The N-terminal basic domain of human parvulin h Par14 is responsible for the entry to the nucleus and high-affinity DNA-binding

Journal of Molecular Biology

Volumn 321, Issue 2, 2002, Pages 235-247

  Surmacz, Tatiana Anna ^a   Bayer, Elena ^b   Rahfeld, Jens Ulrich ^a   Fischer, Gunter ^a   Bayer, Peter ^b  

^a MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

^b MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

Cell cycle; DNA binding; HMG proteins; NMR; Parvulin

Indexed keywords

AMINO ACID; CELLULOSE; CYCLOPHILIN; DOUBLE STRANDED DNA; GREEN FLUORESCENT PROTEIN; LYSINE; MUTANT PROTEIN; SERINE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CELL ACTIVITY; CELL NUCLEUS; CONTROLLED STUDY; DNA BINDING; FEMALE; FLUORESCENCE ANALYSIS; GENE CONSTRUCT; GENE DELETION; GENETIC SIMILARITY; HELA CELL; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; LABORATORY TEST; MOLECULE; NONHUMAN; NUCLEAR LOCALIZATION SIGNAL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY; TARGET CELL; TITRIMETRY;

EID: 0036382919     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00615-0     Document Type: Article

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