By Felix R. Althaus, Hanna E. Kleczkowska (auth.), Rafael Alvarez-Gonzalez (eds.)
This designated factor of Molecular and mobile Biochemistry comprises twenty-two chosen learn papers and experiences from a complete of 1 hundred and ten shows given on the twelfth foreign Symposium on ADP-ribosylation Reactions: From Bacterial Pathogenesis to melanoma, held in Cancun, Mexico, might 10-14, 1997. The Symposium used to be hosted by means of the Sociedad Mexicana de Bioquimica and was once subsidized through the college of North Texas future health technology heart, fortress worthy, TX, united states.
This quantity presents a state of the art resource of data for uncomplicated scientists and clinicians who're attracted to the molecular, biochemical, and mobile facets of protein-(ADP-ribose) move reactions in human overall healthiness and disease.
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Extra resources for ADP-Ribosylation Reactions: From Bacterial Pathogenesis to Cancer
To study the biological function(s) of poly(ADP-ribosyl)ation, we have established stable transfectants (COM3 cells) of the SV40-transformed Chinese hamster cell line C060 which conditionally overexpress the PARP DNA-binding domain upon addition of dexamethasone. We could demonstrate that DNA-binding domain overexpression, which leads to trans-dominant inhibition of poly(ADP-ribosyl)ation, potentiates the cytotoxicity of alkylation treatment and of y-radiation . Likewise, carcinogen-induced gene amplification, viewed as a manifestation of genomic instability, was potentiated by the overexpression of the PARP DNA-binding domain .
Tewari M, Quan LT, O'Rourke K, Desnoyers S, Zeng Z, Beidler DR, Poirier GG, Salvesen GS, Dixit M: Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81: 801-809, 1995 12. : Identification and inhibition of the ICE/CED 3 protease necessary for mammalian apoptosis. Nature 376: 37-43, 1995 13. Negri C, Donzelli M, Bernardi R, Rossi L, Biirkle A, Scovassi AI: Multiparametric staining to identify apoptotic human cells.
2. 3. Althaus FR, Richter C: ADP-ribosylation of proteins. Enzymology and biological significance. Mol Bioi Biochem Biophys 37: 1-237, 1987 de Murcia G, Menissier de Murcia J: Poly (ADP-ribose) polymerase: A molecular nick sensor. Trends Biochem Sci 19: 172-176, 1994 Lindahl T, Satoh MS, Poirier GG, Klungland A: Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks. Trends Biochem Sci 20: 405-411, 1995 4. Molinete M, Vermeulen W, Biirkle A, Menissier-de Murcia J, Kiipper J-H, Hoeijmakers JH, de Murcia G: Overproduction of the poly(ADPribose) polymerase DNA-binding domain blocks alkylation-induced DNA repair synthesis in mammalian cells.