Decreasing the homodimer interaction: A common mechanism shared by the δG91 mutation and deamidation in βA3-crystallin

Molecular Vision

Volumn 16, Issue , 2010, Pages 438-444

  Xu, Jianzhen ^a   Wong, Chiwai ^b   Tan, Xiaorong ^a   Jing, Hongjuan ^a   Zhou, Guangzhou ^a   Song, Wei ^a  

^a HENAN UNIVERSITY OF TECHNOLOGY   (China)

^b GUANGZHOU INSTITUTES OF BIOMEDICINE AND HEALTH   (China)

Author keywords

[No Author keywords available]

Indexed keywords

BETA A3 CRYSTALLIN; CRYSTALLIN; GLUTAMIC ACID; HOMODIMER; LUCIFERASE; MUTANT PROTEIN; UNCLASSIFIED DRUG; AMIDE; BETA CRYSTALLIN; CRYBA1 PROTEIN, HUMAN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BIOINFORMATICS; CATARACT; COMPUTER MODEL; CONGENITAL CATARACT; CONTROLLED STUDY; DEAMINATION; ENZYME ASSAY; GENE DELETION; GENE MUTATION; GENETIC TRANSFECTION; HELA CELL; HYDROPHOBICITY; MOLECULAR CLONING; PATHOGENESIS; PLASMID; PREDICTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; SENILE CATARACT; SITE DIRECTED MUTAGENESIS; TWO HYBRID SYSTEM; ANIMAL; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; MOUSE; MUTATION; PROTEIN BINDING; PROTEIN MULTIMERIZATION;

AMIDES; AMINO ACID SEQUENCE; ANIMALS; BETA-CRYSTALLIN A CHAIN; HELA CELLS; HUMANS; HYDROPHOBICITY; LUCIFERASES; MICE; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; MUTATION; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY;

EID: 77952308046     PISSN: None     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article

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