecular basis augmenting the aberrancies of such interaction. In this scenario, the present review is focused to shed light on studies which will aid to expand our present understanding on disease pathogenesis related to loss of PPI thereby paving the way for putative future therapeutic targets to curb such diseases.The interactions with α-crystallins always aid to protect their structural and functional characteristics. The up-regulation of αB-crystallin in the non-lenticular tissues always decodes as biomarker for various stress related disorders. For better understanding and treatment of various diseases, PPI studies provide overall outline about the structural and functional characteristics of the proteins. This information not only helps to find out the route of cataractogenesis but also aid to identify potential molecules to inhibit/prevent the further development of such complicated phenomenon. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease. Crystallins are the important structural and functional proteins in the eye lens responsible for refractive index. Post-translational modifications (PTMs) and mutations are major causative factors that affect crystallin structural conformation and functional characteristics thus playing a vital role in the etiology of cataractogenesis. The significance of crystallin protein–protein interactions (PPIs) in the lens and non-lenticular tissues is summarized. Aberrancy of PPIs between crystallin, its associated protein and metal ions has been accomplished in various human diseases including cataract. A detailed account on multidimensional structural and functional significance of crystallin PPI in humans must be brought into limelight, in order to understand the biochemical and molecular basis augmenting the aberrancies of such interaction. In this scenario, the present review is focused to shed light on studies which will aid to expand our present understanding on disease pathogenesis related to loss of PPI thereby paving the way for putative future therapeutic targets to curb such diseases. The interactions with α-crystallins always aid to protect their structural and functional characteristics. The up-regulation of αB-crystallin in the non-lenticular tissues always decodes as biomarker for various stress related disorders. For better understanding and treatment of various diseases, PPI studies provide overall outline about the structural and functional characteristics of the proteins. This information not only helps to find out the route of cataractogenesis but also aid to identify potential molecules to inhibit/prevent the further development of such complicated phenomenon. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease. •Structural and functional significance of α-crystallin Protein-protein interaction (PPI) with lens associated proteins are narrated•Merits and demerits of PPI techniques are discussed•Significance of α-crystallin PPI with non-lenticular proteins are illustrated•Future scope of crystallin studies are specified |
| Author | Anbarasu, Kumarasamy Sivakumar, Jeyarajan |
| Author_xml | – sequence: 1 givenname: Kumarasamy surname: Anbarasu fullname: Anbarasu, Kumarasamy email: anbumbt@bdu.ac.in, anbubdu@gmail.com – sequence: 2 givenname: Jeyarajan surname: Sivakumar fullname: Sivakumar, Jeyarajan |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/26365509$$D View this record in MEDLINE/PubMed |
| BookMark | eNqFkc1u1TAQhS1URG8Lb4CQl2wSbMd2EhZIqOJPKmIDa8uxJ-1cJc7FdipVbHgH3pAnwSW3GxZ0Nh5Z3zkanXNGTsISgJDnnNWccf1qXw-DvYJQC8ZVzfqaMfWI7HjXiqpjTJ-QHWuYrCTX6pScpbRnZVSvnpBToRutFOt35MfndcrocYaQcAl2ogmvAo7obHBAl5G6eJuynSYM9BCXDBh-__x13CiGDNG6XKSJ2uBpvgaMFOfDVBy274Ld2IjLmuj1OttAPSawCdJT8ni0U4Jnx_ecfHv_7uvFx-ryy4dPF28vKye1ylU7tD3rWj867blunLRKdNK3YuRcMtUoD4K1gxZeWQ1CDN2gBzm2o_RM9oNtzsnLzbdc_X2FlM2MycE02QDlKsM7oWTDm757GG2l7lrOVVPQF0d0HWbw5hBxtvHW3GdbgNcb4OKSUoTROMx_M8nR4mQ4M3dFmr3ZijR3RRrWm9JSEct_xPf-D8jebDIoed4gRJMcQmnSYwSXjV_w_wZ_AHUtvLs |
| CitedBy_id | crossref_primary_10_1016_j_biochi_2023_10_002 crossref_primary_10_3390_idr16060096 crossref_primary_10_1007_s10989_023_10537_y crossref_primary_10_1007_s00253_024_13017_5 crossref_primary_10_1016_j_bbrc_2016_07_051 crossref_primary_10_1002_bab_2637 crossref_primary_10_1016_j_bbagen_2015_10_018 crossref_primary_10_3390_applbiosci4010005 crossref_primary_10_1016_j_ijbiomac_2018_05_220 crossref_primary_10_1016_j_bbrc_2018_09_028 crossref_primary_10_1080_02713683_2019_1675176 crossref_primary_10_1016_j_ijbiomac_2020_11_158 crossref_primary_10_3390_ijms26062695 crossref_primary_10_3389_fmolb_2016_00053 crossref_primary_10_3390_antiox10010089 |
| Cites_doi | 10.1167/iovs.14-14734 10.1016/j.exer.2008.08.021 10.1155/2014/147648 10.1074/jbc.M112.399972 10.1007/s10549-009-0330-4 10.1074/jbc.M706453200 10.1016/j.brainres.2006.03.058 10.1016/j.bbrc.2014.07.056 10.1074/jbc.M303417200 10.1016/j.jmb.2004.05.054 10.1159/000348308 10.1371/journal.pone.0044077 10.1016/j.exer.2010.11.008 10.1016/S0021-9258(17)36872-2 10.1002/jcb.21598 10.1007/s004010100395 10.1073/pnas.96.11.6137 10.1007/s12177-011-9073-7 10.1093/jnen/59.4.265 10.1016/j.pbiomolbio.2014.02.004 10.1002/ijc.2910550511 10.1074/jbc.M110027200 10.1021/bi700149h 10.1021/bi048151s 10.1016/j.cell.2007.06.044 10.1016/j.bbrc.2014.09.068 10.1091/mbc.e05-01-0010 10.1042/BJ20050339 10.1073/pnas.1308898110 10.1038/onc.2015.12 10.1080/15216540601010096 10.1074/jbc.M512938200 10.1371/journal.pone.0115480 10.1021/bi0518141 10.1242/dev.02262 10.1074/jbc.275.6.3767 10.1016/0014-4835(92)90058-Z 10.1110/ps.035410.108 10.1371/journal.pone.0037256 10.1167/iovs.11-9147 10.1016/j.exer.2008.10.011 10.1371/journal.pone.0113041 10.1074/jbc.M109.013789 10.1096/fj.12-220657 10.1167/iovs.03-0720 10.1016/S0014-5793(00)02136-0 10.1002/pro.583 10.1016/j.pbiomolbio.2014.02.005 10.1371/journal.pone.0031421 10.1038/emboj.2012.318 10.1016/j.bbrc.2012.11.051 10.3390/cancers6010333 10.1007/978-1-4939-2522-3_14 10.1016/j.bpj.2009.10.056 10.1016/0167-4838(93)90107-3 10.1159/000329373 10.1073/pnas.89.17.7958 10.1016/j.exer.2010.01.013 10.1016/j.bbapap.2014.12.019 10.1007/s00018-008-8327-4 10.1074/jbc.M509017200 10.1146/annurev.bi.57.070188.002403 10.1073/pnas.89.21.10449 10.4049/jimmunol.154.1.363 10.1007/s00726-015-1935-z 10.1007/s11010-007-9615-2 10.1111/j.1432-1033.1993.tb17765.x 10.1074/jbc.M404444200 10.1021/pr050473a 10.3233/JAD-2001-3111 10.1016/S1047-8477(02)00545-2 10.1016/j.bbapap.2008.04.008 10.1021/la5007007 10.1371/journal.pone.0065610 10.1098/rstb.2011.0405 10.1038/srep08755 10.2174/156652412798889036 10.1110/ps.04815104 10.1016/S0140-6736(10)62345-8 10.1016/j.preteyeres.2014.11.002 10.1073/pnas.1111014108 10.1021/bi00520a003 10.1038/ncomms6159 10.1016/j.febslet.2007.07.022 10.1371/journal.pone.0028085 10.1111/j.1742-4658.2012.08669.x 10.1002/path.1711660110 10.1021/bi052051k 10.1002/pro.5560020312 10.1038/sj.cdd.4401384 10.1016/j.pbiomolbio.2014.02.006 10.1073/pnas.88.23.10686 10.1016/S0140-6736(03)12981-9 10.1016/j.exer.2008.08.018 10.1016/j.febslet.2006.09.063 10.1016/j.jmb.2007.11.019 10.3233/JAD-2010-1221 10.2144/97222pf02 10.1016/j.febslet.2007.04.033 10.1371/journal.pone.0003175 10.1016/0167-4838(94)90009-4 10.1021/bi061471m 10.5483/BMBRep.2010.43.6.432 10.1006/bbrc.1999.1167 10.1074/jbc.C100107200 10.1016/j.bpj.2011.07.056 10.1167/iovs.07-1259 10.1128/MCB.11.2.803 10.1021/bi051005h 10.1146/annurev.neuro.28.061604.135718 10.2144/97236pf01 10.1186/1471-2415-3-3 10.1167/iovs.02-0950 10.1016/j.bbrc.2011.01.058 10.1016/j.ijbiomac.2015.02.025 10.1021/bi802177g 10.1016/j.bbagen.2012.04.004 10.1002/pro.2095 |
| ContentType | Journal Article |
| Copyright | 2015 Copyright © 2015. Published by Elsevier B.V. |
| Copyright_xml | – notice: 2015 – notice: Copyright © 2015. Published by Elsevier B.V. |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 7S9 L.6 |
| DOI | 10.1016/j.bbagen.2015.09.005 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitleList | MEDLINE MEDLINE - Academic 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 | Chemistry Biology |
| EISSN | 1872-8006 |
| EndPage | 233 |
| ExternalDocumentID | 26365509 10_1016_j_bbagen_2015_09_005 S0304416515002378 |
| Genre | Research Support, Non-U.S. Gov't Journal Article Review |
| GroupedDBID | --- --K --M .~1 0R~ 1B1 1RT 1~. 1~5 23N 3O- 4.4 457 4G. 53G 5GY 5RE 5VS 7-5 71M 8P~ 9JM AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AAXUO ABEFU ABFNM ABGSF ABMAC ABUDA ABXDB ABYKQ ACDAQ ACIUM ACRLP ADBBV ADEZE ADMUD ADUVX AEBSH AEHWI AEKER AFKWA AFTJW AFXIZ AGHFR AGRDE AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CS3 DOVZS EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q GBLVA HLW HVGLF HZ~ IHE J1W KOM LX3 M41 MO0 N9A O-L O9- OAUVE OHT OZT P-8 P-9 PC. Q38 R2- ROL RPZ SBG SCC SDF SDG SDP SES SEW SPCBC SSU SSZ T5K UQL WH7 WUQ XJT XPP ~G- AAHBH AATTM AAXKI AAYWO AAYXX ABWVN ACRPL ACVFH ADCNI ADNMO AEIPS AEUPX AFJKZ AFPUW AGCQF AGQPQ AGRNS AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP BNPGV CITATION SSH -~X .55 .GJ AAYJJ ABJNI AFFNX AI. CGR CUY CVF ECM EIF F5P H~9 K-O MVM NPM RIG TWZ UHS VH1 X7M Y6R YYP ZE2 ZGI ~KM 7X8 7S9 EFKBS L.6 |
| ID | FETCH-LOGICAL-c465t-7b79087dfc6d163c4a5284d72f1140535de207b62d5a6e22b8b6b4f7f4d049ba3 |
| IEDL.DBID | .~1 |
| ISSN | 0304-4165 0006-3002 |
| IngestDate | Sun Aug 24 04:00:59 EDT 2025 Fri Jul 11 15:58:08 EDT 2025 Mon Jul 21 05:48:53 EDT 2025 Tue Jul 01 00:22:05 EDT 2025 Thu Apr 24 22:57:25 EDT 2025 Fri Feb 23 02:34:14 EST 2024 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 1 |
| Keywords | Cataract Crystallin Mutation Protein–protein interaction |
| Language | English |
| License | Copyright © 2015. Published by Elsevier B.V. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c465t-7b79087dfc6d163c4a5284d72f1140535de207b62d5a6e22b8b6b4f7f4d049ba3 |
| Notes | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 ObjectType-Article-1 ObjectType-Feature-2 |
| PMID | 26365509 |
| PQID | 1746871153 |
| PQPubID | 23479 |
| PageCount | 12 |
| ParticipantIDs | proquest_miscellaneous_1825431398 proquest_miscellaneous_1746871153 pubmed_primary_26365509 crossref_citationtrail_10_1016_j_bbagen_2015_09_005 crossref_primary_10_1016_j_bbagen_2015_09_005 elsevier_sciencedirect_doi_10_1016_j_bbagen_2015_09_005 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2016-01-01 |
| PublicationDateYYYYMMDD | 2016-01-01 |
| PublicationDate_xml | – month: 01 year: 2016 text: 2016-01-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | Netherlands |
| PublicationPlace_xml | – name: Netherlands |
| PublicationTitle | Biochimica et biophysica acta |
| PublicationTitleAlternate | Biochim Biophys Acta |
| PublicationYear | 2016 |
| Publisher | Elsevier B.V |
| Publisher_xml | – name: Elsevier B.V |
