The last twenty residues in the head domain of mouse lamin A contain important structural elements for formation of head-to-tail polymers in vitro

Bioscience, Biotechnology and Biochemistry

Volumn 71, Issue 5, 2007, Pages 1252-1259

  Isobe, Kazuhiro ^a   Gohara, Rumi ^a   Ueda, Toshihisa ^a   Takasaki, Yozo ^a   Ando, Shoji ^a  

^a SAGA UNIVERSITY   (Japan)

Author keywords

Cytoskeleton; Head to tail polymer; Intermediate filaments; Lamin A

Indexed keywords

AMINO ACIDS; ELECTRON MICROSCOPY; MUTAGENESIS; PHOSPHORYLATION; POLYMERIZATION; RATS;

CYTOSKELETON; HEAD-TO-TAIL POLYMERS; INTERMEDIATE FILAMENTS; LAMIN A; MUTANTS;

PROTEINS;

CYCLIN DEPENDENT KINASE 1; INTERMEDIATE FILAMENT PROTEIN; LAMIN A; POLYMER; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BACTERIUM; CHEMICAL MODEL; CHEMISTRY; GENE DELETION; GENE VECTOR; GENETICS; IN VITRO STUDY; METABOLISM; MOLECULAR GENETICS; MOUSE; PHOSPHORYLATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; ULTRASTRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; BACTERIA; CDC2 PROTEIN KINASE; GENE DELETION; GENETIC VECTORS; INTERMEDIATE FILAMENT PROTEINS; LAMIN TYPE A; MICE; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; POLYMERS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 34347398102     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60674     Document Type: Article

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