S100P is a novel interaction partner and regulator of IQGAP1

Journal of Biological Chemistry

Volumn 286, Issue 9, 2011, Pages 7227-7238

  Heil, Annika ^a   Nazmi, Ali Reza ^a   Koltzscher, Max ^a   Poeter, Michaela ^a   Austermann, Judith ^a   Assard, Nicole ^b   Baudier, Jacques ^b   Kaibuchi, Kozo ^c   Gerke, Volker ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

^b INSERM   (France)

^c NAGOYA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEINS; CELL STIMULATION; CELLULAR TARGETS; CLOSE PROXIMITY; COMPLEX FORMATIONS; CORTICAL CYTOSKELETON; DIRECT INTERACTIONS; DISSOCIATION CONSTANT; EF-HAND; IN-CELL; INTRACELLULAR CA; PLASMA MEMBRANES; PROTEIN TARGETS; SIGNALING CASCADES; TARGET PROTEINS; TYROSINE PHOSPHORYLATION;

AMINO ACIDS; CALCIUM; CELL MEMBRANES; DISSOCIATION; PHOSPHORYLATION; PROTEINS; SIGNAL TRANSDUCTION; SIGNALING;

SCAFFOLDS (BIOLOGY);

B RAF KINASE; CALCIUM ION; EPIDERMAL GROWTH FACTOR; IQ MOTIF CONTAINING GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 2; MUTANT PROTEIN; PROTEIN S 100; PROTEIN S100P; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL MEMBRANE; CELL STIMULATION; COMPLEX FORMATION; CONTROLLED STUDY; DISSOCIATION CONSTANT; DOWN REGULATION; ENZYME ACTIVATION; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; SIGNAL TRANSDUCTION;

CALCIUM-BINDING PROTEINS; CALMODULIN; CELL MEMBRANE; CYTOSKELETON; DIMERIZATION; HELA CELLS; HUMANS; MAP KINASE KINASE 1; MAP KINASE KINASE 2; MAP KINASE SIGNALING SYSTEM; NEOPLASM PROTEINS; PHOSPHORYLATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS B-RAF; RAS GTPASE-ACTIVATING PROTEINS; RECOMBINANT PROTEINS;

EID: 79953220793     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.135095     Document Type: Article

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