| References | Rekas, Adda, Andrew Aquilina, Barnham, Sunde, Galatis, Williamson, Masters, Anders, Robinson, Cappai, Carver (bb0415) 2004; 340 Sharma, Kumar, Kumar, Quinn (bb0555) 2000; 275 Wu, Zhang, Bian, Taylor, Liang, Ding, Horwitz, Shang (bb0240) 2012; 53 Stege, Renkawek, Overkamp, Verschuure, van Rijk, Reijnen-Aalbers, Boelens, Bosman, de Jong (bb0380) 1999; 262 Ramkumar (bb0015) 2014 Moreau, King (bb0650) 2012; 7 Arrigo, Gibert (bb0465) 2014; 6 Hu, Gong, Cao, Ma, Ji, Deng, Liu, Hu, Chen, Yan, Chen, Liu, Sun, Zhang, Liu, Wawrousek, Li (bb0510) 2012; 12 Takata, Oxford, Demeler, Lampi (bb0630) 2008; 17 Clark, Orr (bb0350) 2000; 59 Wistow, Piatigorsky (bb0010) 1988; 57 Ghosh, Shenoy, Clark (bb0495) 2007; 46 Bakthisaran, Tangirala, Rao (bb0500) 2015; 1854 Boelens (bb0320) 2014; 115 Murphy, LeVine (bb0365) 2010; 19 Murugesan, Santhoshkumar, Sharma (bb0250) 2008; 14 Banerjee, Das (bb0225) 2014; 30 Aoyama, Steiger, Frohli, Schafer, von Deimling, Wiestler, Klemenz (bb0535) 1993; 55 Ramkumar, Fujii, Fujii, Thankappan, Sakaue, Ingu, Natarajaseenivasan, Anbarasu (bb0140) 2014; 20 Fujii, Sakaue, Sasaki, Fujii (bb0070) 2012; 287 Ramkumar, Thankappan, Fujii, Natarajaseenivasan, Anbarasu (bb0165) 2015; 76 Dasgupta, Hohman, Carper (bb0530) 1992; 54 Liang (bb0255) 2004; 13 Xu, Wong, Tan, Jing, Zhou, Song (bb0635) 2010; 16 Hansen, Leslie, Swamy-Mruthinti (bb0155) 2014; 450 Fu, Liang (bb0195) 2001; 7 Delbecq, Jehle, Klevit (bb0670) 2012; 31 Liu, Anbarasu, Liang (bb0085) 2007; 13 Rane, Pan, Singh, Powell, Wu, Cummins, Chen, McLeish, Klein (bb0485) 2003; 278 Augusteyn (bb0005) 2010; 90 Heise, Fort (bb0030) 2011; 4 Klemenz, Frohli, Aoyama, Hoffmann, Simpson, Moritz, Schafer (bb0475) 1991; 11 Liu, Liang (bb0305) 2006; 281 Deng, Li, Fan, Yuan, Xie, Mo, Yan, Zhou, Wang, Ye, Wan, Wu (bb0040) 2010; 43 Ecroyd, Carver (bb0335) 2009; 66 Valapala, Edwards, Hose, Hu, Wawrousek, Lutty, Zigler, Qian, Sinha (bb0150) 2015; 5 Carver, Aquilina, Truscott (bb0050) 1993; 1164 Fan, Huang, Zhu, Zhang, Ye, Luo, Sun, Zhou, Lu (bb0060) 2014; 20 Ramkumar, Fujii, Sakaue, Fujii, Thankappan, Kumari, Natarajaseenivasan, Anbarasu (bb0080) 2015 Raman, Ban, Sakai, Pasta, Ramakrishna, Naiki, Goto, Rao Ch (bb0390) 2005; 392 Raju, Abraham (bb0460) 2013; 430 Rao, Saraswathy, Wu, Katselis, Wawrousek, Bhat (bb0035) 2008; 49 Raju, Abraham (bb0090) 2011; 6 Gupta, Srivastava (bb0605) 2004; 45 Vasavada, Ganguly, Germino, Wang, Weissman (bb0275) 1991; 88 Raju, Santhoshkumar, Sharma (bb0585) 2012; 7 Kumarasamy, Abraham (bb0095) 2008; 3 Murugesan, Santhoshkumar, Sharma (bb0190) 2007; 13 Kong, King (bb0655) 2011; 20 Graw (bb0110) 2009; 88 Cooper, Carver, Truscott (bb0645) 1993; 213 Rao, Srinivas, Sujini, Kumar (bb0210) 2014; 2014 McGreal, Kantorow, Chauss, Wei, Brennan, Kantorow (bb0515) 2012; 1820 Mehlen, Preville, Chareyron, Briolay, Klemenz, Arrigo (bb0540) 1995; 154 Fan, Dong, Mishra, Chen, FitzGerald, Wistow (bb0120) 2012; 279 Biswas, Das (bb0220) 2004; 279 Wilhelmus, Boelens, Otte-Holler, Kamps, de Waal, Verbeek (bb0355) 2006; 1089 Kamradt, Chen, Cryns (bb0525) 2001; 276 Hooi, Raftery, Truscott (bb0660) 2012; 21 Chen, Callis, King (bb0115) 2009; 48 Liu, Liang (bb0310) 2008; 104 Kallur, Aziz, Abraham (bb0560) 2008; 308 Bhattacharyya, Padmanabha Udupa, Wang, Sharma (bb0615) 2006; 45 Koteiche, McHaourab (bb0145) 2006; 281 Das, Kang, Temple, Belfort (bb0330) 2014; 9 Srinivas, Patil, Reddy (bb0590) 2011; 405 Sreelakshmi, Sharma (bb0235) 2006; 12 Waudby, Knowles, Devlin, Skepper, Ecroyd, Carver, Welland, Christodoulou, Dobson, Meehan (bb0425) 2010; 98 Braak, Muller, Rub, Ackermann, Bratzke, de Vos, Del Tredici (bb0405) 2006 Sreelakshmi, Santhoshkumar, Bhattacharyya, Sharma (bb0575) 2004; 43 Hilton, Hochberg, Laganowsky, McGinnigle, Baldwin, Benesch (bb0680) 2013; 368 Li, Liu, Mao, Xiang, Wang, Ma, Dong, Pike, Brown, Reed (bb0045) 2005; 16 Sreelakshmi, Sharma (bb0665) 2005; 44 Liao, Lee, Wu, Chiou (bb0130) 2009; 15 Pereira, Santos, Goncalves, Cardoso, Consonni, Gozzo, Oliveira, Pereira, Figueiredo, Tiroli-Cepeda, Ramos, de Thomaz, Cesar, Franchini (bb0445) 2014; 5 Binger, Ecroyd, Yang, Carver, Howlett, Griffin (bb0340) 2013; 27 Morozov, Wawrousek (bb0550) 2006; 133 Wilmarth, Tanner, Dasari, Nagalla, Riviere, Bafna, Pevzner, David (bb0065) 2006; 5 Shammas, Waudby, Wang, Buell, Knowles, Ecroyd, Welland, Carver, Dobson, Meehan (bb0375) 2011; 101 Kore, Abraham (bb0490) 2014; 453 Goldstein, Muffat, Cherny, Moir, Ericsson, Huang, Mavros, Coccia, Faget, Fitch, Masters, Tanzi, Chylack, Bush (bb0370) 2003; 361 Xu, Bai, Huang, Zhou, Yu, Zhao (bb0020) 2015; 56 Fearon, Finkel, Gillison, Kennedy, Casella, Tomaselli, Morrow, Van Dang (bb0280) 1992; 89 Boyle, Takemoto, Brady, Wawrousek (bb0175) 2003; 3 Gupta, Srivastava (bb0205) 2009; 284 Carver, Aquilina, Cooper, Williams, Truscott (bb0215) 1994; 1204 Papuc, Kurys-Denis, Krupski, Rejdak (bb0435) 2015; 10 Devi, Yao, Vijayalakshmi, Sergeev, Sundaresan, Hejtmancik (bb0180) 2008; 14 Yang, Sinai, Kitts, Kain (bb0290) 1997; 23 Luo, Batalao, Zhou, Zhu (bb0285) 1997; 22 Minton, Wilf (bb0315) 1981; 20 Hayes, Devlin, Quinlan (bb0600) 2008; 283 Takata, Woodbury, Lampi (bb0625) 2009; 15 Song, Hanson, Liu, Chylack, Liang (bb0075) 2008; 14 Ghosh, Shenoy, Clark (bb0620) 2006; 45 Selkoe (bb0360) 2001; 3 Slingsby, Wistow (bb0325) 2014; 115 Bosman, Yehiely, Evans, Cryns (bb0470) 2010; 119 Liu, Song, Hanson, Liang (bb0270) 2008; 87 Reddy, Kumar, Kumar (bb0570) 2006; 58 Romi, Helgeland, Gilhus (bb0135) 2011; 66 Narayanan, Kamps, Boelens, Reif (bb0395) 2006; 580 Mao, Liu, Xiang, Li (bb0545) 2004; 11 Zigler, Sinha (bb0105) 2015; 44 Fu, Liang (bb0300) 2002; 139 Peschek, Braun, Rohrberg, Back, Kriehuber, Kastenmuller, Weinkauf, Buchner (bb0505) 2013; 110 Anbarasu, Ramkumar, Bency (bb0185) 2013; 25 LeVine (bb0385) 1993; 2 Liang (bb0245) 2000; 484 Chung (bb0400) 2015; 1292 Raju, Oonthonpan, Abraham (bb0170) 2012; 7 Lowe, McDermott, Pike, Spendlove, Landon, Mayer (bb0345) 1992; 166 Nalls, Plagnol, Hernandez, Sharma, Sheerin, Saad, Simon-Sanchez, Schulte, Lesage, Sveinbjornsdottir, Stefansson, Martinez, Hardy, Heutink, Brice, Gasser, Singleton, Wood (bb0420) 2011; 377 Kannan, Santhoshkumar, Mooney, Sharma (bb0260) 2013; 8 Nakamura, Sakai, Sadakane, Haga, Goto, Kinouchi, Saito, Fujii (bb0595) 2008; 1784 Fu, Liang (bb0200) 2003; 44 Ahmad, Raman, Ramakrishna, Rao (bb0565) 2008; 375 Lampi, Wilmarth, Murray, David (bb0100) 2014; 115 Bova, Yaron, Huang, Ding, Haley, Stewart, Horwitz (bb0450) 1999; 96 Fort, Lampi (bb0025) 2011; 92 Braak, Del Tredici, Sandmann-Kiel, Rub, Schultz (bb0430) 2001; 102 Moore, West, Dawson, Dawson (bb0410) 2005; 28 Pasta, Raman, Ramakrishna, Rao (bb0675) 2004; 10 Xie, Jin, Li, Luo, Zhu, Ma, Shi (bb0440) 2013; 125 Asomugha, Gupta, Srivastava (bb0610) 2011; 17 Horwitz (bb0055) 1992; 89 Rajasekaran, Connell, Christians, Yan, Taylor, Orosz, Zhang, Stevenson, Peshock, Leopold, Barry, Loscalzo, Odelberg, Benjamin (bb0455) 2007; 130 Malin, Strekalova, Petrovic, Rajanala, Sharma, Ugolkov, Gradishar, Cryns (bb0520) 2015 Lampi, Amyx, Ahmann, Steel (bb0640) 2006; 45 Wang, Spector (bb0580) 1994; 269 Liu, Liang (bb0265) 2005; 11 Liu, Liang (bb0295) 2007; 581 Fu, Liang (bb0230) 2002; 277 Arrigo, Simon, Gibert, Kretz-Remy, Nivon, Czekalla, Guillet, Moulin, Diaz-Latoud, Vicart (bb0480) 2007; 581 Braun, Zacharias, Peschek, Kastenmuller, Zou, Hanzlik, Haslbeck, Rappsilber, Buchner, Weinkauf (bb0125) 2011; 108 Takemoto, Sorensen (bb0160) 2008; 87 Stege (10.1016/j.bbagen.2015.09.005_bb0380) 1999; 262 Fearon (10.1016/j.bbagen.2015.09.005_bb0280) 1992; 89 McGreal (10.1016/j.bbagen.2015.09.005_bb0515) 2012; 1820 Chen (10.1016/j.bbagen.2015.09.005_bb0115) 2009; 48 Liu (10.1016/j.bbagen.2015.09.005_bb0305) 2006; 281 Fu (10.1016/j.bbagen.2015.09.005_bb0230) 2002; 277 Devi (10.1016/j.bbagen.2015.09.005_bb0180) 2008; 14 Ramkumar (10.1016/j.bbagen.2015.09.005_bb0080) 2015 Liu (10.1016/j.bbagen.2015.09.005_bb0085) 2007; 13 Deng (10.1016/j.bbagen.2015.09.005_bb0040) 2010; 43 Raman (10.1016/j.bbagen.2015.09.005_bb0390) 2005; 392 Fort (10.1016/j.bbagen.2015.09.005_bb0025) 2011; 92 Rao (10.1016/j.bbagen.2015.09.005_bb0035) 2008; 49 Carver (10.1016/j.bbagen.2015.09.005_bb0050) 1993; 1164 Hooi (10.1016/j.bbagen.2015.09.005_bb0660) 2012; 21 Srinivas (10.1016/j.bbagen.2015.09.005_bb0590) 2011; 405 Asomugha (10.1016/j.bbagen.2015.09.005_bb0610) 2011; 17 Carver (10.1016/j.bbagen.2015.09.005_bb0215) 1994; 1204 Lowe (10.1016/j.bbagen.2015.09.005_bb0345) 1992; 166 Heise (10.1016/j.bbagen.2015.09.005_bb0030) 2011; 4 Takemoto (10.1016/j.bbagen.2015.09.005_bb0160) 2008; 87 Ramkumar (10.1016/j.bbagen.2015.09.005_bb0165) 2015; 76 Minton (10.1016/j.bbagen.2015.09.005_bb0315) 1981; 20 Braak (10.1016/j.bbagen.2015.09.005_bb0430) 2001; 102 Fu (10.1016/j.bbagen.2015.09.005_bb0195) 2001; 7 Waudby (10.1016/j.bbagen.2015.09.005_bb0425) 2010; 98 Wistow (10.1016/j.bbagen.2015.09.005_bb0010) 1988; 57 Narayanan (10.1016/j.bbagen.2015.09.005_bb0395) 2006; 580 Moore (10.1016/j.bbagen.2015.09.005_bb0410) 2005; 28 Dasgupta (10.1016/j.bbagen.2015.09.005_bb0530) 1992; 54 Anbarasu (10.1016/j.bbagen.2015.09.005_bb0185) 2013; 25 Chung (10.1016/j.bbagen.2015.09.005_bb0400) 2015; 1292 Ramkumar (10.1016/j.bbagen.2015.09.005_bb0015) 2014 Delbecq (10.1016/j.bbagen.2015.09.005_bb0670) 2012; 31 Mehlen (10.1016/j.bbagen.2015.09.005_bb0540) 1995; 154 Horwitz (10.1016/j.bbagen.2015.09.005_bb0055) 1992; 89 Gupta (10.1016/j.bbagen.2015.09.005_bb0205) 2009; 284 Li (10.1016/j.bbagen.2015.09.005_bb0045) 2005; 16 Zigler (10.1016/j.bbagen.2015.09.005_bb0105) 2015; 44 Kannan (10.1016/j.bbagen.2015.09.005_bb0260) 2013; 8 Wang (10.1016/j.bbagen.2015.09.005_bb0580) 1994; 269 Raju (10.1016/j.bbagen.2015.09.005_bb0585) 2012; 7 Das (10.1016/j.bbagen.2015.09.005_bb0330) 2014; 9 Malin (10.1016/j.bbagen.2015.09.005_bb0520) 2015 Liao (10.1016/j.bbagen.2015.09.005_bb0130) 2009; 15 Nalls (10.1016/j.bbagen.2015.09.005_bb0420) 2011; 377 Moreau (10.1016/j.bbagen.2015.09.005_bb0650) 2012; 7 Vasavada (10.1016/j.bbagen.2015.09.005_bb0275) 1991; 88 Raju (10.1016/j.bbagen.2015.09.005_bb0460) 2013; 430 Hu (10.1016/j.bbagen.2015.09.005_bb0510) 2012; 12 Ghosh (10.1016/j.bbagen.2015.09.005_bb0620) 2006; 45 Boyle (10.1016/j.bbagen.2015.09.005_bb0175) 2003; 3 Pasta (10.1016/j.bbagen.2015.09.005_bb0675) 2004; 10 Valapala (10.1016/j.bbagen.2015.09.005_bb0150) 2015; 5 Peschek (10.1016/j.bbagen.2015.09.005_bb0505) 2013; 110 Nakamura (10.1016/j.bbagen.2015.09.005_bb0595) 2008; 1784 Liu (10.1016/j.bbagen.2015.09.005_bb0265) 2005; 11 Shammas (10.1016/j.bbagen.2015.09.005_bb0375) 2011; 101 Raju (10.1016/j.bbagen.2015.09.005_bb0090) 2011; 6 Fujii (10.1016/j.bbagen.2015.09.005_bb0070) 2012; 287 Clark (10.1016/j.bbagen.2015.09.005_bb0350) 2000; 59 Bhattacharyya (10.1016/j.bbagen.2015.09.005_bb0615) 2006; 45 Liang (10.1016/j.bbagen.2015.09.005_bb0255) 2004; 13 Sreelakshmi (10.1016/j.bbagen.2015.09.005_bb0575) 2004; 43 Lampi (10.1016/j.bbagen.2015.09.005_bb0100) 2014; 115 Aoyama (10.1016/j.bbagen.2015.09.005_bb0535) 1993; 55 Takata (10.1016/j.bbagen.2015.09.005_bb0630) 2008; 17 Rao (10.1016/j.bbagen.2015.09.005_bb0210) 2014; 2014 Fan (10.1016/j.bbagen.2015.09.005_bb0060) 2014; 20 Mao (10.1016/j.bbagen.2015.09.005_bb0545) 2004; 11 Murugesan (10.1016/j.bbagen.2015.09.005_bb0250) 2008; 14 Selkoe (10.1016/j.bbagen.2015.09.005_bb0360) 2001; 3 Binger (10.1016/j.bbagen.2015.09.005_bb0340) 2013; 27 Liang (10.1016/j.bbagen.2015.09.005_bb0245) 2000; 484 Liu (10.1016/j.bbagen.2015.09.005_bb0295) 2007; 581 Raju (10.1016/j.bbagen.2015.09.005_bb0170) 2012; 7 Braak (10.1016/j.bbagen.2015.09.005_bb0405) 2006 Sharma (10.1016/j.bbagen.2015.09.005_bb0555) 2000; 275 Fan (10.1016/j.bbagen.2015.09.005_bb0120) 2012; 279 Biswas (10.1016/j.bbagen.2015.09.005_bb0220) 2004; 279 Slingsby (10.1016/j.bbagen.2015.09.005_bb0325) 2014; 115 Cooper (10.1016/j.bbagen.2015.09.005_bb0645) 1993; 213 Kumarasamy (10.1016/j.bbagen.2015.09.005_bb0095) 2008; 3 Kamradt (10.1016/j.bbagen.2015.09.005_bb0525) 2001; 276 Wilhelmus (10.1016/j.bbagen.2015.09.005_bb0355) 2006; 1089 Arrigo (10.1016/j.bbagen.2015.09.005_bb0480) 2007; 581 Hansen (10.1016/j.bbagen.2015.09.005_bb0155) 2014; 450 Romi (10.1016/j.bbagen.2015.09.005_bb0135) 2011; 66 Xie (10.1016/j.bbagen.2015.09.005_bb0440) 2013; 125 Song (10.1016/j.bbagen.2015.09.005_bb0075) 2008; 14 Bosman (10.1016/j.bbagen.2015.09.005_bb0470) 2010; 119 Goldstein (10.1016/j.bbagen.2015.09.005_bb0370) 2003; 361 Papuc (10.1016/j.bbagen.2015.09.005_bb0435) 2015; 10 Rajasekaran (10.1016/j.bbagen.2015.09.005_bb0455) 2007; 130 Fu (10.1016/j.bbagen.2015.09.005_bb0200) 2003; 44 Takata (10.1016/j.bbagen.2015.09.005_bb0625) 2009; 15 Rekas (10.1016/j.bbagen.2015.09.005_bb0415) 2004; 340 Kore (10.1016/j.bbagen.2015.09.005_bb0490) 2014; 453 Gupta (10.1016/j.bbagen.2015.09.005_bb0605) 2004; 45 Lampi (10.1016/j.bbagen.2015.09.005_bb0640) 2006; 45 Fu (10.1016/j.bbagen.2015.09.005_bb0300) 2002; 139 Banerjee (10.1016/j.bbagen.2015.09.005_bb0225) 2014; 30 Murphy (10.1016/j.bbagen.2015.09.005_bb0365) 2010; 19 Bakthisaran (10.1016/j.bbagen.2015.09.005_bb0500) 2015; 1854 Ahmad (10.1016/j.bbagen.2015.09.005_bb0565) 2008; 375 Yang (10.1016/j.bbagen.2015.09.005_bb0290) 1997; 23 Xu (10.1016/j.bbagen.2015.09.005_bb0635) 2010; 16 Augusteyn (10.1016/j.bbagen.2015.09.005_bb0005) 2010; 90 Liu (10.1016/j.bbagen.2015.09.005_bb0270) 2008; 87 Reddy (10.1016/j.bbagen.2015.09.005_bb0570) 2006; 58 Kong (10.1016/j.bbagen.2015.09.005_bb0655) 2011; 20 Murugesan (10.1016/j.bbagen.2015.09.005_bb0190) 2007; 13 Klemenz (10.1016/j.bbagen.2015.09.005_bb0475) 1991; 11 Xu (10.1016/j.bbagen.2015.09.005_bb0020) 2015; 56 Wilmarth (10.1016/j.bbagen.2015.09.005_bb0065) 2006; 5 Ghosh (10.1016/j.bbagen.2015.09.005_bb0495) 2007; 46 Arrigo (10.1016/j.bbagen.2015.09.005_bb0465) 2014; 6 Braun (10.1016/j.bbagen.2015.09.005_bb0125) 2011; 108 LeVine (10.1016/j.bbagen.2015.09.005_bb0385) 1993; 2 Liu (10.1016/j.bbagen.2015.09.005_bb0310) 2008; 104 Koteiche (10.1016/j.bbagen.2015.09.005_bb0145) 2006; 281 Rane (10.1016/j.bbagen.2015.09.005_bb0485) 2003; 278 Ramkumar (10.1016/j.bbagen.2015.09.005_bb0140) 2014; 20 Sreelakshmi (10.1016/j.bbagen.2015.09.005_bb0665) 2005; 44 Hilton (10.1016/j.bbagen.2015.09.005_bb0680) 2013; 368 Ecroyd (10.1016/j.bbagen.2015.09.005_bb0335) 2009; 66 Boelens (10.1016/j.bbagen.2015.09.005_bb0320) 2014; 115 Hayes (10.1016/j.bbagen.2015.09.005_bb0600) 2008; 283 Morozov (10.1016/j.bbagen.2015.09.005_bb0550) 2006; 133 Luo (10.1016/j.bbagen.2015.09.005_bb0285) 1997; 22 Wu (10.1016/j.bbagen.2015.09.005_bb0240) 2012; 53 Pereira (10.1016/j.bbagen.2015.09.005_bb0445) 2014; 5 Sreelakshmi (10.1016/j.bbagen.2015.09.005_bb0235) 2006; 12 Graw (10.1016/j.bbagen.2015.09.005_bb0110) 2009; 88 Kallur (10.1016/j.bbagen.2015.09.005_bb0560) 2008; 308 Bova (10.1016/j.bbagen.2015.09.005_bb0450) 1999; 96 |
| References_xml | – volume: 213 start-page: 321 year: 1993 end-page: 328 ident: bb0645 article-title: 1H-NMR spectroscopy of bovine lens beta-crystallin. The role of the beta B2-crystallin C-terminal extension in aggregation publication-title: Eur. J. Biochem. – volume: 1089 start-page: 67 year: 2006 end-page: 78 ident: bb0355 article-title: Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity publication-title: Brain Res. – volume: 12 start-page: 581 year: 2006 end-page: 587 ident: bb0235 article-title: The interaction between alphaA- and alphaB-crystallin is sequence-specific publication-title: Mol. Vis. – volume: 1204 start-page: 195 year: 1994 end-page: 206 ident: bb0215 article-title: Alpha-crystallin: molecular chaperone and protein surfactant publication-title: Biochim. Biophys. Acta – volume: 7 year: 2012 ident: bb0650 article-title: Cataract-causing defect of a mutant gamma-crystallin proceeds through an aggregation pathway which bypasses recognition by the alpha-crystallin chaperone publication-title: PLoS One – volume: 377 start-page: 641 year: 2011 end-page: 649 ident: bb0420 article-title: Imputation of sequence variants for identification of genetic risks for Parkinson's disease: a meta-analysis of genome-wide association studies publication-title: Lancet – volume: 46 start-page: 6308 year: 2007 end-page: 6317 ident: bb0495 article-title: Interactions between important regulatory proteins and human alphaB crystallin publication-title: Biochemistry – year: 2015 ident: bb0520 article-title: ERK-regulated alphaB-crystallin induction by matrix detachment inhibits anoikis and promotes lung metastasis in vivo publication-title: Oncogene – volume: 110 start-page: E3780 year: 2013 end-page: E3789 ident: bb0505 article-title: Regulated structural transitions unleash the chaperone activity of alphaB-crystallin publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 14 start-page: 1282 year: 2008 end-page: 1287 ident: bb0075 article-title: Protein–protein interactions between lens vimentin and alphaB-crystallin using FRET acceptor photobleaching publication-title: Mol. Vis. – volume: 88 start-page: 10686 year: 1991 end-page: 10690 ident: bb0275 article-title: A contingent replication assay for the detection of protein–protein interactions in animal cells publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 125 start-page: 60 year: 2013 end-page: 68 ident: bb0440 article-title: Modulating autophagy improves cardiac function in a rat model of early-stage dilated cardiomyopathy publication-title: Cardiology – volume: 115 start-page: 21 year: 2014 end-page: 31 ident: bb0100 article-title: Lens beta-crystallins: the role of deamidation and related modifications in aging and cataract publication-title: Prog. Biophys. Mol. Biol. – volume: 108 start-page: 20491 year: 2011 end-page: 20496 ident: bb0125 article-title: Multiple molecular architectures of the eye lens chaperone alphaB-crystallin elucidated by a triple hybrid approach publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 375 start-page: 1040 year: 2008 end-page: 1051 ident: bb0565 article-title: Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant publication-title: J. Mol. Biol. – volume: 6 year: 2011 ident: bb0090 article-title: Congenital cataract causing mutants of alphaA-crystallin/sHSP form aggregates and aggresomes degraded through ubiquitin-proteasome pathway publication-title: PLoS One – volume: 1820 start-page: 921 year: 2012 end-page: 930 ident: bb0515 article-title: AlphaB-crystallin/sHSP protects cytochrome c and mitochondrial function against oxidative stress in lens and retinal cells publication-title: Biochim. Biophys. Acta – volume: 15 start-page: 1429 year: 2009 end-page: 1444 ident: bb0130 article-title: COOH-terminal truncations and site-directed mutations enhance thermostability and chaperone-like activity of porcine αB-crystallin publication-title: Mol. Vis. – volume: 281 start-page: 14273 year: 2006 end-page: 14279 ident: bb0145 article-title: Mechanism of a hereditary cataract phenotype. Mutations in alphaA-crystallin activate substrate binding publication-title: J. Biol. Chem. – volume: 1292 start-page: 195 year: 2015 end-page: 201 ident: bb0400 article-title: Studying nitrosative stress in Parkinson's disease publication-title: Methods Mol. Biol. – volume: 87 start-page: 496 year: 2008 end-page: 501 ident: bb0160 article-title: Protein–protein interactions and lens transparency publication-title: Exp. Eye Res. – volume: 166 start-page: 61 year: 1992 end-page: 68 ident: bb0345 article-title: Alpha B crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease publication-title: J. Pathol. – volume: 13 start-page: 854 year: 2007 end-page: 861 ident: bb0085 article-title: Confocal fluorescence resonance energy transfer microscopy study of protein–protein interactions of lens crystallins in living cells publication-title: Mol. Vis. – volume: 66 start-page: 62 year: 2009 end-page: 81 ident: bb0335 article-title: Crystallin proteins and amyloid fibrils publication-title: Cell. Mol. Life Sci. – volume: 139 start-page: 191 year: 2002 end-page: 198 ident: bb0300 article-title: Unfolding of human lens recombinant betaB2- and gammaC-crystallins publication-title: J. Struct. Biol. – volume: 115 start-page: 52 year: 2014 end-page: 67 ident: bb0325 article-title: Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells publication-title: Prog. Biophys. Mol. Biol. – volume: 2014 start-page: 147648 year: 2014 ident: bb0210 article-title: Protein–protein interaction detection: methods and analysis publication-title: Int. J. Proteomics – volume: 1784 start-page: 1192 year: 2008 end-page: 1199 ident: bb0595 article-title: Differential rate constants of racemization of aspartyl and asparaginyl residues in human alpha A-crystallin mutants publication-title: Biochim. Biophys. Acta – volume: 22 start-page: 350 year: 1997 end-page: 352 ident: bb0285 article-title: Mammalian two-hybrid system: a complementary approach to the yeast two-hybrid system publication-title: Biotechniques – volume: 43 start-page: 432 year: 2010 end-page: 437 ident: bb0040 article-title: Synergistic efficacy of LBH and alphaB-crystallin through inhibiting transcriptional activities of p53 and p21 publication-title: BMB Rep. – volume: 20 start-page: 1002 year: 2014 end-page: 1016 ident: bb0140 article-title: Comparison of effect of gamma ray irradiation on wild-type and N-terminal mutants of alphaA-crystallin publication-title: Mol. Vis. – start-page: 89 year: 2006 end-page: 97 ident: bb0405 article-title: Pathology associated with sporadic Parkinson's disease—where does it end? publication-title: J. Neural Transm. Suppl. – volume: 45 start-page: 13847 year: 2006 end-page: 13854 ident: bb0620 article-title: N- and C-terminal motifs in human alphaB crystallin play an important role in the recognition, selection, and solubilization of substrates publication-title: Biochemistry – volume: 17 start-page: 1565 year: 2008 end-page: 1575 ident: bb0630 article-title: Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin publication-title: Protein Sci. – volume: 154 start-page: 363 year: 1995 end-page: 374 ident: bb0540 article-title: Constitutive expression of human hsp27, drosophila hsp27, or human alpha B-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts publication-title: J. Immunol. – volume: 11 start-page: 321 year: 2005 end-page: 327 ident: bb0265 article-title: Interaction and biophysical properties of human lens Q155* betaB2-crystallin mutant publication-title: Mol. Vis. – volume: 361 start-page: 1258 year: 2003 end-page: 1265 ident: bb0370 article-title: Cytosolic beta-amyloid deposition and supranuclear cataracts in lenses from people with Alzheimer's disease publication-title: Lancet – volume: 23 start-page: 1110 year: 1997 end-page: 1114 ident: bb0290 article-title: Quantification of gene expression with a secreted alkaline phosphatase reporter system publication-title: Biotechniques – volume: 13 start-page: 2301 year: 2007 end-page: 2309 ident: bb0190 article-title: Cataract-causing alphaAG98R mutant shows substrate-dependent chaperone activity publication-title: Mol. Vis. – volume: 277 start-page: 4255 year: 2002 end-page: 4260 ident: bb0230 article-title: Detection of protein–protein interactions among lens crystallins in a mammalian two-hybrid system assay publication-title: J. Biol. Chem. – volume: 130 start-page: 427 year: 2007 end-page: 439 ident: bb0455 article-title: Human alpha B-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice publication-title: Cell – volume: 44 start-page: 1155 year: 2003 end-page: 1159 ident: bb0200 article-title: Alteration of protein–protein interactions of congenital cataract crystallin mutants publication-title: Invest. Ophthalmol. Vis. Sci. – volume: 581 start-page: 3936 year: 2007 end-page: 3942 