The native oligomeric organization of alpha-crystallin, is it necessary for its chaperone function?

Experimental Eye Research

Volumn 79, Issue 6, 2004, Pages 817-821

  Horwitz, Joseph ^a   Huang, Qingling ^a   Ding, Linlin ^a  

^a JULES STEIN EYE INSTITUTE   (United States)

Author keywords

aggregation; alpha crystallin; chaperones; citraconylation; small heat shock proteins

Indexed keywords

ALPHA CRYSTALLIN; ALPHA LACTALBUMIN; CHAPERONE; MALATE DEHYDROGENASE;

CHEMICAL MODIFICATION; CONCENTRATION RESPONSE; CONFERENCE PAPER; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN STRUCTURE; STATISTICAL SIGNIFICANCE;

ALPHA-CRYSTALLIN A CHAIN; ALPHA-CRYSTALLIN B CHAIN; ALPHA-CRYSTALLINS; ANIMALS; CITRACONIC ANHYDRIDES; MOLECULAR CHAPERONES; MOLECULAR WEIGHT; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 11844274723     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2004.05.007     Document Type: Conference Paper

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