Zeitschriftenartikel zum Thema „Phosphoprotein phosphatases“
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Shacter, Emily, Joseph A. McClure, Edward D. Korn und P. Boon Chock. „Immunological characterization of phosphoprotein phosphatases“. Archives of Biochemistry and Biophysics 242, Nr. 2 (November 1985): 523–31. http://dx.doi.org/10.1016/0003-9861(85)90239-5.
Vincent, John B., und Bruce A. Averill. „Sequence homology between purple acid phosphatases and phosphoprotein phosphatases“. FEBS Letters 263, Nr. 2 (24.04.1990): 265–68. http://dx.doi.org/10.1016/0014-5793(90)81389-6.
Miller, W. Todd. „Tyrosine Phosphoprotein Phosphatases. Barry J. Goldstein“. Quarterly Review of Biology 74, Nr. 4 (Dezember 1999): 464–65. http://dx.doi.org/10.1086/394141.
Zhang, Qingxiu, und Francois X. Claret. „Phosphatases: The New Brakes for Cancer Development?“ Enzyme Research 2012 (31.10.2012): 1–11. http://dx.doi.org/10.1155/2012/659649.
Miskei, Márton, Csaba Ádám, László Kovács, Zsolt Karányi und Viktor Dombrádi. „Molecular Evolution of Phosphoprotein Phosphatases in Drosophila“. PLoS ONE 6, Nr. 7 (15.07.2011): e22218. http://dx.doi.org/10.1371/journal.pone.0022218.
Moorhead, Greg B. G., Veerle De Wever, George Templeton und David Kerk. „Evolution of protein phosphatases in plants and animals“. Biochemical Journal 417, Nr. 2 (23.12.2008): 401–9. http://dx.doi.org/10.1042/bj20081986.
Butler, Trent, Jonathan Paul, Nick Europe-Finner, Roger Smith und Eng-Cheng Chan. „Role of serine-threonine phosphoprotein phosphatases in smooth muscle contractility“. American Journal of Physiology-Cell Physiology 304, Nr. 6 (15.03.2013): C485—C504. http://dx.doi.org/10.1152/ajpcell.00161.2012.
Garvanska, Dimitriya H., und Jakob Nilsson. „Specificity determinants of phosphoprotein phosphatases controlling kinetochore functions“. Essays in Biochemistry 64, Nr. 2 (05.06.2020): 325–36. http://dx.doi.org/10.1042/ebc20190065.
Wheeler-Jones, Caroline P. D., Rebecca A. Houliston und Jeremy D. Pearson. „Inhibitors of phosphoprotein phosphatases modulate p42mapk phosphorylation in endothelium“. Blood Coagulation & Fibrinolysis 6, Nr. 2 (April 1995): 173. http://dx.doi.org/10.1097/00001721-199504000-00068.
Burns, Chris J., Shân L. Gyles, Shanta J. Persaud, David Sugden, Barbara J. Whitehouse und Peter M. Jones. „Phosphoprotein Phosphatases Regulate Steroidogenesis by Influencing StAR Gene Transcription“. Biochemical and Biophysical Research Communications 273, Nr. 1 (Juni 2000): 35–39. http://dx.doi.org/10.1006/bbrc.2000.2890.
Ford, S. L., D. R. E. Abayasekara, S. J. Persaud und P. M. Jones. „Role of phosphoprotein phosphatases in the corpus luteum: I Identification and characterisation of serine/threonine phosphoprotein phosphatases in isolated rat luteal cells“. Journal of Endocrinology 150, Nr. 2 (August 1996): 205–11. http://dx.doi.org/10.1677/joe.0.1500205.
MISTRY, Sucharita J., Heng-Chun LI und George F. ATWEH. „Role for protein phosphatases in the cell-cycle-regulated phosphorylation of stathmin“. Biochemical Journal 334, Nr. 1 (15.08.1998): 23–29. http://dx.doi.org/10.1042/bj3340023.
Moradi, Atieh, Shuaijian Dai, Emily Oi Ying Wong, Guang Zhu, Fengchao Yu, Hon-Ming Lam, Zhiyong Wang et al. „Isotopically Dimethyl Labeling-Based Quantitative Proteomic Analysis of Phosphoproteomes of Soybean Cultivars“. Biomolecules 11, Nr. 8 (16.08.2021): 1218. http://dx.doi.org/10.3390/biom11081218.
