About: Human lens beta-crystallin solubility

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scientific article published on 01 April 2000

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rdf:type	Item
description	wetenschappelijk artikel (nl) wüsseschaftlicher Artikel, wo im April 2000 veröffentlicht worden isch (gsw) наукова стаття, опублікована у квітні 2000 (uk) im April 2000 veröffentlichter wissenschaftlicher Artikel (de) article scientifique publié en avril 2000 (fr) artículu científicu espublizáu n'abril de 2000 (ast) scientific article published on 01 April 2000 (en)
publication date	wds:Q73680471-38BF0B65-7CE2-4021-A9DF-1C103F761BA5
publication date	2000-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73680471-E8921452-1322-418C-BB31-8467B4052AF5
language of work or name	English
cites work	wds:Q73680471-06ADA9AA-C4FB-4B9E-AC86-0C7181729CD4 wds:Q73680471-09255970-49B3-4A98-B6E9-5A01AEC4DE7D wds:Q73680471-1893FB14-2AC0-4658-8990-BEE22892031B wds:Q73680471-1CE0A2BD-397A-4011-AD4D-6EDD17D2A03A wds:Q73680471-217F7871-F99F-4A0F-A8B8-24459ABAA6D3 wds:Q73680471-25686C4F-A76A-4AD6-BD1F-2F073315FC91 wds:Q73680471-3558144E-3C41-47CD-8425-D1A72F10FFE1 wds:Q73680471-3BE4BA1B-A8DF-4781-95C5-433CB4658474 wds:Q73680471-42FDEDB7-F389-4906-9EF1-A0DCE973879C wds:Q73680471-449A8F13-3BA8-47AC-84BD-934D45A44C3B wds:Q73680471-470467AA-98E3-4874-9AE8-AE5AD6A6B119 wds:Q73680471-54D8F72E-1A46-47D4-94C6-03457768B30E wds:Q73680471-61F6689B-D1FB-4907-9940-8C26D2AF5535 wds:Q73680471-790E8315-A0A1-4268-A30D-60224EEC2B8D wds:Q73680471-AACFD83E-5F66-447E-8CFC-A5C2C21B7CF5 wds:Q73680471-B0162411-FB67-4E50-804B-FE2389D208E4 wds:Q73680471-C6BD0C97-0E88-483A-B4FF-40B2394D0B23 wds:Q73680471-D3C18ED8-73A7-49B4-87E9-C4A1F123F8E0 wds:Q73680471-D82C704D-63CA-49E0-A837-5F5DA8310664 wds:Q73680471-DDFD29A8-32FC-42C2-9D70-4D9C7DC930B1 wds:Q73680471-E4F5CD91-A085-4DB8-AEA7-744AE086CB40 wds:Q73680471-F94692C5-BE9A-42C3-A825-4C57E0D4CA29 wds:Q73680471-FAC23AA4-73C6-4B09-85F1-D3D3A347005E wds:Q73680471-FB241666-9997-42E6-9D82-363C0F789D0E
cites work	Alpha-crystallin can function as a molecular chaperone Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology Size of human lens beta-crystallin aggregates are distinguished by N-terminal truncation of betaB1. Modifications of the water-insoluble human lens alpha-crystallins Deamidation and disulfide bonding in human lens gamma-crystallins Sequencing of peptides by tandem mass spectrometry and high-energy collision-induced dissociation Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications. Glutathione adducts, not carbamylated lysines, are the major modification of lens alpha-crystallins from renal failure patients Proposal for a common nomenclature for sequence ions in mass spectra of peptides The sequence of human betaB1-crystallin cDNA allows mass spectrometric detection of betaB1 protein missing portions of its N-terminal extension Surface tension of amino acid solutions: A hydrophobicity scale of the amino acid residues Heat-induced changes in the conformation of α- and β-crystalline: Unique thermal stability of α-crystallin Human beta-crystallin. I. Comparative studies on the beta 1, beta 2 and beta 3-crystallins Amino acid sequence of human lens beta B2-crystallin Age-dependent changes in the heat-stable crystallin, beta Bp, of the human lens Sequence of the human lens beta B2-crystallin-encoding cDNA Immobilization of the C-terminal extension of bovine alphaA-crystallin reduces chaperone-like activity Purification of a heat-stable beta-crystallin polypeptide of the bovine lens Disulfide bond formation of cysteine-37 and cysteine-66 of beta B2 crystallin during cataractogenesis of the human lens Glutathione levels of the human crystalline lens in aging and its antioxidant effect against the oxidation of lens proteins Beta H- and beta L-crystallins are populations of aggregates Human beta crystallins: regional and age related changes
author name string	wds:Q73680471-08BB529A-CE8F-41A8-AC25-960F07C9ED88 wds:Q73680471-494F7A3C-6323-441B-86AB-11E5A27D6907 wds:Q73680471-62903BC9-A2FA-44B2-A32D-896F7BC9238B
author name string	J Feng J B Smith D L Smith
rdfs:label	Human lens beta-crystallin solubility (en) Human lens beta-crystallin solubility (nl)
skos:prefLabel	Human lens beta-crystallin solubility (en) Human lens beta-crystallin solubility (nl)
name	Human lens beta-crystallin solubility (en) Human lens beta-crystallin solubility (nl)
title	wds:Q73680471-3DD2C058-037F-4EA8-9828-D3F460FBF6B9
title	Human lens beta-crystallin solubility (en)
page(s)	wds:Q73680471-9B7306D8-FC2F-47DB-8398-3F55BA3FEF30
page(s)	11585-11590
instance of	wds:Q73680471-D194916F-3BF3-43C5-83B0-FD2232FF1AF4
instance of	scholarly article
PubMed ID	wds:Q73680471-4898EE14-C709-43AB-A84C-CE0617B0FAB5
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10766773
PubMed ID	10766773
published in	wds:Q73680471-814C0931-C689-4769-ABE9-D3EE71AE23CF
published in	Journal of Biological Chemistry
issue	wds:Q73680471-652022BA-4F10-483F-95FD-328442D98FD4
volume	wds:Q73680471-62DCC6FE-B414-4579-84EF-2BC5629F59EC
issue	16
volume	275
DOI	wds:Q73680471-9660CB4A-9A8F-47F1-8F91-88AF883E784B
DOI	http://dx.doi.org/10.1074/JBC.275.16.11585
DOI	10.1074/JBC.275.16.11585
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73680471
is cites work of	A novel mutation in CRYBB2 responsible for inherited coronary cataract Human beta-crystallins modified by backbone cleavage, deamidation and oxidation are prone to associate Age-dependent deamidation of lifelong proteins in the human lens Deamidation in human lens betaB2-crystallin destabilizes the dimer Glutamine deamidation: differentiation of glutamic acid and gamma-glutamic acid in peptides by electron capture dissociation Mutation analysis of congenital cataract in a Basotho family identified a new missense allele in CRYBB2. Subfertility in mice harboring a mutation in betaB2-crystallin A missense mutation in CRYBB2 leads to progressive congenital membranous cataract by impacting the solubility and function of βB2-crystallin Identification of a novel CRYBB2 missense mutation causing congenital autosomal dominant cataract.

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