Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domain

Proteins: Structure, Function and Genetics

Volumn 60, Issue 3, 2005, Pages 558-560

  Shaw, Alison Z ^a   Martin Malpartida, Pau ^a   Morales, Begoña ^a   Yraola, Francesc ^b   Royo, Miriam ^b   Macias, Maria J ^a  

^a INSTITUCIÓ CATALANA DE RECERCA I ESTUDIS AVANÇATS ICREA   (Spain)

^b NONE   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

SERINE; THREONINE; UBIQUITIN PROTEIN LIGASE ITCH 3; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; BIOPHYSICS; MAGNETIC RESONANCE SPECTROSCOPY; MICE; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEOMICS; SERINE; THREONINE; UBIQUITIN-PROTEIN LIGASES;

EID: 23044476102     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20466     Document Type: Article

References (20)

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