Structural instability caused by a mutation at a conserved arginine in the α-crystallin domain of Chinese hamster heat shock protein 27

Cell Stress and Chaperones

Volumn 10, Issue 2, 2005, Pages 157-166

  Chávez Zobel, Aura T ^a   Lambert, Herman ^b   Thériault, Jimmy R ^b   Landry, Jacques ^b  

^a UNIVERSIDAD CENTROCCIDENTAL LISANDRO ALVARADO   (Venezuela)

^b LAVAL UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; ARGININE; CHAPERONE; GLUTARALDEHYDE; GLYCEROL; GLYCINE; HEAT SHOCK PROTEIN 27; MUTANT PROTEIN; RECOMBINANT PROTEIN; SERINE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CELL STRAIN 3T3; CHINESE HAMSTER; CONTROLLED STUDY; GEL PERMEATION CHROMATOGRAPHY; GENETIC DISORDER; IMMUNOFLUORESCENCE; IN VITRO STUDY; IN VIVO STUDY; MOUSE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; ARGININE; CONSERVED SEQUENCE; CRICETINAE; CRICETULUS; FLUORESCENT ANTIBODY TECHNIQUE; GLUTARAL; GLYCEROL; HEAT-SHOCK PROTEINS; INCLUSION BODIES; MICE; MICROSCOPY, CONFOCAL; MOLECULAR CHAPERONES; POINT MUTATION; TIME FACTORS;

CRICETULUS GRISEUS;

EID: 21744448008     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1379/CSC-102.1     Document Type: Article

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