Study of MDM2 binding to p53-analogues: Affinity, helicity, and applicability to drug design

Journal of Chemical Information and Modeling

Volumn 49, Issue 4, 2009, Pages 865-876

  Kalid, Ori ^a   Ben Tal, Nir ^a  

^a TEL AVIV UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; HYDROGEN BONDS; PHOSPHORYLATION; SOLVENTS;

CONFORMATIONAL ENSEMBLE; EXPLICIT SOLVENTS; HYDROPHOBIC PACKING; PEPTIDOMIMETIC DRUGS; PROTEIN-PROTEIN INTERACTIONS; PROTOCOL OPTIMIZATION; TECHNICAL ASPECTS; TUMOR SUPPRESSOR PROTEINS;

PROTEINS;

AMINO ACID; PEPTIDE; PROTEIN MDM2; PROTEIN P53;

ALGORITHM; AMINO ACID SUBSTITUTION; ARTICLE; BIOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; DRUG DESIGN; ENERGY TRANSFER; GENETICS; METABOLISM; MOLECULAR MIMICRY; MUTATION; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE;

ALGORITHMS; AMINO ACID SUBSTITUTION; AMINO ACIDS; COMPUTATIONAL BIOLOGY; DRUG DESIGN; ENERGY TRANSFER; MODELS, MOLECULAR; MOLECULAR MIMICRY; MUTATION; PEPTIDES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTO-ONCOGENE PROTEINS C-MDM2; TUMOR SUPPRESSOR PROTEIN P53;

EID: 66149113939     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/ci800352c     Document Type: Article

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