Composite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCF Cdc4 ubiquitin ligase

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 9, 2012, Pages 3287-3292

  Tang, Xiaojing ^a   Orlicky, Stephen ^a   Mittag, Tanja ^b,e   Csizmok, Veronika ^b   Pawson, Tony ^a,c   Forman Kay, Julie D ^b,c   Sicheri, Frank ^a,c   Tyers, Mike ^a,d  

^a MOUNT SINAI HOSPITAL   (Canada)

^b HOSPITAL FOR SICK CHILDREN   (Canada)

^c UNIVERSITY OF TORONTO   (Canada)

^d INSTITUTE FOR RESEARCH IN IMMUNOLOGY AND CANCER   (Canada)

^e ST JUDE CHILDREN S RESEARCH HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CDC 4 ENZYME; CYCLIN DEPENDENT KINASE INHIBITOR; CYCLIN DEPENDENT KINASE INHIBITOR SIC 1; EPITOPE; F BOX PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME PHOSPHORYLATION; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; UBIQUITINATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; CELL CYCLE PROTEINS; CONSENSUS SEQUENCE; CYCLIN-DEPENDENT KINASE INHIBITOR PROTEINS; F-BOX PROTEINS; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN INTERACTION MAPPING; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; STATIC ELECTRICITY; SURFACE PLASMON RESONANCE; UBIQUITIN-PROTEIN LIGASES;

EID: 84857698871     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1116455109     Document Type: Article

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