Covalent modification of proteins by ADP-ribosylation
- 1 April 1986
- journal article
- Published by Elsevier in Trends in Biochemical Sciences
- Vol. 11 (4) , 171-175
- https://doi.org/10.1016/0968-0004(86)90135-0
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Inhibition of DNA polymerase α, DNA polymerase β, terminal deoxynucleotidyl transferase, and DNA ligase II by poly(ADP-ribosyl)ation reaction in vitroPublished by Elsevier ,2004
- Eukaryotic nuclear ADP-ribosylation reactionsBiochemical Journal, 1985
- Primary structure of elongation factor 2 around the site of ADP‐ribosylation is highly conserved from archaebacteria to eukaryotesFEBS Letters, 1985
- ADP-RIBOSYLATIONAnnual Review of Biochemistry, 1985
- Reduced ribosomal binding of eukaryotic elongation factor 2 following ADP-ribosylation. Difference in binding selectivity between polyribosomes and reconstituted monoribosomesBiochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1985
- Time course of polynucleosome relaxation and ADP‐ribosylationEuropean Journal of Biochemistry, 1985
- ADP‐ribosyltransferase from beef liver which ADP‐ribosylates elongation factor‐2FEBS Letters, 1984
- Regulation of DNA ligase activity by poly(ADP-ribose)Nature, 1982
- Mono(ADP-Ribosyl)transferases and Their Effects on Cellular MetabolismCurrent Topics in Cellular Regulation, 1981
- ADP‐Ribosylation of DNA‐Dependent RNA Polymerase of Escherichia coli by an NAD+: Protein ADP‐ribosyltransferase from Bacteriophage T4European Journal of Biochemistry, 1975