Phosphorylation in intrinsically disordered regions regulates the activity of Neurogenin2

BMC Biochemistry

Volumn 15, Issue 1, 2014, Pages

  McDowell, Gary S ^a,c   Hindley, Christopher J ^a,d   Lippens, Guy ^b   Landrieu, Isabelle ^b   Philpott, Anna ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITÉ DES SCIENCES ET TECHNOLOGIES DE LILLE   (France)

^c TUFTS UNIVERSITY   (United States)

^d UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

bHLH proteins; Intrinsic disorder; Neurogenin; Phosphorylation; Protein folding; Protein NMRr; Protein stability; Transcription factor; Xenopus laevis

Indexed keywords

BASIC HELIX LOOP HELIX TRANSCRIPTION FACTOR; CYCLIN DEPENDENT KINASE; INTRINSICALLY DISORDERED PROTEIN; NEUROGENIN 2; NERVE PROTEIN; NGN2 PROTEIN, XENOPUS; XENOPUS PROTEIN;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; EMBRYO; EMBRYO DEVELOPMENT; GENE MUTATION; HYDROPHOBICITY; IN VITRO STUDY; NERVE CELL DIFFERENTIATION; NERVOUS SYSTEM DEVELOPMENT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PHOSPHORYLATION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; XENOPUS LAEVIS; ANIMAL; CHEMISTRY; METABOLISM; PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN TERTIARY STRUCTURE;

XENOPUS LAEVIS;

ANIMALS; INTRINSICALLY DISORDERED PROTEINS; NERVE TISSUE PROTEINS; NEUROGENESIS; PHOSPHORYLATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; XENOPUS LAEVIS; XENOPUS PROTEINS;

EID: 84920774603     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/s12858-014-0024-3     Document Type: Article

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