Mechanism of an ATP-independent Protein Disaggregase: II. Distinct molecular interactions drive multiple steps during aggregate disassembly

Journal of Biological Chemistry

Volumn 288, Issue 19, 2013, Pages 13431-13445

  Jaru Ampornpan, Peera ^a,c   Liang, Fu Cheng ^a   Nisthal, Alex ^b   Nguyen, Thang X ^a   Wang, Pengcheng ^a   Shen, Kuang ^a   Mayo, Steven L ^b   Shan, Shu Ou ^a  

^a California Institute of Technology   (United States)

^b CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^c NATIONAL SCIENCE AND TECHNOLOGY DEVELOPMENT AGENCY   (Thailand)

Author keywords

[No Author keywords available]

Indexed keywords

ANALOGOUS SYSTEMS; DESIGN EFFORT; DISAGGREGATION; MEMBRANE PROTEINS; PROTEIN AGGREGATES; SUBSTRATE BINDING; TARGET PROTEINS;

BINDING ENERGY; BIOLOGICAL MEMBRANES; PROTEINS;

AGGREGATES;

ADENOSINE TRIPHOSPHATE; CHAPERONE; CHLOROPLAST SIGNAL RECOGNITION PARTICLE 43 PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENERGY TRANSFER; ENZYME BINDING; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; HYDROPHOBICITY; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FUNCTION; PROTEIN MOTIF; STRUCTURE ACTIVITY RELATION; SURFACE PROPERTY;

ATP-INDEPENDENT DISAGGREGASE; ENZYME MECHANISMS; KINETICS; MEMBRANE PROTEINS; MOLECULAR CHAPERONE; MUTAGENESIS MECHANISMS; PROTEIN AGGREGATION; PROTEIN BIOGENESIS; SIGNAL RECOGNITION PARTICLE;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARABIDOPSIS PROTEINS; FLUORESCENCE POLARIZATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; KINETICS; LIGHT-HARVESTING PROTEIN COMPLEXES; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; PROTEIN UNFOLDING; SEQUENCE DELETION; SIGNAL RECOGNITION PARTICLE; SUBSTRATE SPECIFICITY; SURFACE PROPERTIES; THERMODYNAMICS;

EID: 84877692332     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.462861     Document Type: Article

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