The role of the conserved COOH-terminal triad in αA-crystallin aggregation and functionality

Molecular Vision

Volumn 13, Issue , 2007, Pages 1758-1768

  Li, Ying ^a   Schmitz, Karl R ^b   Salerno, John C ^a   Koretz, Jane F ^a  

^a RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; AMMONIA; CHAPERONE; DIMER; DITHIOTHREITOL; INSULIN; MONOMER; OLIGOMER; TETRAMER;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; COW; FAST PROTEIN LIQUID CHROMATOGRAPHY; GEL ELECTROPHORESIS; GENE DELETION; GENE OVEREXPRESSION; HYDROPHOBICITY; MOLECULAR WEIGHT; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN QUATERNARY STRUCTURE; SITE DIRECTED MUTAGENESIS; STEADY STATE; TRANSITION TEMPERATURE; WILD TYPE;

ALPHA-CRYSTALLIN A CHAIN; AMINO ACID MOTIFS; ANIMALS; CATTLE; CHROMATOGRAPHY, GEL; CONSERVED SEQUENCE; ELECTROPHORESIS; MOLECULAR CHAPERONES; MUTATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; TEMPERATURE;

EID: 34848908677     PISSN: None     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article

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