ClpB N-terminal domain plays a regulatory role in protein disaggregation

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 50, 2015, Pages E6872-E6881

  Rosenzweig, Rina ^a,b   Farber, Patrick ^c   Velyvis, Algirdas ^a,b   Rennella, Enrico ^a,b   Latham, Michael P ^d   Kay, Lewis E ^a,b,c   Horwich, Arthur L ^e  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c HOSPITAL FOR SICK CHILDREN   (Canada)

^d TEXAS TECH UNIVERSITY   (United States)

^e YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Chaperones; ClpB; Hsp104; Methyl TROSY NMR; Protein disaggregation

Indexed keywords

ADENOSINE TRIPHOSPHATE; PROTEIN CLPB; TYROSINE; CLPB PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; HEAT SHOCK PROTEIN; PROTEIN BINDING;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; DISSOCIATION CONSTANT; HETERONUCLEAR SINGLE QUANTUM COHERENCE; HYDROLYSIS; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN PURIFICATION; SPECTROSCOPY; THERMUS THERMOPHILUS; TRANSVERSE RELAXATION OPTIMIZED SPECTROSCOPY; CHEMICAL PHENOMENA; CHEMISTRY; ESCHERICHIA COLI; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PHYSIOLOGY;

ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING;

EID: 84950124697     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1512783112     Document Type: Article

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