Chaperone-like activity of α-crystallin is enhanced by high-pressure treatment

Biochemical Journal

Volumn 370, Issue 3, 2003, Pages 859-866

  Böde, Csaba ^a   Tölgyesi, Ferenc G ^a   Smeller, Laśzló ^a   Heremans, Karel ^b   Avilov, Sergiy V ^c   Fidy, Judit ^a  

^a SEMMELWEIS UNIVERSITY   (Hungary)

^b UNIVERSITY OF LEUVEN   (Belgium)

^c PALLADIN INSTITUTE OF BIOCHEMISTRY   (Ukraine)

Author keywords

crystallin; Chaperone activity; High pressure; Small heat shock protein

Indexed keywords

FLUORESCENCE; HYDROPHOBICITY; HYDROSTATIC PRESSURE; INFRARED SPECTROSCOPY; LIGHT SCATTERING; OLIGOMERS; RELAXATION PROCESSES;

OLIGOMERIC PROTEINS;

PROTEINS;

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ALPHA CRYSTALLIN; CHAPERONE; DITHIOERYTHRITOL; HEAT SHOCK PROTEIN; INSULIN; OLIGOMER; PROTEIN SUBUNIT; TRYPTOPHAN;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CALCULATION; CONTROLLED STUDY; DISSOCIATION; FLUORESCENCE SPECTROSCOPY; HEATING; HYDROPHOBICITY; HYDROSTATIC PRESSURE; INFRARED SPECTROSCOPY; LENS; LIGHT SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PUBLICATION; RELAXATION TIME; STRUCTURE ACTIVITY RELATION; SURFACE PROPERTY;

ALPHA-CRYSTALLINS; ANIMALS; CATTLE; HYDROSTATIC PRESSURE; MOLECULAR CHAPERONES; PROTEIN CONFORMATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE; TIME FACTORS; TRYPTOPHAN;

ANIMALIA; VERTEBRATA;

EID: 0037444760     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021097     Document Type: Article

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