ADP-ribosylation (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "ADP-ribosylation" in English language version.

refsWebsite

Global rank English rank

40nih.gov

4^th place

25doi.org

2^nd place

3worldcat.org

5^th place

1dartmouth.edu

2,242^nd place

1,513^th place

1semanticscholar.org

11^th place

8^th place

dartmouth.edu

Belenky P, Bogan KL, Brenner C (2007). "NAD+ metabolism in health and disease" (PDF). Trends Biochem. Sci. 32 (1): 12–9. doi:10.1016/j.tibs.2006.11.006. PMID 17161604.

doi.org

Belenky P, Bogan KL, Brenner C (2007). "NAD+ metabolism in health and disease" (PDF). Trends Biochem. Sci. 32 (1): 12–9. doi:10.1016/j.tibs.2006.11.006. PMID 17161604.
Ziegler M (2000). "New functions of a long-known molecule. Emerging roles of NAD in cellular signaling". Eur. J. Biochem. 267 (6): 1550–64. doi:10.1046/j.1432-1327.2000.01187.x. PMID 10712584.
Berger F, Ramírez-Hernández MH, Ziegler M (2004). "The new life of a centenarian: signalling functions of NAD(P)". Trends Biochem. Sci. 29 (3): 111–8. doi:10.1016/j.tibs.2004.01.007. PMID 15003268. S2CID 8820773.
Corda D, Di Girolamo M (2003). "NEW EMBO MEMBER'S REVIEW: Functional aspects of protein mono-ADP-ribosylation". EMBO J. 22 (9): 1953–8. doi:10.1093/emboj/cdg209. PMC 156081. PMID 12727863.
Scarpa ES, Fabrizio G, Di Girolamo M (2013). ". A role in intracellular mono-ADP-ribosylation in cancer biology". FEBS Journal. 280 (15): 3551–3562. doi:10.1111/febs.12290. PMID 23590234.
Krueger, KM; Barbieri, JT (January 1995). "The family of bacterial ADP-ribosylating exotoxins". Clinical Microbiology Reviews. 8 (1): 34–47. doi:10.1128/CMR.8.1.34. PMC 172848. PMID 7704894.
Chambon, P; Weill, J. D.; Mandel, P. (1963). "Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesizing nuclear enzyme". Biochem. Biophys. Res. Commun. 11: 39–43. doi:10.1016/0006-291x(63)90024-x. PMID 14019961.
Collier RJ, Pappenheimer, Jr AM (1964). "STUDIES ON THE MODE OF ACTION OF DIPHTHERIA TOXIN* II. EFFECT OF TOXIN ON AMINO ACID INCORPORATION IN CELL-FREE SYSTEM". Journal of Experimental Medicine. 120 (6): 1019–1039. doi:10.1084/jem.120.6.1019. PMC 2137798. PMID 14238922.
Hassa, P. O.; Haenni, S. S.; Elser, M.; Hottiger, M. O. (2006). "Hassa, P. O.; Haenni, S. S.; Elser, M.; Hottiger, M. O. (2006) "Nuclear ADP-Ribozylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going". Microbiol. Mol. Biol. Rev. 70 (3): 789–829. doi:10.1128/mmbr.00040-05. PMC 1594587. PMID 16959969.
Frye, RA (June 24, 1999). "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". Biochemical and Biophysical Research Communications. 260 (1): 273–9. doi:10.1006/bbrc.1999.0897. PMID 10381378.
Rack, Johannes Gregor Matthias; Morra, Rosa; Barkauskaite, Eva; Kraehenbuehl, Rolf; Ariza, Antonio; Qu, Yue; Ortmayer, Mary; Leidecker, Orsolya; Cameron, David R. (July 16, 2015). "Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens". Molecular Cell. 59 (2): 309–320. doi:10.1016/j.molcel.2015.06.013. ISSN 1097-4164. PMC 4518038. PMID 26166706.
Laing, Sabrina; Unger, Mandy; Koch-Nolte, Friedrich; Haag, Friedrich (July 21, 2010). "ADP-ribosylation of arginine". Amino Acids. 41 (2): 257–269. doi:10.1007/s00726-010-0676-2. PMC 3102197. PMID 20652610.
