The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport

Molecular and Cellular Biology

Volumn 21, Issue 23, 2001, Pages 7944-7955

  Bailer, S M ^a   Balduf, C ^a   Hurt, E ^a  

^a SAARLAND UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; NUCLEAR PROTEIN; NUCLEOPORIN; PROTEIN NSP1P; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CYTOPLASM; DISSOCIATION; GENE MAPPING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT; TEMPERATURE SENSITIVE MUTANT;

ACTIVE TRANSPORT, CELL NUCLEUS; AMINO ACID MOTIFS; CALCIUM-BINDING PROTEINS; CELL NUCLEUS; CYTOPLASM; FUNGAL PROTEINS; MACROMOLECULAR SUBSTANCES; MEMBRANE PROTEINS; MUTAGENESIS, SITE-DIRECTED; NUCLEAR PORE; NUCLEAR PORE COMPLEX PROTEINS; NUCLEAR PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0035158475     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.21.23.7944-7955.2001     Document Type: Article

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