ident: bb0295 article-title: Protein–protein interactions among human lens acidic and basic β-crystallins publication-title: FEBS Lett. – volume: 43 start-page: 15785 year: 2004 end-page: 15795 ident: bb0575 article-title: AlphaA-crystallin interacting regions in the small heat shock protein, alphaB-crystallin publication-title: Biochemistry – volume: 484 start-page: 98 year: 2000 end-page: 101 ident: bb0245 article-title: Interaction between beta-amyloid and lens alphaB-crystallin publication-title: FEBS Lett. – volume: 59 start-page: 265 year: 2000 end-page: 270 ident: bb0350 article-title: Spinocerebellar ataxia type 1—modeling the pathogenesis of a polyglutamine neurodegenerative disorder in transgenic mice publication-title: J. Neuropathol. Exp. Neurol. – volume: 262 start-page: 152 year: 1999 end-page: 156 ident: bb0380 article-title: The molecular chaperone alphaB-crystallin enhances amyloid beta neurotoxicity publication-title: Biochem. Biophys. Res. Commun. – volume: 102 start-page: 449 year: 2001 end-page: 454 ident: bb0430 article-title: Nerve cells expressing heat-shock proteins in Parkinson's disease publication-title: Acta Neuropathol. – volume: 49 start-page: 1161 year: 2008 end-page: 1171 ident: bb0035 article-title: Elevated retina-specific expression of the small heat shock protein, alphaA-crystallin, is associated with photoreceptor protection in experimental uveitis publication-title: Invest. Ophthalmol. Vis. Sci. – volume: 44 start-page: 62 year: 2015 end-page: 85 ident: bb0105 article-title: betaA3/A1-crystallin: more than a lens protein publication-title: Prog. Retin. Eye Res. – volume: 8 year: 2013 ident: bb0260 article-title: Identification of subunit-subunit interaction sites in alphaA-WT crystallin and mutant alphaA-G98R crystallin using isotope-labeled cross-linker and mass spectrometry publication-title: PLoS One – volume: 55 start-page: 760 year: 1993 end-page: 764 ident: bb0535 article-title: Expression of alpha B-crystallin in human brain tumors publication-title: Int. J. Cancer – volume: 28 start-page: 57 year: 2005 end-page: 87 ident: bb0410 article-title: Molecular pathophysiology of Parkinson's disease publication-title: Annu. Rev. Neurosci. – volume: 276 start-page: 16059 year: 2001 end-page: 16063 ident: bb0525 article-title: The small heat shock protein alpha B-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation publication-title: J. Biol. Chem. – volume: 98 start-page: 843 year: 2010 end-page: 851 ident: bb0425 article-title: The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation publication-title: Biophys. J. – volume: 7 year: 2012 ident: bb0170 article-title: Mutations in human alphaA-crystallin/sHSP affect subunit exchange interaction with alphaB-crystallin publication-title: PLoS One – volume: 92 start-page: 98 year: 2011 end-page: 103 ident: bb0025 article-title: New focus on alpha-crystallins in retinal neurodegenerative diseases publication-title: Exp. Eye Res. – volume: 13 start-page: 2476 year: 2004 end-page: 2482 ident: bb0255 article-title: Interactions and chaperone function of alphaA-crystallin with T5P gammaC-crystallin mutant publication-title: Protein Sci. – volume: 89 start-page: 7958 year: 1992 end-page: 7962 ident: bb0280 article-title: Karyoplasmic interaction selection strategy: a general strategy to detect protein–protein interactions in mammalian cells publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 76 start-page: 102 year: 2015 end-page: 108 ident: bb0165 article-title: Interaction of alphaA-crystallin F71L mutant with wild type alphaA- and alphaB-crystallins by mammalian two hybrid assay publication-title: Int. J. Biol. Macromol. – volume: 278 start-page: 27828 year: 2003 end-page: 27835 ident: bb0485 article-title: Heat shock protein 27 controls apoptosis by regulating Akt activation publication-title: J. Biol. Chem. – volume: 4 start-page: 62 year: 2011 end-page: 69 ident: bb0030 article-title: Impact of diabetes on alpha-crystallins and other heat shock proteins in the eye publication-title: J. Ocul. Biol. Dis. Inform. – volume: 48 start-page: 3708 year: 2009 end-page: 3716 ident: bb0115 article-title: Mechanism of the very efficient quenching of tryptophan fluorescence in human gamma D- and gamma S-crystallins: the gamma-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage publication-title: Biochemistry – volume: 66 start-page: 65 year: 2011 end-page: 69 ident: bb0135 article-title: Heat-shock proteins in clinical neurology publication-title: Eur. Neurol. – volume: 14 start-page: 1835 year: 2008 end-page: 1844 ident: bb0250 article-title: Role of alphaBI5 and alphaBT162 residues in subunit interaction during oligomerization of alphaB-crystallin publication-title: Mol. Vis. – volume: 53 start-page: 2541 year: 2012 end-page: 2550 ident: bb0240 article-title: Oligomerization with wt alphaA- and alphaB-crystallins reduces proteasome-mediated degradation of C-terminally truncated alphaA-crystallin publication-title: Invest. Ophthalmol. Vis. Sci. – volume: 115 start-page: 3 year: 2014 end-page: 10 ident: bb0320 article-title: Cell biological roles of alphaB-crystallin publication-title: Prog. Biophys. Mol. Biol. – volume: 101 start-page: 1681 year: 2011 end-page: 1689 ident: bb0375 article-title: Binding of the molecular chaperone alphaB-crystallin to Abeta amyloid fibrils inhibits fibril elongation publication-title: Biophys. J. – volume: 57 start-page: 479 year: 1988 end-page: 504 ident: bb0010 article-title: Lens crystallins: the evolution and expression of proteins for a highly specialized tissue publication-title: Annu. Rev. Biochem. – volume: 30 start-page: 4775 year: 2014 end-page: 4783 ident: bb0225 article-title: Structure and functional properties of a multimeric protein alphaA-crystallin adsorbed on silver nanoparticle surface publication-title: Langmuir – volume: 20 start-page: 4821 year: 1981 end-page: 4826 ident: bb0315 article-title: Effect of macromolecular crowding upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase publication-title: Biochemistry – volume: 581 start-page: 3665 year: 2007 end-page: 3674 ident: bb0480 article-title: Hsp27 (HspB1) and alphaB-crystallin (HspB5) as therapeutic targets publication-title: FEBS Lett. – volume: 45 start-page: 3069 year: 2006 end-page: 3076 ident: bb0615 article-title: Mini-alphaB-crystallin: a functional element of alphaB-crystallin with chaperone-like activity publication-title: Biochemistry – volume: 279 start-page: 2892 year: 2012 end-page: 2904 ident: bb0120 article-title: A role for γS-crystallin in the organization of actin and fiber cell maturation in the mouse lens publication-title: FEBS J. – volume: 287 start-page: 39992 year: 2012 end-page: 40002 ident: bb0070 article-title: A rapid, comprehensive liquid chromatography-mass spectrometry (LC–MS)-based survey of the Asp isomers in crystallins from human cataract lenses publication-title: J, Biol. Chem. – volume: 17 start-page: 2407 year: 2011 end-page: 2420 ident: bb0610 article-title: Structural and functional roles of deamidation of N146 and/or truncation of NH2- or COOH-termini in human alphaB-crystallin publication-title: Mol. Vis. – volume: 15 start-page: 241 year: 2009 end-page: 249 ident: bb0625 article-title: Deamidation alters interactions of beta-crystallins in hetero-oligomers publication-title: Mol. Vis. – volume: 284 start-page: 18481 year: 2009 end-page: 18492 ident: bb0205 article-title: Identification of interaction sites between human betaA3- and alphaA/alphaB-crystallins by mammalian two-hybrid and fluorescence resonance energy transfer acceptor photobleaching methods publication-title: J. Biol. Chem. – volume: 450 start-page: 1668 year: 2014 end-page: 1672 ident: bb0155 article-title: The kinetics of thermal stress induced denaturation of Aquaporin 0 publication-title: Biochem. Biophys. Res. Commun. – volume: 58 start-page: 632 year: 2006 end-page: 641 ident: bb0570 article-title: Chaperone-like activity and hydrophobicity of alpha-crystallin publication-title: IUBMB Life – volume: 5 start-page: 2554 year: 2006 end-page: 2566 ident: bb0065 article-title: Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility? publication-title: J. Proteome Res. – volume: 308 start-page: 85 year: 2008 end-page: 91 ident: bb0560 article-title: C-terminal truncation affects subunit exchange of human alphaA-crystallin with alphaB-crystallin publication-title: Mol. Cell. Biochem. – volume: 133 start-page: 813 year: 2006 end-page: 821 ident: bb0550 article-title: Caspase-dependent secondary lens fiber cell disintegration in alphaA publication-title: Development – volume: 279 start-page: 42648 year: 2004 end-page: 42657 ident: bb0220 article-title: Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function publication-title: J. Biol. Chem. – volume: 119 start-page: 63 year: 2010 end-page: 70 ident: bb0470 article-title: Regulation of alphaB-crystallin gene expression by the transcription factor Ets1 in breast cancer publication-title: Breast Cancer Res. Treat. – volume: 25 start-page: 65 year: 2013 end-page: 74 ident: bb0185 article-title: Towards to clarify the etiology of cataract by crystallin protein–protein interaction studies publication-title: Jpn. Soc. Cataract Refract. Surg. – volume: 7 start-page: 178 year: 2001 end-page: 183 ident: bb0195 article-title: Spectroscopic analysis of lens recombinant betaB2- and gammaC-crystallin publication-title: Mol. Vis. – volume: 20 start-page: 117 year: 2014 end-page: 124 ident: bb0060 article-title: Identification of proteins that interact with alpha A-crystallin using a human proteome microarray publication-title: Mol. Vis. – volume: 27 start-page: 1214 year: 2013 end-page: 1222 ident: bb0340 article-title: Avoiding the oligomeric state: alphaB-crystallin inhibits fragmentation and induces dissociation of apolipoprotein C-II amyloid fibrils publication-title: FASEB J. – volume: 45 start-page: 206 year: 2004 end-page: 214 ident: bb0605 article-title: Effect of deamidation of asparagine 146 on functional and structural properties of human lens alphaB-crystallin publication-title: Invest. Ophthalmol. Vis. Sci. – volume: 405 start-page: 486 year: 2011 end-page: 490 ident: bb0590 article-title: Temperature-dependent coaggregation of eye lens alphaB- and beta-crystallins publication-title: Biochem. Biophys. Res. Commun. – volume: 3 start-page: 3 year: 2003 ident: bb0175 article-title: Morphological characterization of the Alpha A- and Alpha B-crystallin double knockout mouse lens publication-title: BMC Ophthalmol. – volume: 11 start-page: 803 year: 1991 end-page: 812 ident: bb0475 article-title: Alpha B crystallin accumulation is a specific response to Ha-ras and v-mos oncogene expression in mouse NIH 3T3 fibroblasts publication-title: Mol. Cell. Biol. – volume: 14 start-page: 1157 year: 2008 end-page: 1170 ident: bb0180 article-title: Crystallin gene mutations in Indian families with inherited pediatric cataract publication-title: Mol. Vis. – volume: 21 start-page: 1074 year: 2012 end-page: 1079 ident: bb0660 article-title: Age-dependent deamidation of glutamine residues in human gammaS crystallin: deamidation and unstructured regions publication-title: Protein Sci. – volume: 10 start-page: 655 year: 2004 end-page: 662 ident: bb0675 article-title: The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies publication-title: Mol. Vis. – volume: 56 start-page: 816 year: 2015 end-page: 