Žaja, Roko; Mikoč, Andreja; Barkauskaite, Eva; Ahel, Ivan (December 21, 2012). "Molecular Insights into Poly(ADP-ribose) Recognition and Processing". Biomolecules. 3 (1): 1–17. doi:10.3390/biom3010001. PMC 4030884. PMID 24970154.
Liu, Qiang; Florea, Bogdan I.; Filippov, Dmitri V. (2017). "ADP-Ribosylation Goes Normal: Serine as the Major Site of the Modification". Cell Chemical Biology. 24 (4): 431–432. doi:10.1016/j.chembiol.2017.04.003. PMID 28431224.
Leidecker, Orsolya; Bonfiglio, Juan José; Colby, Thomas; Zhang, Qi; Atanassov, Ilian; Zaja, Roko; Palazzo, Luca; Stockum, Anna; Ahel, Ivan; Matic, Ivan (2016). "Serine is a new target residue for endogenous ADP-ribosylation on histones". Nature Chemical Biology. 12 (12): 998–1000. doi:10.1038/nchembio.2180. PMC 5113755. PMID 27723750.
Bonfiglio, Juan José; Fontana, Pietro; Zhang, Qi; Colby, Thomas; Gibbs-Seymour, Ian; Atanassov, Ilian; Bartlett, Edward; Zaja, Roko; Ahel, Ivan; Matic, Ivan (2017). "Serine ADP-Ribosylation Depends on HPF1". Molecular Cell. 65 (5): 932–940.e6. doi:10.1016/j.molcel.2017.01.003. PMC 5344681. PMID 28190768.
Messner, Simon; Altmeyer, Matthias; Zhao, Hongtao; Pozivil, Andrea; Roschitzki, Bernd; Gehrig, Peter; Rutishauser, Dorothea; Huang, Danzhi; Caflisch, Amedeo; Hottiger, Michael O. (2010). "PARP1 ADP-ribosylates lysine residues of the core histone tails". Nucleic Acids Research. 38 (19): 6350–6362. doi:10.1093/nar/gkq463. PMC 2965223. PMID 20525793.
Aredia, F; Scovassi, AI (June 1, 2014). "Involvement of PARPs in cell death". Frontiers in Bioscience. 6 (2): 308–17. doi:10.2741/707. PMID 24896207.
Ryu, Keun Woo; Kim, Dae-Seok; Kraus, W. Lee (January 9, 2015). "New Facets in the Regulation of Gene Expression by ADP-Ribosylation and Poly(ADP-ribose) Polymerases". Chemical Reviews. 115 (6): 2453–2481. doi:10.1021/cr5004248. PMC 4378458. PMID 25575290.
Schreiber, V; Amé, JC; Dollé, P; Schultz, I; Rinaldi, B; Fraulob, V; Ménissier-de Murcia, J; de Murcia, G (June 21, 2002). "Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1". The Journal of Biological Chemistry. 277 (25): 23028–36. doi:10.1074/jbc.m202390200. PMID 11948190.
Pears, Catherine J.; Couto, C. Anne-Marie; Wang, Hong-Yu; Borer, Christine; Kiely, Rhian; Lakin, Nicholas D. (October 28, 2014). "The role of ADP-ribosylation in regulating DNA double-strand break repair". Cell Cycle. 11 (1): 48–56. doi:10.4161/cc.11.1.18793. PMC 3272231. PMID 22186780.
Cheng, Yifan (April 2009). "Toward an atomic model of the 26S proteasome". Current Opinion in Structural Biology. 19 (2): 203–208. doi:10.1016/j.sbi.2009.02.004. PMC 2743420. PMID 19286367.
Cho-Park, Park F.; Steller, Hermann (April 25, 2013). "Proteasome regulation by ADP-ribosylation". Cell. 153 (3): 614–627. doi:10.1016/j.cell.2013.03.040. ISSN 0092-8674. PMC 3676968. PMID 23622245.
Pope, M. R.; Saari, L. L.; Ludden, P. W. (August 5, 1986). "N-glycohydrolysis of adenosine diphosphoribosyl arginine linkages by dinitrogenase reductase activating glycohydrolase (activating enzyme) from Rhodospirillum rubrum". The Journal of Biological Chemistry. 261 (22): 10104–10111. doi:10.1016/S0021-9258(18)67497-6. ISSN 0021-9258. PMID 3090031.
Deng, Qing; Barbieri, Joseph T. (October 2008). "Molecular Mechanisms of the Cytotoxicity of ADP-Ribosylating Toxins". Annual Review of Microbiology. 62 (1): 271–288. doi:10.1146/annurev.micro.62.081307.162848. PMID 18785839.