Abbasian, Nima, James O. Burton, Karl E. Herbert, Barbara-Emily Tregunna, Jeremy R. Brown, Maryam Ghaderi-Najafabadi, Nigel J. Brunskill, Alison H. Goodall und Alan Bevington. „Hyperphosphatemia, Phosphoprotein Phosphatases, and Microparticle Release in Vascular Endothelial Cells“. Journal of the American Society of Nephrology 26, Nr. 9 (05.03.2015): 2152–62. http://dx.doi.org/10.1681/asn.2014070642.
Rietz, A., und JP Spiers. „The relationship between the MMP system, adrenoceptors and phosphoprotein phosphatases“. British Journal of Pharmacology 166, Nr. 4 (17.05.2012): 1225–43. http://dx.doi.org/10.1111/j.1476-5381.2012.01917.x.
Smith, Robert D., und John C. Walker. „Expression of multiple type 1 phosphoprotein phosphatases in Arabidopsis thaliana“. Plant Molecular Biology 21, Nr. 2 (Januar 1993): 307–16. http://dx.doi.org/10.1007/bf00019946.
Taylor, William P., und Theodore S. Widlanski. „Charged with meaning: the structure and mechanism of phosphoprotein phosphatases“. Chemistry & Biology 2, Nr. 11 (November 1995): 713–18. http://dx.doi.org/10.1016/1074-5521(95)90098-5.
Mivechi, N. F., L. D. Trainor und G. M. Hahn. „Purified Mammalian HSP-70 kDa Activates Phosphoprotein Phosphatases in Vitro“. Biochemical and Biophysical Research Communications 192, Nr. 2 (April 1993): 954–63. http://dx.doi.org/10.1006/bbrc.1993.1508.
Pereira, Susana R., Vítor M. Vasconcelos und Agostinho Antunes. „The phosphoprotein phosphatase family of Ser/Thr phosphatases as principal targets of naturally occurring toxins“. Critical Reviews in Toxicology 41, Nr. 2 (Februar 2011): 83–110. http://dx.doi.org/10.3109/10408444.2010.515564.
DESDOUITS, Frédéric, C. Julio SICILIANO, C. Angus NAIRN, Paul GREENGARD und Jean-Antoine GIRAULT. „Dephosphorylation of Ser-137 in DARPP-32 by protein phosphatases 2A and 2C: different roles in vitro and in striatonigral neurons“. Biochemical Journal 330, Nr. 1 (15.02.1998): 211–16. http://dx.doi.org/10.1042/bj3300211.
Palmer, Frederick B. St C. „Identification of the phosphomonoesterases that hydrolyze lysopolyphosphoinositides in rat brain and liver“. Biochemistry and Cell Biology 65, Nr. 10 (01.10.1987): 890–98. http://dx.doi.org/10.1139/o87-115.
Lajarín-Cuesta, Rocío, Raquel L. Arribas und Cristóbal De Los Ríos. „Ligands for Ser/Thr phosphoprotein phosphatases: a patent review (2005-2015)“. Expert Opinion on Therapeutic Patents 26, Nr. 3 (07.02.2016): 389–407. http://dx.doi.org/10.1517/13543776.2016.1135903.
Ádám, Csaba, László Henn, Márton Miskei, Miklós Erdélyi, Péter Friedrich und Viktor Dombrádi. „Conservation of male-specific expression of novel phosphoprotein phosphatases in Drosophila“. Development Genes and Evolution 220, Nr. 3-4 (15.07.2010): 123–28. http://dx.doi.org/10.1007/s00427-010-0332-6.
Pazy, Y., M. A. Motaleb, M. T. Guarnieri, N. W. Charon, R. Zhao und R. E. Silversmith. „Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate“. Proceedings of the National Academy of Sciences 107, Nr. 5 (14.01.2010): 1924–29. http://dx.doi.org/10.1073/pnas.0911185107.
Mukhopadhyay, Subhendu, Vinayak Kapatral, Wenbin Xu und A. M. Chakrabarty. „Characterization of a Hank’s Type Serine/Threonine Kinase and Serine/Threonine Phosphoprotein Phosphatase inPseudomonas aeruginosa“. Journal of Bacteriology 181, Nr. 21 (01.11.1999): 6615–22. http://dx.doi.org/10.1128/jb.181.21.6615-6622.1999.
Ohno, J., K. Fukuyama, A. Hara und W. L. Epstein. „Immuno- and enzyme-histochemical detection of phosphoprotein phosphatase in rat epidermis.“ Journal of Histochemistry & Cytochemistry 37, Nr. 5 (Mai 1989): 629–34. http://dx.doi.org/10.1177/37.5.2539408.
