Binding of the merlin-i product of the neurofibromatosis type 2 tumour suppressor gene to a novel site in β-fodrin is regulated by association between merlin domains

Biochemical Journal

Volumn 358, Issue 3, 2001, Pages 727-735

  Neill, G W ^a   Crompton, M R ^a  

^a UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

Ezrin radixin moesin; Schwannomin; Spectrin

Indexed keywords

ASSAYS; CLONING; DIMERIZATION; GENES; HYBRID SENSORS; TUMORS; YEAST;

MERLIN DOMAINS;

NEUROLOGY;

BETA FODRIN; EZRIN; FODRIN; GLUTAMIC ACID; LEUCINE; LYSINE; MERLIN; MERLIN 1; MOESIN; PROLINE; RADIXIN; SPECTRIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CANCER INHIBITION; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CYTOSKELETON; DIMERIZATION; EXON; GENE MUTATION; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; IN VITRO STUDY; LEUKEMIA CELL LINE; NEUROFIBROMATOSIS; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; TUMOR SUPPRESSOR GENE;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BINDING SITES; CARRIER PROTEINS; CELL LINE; CLONING, MOLECULAR; GENES, NEUROFIBROMATOSIS 2; HUMANS; MAMMALS; MEMBRANE PROTEINS; MICROFILAMENT PROTEINS; MOLECULAR SEQUENCE DATA; NEUROFIBROMIN 2; PROTEIN BIOSYNTHESIS; PROTEIN ISOFORMS; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; RETICULOCYTES; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECTRIN; TRANSCRIPTION, GENETIC; TRANSFECTION;

EID: 0035884301     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3580727     Document Type: Article

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