826 ident: bb0020 article-title: Knockout of alphaA-crystallin inhibits ocular neovascularization publication-title: Invest. Ophthalmol. Vis. Sci. – volume: 3 year: 2008 ident: bb0095 article-title: Interaction of C-terminal truncated human αA-crystallins with target proteins publication-title: PLoS ONE – start-page: 1 year: 2014 end-page: 112 ident: bb0015 article-title: Protein–protein interaction between recombinant alpha crystallin and its mutants to comprehend the basis towards the progression of cataract publication-title: Department of Marine Biotechnology, vol. PhD, Bharathidasan University, Tiruchirapalli – volume: 96 start-page: 6137 year: 1999 end-page: 6142 ident: bb0450 article-title: Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 11 start-page: 512 year: 2004 end-page: 526 ident: bb0545 article-title: Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis publication-title: Cell Death Differ. – volume: 275 start-page: 3767 year: 2000 end-page: 3771 ident: bb0555 article-title: Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin publication-title: J. Biol. Chem. – volume: 430 start-page: 107 year: 2013 end-page: 112 ident: bb0460 article-title: Mutants of human alphaB-crystallin cause enhanced protein aggregation and apoptosis in mammalian cells: influence of co-expression of HspB1 publication-title: Biochem. Biophys. Res. Commun. – volume: 31 start-page: 4587 year: 2012 end-page: 4594 ident: bb0670 article-title: Binding determinants of the small heat shock protein, alphaB-crystallin: recognition of the ‘IxI’ motif publication-title: EMBO J. – volume: 5 start-page: 8755 year: 2015 ident: bb0150 article-title: betaA3/A1-crystallin is a critical mediator of STAT3 signaling in optic nerve astrocytes publication-title: Sci. Rep. – volume: 2 start-page: 404 year: 1993 end-page: 410 ident: bb0385 article-title: Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution publication-title: Protein Sci. – volume: 269 start-page: 13601 year: 1994 end-page: 13608 ident: bb0580 article-title: The chaperone activity of bovine alpha crystallin. Interaction with other lens crystallins in native and denatured states publication-title: J. Biol. Chem. – volume: 54 start-page: 461 year: 1992 end-page: 470 ident: bb0530 article-title: Hypertonic stress induces alpha B-crystallin expression publication-title: Exp. Eye Res. – year: 2015 ident: bb0080 article-title: Real-time heterogeneous protein-protein interaction between alphaA-crystallin N-terminal mutants and alphaB-crystallin using quartz crystal microbalance (QCM) publication-title: Amino Acids – volume: 88 start-page: 173 year: 2009 end-page: 189 ident: bb0110 article-title: Genetics of crystallins: cataract and beyond publication-title: Exp. Eye Res. – volume: 44 start-page: 12245 year: 2005 end-page: 12252 ident: bb0665 article-title: Recognition sequence 2 (residues 60–71) plays a role in oligomerization and exchange dynamics of alphaB-crystallin publication-title: Biochemistry – volume: 580 start-page: 5941 year: 2006 end-page: 5946 ident: bb0395 article-title: AlphaB-crystallin competes with Alzheimer's disease beta-amyloid peptide for peptide-peptide interactions and induces oxidation of Abeta-Met35 publication-title: FEBS Lett. – volume: 5 start-page: 5159 year: 2014 ident: bb0445 article-title: alphaB-crystallin interacts with and prevents stress-activated proteolysis of focal adhesion kinase by calpain in cardiomyocytes publication-title: Nat. Commun. – volume: 90 start-page: 643 year: 2010 end-page: 654 ident: bb0005 article-title: On the growth and internal structure of the human lens publication-title: Exp. Eye Res. – volume: 6 start-page: 333 year: 2014 end-page: 365 ident: bb0465 article-title: HspB1, HspB5 and HspB4 in human cancers: potent oncogenic role of some of their client proteins publication-title: Cancers – volume: 453 start-page: 326 year: 2014 end-page: 331 ident: bb0490 article-title: Inflammatory cytokines, interleukin-1 beta and tumor necrosis factor-alpha, upregulated in glioblastoma multiforme, raise the levels of CRYAB in exosomes secreted by U373 glioma cells publication-title: Biochem. Biophys. Res. Commun. – volume: 16 start-page: 438 year: 2010 end-page: 444 ident: bb0635 article-title: Decreasing the homodimer interaction: a common mechanism shared by the deltaG91 mutation and deamidation in betaA3-crystallin publication-title: Mol. Vis. – volume: 87 start-page: 515 year: 2008 end-page: 520 ident: bb0270 article-title: Protein–protein interactions involving congenital cataract T5P gammaC-crystallin mutant: a confocal fluorescence microscopy study publication-title: Exp. Eye Res. – volume: 368 start-page: 20110405 year: 2013 ident: bb0680 article-title: C-terminal interactions mediate the quaternary dynamics of alphaB-crystallin publication-title: Philos. Trans. R. Soc. Lond. Ser. B Biol. Sci. – volume: 89 start-page: 10449 year: 1992 end-page: 10453 ident: bb0055 article-title: Alpha-crystallin can function as a molecular chaperone publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 19 start-page: 311 year: 2010 end-page: 323 ident: bb0365 article-title: Alzheimer's disease and the amyloid-beta peptide publication-title: J. Alzheimers Dis. – volume: 12 start-page: 177 year: 2012 end-page: 187 ident: bb0510 article-title: AlphaA- and alphaB-crystallins interact with caspase-3 and Bax to guard mouse lens development publication-title: Curr. Mol. Med. – volume: 20 start-page: 513 year: 2011 end-page: 528 ident: bb0655 article-title: Contributions of aromatic pairs to the folding and stability of long-lived human gammaD-crystallin publication-title: Protein Sci. – volume: 10 year: 2015 ident: bb0435 article-title: Humoral response against small heat shock proteins in Parkinson's disease publication-title: PLoS One – volume: 45 start-page: 3146 year: 2006 end-page: 3153 ident: bb0640 article-title: Deamidation in human lens betaB2-crystallin destabilizes the dimer publication-title: Biochemistry – volume: 1164 start-page: 22 year: 1993 end-page: 28 ident: bb0050 article-title: An investigation into the stability of alpha-crystallin by NMR spectroscopy; evidence for a two-domain structure publication-title: Biochim. Biophys. Acta – volume: 3 start-page: 75 year: 2001 end-page: 80 ident: bb0360 article-title: Alzheimer's disease results from the cerebral accumulation and cytotoxicity of amyloid beta-protein publication-title: J. Alzheimers Dis. – volume: 283 start-page: 10500 year: 2008 end-page: 10512 ident: bb0600 article-title: Truncation of alphaB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells publication-title: J. Biol. Chem. – volume: 7 year: 2012 ident: bb0585 article-title: alphaA-Crystallin-derived mini-chaperone modulates stability and function of cataract causing alphaAG98R-crystallin publication-title: PLoS One – volume: 16 start-page: 4437 year: 2005 end-page: 4453 ident: bb0045 article-title: Calcium-activated RAF/MEK/ERK signaling pathway mediates p53-dependent apoptosis and is abrogated by alpha B-crystallin through inhibition of RAS activation publication-title: Mol. Biol. Cell – volume: 281 start-page: 2624 year: 2006 end-page: 2630 ident: bb0305 article-title: Domain interaction sites of human lens betaB2-crystallin publication-title: J. Biol. Chem. – volume: 104 start-page: 51 year: 2008 end-page: 58 ident: bb0310 article-title: Confocal fluorescence microscopy study of interaction between lens MIP26/AQP0 and crystallins in living cells publication-title: J. Cell. Biochem. – volume: 1854 start-page: 291 year: 2015 end-page: 319 ident: bb0500 article-title: Small heat shock proteins: role in cellular functions and pathology publication-title: Biochim. Biophys. Acta – volume: 9 year: 2014 ident: bb0330 article-title: Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulations publication-title: PLoS One – volume: 392 start-page: 573 year: 2005 end-page: 581 ident: bb0390 article-title: AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin publication-title: Biochem. J. – volume: 340 start-page: 1167 year: 2004 end-page: 1183 ident: bb0415 article-title: Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity publication-title: J. Mol. Biol. – volume: 56 start-page: 816 year: 2015 ident: 10.1016/j.bbagen.2015.09.005_bb0020 article-title: Knockout of alphaA-crystallin inhibits ocular neovascularization publication-title: Invest. Ophthalmol. Vis. Sci. doi: 10.1167/iovs.14-14734 – volume: 87 start-page: 515 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0270 article-title: Protein–protein interactions involving congenital cataract T5P gammaC-crystallin mutant: a confocal fluorescence microscopy study publication-title: Exp. Eye Res. doi: 10.1016/j.exer.2008.08.021 – volume: 2014 start-page: 147648 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0210 article-title: Protein–protein interaction detection: methods and analysis publication-title: Int. J. Proteomics doi: 10.1155/2014/147648 – volume: 287 start-page: 39992 year: 2012 ident: 10.1016/j.bbagen.2015.09.005_bb0070 article-title: A rapid, comprehensive liquid chromatography-mass spectrometry (LC–MS)-based survey of the Asp isomers in crystallins from human cataract lenses publication-title: J, Biol. Chem. doi: 10.1074/jbc.M112.399972 – volume: 119 start-page: 63 year: 2010 ident: 10.1016/j.bbagen.2015.09.005_bb0470 article-title: Regulation of alphaB-crystallin gene expression by the transcription factor Ets1 in breast cancer publication-title: Breast Cancer Res. Treat. doi: 10.1007/s10549-009-0330-4 – volume: 283 start-page: 10500 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0600 article-title: Truncation of alphaB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells publication-title: J. Biol. Chem. doi: 10.1074/jbc.M706453200 – volume: 1089 start-page: 67 year: 2006 ident: 10.1016/j.bbagen.2015.09.005_bb0355 article-title: Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity publication-title: Brain Res. doi: 10.1016/j.brainres.2006.03.058 – volume: 450 start-page: 1668 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0155 article-title: The kinetics of thermal stress induced denaturation of Aquaporin 0 publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2014.07.056 – volume: 278 start-page: 27828 year: 2003 ident: 10.1016/j.bbagen.2015.09.005_bb0485 article-title: Heat shock protein 27 controls apoptosis by regulating Akt activation publication-title: J. Biol. Chem. doi: 10.1074/jbc.M303417200 – volume: 340 start-page: 1167 year: 2004 ident: 10.1016/j.bbagen.2015.09.005_bb0415 article-title: Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2004.05.054 – volume: 125 start-page: 60 year: 2013 ident: 10.1016/j.bbagen.2015.09.005_bb0440 article-title: Modulating autophagy improves cardiac function in a rat model of early-stage dilated cardiomyopathy publication-title: Cardiology doi: 10.1159/000348308 – volume: 7 year: 2012 ident: 10.1016/j.bbagen.2015.09.005_bb0585 article-title: alphaA-Crystallin-derived mini-chaperone modulates stability and function of cataract causing alphaAG98R-crystallin publication-title: PLoS One doi: 10.1371/journal.pone.0044077 – volume: 92 start-page: 98 year: 2011 ident: 10.1016/j.bbagen.2015.09.005_bb0025 article-title: New focus on alpha-crystallins in retinal neurodegenerative diseases publication-title: Exp. Eye Res. doi: 10.1016/j.exer.2010.11.008 – volume: 269 start-page: 13601 year: 