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Q37695350-98C7850B-9AC2-440B-9E6E-C0688AB4AC53
Q37695350-98C7850B-9AC2-440B-9E6E-C0688AB4AC53
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http://www.wikidata.org/entity/statement/Q37695350-98C7850B-9AC2-440B-9E6E-C0688AB4AC53
The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes.
P2860
Q37695350-98C7850B-9AC2-440B-9E6E-C0688AB4AC53
BestRank
Statement
http://www.wikidata.org/entity/statement/Q37695350-98C7850B-9AC2-440B-9E6E-C0688AB4AC53
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7ec91e0d93b0626894c6b425276f7ea558cf4f34
P2860
The chaperone proteins HSP70, HSP40/DnaJ and GRP78/BiP suppress misfolding and formation of β-sheet-containing aggregates by human amylin: a potential role for defective chaperone biology in Type 2 diabetes.