How Hsp70 molecular machines interact with their substrates to mediate diverse physiological functions

Journal of Molecular Biology

Volumn 427, Issue 7, 2015, Pages 1575-1588

  Clerico, Eugenia M ^a   Tilitsky, Joseph M ^a   Meng, Wenli ^a   Gierasch, Lila M ^a  

^a UNIVERSITY OF MASSACHUSETTS   (United States)

Author keywords

chaperone substrates; complex disassembly; disaggregation; Hsp70 molecular chaperone; protein folding

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONIN 60; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; J PROTEIN; PROTEIN DNAJ; UNCLASSIFIED DRUG; LIGAND; PROTEIN BINDING;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; BINDING SITE; CELL MEMBRANE TRANSPORT; HEAT SHOCK RESPONSE; HYDROLYSIS; HYDROPHOBICITY; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN TERTIARY STRUCTURE; PROTEIN TRANSPORT; REVIEW; RIBOSOME; SURFACE CHARGE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; PHYSIOLOGY; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; PROTEIN UNFOLDING;

ANIMALS; HEAT-SHOCK RESPONSE; HSP70 HEAT-SHOCK PROTEINS; HUMANS; LIGANDS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN UNFOLDING;

EID: 84924139172     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2015.02.004     Document Type: Review

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