nih.gov

pubmed.ncbi.nlm.nih.gov

Belenky P, Bogan KL, Brenner C (2007). "NAD+ metabolism in health and disease" (PDF). Trends Biochem. Sci. 32 (1): 12–9. doi:10.1016/j.tibs.2006.11.006. PMID 17161604.
Ziegler M (2000). "New functions of a long-known molecule. Emerging roles of NAD in cellular signaling". Eur. J. Biochem. 267 (6): 1550–64. doi:10.1046/j.1432-1327.2000.01187.x. PMID 10712584.
Berger F, Ramírez-Hernández MH, Ziegler M (2004). "The new life of a centenarian: signalling functions of NAD(P)". Trends Biochem. Sci. 29 (3): 111–8. doi:10.1016/j.tibs.2004.01.007. PMID 15003268. S2CID 8820773.
Corda D, Di Girolamo M (2003). "NEW EMBO MEMBER'S REVIEW: Functional aspects of protein mono-ADP-ribosylation". EMBO J. 22 (9): 1953–8. doi:10.1093/emboj/cdg209. PMC 156081. PMID 12727863.
Scarpa ES, Fabrizio G, Di Girolamo M (2013). ". A role in intracellular mono-ADP-ribosylation in cancer biology". FEBS Journal. 280 (15): 3551–3562. doi:10.1111/febs.12290. PMID 23590234.
Krueger, KM; Barbieri, JT (January 1995). "The family of bacterial ADP-ribosylating exotoxins". Clinical Microbiology Reviews. 8 (1): 34–47. doi:10.1128/CMR.8.1.34. PMC 172848. PMID 7704894.
Chambon, P; Weill, J. D.; Mandel, P. (1963). "Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesizing nuclear enzyme". Biochem. Biophys. Res. Commun. 11: 39–43. doi:10.1016/0006-291x(63)90024-x. PMID 14019961.
Collier RJ, Pappenheimer, Jr AM (1964). "STUDIES ON THE MODE OF ACTION OF DIPHTHERIA TOXIN* II. EFFECT OF TOXIN ON AMINO ACID INCORPORATION IN CELL-FREE SYSTEM". Journal of Experimental Medicine. 120 (6): 1019–1039. doi:10.1084/jem.120.6.1019. PMC 2137798. PMID 14238922.
Hassa, P. O.; Haenni, S. S.; Elser, M.; Hottiger, M. O. (2006). "Hassa, P. O.; Haenni, S. S.; Elser, M.; Hottiger, M. O. (2006) "Nuclear ADP-Ribozylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going". Microbiol. Mol. Biol. Rev. 70 (3): 789–829. doi:10.1128/mmbr.00040-05. PMC 1594587. PMID 16959969.
Frye, RA (June 24, 1999). "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". Biochemical and Biophysical Research Communications. 260 (1): 273–9. doi:10.1006/bbrc.1999.0897. PMID 10381378.
Rack, Johannes Gregor Matthias; Morra, Rosa; Barkauskaite, Eva; Kraehenbuehl, Rolf; Ariza, Antonio; Qu, Yue; Ortmayer, Mary; Leidecker, Orsolya; Cameron, David R. (July 16, 2015). "Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens". Molecular Cell. 59 (2): 309–320. doi:10.1016/j.molcel.2015.06.013. ISSN 1097-4164. PMC 4518038. PMID 26166706.
Laing, Sabrina; Unger, Mandy; Koch-Nolte, Friedrich; Haag, Friedrich (July 21, 2010). "ADP-ribosylation of arginine". Amino Acids. 41 (2): 257–269. doi:10.1007/s00726-010-0676-2. PMC 3102197. PMID 20652610.
Žaja, Roko; Mikoč, Andreja; Barkauskaite, Eva; Ahel, Ivan (December 21, 2012). "Molecular Insights into Poly(ADP-ribose) Recognition and Processing". Biomolecules. 3 (1): 1–17. doi:10.3390/biom3010001. PMC 4030884. PMID 24970154.
Liu, Qiang; Florea, Bogdan I.; Filippov, Dmitri V. (2017). "ADP-Ribosylation Goes Normal: Serine as the Major Site of the Modification". Cell Chemical Biology. 24 (4): 431–432. doi:10.1016/j.chembiol.2017.04.003. PMID 28431224.