Perry, M. D., und G. I. Sandle. „Regulation of colonic apical potassium (BK) channels by cAMP and somatostatin“. American Journal of Physiology-Gastrointestinal and Liver Physiology 297, Nr. 1 (Juli 2009): G159—G167. http://dx.doi.org/10.1152/ajpgi.00132.2009.
Pidoux, Guillaume, und Kjetil Taskén. „Specificity and spatial dynamics of protein kinase A signaling organized by A-kinase-anchoring proteins“. Journal of Molecular Endocrinology 44, Nr. 5 (11.02.2010): 271–84. http://dx.doi.org/10.1677/jme-10-0010.
Whalley, T., I. Crossley und M. Whitaker. „Phosphoprotein inhibition of calcium-stimulated exocytosis in sea urchin eggs.“ Journal of Cell Biology 113, Nr. 4 (15.05.1991): 769–78. http://dx.doi.org/10.1083/jcb.113.4.769.
Comolli, J., W. Taylor, J. Rehman und J. W. Hastings. „Inhibitors of Serine/Threonine Phosphoprotein Phosphatases Alter Circadian Properties in Gonyaulax polyedra“. Plant Physiology 111, Nr. 1 (01.05.1996): 285–91. http://dx.doi.org/10.1104/pp.111.1.285.
Macaulay, S. L., Julie D. Newman, J. D. Mc Armstrong und J. Bornstein. „Activation of phosphoprotein phosphatases by growth hormone sequences with insulin-like activity“. Molecular and Cellular Biochemistry 74, Nr. 1 (März 1987): 95–101. http://dx.doi.org/10.1007/bf00221916.
Turowski, Patric, Timothy Myles, Brian A. Hemmings, Anne Fernandez und Ned J. C. Lamb. „Vimentin Dephosphorylation by Protein Phosphatase 2A Is Modulated by the Targeting Subunit B55“. Molecular Biology of the Cell 10, Nr. 6 (Juni 1999): 1997–2015. http://dx.doi.org/10.1091/mbc.10.6.1997.
Seok, Seung-Hyeon. „Structural Insights into Protein Regulation by Phosphorylation and Substrate Recognition of Protein Kinases/Phosphatases“. Life 11, Nr. 9 (13.09.2021): 957. http://dx.doi.org/10.3390/life11090957.
Al-Nedawi, K. N., Z. Pawłowska und C. S. Cierniewski. „Interferon gamma bound to endothelial cells is phosphorylated by ecto-protein kinases.“ Acta Biochimica Polonica 46, Nr. 3 (30.09.1999): 693–702. http://dx.doi.org/10.18388/abp.1999_4141.
Polanowska-Grabowska, Renata, Carl G. Simon, Rocco Falchetto, Jeffrey Shabanowitz, Donald F. Hunt und Adrian R. L. Gear. „Platelet Adhesion to Collagen Under Flow Causes Dissociation of a Phosphoprotein Complex of Heat-Shock Proteins and Protein Phosphatase 1“. Blood 90, Nr. 4 (15.08.1997): 1516–26. http://dx.doi.org/10.1182/blood.v90.4.1516.
Polanowska-Grabowska, Renata, Carl G. Simon, Rocco Falchetto, Jeffrey Shabanowitz, Donald F. Hunt und Adrian R. L. Gear. „Platelet Adhesion to Collagen Under Flow Causes Dissociation of a Phosphoprotein Complex of Heat-Shock Proteins and Protein Phosphatase 1“. Blood 90, Nr. 4 (15.08.1997): 1516–26. http://dx.doi.org/10.1182/blood.v90.4.1516.1516_1516_1526.
Nilsson, Jakob. „Protein phosphatases in the regulation of mitosis“. Journal of Cell Biology 218, Nr. 2 (16.11.2018): 395–409. http://dx.doi.org/10.1083/jcb.201809138.
Zgajnar, Nadia R., Cristina Daneri-Becerra, Ana Cauerhff und Mario D. Galigniana. „The Scaffold Immunophilin FKBP51 Is a Phosphoprotein That Undergoes Dynamic Mitochondrial-Nuclear Shuttling“. Cells 11, Nr. 23 (25.11.2022): 3771. http://dx.doi.org/10.3390/cells11233771.
