Structure-activity relationships of peptidomimetics that inhibit PPI of HER2-HER3

Biopolymers

Volumn 101, Issue 6, 2014, Pages 693-702

  Kanthala, Shanthi ^a   Gauthier, Ted ^b   Satyanarayanajois, Seetharama ^a  

^a UNIVERSITY OF LOUISIANA AT MONROE   (United States)

^b LOUISIANA STATE UNIVERSITY AGRICULTURAL CENTER   (United States)

Author keywords

breast cancer; docking; enzyme fragment complementation assay; HER2; lung cancer; peptidomimetic; protein protein interaction

Indexed keywords

AMINO ACIDS; BIOLOGICAL ORGANS; CELL CULTURE; CELLS; DISEASES; DOCKING; FUNCTIONAL GROUPS; PROTEINS;

BREAST CANCER; FRAGMENT COMPLEMENTATION; HER2; LUNG CANCER; PEPTIDOMIMETICS; PROTEIN-PROTEIN INTERACTIONS;

ENZYME INHIBITION;

AMIDE; DEXTRO AMINO ACID; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; FUNCTIONAL GROUP; PEPTIDOMIMETIC AGENT; PROTEIN HER3; UNCLASSIFIED DRUG; EPIDERMAL GROWTH FACTOR RECEPTOR 3; PEPTIDE; PROTEIN BINDING;

AMINO TERMINAL SEQUENCE; ANTIPROLIFERATIVE ACTIVITY; ARTICLE; ASSAY; BREAST CANCER; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CYCLIZATION; DIMERIZATION; DRUG CONFORMATION; ENZYME FRAGMENT COMPLEMENTATION ASSAY; HUMAN; HUMAN CELL; LUNG CANCER; MOLECULAR DOCKING; OVARY CANCER; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROXIMITY LIGATION ASSAY; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; WESTERN BLOTTING; AMINO ACID SEQUENCE; BINDING COMPETITION; BIOASSAY; CELL PROLIFERATION; CHEMISTRY; DRUG EFFECTS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION; PROTEIN MULTIMERIZATION; SYNTHESIS; TUMOR CELL LINE;

AMINO ACID SEQUENCE; BINDING, COMPETITIVE; BIOLOGICAL ASSAY; BLOTTING, WESTERN; CELL LINE, TUMOR; CELL PROLIFERATION; HUMANS; MOLECULAR DOCKING SIMULATION; MOLECULAR SEQUENCE DATA; PEPTIDES; PEPTIDOMIMETICS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN MULTIMERIZATION; RECEPTOR, ERBB-2; RECEPTOR, ERBB-3; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84897052943     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.22441     Document Type: Article

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