1994 ident: 10.1016/j.bbagen.2015.09.005_bb0580 article-title: The chaperone activity of bovine alpha crystallin. Interaction with other lens crystallins in native and denatured states publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)36872-2 – volume: 13 start-page: 854 year: 2007 ident: 10.1016/j.bbagen.2015.09.005_bb0085 article-title: Confocal fluorescence resonance energy transfer microscopy study of protein–protein interactions of lens crystallins in living cells publication-title: Mol. Vis. – volume: 25 start-page: 65 year: 2013 ident: 10.1016/j.bbagen.2015.09.005_bb0185 article-title: Towards to clarify the etiology of cataract by crystallin protein–protein interaction studies publication-title: Jpn. Soc. Cataract Refract. Surg. – volume: 104 start-page: 51 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0310 article-title: Confocal fluorescence microscopy study of interaction between lens MIP26/AQP0 and crystallins in living cells publication-title: J. Cell. Biochem. doi: 10.1002/jcb.21598 – volume: 102 start-page: 449 year: 2001 ident: 10.1016/j.bbagen.2015.09.005_bb0430 article-title: Nerve cells expressing heat-shock proteins in Parkinson's disease publication-title: Acta Neuropathol. doi: 10.1007/s004010100395 – volume: 96 start-page: 6137 year: 1999 ident: 10.1016/j.bbagen.2015.09.005_bb0450 article-title: Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.96.11.6137 – volume: 4 start-page: 62 year: 2011 ident: 10.1016/j.bbagen.2015.09.005_bb0030 article-title: Impact of diabetes on alpha-crystallins and other heat shock proteins in the eye publication-title: J. Ocul. Biol. Dis. Inform. doi: 10.1007/s12177-011-9073-7 – volume: 59 start-page: 265 year: 2000 ident: 10.1016/j.bbagen.2015.09.005_bb0350 article-title: Spinocerebellar ataxia type 1—modeling the pathogenesis of a polyglutamine neurodegenerative disorder in transgenic mice publication-title: J. Neuropathol. Exp. Neurol. doi: 10.1093/jnen/59.4.265 – volume: 115 start-page: 21 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0100 article-title: Lens beta-crystallins: the role of deamidation and related modifications in aging and cataract publication-title: Prog. Biophys. Mol. Biol. doi: 10.1016/j.pbiomolbio.2014.02.004 – volume: 14 start-page: 1282 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0075 article-title: Protein–protein interactions between lens vimentin and alphaB-crystallin using FRET acceptor photobleaching publication-title: Mol. Vis. – volume: 55 start-page: 760 year: 1993 ident: 10.1016/j.bbagen.2015.09.005_bb0535 article-title: Expression of alpha B-crystallin in human brain tumors publication-title: Int. J. Cancer doi: 10.1002/ijc.2910550511 – volume: 277 start-page: 4255 year: 2002 ident: 10.1016/j.bbagen.2015.09.005_bb0230 article-title: Detection of protein–protein interactions among lens crystallins in a mammalian two-hybrid system assay publication-title: J. Biol. Chem. doi: 10.1074/jbc.M110027200 – volume: 46 start-page: 6308 year: 2007 ident: 10.1016/j.bbagen.2015.09.005_bb0495 article-title: Interactions between important regulatory proteins and human alphaB crystallin publication-title: Biochemistry doi: 10.1021/bi700149h – volume: 43 start-page: 15785 year: 2004 ident: 10.1016/j.bbagen.2015.09.005_bb0575 article-title: AlphaA-crystallin interacting regions in the small heat shock protein, alphaB-crystallin publication-title: Biochemistry doi: 10.1021/bi048151s – volume: 130 start-page: 427 year: 2007 ident: 10.1016/j.bbagen.2015.09.005_bb0455 article-title: Human alpha B-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice publication-title: Cell doi: 10.1016/j.cell.2007.06.044 – volume: 453 start-page: 326 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0490 article-title: Inflammatory cytokines, interleukin-1 beta and tumor necrosis factor-alpha, upregulated in glioblastoma multiforme, raise the levels of CRYAB in exosomes secreted by U373 glioma cells publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2014.09.068 – volume: 16 start-page: 4437 year: 2005 ident: 10.1016/j.bbagen.2015.09.005_bb0045 article-title: Calcium-activated RAF/MEK/ERK signaling pathway mediates p53-dependent apoptosis and is abrogated by alpha B-crystallin through inhibition of RAS activation publication-title: Mol. Biol. Cell doi: 10.1091/mbc.e05-01-0010 – volume: 392 start-page: 573 year: 2005 ident: 10.1016/j.bbagen.2015.09.005_bb0390 article-title: AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin publication-title: Biochem. J. doi: 10.1042/BJ20050339 – volume: 110 start-page: E3780 year: 2013 ident: 10.1016/j.bbagen.2015.09.005_bb0505 article-title: Regulated structural transitions unleash the chaperone activity of alphaB-crystallin publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1308898110 – year: 2015 ident: 10.1016/j.bbagen.2015.09.005_bb0520 article-title: ERK-regulated alphaB-crystallin induction by matrix detachment inhibits anoikis and promotes lung metastasis in vivo publication-title: Oncogene doi: 10.1038/onc.2015.12 – volume: 14 start-page: 1835 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0250 article-title: Role of alphaBI5 and alphaBT162 residues in subunit interaction during oligomerization of alphaB-crystallin publication-title: Mol. Vis. – volume: 58 start-page: 632 year: 2006 ident: 10.1016/j.bbagen.2015.09.005_bb0570 article-title: Chaperone-like activity and hydrophobicity of alpha-crystallin publication-title: IUBMB Life doi: 10.1080/15216540601010096 – volume: 281 start-page: 14273 year: 2006 ident: 10.1016/j.bbagen.2015.09.005_bb0145 article-title: Mechanism of a hereditary cataract phenotype. Mutations in alphaA-crystallin activate substrate binding publication-title: J. Biol. Chem. doi: 10.1074/jbc.M512938200 – volume: 10 year: 2015 ident: 10.1016/j.bbagen.2015.09.005_bb0435 article-title: Humoral response against small heat shock proteins in Parkinson's disease publication-title: PLoS One doi: 10.1371/journal.pone.0115480 – volume: 45 start-page: 3069 year: 2006 ident: 10.1016/j.bbagen.2015.09.005_bb0615 article-title: Mini-alphaB-crystallin: a functional element of alphaB-crystallin with chaperone-like activity publication-title: Biochemistry doi: 10.1021/bi0518141 – volume: 13 start-page: 2301 year: 2007 ident: 10.1016/j.bbagen.2015.09.005_bb0190 article-title: Cataract-causing alphaAG98R mutant shows substrate-dependent chaperone activity publication-title: Mol. Vis. – volume: 11 start-page: 321 year: 2005 ident: 10.1016/j.bbagen.2015.09.005_bb0265 article-title: Interaction and biophysical properties of human lens Q155* betaB2-crystallin mutant publication-title: Mol. Vis. – volume: 133 start-page: 813 year: 2006 ident: 10.1016/j.bbagen.2015.09.005_bb0550 article-title: Caspase-dependent secondary lens fiber cell disintegration in alphaA−/alphaB-crystallin double-knockout mice publication-title: Development doi: 10.1242/dev.02262 – volume: 275 start-page: 3767 year: 2000 ident: 10.1016/j.bbagen.2015.09.005_bb0555 article-title: Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin publication-title: J. Biol. Chem. doi: 10.1074/jbc.275.6.3767 – volume: 14 start-page: 1157 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0180 article-title: Crystallin gene mutations in Indian families with inherited pediatric cataract publication-title: Mol. Vis. – volume: 54 start-page: 461 year: 1992 ident: 10.1016/j.bbagen.2015.09.005_bb0530 article-title: Hypertonic stress induces alpha B-crystallin expression publication-title: Exp. Eye Res. doi: 10.1016/0014-4835(92)90058-Z – volume: 17 start-page: 1565 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0630 article-title: Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin publication-title: Protein Sci. doi: 10.1110/ps.035410.108 – volume: 7 year: 2012 ident: 10.1016/j.bbagen.2015.09.005_bb0650 article-title: Cataract-causing defect of a mutant gamma-crystallin proceeds through an aggregation pathway which bypasses recognition by the alpha-crystallin chaperone publication-title: PLoS One doi: 10.1371/journal.pone.0037256 – volume: 53 start-page: 2541 year: 2012 ident: 10.1016/j.bbagen.2015.09.005_bb0240 article-title: Oligomerization with wt alphaA- and alphaB-crystallins reduces proteasome-mediated degradation of C-terminally truncated alphaA-crystallin publication-title: Invest. Ophthalmol. Vis. Sci. doi: 10.1167/iovs.11-9147 – volume: 88 start-page: 173 year: 2009 ident: 10.1016/j.bbagen.2015.09.005_bb0110 article-title: Genetics of crystallins: cataract and beyond publication-title: Exp. Eye Res. doi: 10.1016/j.exer.2008.10.011 – volume: 9 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0330 article-title: Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulations publication-title: PLoS One doi: 10.1371/journal.pone.0113041 – volume: 284 start-page: 18481 year: 2009 ident: 10.1016/j.bbagen.2015.09.005_bb0205 article-title: Identification of interaction sites between human betaA3- and alphaA/alphaB-crystallins by mammalian two-hybrid and fluorescence resonance energy transfer acceptor photobleaching methods publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.013789 – volume: 27 start-page: 1214 year: 2013 ident: 10.1016/j.bbagen.2015.09.005_bb0340 article-title: Avoiding the oligomeric state: alphaB-crystallin inhibits fragmentation and induces dissociation of apolipoprotein C-II amyloid fibrils publication-title: FASEB J. doi: 10.1096/fj.12-220657 – volume: 45 start-page: 206 year: 2004 ident: 10.1016/j.bbagen.2015.09.005_bb0605 article-title: Effect of deamidation of asparagine 146 on functional and structural properties of human lens alphaB-crystallin publication-title: Invest. Ophthalmol. Vis. Sci. doi: 10.1167/iovs.03-0720 – volume: 484 start-page: 98 year: 2000 ident: 10.1016/j.bbagen.2015.09.005_bb0245 article-title: Interaction between beta-amyloid and lens alphaB-crystallin publication-title: FEBS Lett. doi: 10.1016/S0014-5793(00)02136-0 – volume: 20 start-page: 513 year: 2011 ident: 10.1016/j.bbagen.2015.09.005_bb0655 article-title: Contributions of aromatic pairs to the folding and stability of long-lived human gammaD-crystallin publication-title: Protein Sci. doi: 10.1002/pro.583 – volume: 115 start-page: 3 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0320 article-title: Cell biological roles of alphaB-crystallin publication-title: Prog. Biophys. Mol. Biol. doi: 10.1016/j.pbiomolbio.2014.02.005 – volume: 7 year: 2012 ident: 10.1016/j.bbagen.2015.09.005_bb0170 article-title: Mutations in human alphaA-crystallin/sHSP affect subunit exchange interaction with alphaB-crystallin publication-title: PLoS One doi: 10.1371/journal.pone.0031421 – volume: 31 start-page: 4587 year: 2012 ident: 10.1016/j.bbagen.2015.09.005_bb0670 article-title: Binding determinants of the small heat shock protein, alphaB-crystallin: recognition of the ‘IxI’ motif publication-title: EMBO J. doi: 10.1038/emboj.2012.318 – volume: 430 start-page: 107 year: 2013 ident: 10.1016/j.bbagen.2015.09.005_bb0460 article-title: Mutants of human alphaB-crystallin cause enhanced protein aggregation and apoptosis in mammalian cells: influence of co-expression of HspB1 publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2012.11.051 – volume: 6 start-page: 333 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0465 article-title: HspB1, HspB5 and HspB4 in human cancers: potent oncogenic role of some of their client proteins