Small heat shock protein IbpB acts as a robust chaperone in living cells by hierarchically activating its multi-type substrate-binding residues

Journal of Biological Chemistry

Volumn 288, Issue 17, 2013, Pages 11897-11906

  Fu, Xinmiao ^a   Shi, Xiaodong ^a,b   Yin, Linxiang ^a   Liu, Jiafeng ^a   Joo, Keehyoung ^c   Lee, Jooyoung ^c   Chang, Zengyi ^a  

^a PEKING UNIVERSITY   (China)

^b XUZHOU MEDICAL UNIVERSITY   (China)

^c Korea Institute for Advanced Study   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH CONDITIONS; HEAT SHOCK TEMPERATURE; MOLECULAR CHAPERONES; SMALL HEAT SHOCK PROTEINS; STRUCTURAL INSIGHTS; SUBSTRATE PROTEINS; SUBSTRATE-BINDING; TEMPERATURE ELEVATION;

AMINO ACIDS; ESCHERICHIA COLI; GENE ENCODING; OLIGOMERIZATION; OLIGOMERS; PROTEINS;

SUBSTRATES;

4 BENZOYLPHENYLALANINE; CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN IBPB; PHENYLALANINE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; HEAT SHOCK; HYDROPHOBICITY; IN VIVO STUDY; LOW TEMPERATURE; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE; RESIDUE ANALYSIS; TEMPERATURE DEPENDENCE;

BINDING SITES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; HEAT-SHOCK RESPONSE; HOT TEMPERATURE; PEPTIDE MAPPING; PROTEIN MULTIMERIZATION;

ESCHERICHIA COLI;

EID: 84876933888     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.450437     Document Type: Article

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