The human mitochondrial transcription termination factor (mTERF) is fully active in vitro in the non-phosphorylated form

Journal of Biological Chemistry

Volumn 280, Issue 27, 2005, Pages 25499-25505

  Asin Cayuela, Jordi ^a   Schwend, Thomas ^a   Farge, Géraldine ^a   Gustafsson, Claes M ^a  

^a KAROLINSKA UNIVERSITY HOSPITAL   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; ELECTROPHORESIS; MONOMERS; POLYMERIZATION; PROTEINS; RNA;

ELECTROSPRAY; MITOCHONDRIAL TRANSCRIPTION; MITOCHONDRIAL TRANSCRIPTION TERMINATION FACTORS (MTERF);

BIOCHEMISTRY;

CELL PROTEIN; MITOCHONDRIAL DNA; MITOCHONDRIAL TRANSCRIPTION TERMINATION FACTOR; MONOMER; RNA 16S; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; ELECTROSPRAY MASS SPECTROMETRY; GENE ACTIVITY; GENE SEQUENCE; IN VITRO STUDY; INSECT CELL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN POLYMERIZATION; PROTEIN PROCESSING; PROTEIN STABILITY; PROTEIN STRUCTURE; RNA GENE; RNA TRANSCRIPTION; STRUCTURE ANALYSIS; TRANSCRIPTION TERMINATION; TWO DIMENSIONAL ELECTROPHORESIS;

ANIMALS; BASIC-LEUCINE ZIPPER TRANSCRIPTION FACTORS; CELLS, CULTURED; HUMANS; MITOCHONDRIA; MOLECULAR WEIGHT; PHOSPHORYLATION; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPODOPTERA; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC;

INSECTA;

EID: 21844466466     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M501145200     Document Type: Article

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