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Q34288930-27BB467A-F443-4B62-98DA-315599AE224E
Q34288930-27BB467A-F443-4B62-98DA-315599AE224E
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34288930-27BB467A-F443-4B62-98DA-315599AE224E
Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.
P2860
Q34288930-27BB467A-F443-4B62-98DA-315599AE224E
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34288930-27BB467A-F443-4B62-98DA-315599AE224E
rank
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wasDerivedFrom
ab9e7ccd55e40c5bb0154f77dc62d4a7b3828188
P2860
The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro.