An invisible ubiquitin conformation is required for efficient phosphorylation by PINK1

EMBO Journal

Volumn 36, Issue 24, 2017, Pages 3555-3572

  Gladkova, Christina ^a   Schubert, Alexander F ^a   Wagstaff, Jane L ^a   Pruneda, Jonathan N ^a   Freund, Stefan MV ^a   Komander, David ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

nuclear magnetic resonance; Parkin; Parkinson's disease; PINK1; ubiquitin phosphorylation

Indexed keywords

PINK1 PROTEIN; PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE; SERINE; UBIQUITIN; UNCLASSIFIED DRUG; PTEN-INDUCED PUTATIVE KINASE;

ARTICLE; BETA SHEET; CHEMICAL EXCHANGE SATURATION TRANSFER; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME SUBSTRATE; NUCLEAR MAGNETIC RESONANCE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; UBIQUITINATION; CHEMISTRY; CONFORMATION; CRYSTALLIZATION; ENZYME SPECIFICITY; GENETICS; HUMAN; METABOLISM; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHORYLATION; PROTEIN DOMAIN; PROTEIN STABILITY; STRUCTURAL MODEL;

CRYSTALLIZATION; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MODELS, STRUCTURAL; MOLECULAR CONFORMATION; PHOSPHORYLATION; POINT MUTATION; PROTEIN DOMAINS; PROTEIN KINASES; PROTEIN STABILITY; SUBSTRATE SPECIFICITY; UBIQUITIN;

EID: 85033707007     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201797876     Document Type: Article

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