Intrinsic disorder is a key characteristic in partners that bind 14-3-3 proteins

Proteins: Structure, Function and Genetics

Volumn 63, Issue 1, 2006, Pages 35-42

  Bustos, Diego M ^a   Iglesias, Alberto A ^b  

^a INSTITUTO DE INVESTIGACIONES BIOTECNOLÓGICAS   (Argentina)

^b UNIVERSIDAD NACIONAL DEL LITORAL   (Argentina)

Author keywords

14 3 3 binding site; Intrinsically disordered protein; Protein protein interaction

Indexed keywords

CHAPERONE; PROTEIN 14 3 3; RNA; TRANSCRIPTION FACTOR; TUMOR PROTEIN;

ARTICLE; BINDING AFFINITY; BINDING SITE; CELL METABOLISM; CELL STRUCTURE; CLASSIFICATION; CONSENSUS SEQUENCE; ENTROPY; PLEIOTROPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; THERMODYNAMICS;

14-3-3 PROTEINS; ANIMALS; BINDING SITES; CAENORHABDITIS ELEGANS; COMPUTATIONAL BIOLOGY; DROSOPHILA MELANOGASTER; HUMANS; MODELS, MOLECULAR; MODELS, THEORETICAL; MOLECULAR CONFORMATION; PHOSPHORYLATION; POLYOMAVIRUS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEOMICS; RNA; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 33645034035     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20888     Document Type: Article

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