| http://purl.uniprot.org/citations/24704203 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24704203 | http://www.w3.org/2000/01/rdf-schema#comment | "Cataract is characterized by the formation of light-scattering protein aggregates in the lens. β/γ-Crystallins are the predominant structural proteins in the cytosol of lens fiber cells, and more than fifty β/γ-crystallin mutations have been linked to autosomal dominant congenital cataract. However, the structural role of these mutations in the formation of the core structures of amorphous aggregates or amyloid-like fibrils has not been elucidated yet. In this research, we studied the effects of the V187M and R188H mutations on the aggregation and fibrillization of βB2-crystallin during acid denaturation. The behavior of V187M was the same as the WT protein, suggesting that the residue at position 187 contributed little to the aggregation/fibrillization process. R188H promoted the formation of amorphous aggregates at pH above 3 and accelerated fibrillization at pH 3. The distinct behaviors of the mutants suggested that the residue at position 188 might play a regulatory role in βB2-crystallin aggregation/fibrillization but not reside in the core of the aggregates/fibrils."xsd:string |
| http://purl.uniprot.org/citations/24704203 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2014.03.119"xsd:string |
| http://purl.uniprot.org/citations/24704203 | http://purl.uniprot.org/core/author | "Zhang K."xsd:string |
| http://purl.uniprot.org/citations/24704203 | http://purl.uniprot.org/core/author | "Yao K."xsd:string |
| http://purl.uniprot.org/citations/24704203 | http://purl.uniprot.org/core/author | "Yan Y.B."xsd:string |
| http://purl.uniprot.org/citations/24704203 | http://purl.uniprot.org/core/author | "Xi Y.B."xsd:string |
| http://purl.uniprot.org/citations/24704203 | http://purl.uniprot.org/core/author | "Ji S.R."xsd:string |
| http://purl.uniprot.org/citations/24704203 | http://purl.uniprot.org/core/author | "Dai A.B."xsd:string |
| http://purl.uniprot.org/citations/24704203 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24704203 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
| http://purl.uniprot.org/citations/24704203 | http://purl.uniprot.org/core/pages | "244-249"xsd:string |
| http://purl.uniprot.org/citations/24704203 | http://purl.uniprot.org/core/title | "Cataract-linked mutation R188H promotes betaB2-crystallin aggregation and fibrillization during acid denaturation."xsd:string |
| http://purl.uniprot.org/citations/24704203 | http://purl.uniprot.org/core/volume | "447"xsd:string |
| http://purl.uniprot.org/citations/24704203 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24704203 |
| http://purl.uniprot.org/citations/24704203 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/24704203 |
| http://purl.uniprot.org/uniprot/#_A0A0H3W5H9-mappedCitation-24704203 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24704203 |
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| http://purl.uniprot.org/uniprot/#_A0A0H3W5Q8-mappedCitation-24704203 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24704203 |
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| http://purl.uniprot.org/uniprot/P43320 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/24704203 |
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