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

Volumn 99, Issue 17, 2002, Pages 11085-11090

CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90

(4) Rüdiger, Stefan a Freund, Stefan M V a Veprintsev, Dmitry B a Fersht, Alan R a

a MEDICAL RESEARCH COUNCIL (United Kingdom)

Author keywords

Molecular chaperones; Protein folding; Transcription factors

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 90; PROTEIN P53; TRANSCRIPTION FACTOR;

ARTICLE; CROSS CORRELATED RELAXATION ENHANCED POLARIZATION TRANSFER; HUMAN; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; TUMOR SUPPRESSOR GENE;

BINDING SITES; HSP90 HEAT-SHOCK PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; TUMOR SUPPRESSOR PROTEIN P53;

EID: 0037143625 PISSN: 00278424 EISSN: None Source Type: Journal
DOI: 10.1073/pnas.132393699 Document Type: Article

Times cited : (88)

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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.