SCOPUS 정보 검색 플랫폼

Archives of Biochemistry and Biophysics

Volumn 531, Issue 1-2, 2013, Pages 80-89

Intrinsically disordered proteins undergo and assist folding transitions in the proteome

(4) Kovacs, D a Szabo, B b Pancsa, R a Tompa, P a,b

a VRIJE UNIVERSITEIT BRUSSEL (Belgium)

b INSTITUTE OF EXPERIMENTAL MEDICINE (Hungary)

Author keywords

Chaperone; Disordered protein; Induced folding; Ubiquitin ligase; Ubiquitin proteasome system; Unstructured protein

Indexed keywords

CHAPERONE; PROTEOME; PROTEIN;

CELL FUNCTION; EMBRYO DEVELOPMENT; MOLECULAR DYNAMICS; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STRUCTURE; QUALITY CONTROL; REVIEW; CHEMICAL STRUCTURE; CHEMISTRY;

MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEINS; PROTEOME;

MLCS; MLOWN;

EID: 84875826727 PISSN: 00039861 EISSN: 10960384 Source Type: Journal
DOI: 10.1016/j.abb.2012.09.010 Document Type: Review

Times cited : (40)

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