Leidecker, Orsolya; Bonfiglio, Juan José; Colby, Thomas; Zhang, Qi; Atanassov, Ilian; Zaja, Roko; Palazzo, Luca; Stockum, Anna; Ahel, Ivan; Matic, Ivan (2016). "Serine is a new target residue for endogenous ADP-ribosylation on histones". Nature Chemical Biology. 12 (12): 998–1000. doi:10.1038/nchembio.2180. PMC 5113755. PMID 27723750.
Bonfiglio, Juan José; Fontana, Pietro; Zhang, Qi; Colby, Thomas; Gibbs-Seymour, Ian; Atanassov, Ilian; Bartlett, Edward; Zaja, Roko; Ahel, Ivan; Matic, Ivan (2017). "Serine ADP-Ribosylation Depends on HPF1". Molecular Cell. 65 (5): 932–940.e6. doi:10.1016/j.molcel.2017.01.003. PMC 5344681. PMID 28190768.
Messner, Simon; Altmeyer, Matthias; Zhao, Hongtao; Pozivil, Andrea; Roschitzki, Bernd; Gehrig, Peter; Rutishauser, Dorothea; Huang, Danzhi; Caflisch, Amedeo; Hottiger, Michael O. (2010). "PARP1 ADP-ribosylates lysine residues of the core histone tails". Nucleic Acids Research. 38 (19): 6350–6362. doi:10.1093/nar/gkq463. PMC 2965223. PMID 20525793.
Scovassi, AI; Denegri, M; Donzelli, M; Rossi, L; Bernardi, R; Mandarino, A; Frouin, I; Negri, C (1998). "Poly(ADP-ribose) synthesis in cells undergoing apoptosis: an attempt to face death before PARP degradation". European Journal of Histochemistry. 42 (4): 251–8. PMID 10068897.
Aredia, F; Scovassi, AI (June 1, 2014). "Involvement of PARPs in cell death". Frontiers in Bioscience. 6 (2): 308–17. doi:10.2741/707. PMID 24896207.
Ryu, Keun Woo; Kim, Dae-Seok; Kraus, W. Lee (January 9, 2015). "New Facets in the Regulation of Gene Expression by ADP-Ribosylation and Poly(ADP-ribose) Polymerases". Chemical Reviews. 115 (6): 2453–2481. doi:10.1021/cr5004248. PMC 4378458. PMID 25575290.
Schreiber, V; Amé, JC; Dollé, P; Schultz, I; Rinaldi, B; Fraulob, V; Ménissier-de Murcia, J; de Murcia, G (June 21, 2002). "Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1". The Journal of Biological Chemistry. 277 (25): 23028–36. doi:10.1074/jbc.m202390200. PMID 11948190.
Pears, Catherine J.; Couto, C. Anne-Marie; Wang, Hong-Yu; Borer, Christine; Kiely, Rhian; Lakin, Nicholas D. (October 28, 2014). "The role of ADP-ribosylation in regulating DNA double-strand break repair". Cell Cycle. 11 (1): 48–56. doi:10.4161/cc.11.1.18793. PMC 3272231. PMID 22186780.
Cheng, Yifan (April 2009). "Toward an atomic model of the 26S proteasome". Current Opinion in Structural Biology. 19 (2): 203–208. doi:10.1016/j.sbi.2009.02.004. PMC 2743420. PMID 19286367.
Cho-Park, Park F.; Steller, Hermann (April 25, 2013). "Proteasome regulation by ADP-ribosylation". Cell. 153 (3): 614–627. doi:10.1016/j.cell.2013.03.040. ISSN 0092-8674. PMC 3676968. PMID 23622245.
Pope, M. R.; Saari, L. L.; Ludden, P. W. (August 5, 1986). "N-glycohydrolysis of adenosine diphosphoribosyl arginine linkages by dinitrogenase reductase activating glycohydrolase (activating enzyme) from Rhodospirillum rubrum". The Journal of Biological Chemistry. 261 (22): 10104–10111. doi:10.1016/S0021-9258(18)67497-6. ISSN 0021-9258. PMID 3090031.
Deng, Qing; Barbieri, Joseph T. (October 2008). "Molecular Mechanisms of the Cytotoxicity of ADP-Ribosylating Toxins". Annual Review of Microbiology. 62 (1): 271–288. doi:10.1146/annurev.micro.62.081307.162848. PMID 18785839.