publication-title: Cancers doi: 10.3390/cancers6010333 – volume: 1292 start-page: 195 year: 2015 ident: 10.1016/j.bbagen.2015.09.005_bb0400 article-title: Studying nitrosative stress in Parkinson's disease publication-title: Methods Mol. Biol. doi: 10.1007/978-1-4939-2522-3_14 – volume: 98 start-page: 843 year: 2010 ident: 10.1016/j.bbagen.2015.09.005_bb0425 article-title: The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation publication-title: Biophys. J. doi: 10.1016/j.bpj.2009.10.056 – volume: 10 start-page: 655 year: 2004 ident: 10.1016/j.bbagen.2015.09.005_bb0675 article-title: The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies publication-title: Mol. Vis. – volume: 1164 start-page: 22 year: 1993 ident: 10.1016/j.bbagen.2015.09.005_bb0050 article-title: An investigation into the stability of alpha-crystallin by NMR spectroscopy; evidence for a two-domain structure publication-title: Biochim. Biophys. Acta doi: 10.1016/0167-4838(93)90107-3 – volume: 66 start-page: 65 year: 2011 ident: 10.1016/j.bbagen.2015.09.005_bb0135 article-title: Heat-shock proteins in clinical neurology publication-title: Eur. Neurol. doi: 10.1159/000329373 – volume: 89 start-page: 7958 year: 1992 ident: 10.1016/j.bbagen.2015.09.005_bb0280 article-title: Karyoplasmic interaction selection strategy: a general strategy to detect protein–protein interactions in mammalian cells publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.89.17.7958 – volume: 90 start-page: 643 year: 2010 ident: 10.1016/j.bbagen.2015.09.005_bb0005 article-title: On the growth and internal structure of the human lens publication-title: Exp. Eye Res. doi: 10.1016/j.exer.2010.01.013 – volume: 1854 start-page: 291 year: 2015 ident: 10.1016/j.bbagen.2015.09.005_bb0500 article-title: Small heat shock proteins: role in cellular functions and pathology publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbapap.2014.12.019 – volume: 66 start-page: 62 year: 2009 ident: 10.1016/j.bbagen.2015.09.005_bb0335 article-title: Crystallin proteins and amyloid fibrils publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-008-8327-4 – volume: 281 start-page: 2624 year: 2006 ident: 10.1016/j.bbagen.2015.09.005_bb0305 article-title: Domain interaction sites of human lens betaB2-crystallin publication-title: J. Biol. Chem. doi: 10.1074/jbc.M509017200 – volume: 57 start-page: 479 year: 1988 ident: 10.1016/j.bbagen.2015.09.005_bb0010 article-title: Lens crystallins: the evolution and expression of proteins for a highly specialized tissue publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.bi.57.070188.002403 – start-page: 89 year: 2006 ident: 10.1016/j.bbagen.2015.09.005_bb0405 article-title: Pathology associated with sporadic Parkinson's disease—where does it end? publication-title: J. Neural Transm. Suppl. – volume: 89 start-page: 10449 year: 1992 ident: 10.1016/j.bbagen.2015.09.005_bb0055 article-title: Alpha-crystallin can function as a molecular chaperone publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.89.21.10449 – volume: 16 start-page: 438 year: 2010 ident: 10.1016/j.bbagen.2015.09.005_bb0635 article-title: Decreasing the homodimer interaction: a common mechanism shared by the deltaG91 mutation and deamidation in betaA3-crystallin publication-title: Mol. Vis. – volume: 154 start-page: 363 year: 1995 ident: 10.1016/j.bbagen.2015.09.005_bb0540 article-title: Constitutive expression of human hsp27, drosophila hsp27, or human alpha B-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts publication-title: J. Immunol. doi: 10.4049/jimmunol.154.1.363 – year: 2015 ident: 10.1016/j.bbagen.2015.09.005_bb0080 article-title: Real-time heterogeneous protein-protein interaction between alphaA-crystallin N-terminal mutants and alphaB-crystallin using quartz crystal microbalance (QCM) publication-title: Amino Acids doi: 10.1007/s00726-015-1935-z – volume: 308 start-page: 85 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0560 article-title: C-terminal truncation affects subunit exchange of human alphaA-crystallin with alphaB-crystallin publication-title: Mol. Cell. Biochem. doi: 10.1007/s11010-007-9615-2 – volume: 213 start-page: 321 year: 1993 ident: 10.1016/j.bbagen.2015.09.005_bb0645 article-title: 1H-NMR spectroscopy of bovine lens beta-crystallin. The role of the beta B2-crystallin C-terminal extension in aggregation publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1993.tb17765.x – volume: 20 start-page: 117 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0060 article-title: Identification of proteins that interact with alpha A-crystallin using a human proteome microarray publication-title: Mol. Vis. – volume: 279 start-page: 42648 year: 2004 ident: 10.1016/j.bbagen.2015.09.005_bb0220 article-title: Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function publication-title: J. Biol. Chem. doi: 10.1074/jbc.M404444200 – volume: 5 start-page: 2554 year: 2006 ident: 10.1016/j.bbagen.2015.09.005_bb0065 article-title: Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility? publication-title: J. Proteome Res. doi: 10.1021/pr050473a – volume: 3 start-page: 75 year: 2001 ident: 10.1016/j.bbagen.2015.09.005_bb0360 article-title: Alzheimer's disease results from the cerebral accumulation and cytotoxicity of amyloid beta-protein publication-title: J. Alzheimers Dis. doi: 10.3233/JAD-2001-3111 – volume: 139 start-page: 191 year: 2002 ident: 10.1016/j.bbagen.2015.09.005_bb0300 article-title: Unfolding of human lens recombinant betaB2- and gammaC-crystallins publication-title: J. Struct. Biol. doi: 10.1016/S1047-8477(02)00545-2 – volume: 1784 start-page: 1192 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0595 article-title: Differential rate constants of racemization of aspartyl and asparaginyl residues in human alpha A-crystallin mutants publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbapap.2008.04.008 – volume: 30 start-page: 4775 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0225 article-title: Structure and functional properties of a multimeric protein alphaA-crystallin adsorbed on silver nanoparticle surface publication-title: Langmuir doi: 10.1021/la5007007 – volume: 8 year: 2013 ident: 10.1016/j.bbagen.2015.09.005_bb0260 article-title: Identification of subunit-subunit interaction sites in alphaA-WT crystallin and mutant alphaA-G98R crystallin using isotope-labeled cross-linker and mass spectrometry publication-title: PLoS One doi: 10.1371/journal.pone.0065610 – volume: 368 start-page: 20110405 year: 2013 ident: 10.1016/j.bbagen.2015.09.005_bb0680 article-title: C-terminal interactions mediate the quaternary dynamics of alphaB-crystallin publication-title: Philos. Trans. R. Soc. Lond. Ser. B Biol. Sci. doi: 10.1098/rstb.2011.0405 – volume: 5 start-page: 8755 year: 2015 ident: 10.1016/j.bbagen.2015.09.005_bb0150 article-title: betaA3/A1-crystallin is a critical mediator of STAT3 signaling in optic nerve astrocytes publication-title: Sci. Rep. doi: 10.1038/srep08755 – volume: 12 start-page: 177 year: 2012 ident: 10.1016/j.bbagen.2015.09.005_bb0510 article-title: AlphaA- and alphaB-crystallins interact with caspase-3 and Bax to guard mouse lens development publication-title: Curr. Mol. Med. doi: 10.2174/156652412798889036 – volume: 13 start-page: 2476 year: 2004 ident: 10.1016/j.bbagen.2015.09.005_bb0255 article-title: Interactions and chaperone function of alphaA-crystallin with T5P gammaC-crystallin mutant publication-title: Protein Sci. doi: 10.1110/ps.04815104 – volume: 377 start-page: 641 year: 2011 ident: 10.1016/j.bbagen.2015.09.005_bb0420 article-title: Imputation of sequence variants for identification of genetic risks for Parkinson's disease: a meta-analysis of genome-wide association studies publication-title: Lancet doi: 10.1016/S0140-6736(10)62345-8 – volume: 44 start-page: 62 year: 2015 ident: 10.1016/j.bbagen.2015.09.005_bb0105 article-title: betaA3/A1-crystallin: more than a lens protein publication-title: Prog. Retin. Eye Res. doi: 10.1016/j.preteyeres.2014.11.002 – volume: 108 start-page: 20491 year: 2011 ident: 10.1016/j.bbagen.2015.09.005_bb0125 article-title: Multiple molecular architectures of the eye lens chaperone alphaB-crystallin elucidated by a triple hybrid approach publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1111014108 – volume: 20 start-page: 4821 year: 1981 ident: 10.1016/j.bbagen.2015.09.005_bb0315 article-title: Effect of macromolecular crowding upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase publication-title: Biochemistry doi: 10.1021/bi00520a003 – volume: 5 start-page: 5159 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0445 article-title: alphaB-crystallin interacts with and prevents stress-activated proteolysis of focal adhesion kinase by calpain in cardiomyocytes publication-title: Nat. Commun. doi: 10.1038/ncomms6159 – volume: 581 start-page: 3936 year: 2007 ident: 10.1016/j.bbagen.2015.09.005_bb0295 article-title: Protein–protein interactions among human lens acidic and basic β-crystallins publication-title: FEBS Lett. doi: 10.1016/j.febslet.2007.07.022 – volume: 17 start-page: 2407 year: 2011 ident: 10.1016/j.bbagen.2015.09.005_bb0610 article-title: Structural and functional roles of deamidation of N146 and/or truncation of NH2- or COOH-termini in human alphaB-crystallin publication-title: Mol. Vis. – volume: 6 year: 2011 ident: 10.1016/j.bbagen.2015.09.005_bb0090 article-title: Congenital cataract causing mutants of alphaA-crystallin/sHSP form aggregates and aggresomes degraded through ubiquitin-proteasome pathway publication-title: PLoS One doi: 10.1371/journal.pone.0028085 – volume: 279 start-page: 2892 year: 2012 ident: 10.1016/j.bbagen.2015.09.005_bb0120 article-title: A role for γS-crystallin in the organization of actin and fiber cell maturation in the mouse lens publication-title: FEBS J. doi: 10.1111/j.1742-4658.2012.08669.x – volume: 166 start-page: 61 year: 1992 ident: 10.1016/j.bbagen.2015.09.005_bb0345 article-title: Alpha B crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease publication-title: J. Pathol. doi: 10.1002/path.1711660110 – volume: 45 start-page: 3146 year: 2006 ident: 10.1016/j.bbagen.2015.09.005_bb0640 article-title: Deamidation in human lens betaB2-crystallin destabilizes the dimer publication-title: Biochemistry doi: 10.1021/bi052051k – volume: 2 start-page: 404 year: 1993 ident: 10.1016/j.bbagen.2015.09.005_bb0385 article-title: Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution publication-title: Protein Sci. doi: 10.1002/pro.5560020312 – volume: 11 start-page: 512 year: 2004 ident: 10.1016/j.bbagen.2015.09.005_bb0545 article-title: Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis publication-title: Cell Death Differ. doi: 10.1038/sj.cdd.4401384 – volume: 115 start-page: 52 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0325 article-title: Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells publication-title: Prog. Biophys. Mol. Biol. doi: 10.1016/j.pbiomolbio.2014.02.006 – volume: 88 start-page: 10686 year: 1991 ident: 10.1016/j.bbagen.2015.09.005_bb0275 article-title: A contingent replication assay for the detection of protein–protein interactions in animal cells publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.88.23.10686 – volume: 361 start-page: 1258 year: 2003 ident: 10.1016/j.bbagen.2015.09.005_bb0370 article-title: Cytosolic beta-amyloid deposition and supranuclear cataracts in lenses