Interrogation of MDM2 phosphorylation in p53 activation using native chemical ligation: The functional role of Ser17 phosphorylation in MDM2 reexamined

Journal of the American Chemical Society

Volumn 134, Issue 15, 2012, Pages 6855-6864

  Zhan, Changyou ^a   Varney, Kristen ^a   Yuan, Weirong ^a   Zhao, Le ^a   Lu, Wuyuan ^a  

^a UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING DOMAIN; CELLULAR STRESS; FLUORESCENCE POLARIZATION; MOLECULAR MECHANISM; N-TERMINALS; NATIVE CHEMICAL LIGATION; NEGATIVE REGULATORS; PEPTIDE BINDING; PEPTIDE LIGAND; SINGLE SITES; SPECTROSCOPIC TECHNIQUE; STRESS-INDUCED; TRANSACTIVATION ACTIVITY; TUMOR SUPPRESSOR PROTEINS; UBIQUITIN LIGASES;

LIGANDS; PEPTIDES;

PHOSPHORYLATION;

ASPARTIC ACID; PROTEIN MDM2; PROTEIN P53; SERINE;

ARTICLE; CHEMICAL MODIFICATION; CIRCULAR DICHROISM; COMPLEX FORMATION; DISSOCIATION CONSTANT; FLUORESCENCE POLARIZATION; GENE MUTATION; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SURFACE PLASMON RESONANCE; SYNTHESIS;

BINDING SITES; HUMANS; PHOSPHOSERINE; PROTEIN BINDING; PROTO-ONCOGENE PROTEINS C-MDM2; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84859967520     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja301255n     Document Type: Article

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