Folding mechanism of the C-terminal domain of nucleophosmin: Residual structure in the denatured state and its pathophysiological significance

FASEB Journal

Volumn 23, Issue 8, 2009, Pages 2360-2365

  Scaloni, Flavio ^a   Gianni, Stefano ^a   Federici, Luca ^b   Falini, Brunangelo ^c   Brunori, Maurizio ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b UNIVERSITY OF CHIETI   (Italy)

^c UNIVERSITY OF PERUGIA   (Italy)

Author keywords

Acute myeloid leukemia; Ground state effect; Hammond effect; Kinetics; Protein stability

Indexed keywords

NUCLEOPHOSMIN; NUCLEAR PROTEIN; RECOMBINANT PROTEIN;

ACUTE GRANULOCYTIC LEUKEMIA; ARTICLE; MUTANT; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; IN VITRO STUDY; KINETICS; METABOLISM; MUTATION; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; THERMODYNAMICS;

HUMANS; KINETICS; LEUKEMIA, MYELOID, ACUTE; MODELS, MOLECULAR; MUTATION; NUCLEAR PROTEINS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; THERMODYNAMICS;

EID: 68849105588     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.08-128306     Document Type: Article

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