from people with Alzheimer's disease publication-title: Lancet doi: 10.1016/S0140-6736(03)12981-9 – volume: 87 start-page: 496 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0160 article-title: Protein–protein interactions and lens transparency publication-title: Exp. Eye Res. doi: 10.1016/j.exer.2008.08.018 – volume: 580 start-page: 5941 year: 2006 ident: 10.1016/j.bbagen.2015.09.005_bb0395 article-title: AlphaB-crystallin competes with Alzheimer's disease beta-amyloid peptide for peptide-peptide interactions and induces oxidation of Abeta-Met35 publication-title: FEBS Lett. doi: 10.1016/j.febslet.2006.09.063 – volume: 375 start-page: 1040 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0565 article-title: Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2007.11.019 – volume: 19 start-page: 311 year: 2010 ident: 10.1016/j.bbagen.2015.09.005_bb0365 article-title: Alzheimer's disease and the amyloid-beta peptide publication-title: J. Alzheimers Dis. doi: 10.3233/JAD-2010-1221 – volume: 22 start-page: 350 year: 1997 ident: 10.1016/j.bbagen.2015.09.005_bb0285 article-title: Mammalian two-hybrid system: a complementary approach to the yeast two-hybrid system publication-title: Biotechniques doi: 10.2144/97222pf02 – volume: 581 start-page: 3665 year: 2007 ident: 10.1016/j.bbagen.2015.09.005_bb0480 article-title: Hsp27 (HspB1) and alphaB-crystallin (HspB5) as therapeutic targets publication-title: FEBS Lett. doi: 10.1016/j.febslet.2007.04.033 – volume: 7 start-page: 178 year: 2001 ident: 10.1016/j.bbagen.2015.09.005_bb0195 article-title: Spectroscopic analysis of lens recombinant betaB2- and gammaC-crystallin publication-title: Mol. Vis. – volume: 12 start-page: 581 year: 2006 ident: 10.1016/j.bbagen.2015.09.005_bb0235 article-title: The interaction between alphaA- and alphaB-crystallin is sequence-specific publication-title: Mol. Vis. – volume: 3 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0095 article-title: Interaction of C-terminal truncated human αA-crystallins with target proteins publication-title: PLoS ONE doi: 10.1371/journal.pone.0003175 – volume: 1204 start-page: 195 year: 1994 ident: 10.1016/j.bbagen.2015.09.005_bb0215 article-title: Alpha-crystallin: molecular chaperone and protein surfactant publication-title: Biochim. Biophys. Acta doi: 10.1016/0167-4838(94)90009-4 – volume: 45 start-page: 13847 year: 2006 ident: 10.1016/j.bbagen.2015.09.005_bb0620 article-title: N- and C-terminal motifs in human alphaB crystallin play an important role in the recognition, selection, and solubilization of substrates publication-title: Biochemistry doi: 10.1021/bi061471m – volume: 43 start-page: 432 year: 2010 ident: 10.1016/j.bbagen.2015.09.005_bb0040 article-title: Synergistic efficacy of LBH and alphaB-crystallin through inhibiting transcriptional activities of p53 and p21 publication-title: BMB Rep. doi: 10.5483/BMBRep.2010.43.6.432 – volume: 262 start-page: 152 year: 1999 ident: 10.1016/j.bbagen.2015.09.005_bb0380 article-title: The molecular chaperone alphaB-crystallin enhances amyloid beta neurotoxicity publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1999.1167 – volume: 276 start-page: 16059 year: 2001 ident: 10.1016/j.bbagen.2015.09.005_bb0525 article-title: The small heat shock protein alpha B-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation publication-title: J. Biol. Chem. doi: 10.1074/jbc.C100107200 – volume: 101 start-page: 1681 year: 2011 ident: 10.1016/j.bbagen.2015.09.005_bb0375 article-title: Binding of the molecular chaperone alphaB-crystallin to Abeta amyloid fibrils inhibits fibril elongation publication-title: Biophys. J. doi: 10.1016/j.bpj.2011.07.056 – volume: 49 start-page: 1161 year: 2008 ident: 10.1016/j.bbagen.2015.09.005_bb0035 article-title: Elevated retina-specific expression of the small heat shock protein, alphaA-crystallin, is associated with photoreceptor protection in experimental uveitis publication-title: Invest. Ophthalmol. Vis. Sci. doi: 10.1167/iovs.07-1259 – volume: 15 start-page: 1429 year: 2009 ident: 10.1016/j.bbagen.2015.09.005_bb0130 article-title: COOH-terminal truncations and site-directed mutations enhance thermostability and chaperone-like activity of porcine αB-crystallin publication-title: Mol. Vis. – volume: 11 start-page: 803 year: 1991 ident: 10.1016/j.bbagen.2015.09.005_bb0475 article-title: Alpha B crystallin accumulation is a specific response to Ha-ras and v-mos oncogene expression in mouse NIH 3T3 fibroblasts publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.11.2.803 – volume: 44 start-page: 12245 year: 2005 ident: 10.1016/j.bbagen.2015.09.005_bb0665 article-title: Recognition sequence 2 (residues 60–71) plays a role in oligomerization and exchange dynamics of alphaB-crystallin publication-title: Biochemistry doi: 10.1021/bi051005h – start-page: 1 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0015 article-title: Protein–protein interaction between recombinant alpha crystallin and its mutants to comprehend the basis towards the progression of cataract – volume: 15 start-page: 241 year: 2009 ident: 10.1016/j.bbagen.2015.09.005_bb0625 article-title: Deamidation alters interactions of beta-crystallins in hetero-oligomers publication-title: Mol. Vis. – volume: 28 start-page: 57 year: 2005 ident: 10.1016/j.bbagen.2015.09.005_bb0410 article-title: Molecular pathophysiology of Parkinson's disease publication-title: Annu. Rev. Neurosci. doi: 10.1146/annurev.neuro.28.061604.135718 – volume: 23 start-page: 1110 year: 1997 ident: 10.1016/j.bbagen.2015.09.005_bb0290 article-title: Quantification of gene expression with a secreted alkaline phosphatase reporter system publication-title: Biotechniques doi: 10.2144/97236pf01 – volume: 3 start-page: 3 year: 2003 ident: 10.1016/j.bbagen.2015.09.005_bb0175 article-title: Morphological characterization of the Alpha A- and Alpha B-crystallin double knockout mouse lens publication-title: BMC Ophthalmol. doi: 10.1186/1471-2415-3-3 – volume: 44 start-page: 1155 year: 2003 ident: 10.1016/j.bbagen.2015.09.005_bb0200 article-title: Alteration of protein–protein interactions of congenital cataract crystallin mutants publication-title: Invest. Ophthalmol. Vis. Sci. doi: 10.1167/iovs.02-0950 – volume: 405 start-page: 486 year: 2011 ident: 10.1016/j.bbagen.2015.09.005_bb0590 article-title: Temperature-dependent coaggregation of eye lens alphaB- and beta-crystallins publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2011.01.058 – volume: 76 start-page: 102 year: 2015 ident: 10.1016/j.bbagen.2015.09.005_bb0165 article-title: Interaction of alphaA-crystallin F71L mutant with wild type alphaA- and alphaB-crystallins by mammalian two hybrid assay publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2015.02.025 – volume: 48 start-page: 3708 year: 2009 ident: 10.1016/j.bbagen.2015.09.005_bb0115 article-title: Mechanism of the very efficient quenching of tryptophan fluorescence in human gamma D- and gamma S-crystallins: the gamma-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage publication-title: Biochemistry doi: 10.1021/bi802177g – volume: 20 start-page: 1002 year: 2014 ident: 10.1016/j.bbagen.2015.09.005_bb0140 article-title: Comparison of effect of gamma ray irradiation on wild-type and N-terminal mutants of alphaA-crystallin publication-title: Mol. Vis. – volume: 1820 start-page: 921 year: 2012 ident: 10.1016/j.bbagen.2015.09.005_bb0515 article-title: AlphaB-crystallin/sHSP protects cytochrome c and mitochondrial function against oxidative stress in lens and retinal cells publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbagen.2012.04.004 – volume: 21 start-page: 1074 year: 2012 ident: 10.1016/j.bbagen.2015.09.005_bb0660 article-title: Age-dependent deamidation of glutamine residues in human gammaS crystallin: deamidation and unstructured regions publication-title: Protein Sci. doi: 10.1002/pro.2095 |
| SSID | ssj0000595 ssj0025309 |
| Score | 2.2367907 |
| SecondaryResourceType | review_article |
| Snippet | Crystallins are the important structural and functional proteins in the eye lens responsible for refractive index. Post-translational modifications (PTMs) and... BACKGROUNDCrystallins are the important structural and functional proteins in the eye lens responsible for refractive index. Post-translational modifications... |
| SourceID | proquest pubmed crossref elsevier |
| SourceType | Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 222 |
| SubjectTerms | Binding Sites biomarkers Cardiomyopathies - metabolism Cataract Cataract - metabolism Crystallin crystallins Crystallins - chemistry Crystallins - metabolism etiology eye lens functional properties human diseases Humans metal ions Mutation Neoplasms - metabolism Neurodegenerative Diseases - metabolism pathogenesis post-translational modification Protein Binding Protein Interaction Mapping protein-protein interactions Protein–protein interaction refractive index tissues |
| Title | Multidimensional significance of crystallin protein–protein interactions and their implications in various human diseases |
| URI | https://dx.doi.org/10.1016/j.bbagen.2015.09.005 https://www.ncbi.nlm.nih.gov/pubmed/26365509 https://www.proquest.com/docview/1746871153 https://www.proquest.com/docview/1825431398 |
| Volume | 1860 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3dS9xAEB9EkfalWPt11coW-preJdmP5FEO5eyhD7ZS35bsbhauSE7uzoIUSv-H_of9Szqzu9EWagWf8sEkLDuT-cjM_AbgnZG24dwXWau8zHjtctSDNM3deIEGxzobAEyPT-TkjH84F-drMO57YaisMun-qNODtk53hmk3h5ez2fAjJfXQnUCDTIZHUcMv54qk_P332zIPdB9EzCTwjKj79rlQ42UMfrSEgpqLgHZKQ-z-bZ7ucj-DGTrcgifJf2T7cYlPYa3ttmEzTpS83oZH436A2zP4FpprHcH3R-gNRsUaVBpEnGZzz-ziGp1DQuVmAa9h1v368TOdMQKSWMS2hyVrOsdCToHN_ihBRxr2FYPt-dWShWF_LOV7ls_h7PDg03iSpVkLmeVSrDJlVD2qlPNWOnTRLG8EGi6nCo8BE2HAuLYYKSMLJxrZFoWpjDTcK88dxhimKV_Aejfv2lfAhKu4sHVeejnipikq56THV5d5WfHclgMo-y3WNgGR0zyMC91XnH3RkTGaGKNHtUbGDCC7eeoyAnHcQ6967um_BEqjrbjnybc9szVyjBIoTdfiTmqM3iQGmGgk_kNTBXiBsq4G8DJKys16C1lKjAjr1w9e2w48xqv0D2gX1leLq_YNekUrsxfEfg829o-mkxM6Tk8_T38D8HkQWw |
| linkProvider | Elsevier |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1La9wwEB7SDSW9lCZtk-0jUaFXs2tbD_sYloTNay9NIDdhSRZsCd6wuymEXPIf8g_zSzojy3lA20BvxpaM0MjzzXhmvgH4bqStOPdZUisvE166FPUgdXM3XiDgWGcDgenJRI7P-OG5OF-BUVcLQ2mVUfe3Oj1o63hnEHdzcDmdDn5QUA_NCQRkAh5VvIJVYqcSPVjdPTgaTx4VsgjNV2h8QhO6CrqQ5mUMfrdEhJqKQHhKfez-jFB_s0ADEu2_g7fRhGS77SrXYaVuNuB121TyegPWRl0Pt_dwE-prHTH4t-wbjPI1KDuIhM1mntn5NdqHRMzNAmXDtLm_vYtXjLgk5m3lw4JVjWMhrMCmT7LQcQz7hf727GrBQr8_FkM-iw9wtr93Ohonsd1CYrkUy0QZVQ4L5byVDq00yyuB2OVU5tFnIhoYV2dDZWTmRCXrLDOFkYZ75blDN8NU-UfoNbOm3gImXMGFLdPcyyE3VVY4Jz2-Ok_zgqc270PebbG2kYucWmJc6C7p7KduBaNJMHpYahRMH5KHWZctF8cL41UnPf3sTGmEixdmfuuErVFiFEOpmhp3UqMDJ9HHRJz4x5giMAzkZdGHzfakPKw3k7lEp7D89N9r24G18enJsT4-mBx9hjf4JP4S-gK95fyq_opG0tJsx4_gN6oPEWk |
| 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=Multidimensional+significance+of+crystallin+protein-protein+interactions+and+their+implications+in+various+human+diseases&rft.jtitle=Biochimica+et+biophysica+acta&rft.au=Anbarasu%2C+Kumarasamy&rft.au=Sivakumar%2C+Jeyarajan&rft.date=2016-01-01&rft.issn=0006-3002&rft.volume=1860&rft.issue=1+Pt+B&rft.spage=222&rft_id=info:doi/10.1016%2Fj.bbagen.2015.09.005&rft_id=info%3Apmid%2F26365509&rft.externalDocID=26365509 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0304-4165&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0304-4165&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0304-4165&client=summon |