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ADP-Ribosylierung (German Wikipedia)

Analysis of information sources in references of the Wikipedia article "ADP-Ribosylierung" in German language version.

refsWebsite
Global rank German rank
23doi.org
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10nih.gov
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doi.org

  • Peter Belenky, Katrina L. Bogan, Charles Brenner: NAD+ metabolism in health and disease. In: Trends in Biochemical Sciences. Band 32, Nr. 1, Januar 2007, S. 12–19, doi:10.1016/j.tibs.2006.11.006.
  • Mathias Ziegler: New functions of a long‐known molecule: Emerging roles of NAD in cellular signaling. In: European Journal of Biochemistry. Band 267, Nr. 6, März 2000, S. 1550–1564, doi:10.1046/j.1432-1327.2000.01187.x.
  • F Berger: The new life of a centenarian: signalling functions of NAD(P). In: Trends in Biochemical Sciences. Band 29, Nr. 3, März 2004, S. 111–118, doi:10.1016/j.tibs.2004.01.007.
  • D. Corda: NEW EMBO MEMBER'S REVIEW: Functional aspects of protein mono-ADP-ribosylation. In: The EMBO Journal. Band 22, Nr. 9, 1. Mai 2003, S. 1953–1958, doi:10.1093/emboj/cdg209, PMID 12727863.
  • Emanuele S. Scarpa, Gaia Fabrizio, Maria Di Girolamo: A role of intracellular mono‐ ADP ‐ribosylation in cancer biology. In: The FEBS Journal. Band 280, Nr. 15, August 2013, S. 3551–3562, doi:10.1111/febs.12290.
  • K M Krueger, J T Barbieri: The family of bacterial ADP-ribosylating exotoxins. In: Clinical Microbiology Reviews. Band 8, Nr. 1, Januar 1995, S. 34–47, doi:10.1128/CMR.8.1.34, PMID 7704894.
  • P. Chambon, J.D. Weill, P. Mandel: Nicotinamide mononucleotide activation of a new DNA-dependent polyadenylic acid synthesizing nuclear enzyme. In: Biochemical and Biophysical Research Communications. Band 11, Nr. 1, April 1963, S. 39–43, doi:10.1016/0006-291X(63)90024-X.
  • OSAMU HAYAISHI, KUNIHIRO UEDA: Adp-Ribosylation Reactions. Elsevier, 1982, Poly- and Mono(ADP-ribosyl)ation Reactions: Their Significance in Molecular Biology, S. 3–16, doi:10.1016/b978-0-12-333660-6.50006-0.
  • R. J. Collier, A. M. Pappenheimer: STUDIES ON THE MODE OF ACTION OF DIPHTHERIA TOXIN. In: The Journal of Experimental Medicine. Band 120, Nr. 6, 1. Dezember 1964, S. 1019–1039, doi:10.1084/jem.120.6.1019, PMID 14238922.
  • Paul O. Hassa, Sandra S. Haenni, Michael Elser, Michael O. Hottiger: Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going? In: Microbiology and Molecular Biology Reviews. Band 70, Nr. 3, September 2006, S. 789–829, doi:10.1128/MMBR.00040-05, PMID 16959969.
  • Roy A. Frye: Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity. In: Biochemical and Biophysical Research Communications. Band 260, Nr. 1, Juni 1999, S. 273–279, doi:10.1006/bbrc.1999.0897.
  • Johannes Gregor Matthias Rack, Rosa Morra, Eva Barkauskaite, Rolf Kraehenbuehl, Antonio Ariza, Yue Qu, Mary Ortmayer, Orsolya Leidecker, David R. Cameron, Ivan Matic, Anton Y. Peleg, David Leys, Ana Traven, Ivan Ahel: Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens. In: Molecular Cell. Band 59, Nr. 2, Juli 2015, S. 309–320, doi:10.1016/j.molcel.2015.06.013, PMID 26166706.
