Point mutations in dimerization motifs of the transmembrane domain stabilize active or inactive state of the EphA2 receptor tyrosine kinase

Journal of Biological Chemistry

Volumn 289, Issue 21, 2014, Pages 14955-14964

  Sharonov, George V ^a,b   Bocharov, Eduard V ^a   Kolosov, Peter M ^c   Astapova, Maria V ^a   Arseniev, Alexander S ^a   Feofanov, Alexey V ^a,b  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

^c INSTITUTE OF HIGHER NERVOUS ACTIVITY AND NEUROPHYSIOLOGY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; CELL ADHESION; CELL MEMBRANES; CHEMICAL ACTIVATION; DIMERIZATION; ENZYMES; LIGANDS; SIGNAL TRANSDUCTION;

CYTOPLASMIC DOMAINS; EXTRACELLULAR; HUMAN TISSUES; KINASE ACTIVITY; POINT MUTATIONS; RECEPTOR TYROSINE KINASE; TRANS-MEMBRANE DOMAINS; TRANSMEMBRANE DOMAIN;

AMINO ACIDS;

EPHRIN; EPHRIN RECEPTOR A2;

AMINO ACID SUBSTITUTION; ANTIBODY SPECIFICITY; ARTICLE; CONFOCAL MICROSCOPY; CONTROLLED STUDY; DIMERIZATION; ENZYME ACTIVATION; ENZYME INACTIVATION; FLOW CYTOMETRY; HUMAN; HUMAN CELL; MOLECULAR CLONING; MUTAGENESIS; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SIGNAL TRANSDUCTION;

ALTERNATIVE DIMERIZATION; CELL SURFACE RECEPTOR; EPH RECEPTOR; FLOW CYTOMETRY; MEMBRANE PROTEINS; PROTEIN DOMAINS; RECEPTOR TYROSINE KINASE; TRANSMEMBRANE DOMAIN;

AMINO ACID MOTIFS; BINDING SITES; FLOW CYTOMETRY; HEK293 CELLS; HUMANS; LUMINESCENT PROTEINS; MICROSCOPY, CONFOCAL; MODELS, MOLECULAR; POINT MUTATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; RECEPTOR, EPHA2;

EID: 84901433916     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.558783     Document Type: Article

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