In vitro poly(ADP-ribosyl)ation of seminal ribonuclease.

PolyADP-ribosylation is involved in neurotrophic activity.

PolyADP-ribosylation is a transient posttranslational modification of proteins, mainly catalyzed by poly(ADP-ribose)polymerase-1 (PARP-1). This highly conserved nuclear protein is activated rapidly in response to DNA nick formation and promotes a fast DNA repair. Here, we examine a possible association between polyADP-ribosylation and the activity of neurotrophins and neuroprotective peptides t...

PolyADP-Ribosylation in Postfertilization and Genome Reprogramming: Implications for Carcinogenesis

Structure and properties of seminal ribonuclease.

Brand, R. C. & Planta, R. J. (1975) Mol. Biol. Rep. 2, 321-325 Klootwijk, J. & Planta, R. J. (1973) Eur. J. Biochem. 39, 325-333 Maden, B. E. H. & Salim, M. (1974) J. Mol. Biol. 88, 133-164 Maden, B. E. H., Forbes, J., De Jonge, P. & Klootwijk, J. (1975) FEBSLerr. 59,60-63 Perry, R. P. (1976) Annu. Rev. Biochem. 45, 605-629 Planta, R. J., Van den Bos, R. C. & Klootwijk, J. (1972) in Ribosomes: ...

PolyADP-Ribosylation Is Required for Pronuclear Fusion during Postfertilization in Mice

BACKGROUND During fertilization, pronuclear envelope breakdown (PNEB) is followed by the mingling of male and female genomes. Dynamic chromatin and protein rearrangements require posttranslational modification (PTM) for the postfertilization development. METHODOLOGY/PRINCIPAL FINDINGS Inhibition of poly(ADP-ribose) polymerase activity (PARylation) by either PJ-34 or 5-AIQ resulted in developm...

Cytotoxicity of bovine seminal ribonuclease: monomer versus dimer.

Bovine seminal ribonuclease (BS-RNase) is a homologue of bovine pancreatic ribonuclease (RNase A). Unlike RNase A, BS-RNase has notable toxicity for human tumor cells. Wild-type BS-RNase is a homodimer linked by two intermolecular disulfide bonds. This quaternary structure endows BS-RNase with resistance to inhibition by the cytosolic ribonuclease inhibitor protein (RI), which binds tightly to ...