Identification of prolidase as a high affinity ligand of the ErbB2 receptor and its regulation of ErbB2 signaling and cell growth

Cell Death and Disease

Volumn 5, Issue 5, 2014, Pages

  Yang, L ^a   Li, Y ^a   Zhang, Y ^a  

^a ROSWELL PARK CANCER INSTITUTE   (United States)

Author keywords

ErbB2; ErbB2 ligand; Her2; PEPD; Prolidase

Indexed keywords

DIMER; DNA; EPIDERMAL GROWTH FACTOR RECEPTOR 2; HOMODIMER; MONOMER; PROLINE DIPEPTIDASE;

ANCHORAGE INDEPENDENT GROWTH; ARTICLE; BINDING AFFINITY; CELL GROWTH; CELL INVASION; CELL MIGRATION; CONFOCAL MICROSCOPY; CONTROLLED STUDY; DIMERIZATION; DNA SYNTHESIS; ENZYME ACTIVITY; GENE OVEREXPRESSION; GENE SILENCING; GENETIC TRANSFECTION; IMMUNOFLUORESCENCE; INTERNALIZATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SIGNAL TRANSDUCTION; TARGET CELL; WESTERN BLOTTING;

ANIMALS; BINDING SITES; CELL LINE, TUMOR; CELL MOVEMENT; CELL PROLIFERATION; CHO CELLS; CRICETINAE; CRICETULUS; DIPEPTIDASES; DNA REPLICATION; DOSE-RESPONSE RELATIONSHIP, DRUG; FEMALE; HUMANS; LIGANDS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN MULTIMERIZATION; PROTEOLYSIS; RECEPTOR, ERBB-2; SIGNAL TRANSDUCTION; SRC-FAMILY KINASES; TIME FACTORS; TRANSFECTION;

EID: 84900986976     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2014.187     Document Type: Article

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