The mammalian small heat-shock protein Hsp20 forms dimers and is a poor chaperone

European Journal of Biochemistry

Volumn 258, Issue 3, 1998, Pages 1014-1021

  Van De Klundert, Francy A J M ^a   Smulders, Ronald H P H ^a   Gijsen, Mariken L J ^a,b   Lindner, Robyn A ^b   Jaenicke, Rainer ^c   Carver, John A ^b   De Jong, Wilfried W ^a  

^a RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

^b UNIVERSITY OF WOLLONGONG   (Australia)

^c UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Chaperone like activity; Dimer; Oligomer; Protein structure; Small heat shock protein

Indexed keywords

CHAPERONE; DIMER; HEAT SHOCK PROTEIN;

ARTICLE; ESCHERICHIA COLI; MAMMAL; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; DIMERIZATION; DNA, COMPLEMENTARY; ESCHERICHIA COLI; HEAT-SHOCK PROTEINS; HSP20 HEAT-SHOCK PROTEINS; HUMANS; MICE; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MYOCARDIUM; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PHOSPHOPROTEINS; RATS; RECOMBINANT PROTEINS;

ESCHERICHIA COLI; MAMMALIA;

EID: 0032535631     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2581014.x     Document Type: Article

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