Protein phosphorylation sites regulate the function of the bipartite NLS of nucleolin

European Journal of Cell Biology

Volumn 73, Issue 4, 1997, Pages 287-297

  Schwab, Markus S ^a   Dreyer, Christine ^a  

^a MAX PLANCK INSTITUTE FOR DEVELOPMENTAL BIOLOGY   (Germany)

Author keywords

Cell cycle; Embryogenesis; Nuclear translocation; Nucleolin; Protein phosphorylation; Xenopus laevis

Indexed keywords

HYBRID PROTEIN; MALTOSE BINDING PROTEIN; NUCLEOLIN; PROTEIN KINASE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CELL CYCLE; CONFOCAL LASER MICROSCOPY; CONSENSUS SEQUENCE; CONTROLLED STUDY; CYTOPLASM; DEPHOSPHORYLATION; EMBRYO; EMBRYO DEVELOPMENT; FERTILIZATION; GENE OVEREXPRESSION; NONHUMAN; NUCLEOLUS; OOCYTE DEVELOPMENT; OOCYTE MATURATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN TRANSPORT; XENOPUS LAEVIS;

ANIMALIA; XENOPUS LAEVIS;

EID: 0030799394     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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