| http://purl.uniprot.org/citations/23590631 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23590631 | http://www.w3.org/2000/01/rdf-schema#comment | "Mice with deletion of genes for small heat shock proteins αA- and αB-crystallin (αA/αB(-/-)) develop cataracts. We used proteomic analysis to identify lens proteins that change in abundance after deletion of these α-crystallin genes. Wild-type (WT) and αA/αB(-/-) knockout (DKO) mice were compared using two-dimensional difference gel electrophoresis and mass spectrometric analysis, and protein identifications were validated by Mascot proteomic software. The abundance of histones H2A, H4, and H2B fragment, and a low molecular weight β1-catenin increased 2-3-fold in postnatal day 2 lenses of DKO lenses compared with WT lenses. Additional major increases were observed in abundance of βB2-crystallin and vimentin in 30-day-old lenses of DKO animals compared with WT animals. Lenses of DKO mice were comprised of nine protein spots containing βB2-crystallin at 10-40-fold higher abundance and three protein spots containing vimentin at ≥2-fold higher abundance than in WT lenses. Gel permeation chromatography identified a unique 328 kDa protein in DKO lenses, containing β-crystallin, demonstrating aggregation of β-crystallin in the absence of α-crystallins. Together, these changes provide biochemical evidence for possible functions of specific cell adhesion proteins, cytoskeletal proteins, and crystallins in lens opacities caused by the absence of the major chaperones, αA- and αB-crystallins."xsd:string |
| http://purl.uniprot.org/citations/23590631 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi400180d"xsd:string |
| http://purl.uniprot.org/citations/23590631 | http://purl.uniprot.org/core/author | "Ravi N."xsd:string |
| http://purl.uniprot.org/citations/23590631 | http://purl.uniprot.org/core/author | "Townsend R.R."xsd:string |
| http://purl.uniprot.org/citations/23590631 | http://purl.uniprot.org/core/author | "Andley U.P."xsd:string |
| http://purl.uniprot.org/citations/23590631 | http://purl.uniprot.org/core/author | "Hamilton P.D."xsd:string |
| http://purl.uniprot.org/citations/23590631 | http://purl.uniprot.org/core/author | "Malone J.P."xsd:string |
| http://purl.uniprot.org/citations/23590631 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23590631 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/23590631 | http://purl.uniprot.org/core/pages | "2933-2948"xsd:string |
| http://purl.uniprot.org/citations/23590631 | http://purl.uniprot.org/core/title | "Comparative proteomic analysis identifies age-dependent increases in the abundance of specific proteins after deletion of the small heat shock proteins alphaA- and alphaB-crystallin."xsd:string |
| http://purl.uniprot.org/citations/23590631 | http://purl.uniprot.org/core/volume | "52"xsd:string |
| http://purl.uniprot.org/citations/23590631 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23590631 |
| http://purl.uniprot.org/citations/23590631 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/23590631 |
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| http://purl.uniprot.org/uniprot/#_A0A494B9Q6-mappedCitation-23590631 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23590631 |
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| http://purl.uniprot.org/uniprot/#_Q52L78-mappedCitation-23590631 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23590631 |
| http://purl.uniprot.org/uniprot/#_Q6P3C8-mappedCitation-23590631 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23590631 |
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| http://purl.uniprot.org/uniprot/P23927 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/23590631 |