  • Sabrina Laing, Mandy Unger, Friedrich Koch-Nolte, Friedrich Haag: ADP-ribosylation of arginine. In: Amino Acids. Band 41, Nr. 2, Juli 2011, S. 257–269, doi:10.1007/s00726-010-0676-2, PMID 20652610.
  • Roko Žaja, Andreja Mikoč, Eva Barkauskaite, Ivan Ahel: Molecular Insights into Poly(ADP-ribose) Recognition and Processing. In: Biomolecules. Band 3, Nr. 4, 21. Dezember 2012, S. 1–17, doi:10.3390/biom3010001, PMID 24970154.
  • Qiang Liu, Bogdan I. Florea, Dmitri V. Filippov: ADP-Ribosylation Goes Normal: Serine as the Major Site of the Modification. In: Cell Chemical Biology. Band 24, Nr. 4, April 2017, S. 431–432, doi:10.1016/j.chembiol.2017.04.003.
  • Orsolya Leidecker, Juan José Bonfiglio, Thomas Colby, Qi Zhang, Ilian Atanassov, Roko Zaja, Luca Palazzo, Anna Stockum, Ivan Ahel, Ivan Matic: Serine is a new target residue for endogenous ADP-ribosylation on histones. In: Nature Chemical Biology. Band 12, Nr. 12, 10. Oktober 2016, S. 998–1000, doi:10.1038/nchembio.2180, PMID 27723750.
  • Juan José Bonfiglio, Pietro Fontana, Qi Zhang, Thomas Colby, Ian Gibbs-Seymour, Ilian Atanassov, Edward Bartlett, Roko Zaja, Ivan Ahel, Ivan Matic: Serine ADP-Ribosylation Depends on HPF1. In: Molecular Cell. Band 65, Nr. 5, März 2017, S. 932–940.e6, doi:10.1016/j.molcel.2017.01.003, PMID 28190768.
  • Sabrina Laing, Friedrich Koch-Nolte, Friedrich Haag, Friedrich Buck: Strategies for the identification of arginine ADP-ribosylation sites. In: Journal of Proteomics. Band 75, Nr. 1, Dezember 2011, S. 169–176, doi:10.1016/j.jprot.2011.07.003.
  • Lee J. McDonald, Joel Moss: Enzymatic and nonenzymatic ADP-ribosylation of cysteine. In: Molecular and Cellular Biochemistry. Band 138, Nr. 1-2, 1994, S. 221–226, doi:10.1007/bf00928465.
  • Simon Messner, Matthias Altmeyer, Hongtao Zhao, Andrea Pozivil, Bernd Roschitzki, Peter Gehrig, Dorothea Rutishauser, Danzhi Huang, Amedeo Caflisch, Michael O. Hottiger: PARP1 ADP-ribosylates lysine residues of the core histone tails. In: Nucleic Acids Research. Band 38, Nr. 19, Oktober 2010, S. 6350–6362, doi:10.1093/nar/gkq463, PMID 20525793.
  • N.J. Oppenheimer, J.W. Bodley: Diphtheria toxin. Site and configuration of ADP-ribosylation of diphthamide in elongation factor 2. In: Journal of Biological Chemistry. Band 256, Nr. 16, August 1981, S. 8579–8581, doi:10.1016/s0021-9258(19)68883-6.
  • J A Smith, L A Stocken: Chemical and metabolic properties of adenosine diphosphate ribose derivatives of nuclear proteins. In: Biochemical Journal. Band 147, Nr. 3, 1. Juni 1975, S. 523–529, doi:10.1042/bj1470523.
  • D R Manning, B A Fraser, R A Kahn, A G Gilman: ADP-ribosylation of transducin by islet-activation protein. Identification of asparagine as the site of ADP-ribosylation. In: Journal of Biological Chemistry. Band 259, Nr. 2, Januar 1984, S. 749–756, doi:10.1016/s0021-9258(17)43521-6.

