EphA2 receptor unliganded dimers suppress EphA2 pro-tumorigenic signaling

Journal of Biological Chemistry

Volumn 290, Issue 45, 2015, Pages 27271-27279

  Singh, Deo R ^a   Ahmed, Fozia ^a   King, Christopher ^b   Gupta, Nisha ^a   Salotto, Matt ^a   Pasquale, Elena B ^c   Hristova, Kalina ^a,b  

^a Johns Hopkins University   (United States)

^b JOHNS HOPKINS UNIVERSITY   (United States)

^c BURNHAM INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; DIMERS; DISEASES; ENZYMES; LIGANDS;

CELL MIGRATION; EPHRIN LIGANDS; MECHANISM MODEL; OVER-EXPRESSION; RECEPTOR TYROSINE KINASE; THERAPEUTIC STRATEGY; TYROSINE PHOSPHORYLATION; WILD TYPES;

PHOSPHORYLATION;

EPHRIN A5; EPHRIN RECEPTOR A2; LIGAND; ONCOPROTEIN;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELL MIGRATION; CONTROLLED STUDY; DIMERIZATION; LIGAND BINDING; OSMOTIC STRESS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SIGNAL TRANSDUCTION; AMINO ACID SUBSTITUTION; CELL MOTION; CHEMISTRY; GENETICS; HEK293 CELL LINE; HUMAN; METABOLISM; OSMOTIC PRESSURE; PHOSPHORYLATION; PROTEIN DOMAIN; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; CELL MOVEMENT; HEK293 CELLS; HUMANS; LIGANDS; MUTAGENESIS, SITE-DIRECTED; ONCOGENE PROTEINS; OSMOTIC PRESSURE; PHOSPHORYLATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; RECEPTOR, EPHA2; SIGNAL TRANSDUCTION;

EID: 84946599580     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.676866     Document Type: Article

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