Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity

Biochemical and Biophysical Research Communications

Volumn 412, Issue 1, 2011, Pages 115-120

  Bao, Baolong ^a,b   Wijeratne, Subhashinee S K ^a   Rodriguez Melendez, Rocio ^a   Zempleni, Janos ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^b SHANGHAI OCEAN UNIVERSITY   (China)

Author keywords

Biotin; Carboxylases; Holocarboxylase synthetase; Nucleus; Translation

Indexed keywords

CARBOXYLYASE; METHIONINE 58; METHIONINE DERIVATIVE; MULTIPROTEIN COMPLEX; RECOMBINANT HOLOCARBOXYLASE SYNTHETASE; UNCLASSIFIED DRUG;

ARTICLE; BIOTINYLATION; CATALYSIS; CELL NUCLEUS; CELL STRAIN HEK293; CONFOCAL MICROSCOPY; CONTROLLED STUDY; CYTOPLASM; EPIGENETICS; HUMAN; HUMAN CELL; IN VITRO STUDY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; WESTERN BLOTTING;

CARBON-NITROGEN LIGASES; CATALYSIS; CELL NUCLEUS; HEK293 CELLS; HUMANS; METHIONINE; NUCLEAR PROTEINS; PEPTIDE CHAIN INITIATION, TRANSLATIONAL; RECOMBINANT PROTEINS;

EID: 80051783353     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.07.055     Document Type: Article

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