nih.gov

ncbi.nlm.nih.gov

  • D. Corda: NEW EMBO MEMBER'S REVIEW: Functional aspects of protein mono-ADP-ribosylation. In: The EMBO Journal. Band 22, Nr. 9, 1. Mai 2003, S. 1953–1958, doi:10.1093/emboj/cdg209, PMID 12727863.
  • K M Krueger, J T Barbieri: The family of bacterial ADP-ribosylating exotoxins. In: Clinical Microbiology Reviews. Band 8, Nr. 1, Januar 1995, S. 34–47, doi:10.1128/CMR.8.1.34, PMID 7704894.
  • R. J. Collier, A. M. Pappenheimer: STUDIES ON THE MODE OF ACTION OF DIPHTHERIA TOXIN. In: The Journal of Experimental Medicine. Band 120, Nr. 6, 1. Dezember 1964, S. 1019–1039, doi:10.1084/jem.120.6.1019, PMID 14238922.
  • Paul O. Hassa, Sandra S. Haenni, Michael Elser, Michael O. Hottiger: Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going? In: Microbiology and Molecular Biology Reviews. Band 70, Nr. 3, September 2006, S. 789–829, doi:10.1128/MMBR.00040-05, PMID 16959969.
  • Johannes Gregor Matthias Rack, Rosa Morra, Eva Barkauskaite, Rolf Kraehenbuehl, Antonio Ariza, Yue Qu, Mary Ortmayer, Orsolya Leidecker, David R. Cameron, Ivan Matic, Anton Y. Peleg, David Leys, Ana Traven, Ivan Ahel: Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens. In: Molecular Cell. Band 59, Nr. 2, Juli 2015, S. 309–320, doi:10.1016/j.molcel.2015.06.013, PMID 26166706.
  • Sabrina Laing, Mandy Unger, Friedrich Koch-Nolte, Friedrich Haag: ADP-ribosylation of arginine. In: Amino Acids. Band 41, Nr. 2, Juli 2011, S. 257–269, doi:10.1007/s00726-010-0676-2, PMID 20652610.
  • Roko Žaja, Andreja Mikoč, Eva Barkauskaite, Ivan Ahel: Molecular Insights into Poly(ADP-ribose) Recognition and Processing. In: Biomolecules. Band 3, Nr. 4, 21. Dezember 2012, S. 1–17, doi:10.3390/biom3010001, PMID 24970154.
  • Orsolya Leidecker, Juan José Bonfiglio, Thomas Colby, Qi Zhang, Ilian Atanassov, Roko Zaja, Luca Palazzo, Anna Stockum, Ivan Ahel, Ivan Matic: Serine is a new target residue for endogenous ADP-ribosylation on histones. In: Nature Chemical Biology. Band 12, Nr. 12, 10. Oktober 2016, S. 998–1000, doi:10.1038/nchembio.2180, PMID 27723750.
  • Juan José Bonfiglio, Pietro Fontana, Qi Zhang, Thomas Colby, Ian Gibbs-Seymour, Ilian Atanassov, Edward Bartlett, Roko Zaja, Ivan Ahel, Ivan Matic: Serine ADP-Ribosylation Depends on HPF1. In: Molecular Cell. Band 65, Nr. 5, März 2017, S. 932–940.e6, doi:10.1016/j.molcel.2017.01.003, PMID 28190768.
  • Simon Messner, Matthias Altmeyer, Hongtao Zhao, Andrea Pozivil, Bernd Roschitzki, Peter Gehrig, Dorothea Rutishauser, Danzhi Huang, Amedeo Caflisch, Michael O. Hottiger: PARP1 ADP-ribosylates lysine residues of the core histone tails. In: Nucleic Acids Research. Band 38, Nr. 19, Oktober 2010, S. 6350–6362, doi:10.1093/nar/gkq463, PMID 20525793.