Kochinyan, Samvel, Luo Sun, Inca Ghosh, Tanya Barshevsky, Jie Xu und Ming-Qun Xu. „Use of intein-mediated phosphoprotein arrays to study substrate specificity of protein phosphatases“. BioTechniques 42, Nr. 1 (Januar 2007): 63–69. http://dx.doi.org/10.2144/000112311.
Lyons, Scott P., Nicole P. Jenkins, Isha Nasa, Meng S. Choy, Mark E. Adamo, Rebecca Page, Wolfgang Peti, Greg B. Moorhead und Arminja N. Kettenbach. „A Quantitative Chemical Proteomic Strategy for Profiling Phosphoprotein Phosphatases from Yeast to Humans“. Molecular & Cellular Proteomics 17, Nr. 12 (18.09.2018): 2448–61. http://dx.doi.org/10.1074/mcp.ra118.000822.
Vickroy, Thomas W., Wendi L. Malphurs und Marie L. Carriger. „Regulation of stimulus-dependent hippocampal acetylcholine release by okadaic acid-sensitive phosphoprotein phosphatases“. Neuroscience Letters 191, Nr. 3 (Mai 1995): 200–204. http://dx.doi.org/10.1016/0304-3940(95)11576-i.
Matta, Csaba, Ali Mobasheri, Pál Gergely und Róza Zákány. „Ser/Thr-phosphoprotein phosphatases in chondrogenesis: neglected components of a two-player game“. Cellular Signalling 26, Nr. 10 (Oktober 2014): 2175–85. http://dx.doi.org/10.1016/j.cellsig.2014.06.013.
Chen, Lei, Qingling He, Yamin Liu, Yafei Wu, Dongsheng Ni, Jianing Liu, Yanxia Hu et al. „PPP3CB Inhibits Migration of G401 Cells via Regulating Epithelial-to-Mesenchymal Transition and Promotes G401 Cells Growth“. International Journal of Molecular Sciences 20, Nr. 2 (11.01.2019): 275. http://dx.doi.org/10.3390/ijms20020275.
Wagner, Volker, Gunther Geßner, Ines Heiland, Marc Kaminski, Susan Hawat, Kai Scheffler und Maria Mittag. „Analysis of the Phosphoproteome of Chlamydomonas reinhardtii Provides New Insights into Various Cellular Pathways“. Eukaryotic Cell 5, Nr. 3 (März 2006): 457–68. http://dx.doi.org/10.1128/ec.5.3.457-468.2006.
Lu, D. J., A. Takai, T. L. Leto und S. Grinstein. „Modulation of neutrophil activation by okadaic acid, a protein phosphatase inhibitor“. American Journal of Physiology-Cell Physiology 262, Nr. 1 (01.01.1992): C39—C49. http://dx.doi.org/10.1152/ajpcell.1992.262.1.c39.
Nasa, Isha, Lauren E. Cressey, Thomas Kruse, Emil P. T. Hertz, Jiang Gui, Lee M. Graves, Jakob Nilsson und Arminja N. Kettenbach. „Quantitative kinase and phosphatase profiling reveal that CDK1 phosphorylates PP2Ac to promote mitotic entry“. Science Signaling 13, Nr. 648 (08.09.2020): eaba7823. http://dx.doi.org/10.1126/scisignal.aba7823.
Lai, Yvonne, Blaise Z. Peterson und William A. Catterall. „Selective Dephosphorylation of the Subunits of Skeletal Muscle Calcium Channels by Purified Phosphoprotein Phosphatases“. Journal of Neurochemistry 61, Nr. 4 (Oktober 1993): 1333–39. http://dx.doi.org/10.1111/j.1471-4159.1993.tb13626.x.
Bhoola, R. „MODULATION OF THE RHYTHMIC PATTERNS OF EXPRESSION OF PHOSPHOPROTEIN PHOSPHATASES IN HUMAN LEUKAEMIA CELLS“. Cell Biology International 24, Nr. 8 (August 2000): 539–47. http://dx.doi.org/10.1006/cbir.2000.0568.
Nasa, Isha, und Arminja N. Kettenbach. „Effects of carboxyl-terminal methylation on holoenzyme function of the PP2A subfamily“. Biochemical Society Transactions 48, Nr. 5 (14.10.2020): 2015–27. http://dx.doi.org/10.1042/bst20200177.
Matange, Nishad, Marjetka Podobnik und Sandhya S. Visweswariah. „Metallophosphoesterases: structural fidelity with functional promiscuity“. Biochemical Journal 467, Nr. 2 (02.04.2015): 201–16. http://dx.doi.org/10.1042/bj20150028.