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Протеинфосфатаза 1 (Russian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Протеинфосфатаза 1" in Russian language version.

refsWebsite
Global rank Russian rank
14nih.gov
4th place
6th place
13doi.org
2nd place
3rd place
1harvard.edu
18th place
63rd place
1worldcat.org
5th place
5th place

doi.org

  • Distinct roles of PP1 and PP2A-like phosphatases in control of microtubule dynamics during mitosis. The EMBO Journal. 16 (18): 5537–49. September 1997. doi:10.1093/emboj/16.18.5537. PMID 9312013.
  • Identification of binding sites on protein targeting to glycogen for enzymes of glycogen metabolism. The Journal of Biological Chemistry. 275 (45): 35034–9. November 2000. doi:10.1074/jbc.M005541200. PMID 10938087.{{cite journal}}: Википедия:Обслуживание CS1 (не помеченный открытым DOI) (ссылка)
  • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature. 376 (6543): 745–53. August 1995. Bibcode:1995Natur.376..745G. doi:10.1038/376745a0. PMID 7651533.
  • From promiscuity to precision: protein phosphatases get a makeover. Molecular Cell. 33 (5): 537–45. March 2009. doi:10.1016/j.molcel.2009.02.015. PMID 19285938.
  • PPP1R6, a novel member of the family of glycogen-targetting subunits of protein phosphatase 1. FEBS Letters. 418 (1–2): 210–4. November 1997. doi:10.1016/S0014-5793(97)01385-9. PMID 9414128.
  • Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1. The EMBO Journal. 16 (8): 1876–87. April 1997. doi:10.1093/emboj/16.8.1876. PMID 9155014.
  • The structure and mechanism of protein phosphatases: insights into catalysis and regulation. Annual Review of Biophysics and Biomolecular Structure. 27: 133–64. 1998. doi:10.1146/annurev.biophys.27.1.133. PMID 9646865.
  • Crystal structure of Ssu72, an essential eukaryotic phosphatase specific for the C-terminal domain of RNA polymerase II, in complex with a transition state analogue. The Biochemical Journal. 434 (3): 435–44. March 2011. doi:10.1042/BJ20101471. PMID 21204787.
  • Serine/threonine protein phosphatases. The Biochemical Journal. 311 ( Pt 1) (1): 17–29. October 1995. doi:10.1042/bj3110017. PMID 7575450.
  • Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants. FEBS Letters. 264 (2): 187–92. May 1990. doi:10.1016/0014-5793(90)80245-E. PMID 2162782.
  • Phosphoprotein phosphatase activities in Alzheimer disease brain. Journal of Neurochemistry. 61 (3): 921–7. September 1993. doi:10.1111/j.1471-4159.1993.tb03603.x. PMID 8395566.
  • Regulation of HIV-1 transcription by protein phosphatase 1. Current HIV Research. 5 (1): 3–9. January 2007. doi:10.2174/157016207779316279. PMID 17266553.
  • Role of protein phosphatase 1 in dephosphorylation of Ebola virus VP30 protein and its targeting for the inhibition of viral transcription. The Journal of Biological Chemistry. 289 (33): 22723–38. August 2014. doi:10.1074/jbc.M114.575050. PMID 24936058.{{cite journal}}: Википедия:Обслуживание CS1 (не помеченный открытым DOI) (ссылка)

harvard.edu

ui.adsabs.harvard.edu

nih.gov

pubmed.ncbi.nlm.nih.gov

  • Distinct roles of PP1 and PP2A-like phosphatases in control of microtubule dynamics during mitosis. The EMBO Journal. 16 (18): 5537–49. September 1997. doi:10.1093/emboj/16.18.5537. PMID 9312013.
  • Identification of binding sites on protein targeting to glycogen for enzymes of glycogen metabolism. The Journal of Biological Chemistry. 275 (45): 35034–9. November 2000. doi:10.1074/jbc.M005541200. PMID 10938087.{{cite journal}}: Википедия:Обслуживание CS1 (не помеченный открытым DOI) (ссылка)
  • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature. 376 (6543): 745–53. August 1995. Bibcode:1995Natur.376..745G. doi:10.1038/376745a0. PMID 7651533.
  • From promiscuity to precision: protein phosphatases get a makeover. Molecular Cell. 33 (5): 537–45. March 2009. doi:10.1016/j.molcel.2009.02.015. PMID 19285938.
  • PPP1R6, a novel member of the family of glycogen-targetting subunits of protein phosphatase 1. FEBS Letters. 418 (1–2): 210–4. November 1997. doi:10.1016/S0014-5793(97)01385-9. PMID 9414128.
  • Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1. The EMBO Journal. 16 (8): 1876–87. April 1997. doi:10.1093/emboj/16.8.1876. PMID 9155014.
  • The structure and mechanism of protein phosphatases: insights into catalysis and regulation. Annual Review of Biophysics and Biomolecular Structure. 27: 133–64. 1998. doi:10.1146/annurev.biophys.27.1.133. PMID 9646865.
  • Crystal structure of Ssu72, an essential eukaryotic phosphatase specific for the C-terminal domain of RNA polymerase II, in complex with a transition state analogue. The Biochemical Journal. 434 (3): 435–44. March 2011. doi:10.1042/BJ20101471. PMID 21204787.
  • Serine/threonine protein phosphatases. The Biochemical Journal. 311 ( Pt 1) (1): 17–29. October 1995. doi:10.1042/bj3110017. PMID 7575450.
  • Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants. FEBS Letters. 264 (2): 187–92. May 1990. doi:10.1016/0014-5793(90)80245-E. PMID 2162782.
  • Phosphoprotein phosphatase activities in Alzheimer disease brain. Journal of Neurochemistry. 61 (3): 921–7. September 1993. doi:10.1111/j.1471-4159.1993.tb03603.x. PMID 8395566.
  • Regulation of HIV-1 transcription by protein phosphatase 1. Current HIV Research. 5 (1): 3–9. January 2007. doi:10.2174/157016207779316279. PMID 17266553.
  • Role of protein phosphatase 1 in dephosphorylation of Ebola virus VP30 protein and its targeting for the inhibition of viral transcription. The Journal of Biological Chemistry. 289 (33): 22723–38. August 2014. doi:10.1074/jbc.M114.575050. PMID 24936058.{{cite journal}}: Википедия:Обслуживание CS1 (не помеченный открытым DOI) (ссылка)
  • Protein phosphatase 1--targeted in many directions. Journal of Cell Science. 115 (Pt 2): 241–56. January 2002. PMID 11839776.

worldcat.org

  • Jeremy M. Berg. Biochemistry. — 7th ed. — New York: W.H. Freeman, 2012. — xxxii, 1054, 43, 41, 48 pages с. — ISBN 978-1-4292-2936-4, 1-4292-2936-5, 978-1-4292-7635-1, 1-4292-7635-5, 978-1-4292-7396-1, 1-4292-7396-8.