The N-terminal K homology domain of the poly(rC)-binding protein is a major determinant for binding to the poliovirus 5'-untranslated region and acts as an inhibitor of viral translation

Journal of Biological Chemistry

Volumn 274, Issue 53, 1999, Pages 38163-38170

  Silvera, Deborah ^a   Gamarnik, Andrea V ^a   Andino, Raul ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; ARTICLE; COMPLEX FORMATION; COMPUTER MODEL; HUMAN; HUMAN CELL; POLIOMYELITIS VIRUS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; RECEPTOR AFFINITY; REPORTER GENE; RNA REPLICATION; SEQUENCE HOMOLOGY; TRANSLATION REGULATION; VIRUS INHIBITION; VIRUS TRANSCRIPTION; XENOPUS LAEVIS;

5' UNTRANSLATED REGIONS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BASE SEQUENCE; BINDING SITES; DNA PRIMERS; DNA-BINDING PROTEINS; HELA CELLS; HETEROGENEOUS-NUCLEAR RIBONUCLEOPROTEINS; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; POLIOVIRUS; PROTEIN BIOSYNTHESIS; RIBOSOMES; RNA, VIRAL; RNA-BINDING PROTEINS; TRANSCRIPTION FACTORS;

ANIMALIA; DNA VIRUSES; POLIOVIRUS; XENOPUS LAEVIS;

EID: 0033621483     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.53.38163     Document Type: Article

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