Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts

RNA

Volumn 14, Issue 2, 2008, Pages 297-309

  Portnoy, Victoria ^a   Palnizky, Gili ^a   Yehudai Resheff, Shlomit ^a   Glaser, Fabian ^a   Schuster, Gadi ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

Human; Phosphorolysis; PNPase; Polyadenylation; RNA degradation

Indexed keywords

BACTERIAL ENZYME; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE;

ARTICLE; CHLOROPLAST; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; ESCHERICHIA COLI; HUMAN; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; RNA BINDING; RNA METABOLISM; STREPTOMYCES ANTIBIOTICUS; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; CHLOROPLASTS; CONSERVED SEQUENCE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; EXORIBONUCLEASES; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; PHOSPHATES; PLANT PROTEINS; POLYADENYLATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; RNA, MESSENGER; SPINACIA OLERACEA;

ARCHAEA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PROKARYOTA;

EID: 38649100934     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.698108     Document Type: Article

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