Collapsin response mediator proteins (CRMPs) are a new class of microtubule-associated protein (MAP) that selectively interacts with assembled microtubules via a taxol-sensitive binding interaction

Journal of Biological Chemistry

Volumn 286, Issue 48, 2011, Pages 41466-41478

  Lin, Pao Chun ^b   Chan, Perry M ^a   Hall, Christine ^c   Manser, Ed ^a,b  

^a Neuroscience Research Partnership   (Singapore)

^b INSTITUTE OF MEDICAL BIOLOGY   (Singapore)

^c UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING INTERACTION; BINDING MOTIF; C-TERMINAL REGIONS; CELL-BASED ASSAYS; EPOTHILONES; GLYCOGEN SYNTHASE KINASE-3; IN-VITRO ASSAYS; IN-VIVO; MICROTUBULE ASSOCIATED PROTEIN; MICROTUBULES; MODE OF ACTION; MULTIPLE GENES; NEURODEGENERATION; SPINDLE POSITION;

ACTIVATION ANALYSIS; ASSAYS; BINDING ENERGY; CELLS; ENZYMES; GENES;

PROTEINS;

COLLAPSIN RESPONSE MEDIATOR PROTEIN; COLLAPSIN RESPONSE MEDIATOR PROTEIN 1; COLLAPSIN RESPONSE MEDIATOR PROTEIN 2; EPOTHILONE B; GLYCOGEN SYNTHASE KINASE 3BETA; MICROTUBULE ASSOCIATED PROTEIN; PACLITAXEL; UNCLASSIFIED DRUG;

ANAPHASE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DEPOLYMERIZATION; ENZYME ACTIVITY; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; MICROTUBULE; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION; UPREGULATION;

AMINO ACID MOTIFS; ANAPHASE; ANIMALS; CERCOPITHECUS AETHIOPS; COS CELLS; EPOTHILONES; GLYCOGEN SYNTHASE KINASE 3; INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS; MICE; MICROTUBULE-ASSOCIATED PROTEINS; MICROTUBULES; MITOTIC SPINDLE APPARATUS; NERVE TISSUE PROTEINS; NIH 3T3 CELLS; PACLITAXEL; PROTEIN STRUCTURE, TERTIARY; RATS; SEMAPHORIN-3A; TUBULIN MODULATORS;

EID: 82355184535     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.283580     Document Type: Article

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