The linker of the interferon response factor 3 transcription factor is not unfolded

Biochemistry

Volumn 51, Issue 32, 2012, Pages 6320-6327

  Shukla, Hem ^a   Vaitiekunas, Paulius ^a   Majumdar, Ananya K ^a   Dragan, Anatoly I ^a,b   Dimitriadis, Emilios K ^c   Kotova, Svetlana ^c   Crane Robinson, Colyn ^a,d   Privalov, Peter L ^a  

^a JOHNS HOPKINS UNIVERSITY   (United States)

^b UNIVERSITY OF MARYLAND BALTIMORE COUNTY   (United States)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

^d UNIVERSITY OF PORTSMOUTH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINAL DOMAINS; DIMERIZATION DOMAIN; DNA PROBE; DNA-BINDING; GLOBULAR PROTEINS; INTERFERON RESPONSE; N-TERMINAL DOMAINS; N-TERMINALS; NUCLEAR EXPORT SIGNALS; RECOGNITION SITE; STRUCTURAL DOMAINS; WILD TYPES;

ANTIBIOTICS; ATOMIC FORCE MICROSCOPY; BENDING (DEFORMATION); DIMERS; GLYCOPROTEINS; PHOSPHORYLATION; PLANTS (BOTANY); TRANSCRIPTION FACTORS; VIRUSES;

DNA;

BETA INTERFERON; GLOBULAR PROTEIN; INTERFERON REGULATORY FACTOR 3; NITROGEN 15; TRANSCRIPTION FACTOR;

AMINO TERMINAL SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; DIMERIZATION; DNA BINDING; DNA PROBE; GENE AMPLIFICATION; LIGHT SCATTERING; NONHUMAN; NUCLEAR EXPORT SIGNAL; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN SYNTHESIS; PROTEIN UNFOLDING;

DNA; INTERFERON REGULATORY FACTOR-3; MICROSCOPY, ATOMIC FORCE; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN UNFOLDING;

EID: 84865130246     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300260s     Document Type: Article

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