ncbi.nlm.nih.gov

Corda D, Di Girolamo M (2003). "NEW EMBO MEMBER'S REVIEW: Functional aspects of protein mono-ADP-ribosylation". EMBO J. 22 (9): 1953–8. doi:10.1093/emboj/cdg209. PMC 156081. PMID 12727863.
Krueger, KM; Barbieri, JT (January 1995). "The family of bacterial ADP-ribosylating exotoxins". Clinical Microbiology Reviews. 8 (1): 34–47. doi:10.1128/CMR.8.1.34. PMC 172848. PMID 7704894.
Collier RJ, Pappenheimer, Jr AM (1964). "STUDIES ON THE MODE OF ACTION OF DIPHTHERIA TOXIN* II. EFFECT OF TOXIN ON AMINO ACID INCORPORATION IN CELL-FREE SYSTEM". Journal of Experimental Medicine. 120 (6): 1019–1039. doi:10.1084/jem.120.6.1019. PMC 2137798. PMID 14238922.
Hassa, P. O.; Haenni, S. S.; Elser, M.; Hottiger, M. O. (2006). "Hassa, P. O.; Haenni, S. S.; Elser, M.; Hottiger, M. O. (2006) "Nuclear ADP-Ribozylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going". Microbiol. Mol. Biol. Rev. 70 (3): 789–829. doi:10.1128/mmbr.00040-05. PMC 1594587. PMID 16959969.
Rack, Johannes Gregor Matthias; Morra, Rosa; Barkauskaite, Eva; Kraehenbuehl, Rolf; Ariza, Antonio; Qu, Yue; Ortmayer, Mary; Leidecker, Orsolya; Cameron, David R. (July 16, 2015). "Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens". Molecular Cell. 59 (2): 309–320. doi:10.1016/j.molcel.2015.06.013. ISSN 1097-4164. PMC 4518038. PMID 26166706.
Laing, Sabrina; Unger, Mandy; Koch-Nolte, Friedrich; Haag, Friedrich (July 21, 2010). "ADP-ribosylation of arginine". Amino Acids. 41 (2): 257–269. doi:10.1007/s00726-010-0676-2. PMC 3102197. PMID 20652610.
Žaja, Roko; Mikoč, Andreja; Barkauskaite, Eva; Ahel, Ivan (December 21, 2012). "Molecular Insights into Poly(ADP-ribose) Recognition and Processing". Biomolecules. 3 (1): 1–17. doi:10.3390/biom3010001. PMC 4030884. PMID 24970154.
Leidecker, Orsolya; Bonfiglio, Juan José; Colby, Thomas; Zhang, Qi; Atanassov, Ilian; Zaja, Roko; Palazzo, Luca; Stockum, Anna; Ahel, Ivan; Matic, Ivan (2016). "Serine is a new target residue for endogenous ADP-ribosylation on histones". Nature Chemical Biology. 12 (12): 998–1000. doi:10.1038/nchembio.2180. PMC 5113755. PMID 27723750.
Bonfiglio, Juan José; Fontana, Pietro; Zhang, Qi; Colby, Thomas; Gibbs-Seymour, Ian; Atanassov, Ilian; Bartlett, Edward; Zaja, Roko; Ahel, Ivan; Matic, Ivan (2017). "Serine ADP-Ribosylation Depends on HPF1". Molecular Cell. 65 (5): 932–940.e6. doi:10.1016/j.molcel.2017.01.003. PMC 5344681. PMID 28190768.
Messner, Simon; Altmeyer, Matthias; Zhao, Hongtao; Pozivil, Andrea; Roschitzki, Bernd; Gehrig, Peter; Rutishauser, Dorothea; Huang, Danzhi; Caflisch, Amedeo; Hottiger, Michael O. (2010). "PARP1 ADP-ribosylates lysine residues of the core histone tails". Nucleic Acids Research. 38 (19): 6350–6362. doi:10.1093/nar/gkq463. PMC 2965223. PMID 20525793.
Ryu, Keun Woo; Kim, Dae-Seok; Kraus, W. Lee (January 9, 2015). "New Facets in the Regulation of Gene Expression by ADP-Ribosylation and Poly(ADP-ribose) Polymerases". Chemical Reviews. 115 (6): 2453–2481. doi:10.1021/cr5004248. PMC 4378458. PMID 25575290.
Pears, Catherine J.; Couto, C. Anne-Marie; Wang, Hong-Yu; Borer, Christine; Kiely, Rhian; Lakin, Nicholas D. (October 28, 2014). "The role of ADP-ribosylation in regulating DNA double-strand break repair". Cell Cycle. 11 (1): 48–56. doi:10.4161/cc.11.1.18793. PMC 3272231. PMID 22186780.
Cheng, Yifan (April 2009). "Toward an atomic model of the 26S proteasome". Current Opinion in Structural Biology. 19 (2): 203–208. doi:10.1016/j.sbi.2009.02.004. PMC 2743420. PMID 19286367.
Cho-Park, Park F.; Steller, Hermann (April 25, 2013). "Proteasome regulation by ADP-ribosylation". Cell. 153 (3): 614–627. doi:10.1016/j.cell.2013.03.040. ISSN 0092-8674. PMC 3676968. PMID 23622245.

