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

Volumn 104, Issue 7, 2007, Pages 2145-2150

Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones

(3) Park, Eun Sun a,b Fenton, Wayne A c Horwich, Arthur L a,b,c

a YALE UNIVERSITY SCHOOL OF MEDICINE (United States)

b HOWARD HUGHES MEDICAL INSTITUTE (United States)

c SCRIPPS RESEARCH INSTITUTE (United States)

Author keywords

Chaperonin; Protein folding; Topology

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; CIS ACTING ELEMENT; DISULFIDE; SECRETORY PROTEIN; TRYPSINOGEN;

ARTICLE; COMPLEX FORMATION; DISULFIDE BOND; ENCAPSULATION; HYDROPHILICITY; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

ANIMALS; CATTLE; DISULFIDES; GROEL PROTEIN; GROES PROTEIN; MASS SPECTROMETRY; PROTEIN CONFORMATION; PROTEIN FOLDING; TRYPSINOGEN;

EID: 33847777828 PISSN: 00278424 EISSN: None Source Type: Journal
DOI: 10.1073/pnas.0610989104 Document Type: Article

Times cited : (11)

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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.