Small nonphosphorylated Grb2-SH2 domain antagonists evaluated by surface plasmon resonance technology

Biopolymers - Peptide Science Section

Volumn 80, Issue 5, 2005, Pages 628-635

  Lung, Feng Di T ^a,b   Chang, Chiung Wen ^b   Chong, Meng Chin ^b   Liou, Chien Chung ^a   Li, Peng ^c   Peach, Megan L ^c   Nicklaus, Marc C ^c   Lou, Bih Show ^d   Roller, Peter P ^c  

^a TUNGHAI UNIVERSITY   (Taiwan)

^b CHINA MEDICAL UNIVERSITY   (Taiwan)

^c NATIONAL CANCER INSTITUTE   (United States)

^d CHANG GUNG UNIVERSITY   (Taiwan)

Author keywords

BIACORE X; Grb2; Peptides; Ras; SH2 domain; Signal transduction pathway; Surface plasmon resonance

Indexed keywords

CELL CULTURE; ENZYME INHIBITION; HYDROGEN BONDS; PROTEINS; SURFACE PLASMON RESONANCE;

BIACORE X; GRB2; RAS; SH2 DOMAIN; SIGNAL TRANSDUCTION PATHWAY;

POLYPEPTIDES;

9 FLUORENYLMETHOXYCARBONYLGLUTAMYLTYROSYL ALPHA AMINOISOBUTYRYLASPARAGINAMIDE; ARGININE; CARBONYL DERIVATIVE; GLUTAMINE; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; PEPTIDE DERIVATIVE; PROTEIN GRB2 SH2 DOMAIN ANTAGONIST; PROTEIN SH2; UNCLASSIFIED DRUG;

ARTICLE; CELL DIFFERENTIATION; CELL PROLIFERATION; DRUG POTENCY; IC 50; INHIBITION KINETICS; MOLECULAR MODEL; ONCOGENE RAS; PEPTIDE SYNTHESIS; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN PURIFICATION; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAIN; SURFACE PLASMON RESONANCE;

DRUG EVALUATION, PRECLINICAL; FLUORENES; MODELS, MOLECULAR; MOLECULAR CONFORMATION; PEPTIDES; PHOSPHORYLATION; SRC HOMOLOGY DOMAINS; STRUCTURE-ACTIVITY RELATIONSHIP; SURFACE PLASMON RESONANCE;

EID: 27944488246     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.20209     Document Type: Article

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