semanticscholar.org

api.semanticscholar.org

Berger F, Ramírez-Hernández MH, Ziegler M (2004). "The new life of a centenarian: signalling functions of NAD(P)". Trends Biochem. Sci. 29 (3): 111–8. doi:10.1016/j.tibs.2004.01.007. PMID 15003268. S2CID 8820773.

worldcat.org

search.worldcat.org

Rack, Johannes Gregor Matthias; Morra, Rosa; Barkauskaite, Eva; Kraehenbuehl, Rolf; Ariza, Antonio; Qu, Yue; Ortmayer, Mary; Leidecker, Orsolya; Cameron, David R. (July 16, 2015). "Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens". Molecular Cell. 59 (2): 309–320. doi:10.1016/j.molcel.2015.06.013. ISSN 1097-4164. PMC 4518038. PMID 26166706.
Cho-Park, Park F.; Steller, Hermann (April 25, 2013). "Proteasome regulation by ADP-ribosylation". Cell. 153 (3): 614–627. doi:10.1016/j.cell.2013.03.040. ISSN 0092-8674. PMC 3676968. PMID 23622245.
Pope, M. R.; Saari, L. L.; Ludden, P. W. (August 5, 1986). "N-glycohydrolysis of adenosine diphosphoribosyl arginine linkages by dinitrogenase reductase activating glycohydrolase (activating enzyme) from Rhodospirillum rubrum". The Journal of Biological Chemistry. 261 (22): 10104–10111. doi:10.1016/S0021-9258(18)67497-6. ISSN 0021-9258. PMID 3090031.