Artykuły w czasopismach na temat „Phosphorylation”
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Hizli, Asli A., Yong Chi, Jherek Swanger, John H. Carter, Yi Liao, Markus Welcker, Alexey G. Ryazanov i Bruce E. Clurman. "Phosphorylation of Eukaryotic Elongation Factor 2 (eEF2) by Cyclin A–Cyclin-Dependent Kinase 2 Regulates Its Inhibition by eEF2 Kinase". Molecular and Cellular Biology 33, nr 3 (26.11.2012): 596–604. http://dx.doi.org/10.1128/mcb.01270-12.
Pełny tekst źródłaCoulonval, Katia, Hugues Kooken i Pierre P. Roger. "Coupling of T161 and T14 phosphorylations protects cyclin B–CDK1 from premature activation". Molecular Biology of the Cell 22, nr 21 (listopad 2011): 3971–85. http://dx.doi.org/10.1091/mbc.e11-02-0136.
Pełny tekst źródłaADAMS, Ryan A., Xinran LIU, David S. WILLIAMS i Alexandra C. NEWTON. "Differential spatial and temporal phosphorylation of the visual receptor, rhodopsin, at two primary phosphorylation sites in mice exposed to light". Biochemical Journal 374, nr 2 (1.09.2003): 537–43. http://dx.doi.org/10.1042/bj20030408.
Pełny tekst źródłaVanoosthuyse, Vincent, i Kevin G. Hardwick. "The Complexity of Bub1 Regulation: Phosphorylation, Phosphorylation, Phosphorylation". Cell Cycle 2, nr 2 (7.03.2003): 118–19. http://dx.doi.org/10.4161/cc.2.2.343.
Pełny tekst źródłaPant, Harish C., i Veeranna. "Neurofilament phosphorylation". Biochemistry and Cell Biology 73, nr 9-10 (1.09.1995): 575–92. http://dx.doi.org/10.1139/o95-063.
Pełny tekst źródłaKabachnik, M. I., L. S. Zakharov, E. I. Goryunov i I. Yu Kudryavtsev. "Catalytic phosphorylation of polyfluoroalkanols. 11. ?-Polyfluoroalkylbenzyldichlorophosphates as phosphorylating agents in the catalytic phosphorylation of primary polyfluoroalkanols". Bulletin of the Academy of Sciences of the USSR Division of Chemical Science 38, nr 7 (lipiec 1989): 1522–26. http://dx.doi.org/10.1007/bf00978451.
Pełny tekst źródłaBhattacharyya, Sumit, Alip Borthakur, Arivarasu N. Anbazhagan, Shivani Katyal, Pradeep K. Dudeja i Joanne K. Tobacman. "Specific effects of BCL10 Serine mutations on phosphorylations in canonical and noncanonical pathways of NF-κB activation following carrageenan". American Journal of Physiology-Gastrointestinal and Liver Physiology 301, nr 3 (wrzesień 2011): G475—G486. http://dx.doi.org/10.1152/ajpgi.00071.2011.
Pełny tekst źródłaCarty, DJ, DL Freas i AR Gear. "ADP causes subsecond changes in protein phosphorylation of platelets". Blood 70, nr 2 (1.08.1987): 511–15. http://dx.doi.org/10.1182/blood.v70.2.511.511.
Pełny tekst źródłaCarty, DJ, DL Freas i AR Gear. "ADP causes subsecond changes in protein phosphorylation of platelets". Blood 70, nr 2 (1.08.1987): 511–15. http://dx.doi.org/10.1182/blood.v70.2.511.bloodjournal702511.
Pełny tekst źródłaLanglais, Paul, Zhengping Yi i Lawrence J. Mandarino. "The Identification of Raptor as a Substrate for p44/42 MAPK". Endocrinology 152, nr 4 (15.02.2011): 1264–73. http://dx.doi.org/10.1210/en.2010-1271.
Pełny tekst źródłaViolin, Jonathan D., Jin Zhang, Roger Y. Tsien i Alexandra C. Newton. "A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C". Journal of Cell Biology 161, nr 5 (2.06.2003): 899–909. http://dx.doi.org/10.1083/jcb.200302125.
Pełny tekst źródłaVary, Thomas C., i Christopher J. Lynch. "Meal feeding enhances formation of eIF4F in skeletal muscle: role of increased eIF4E availability and eIF4G phosphorylation". American Journal of Physiology-Endocrinology and Metabolism 290, nr 4 (kwiecień 2006): E631—E642. http://dx.doi.org/10.1152/ajpendo.00460.2005.
Pełny tekst źródłaNorling, L. L., i M. Landt. "Comparison of Ca2+-dependent phosphorylation in viable dispersed brain cells with calmodulin-dependent protein kinase activity in cell-free preparations of rat brain". Biochemical Journal 232, nr 3 (15.12.1985): 629–35. http://dx.doi.org/10.1042/bj2320629.
Pełny tekst źródłaDusi, S., M. Donini i F. Rossi. "Tyrosine phosphorylation and activation of NADPH oxidase in human neutrophils: a possible role for MAP kinases and for a 75 kDa protein". Biochemical Journal 304, nr 1 (15.11.1994): 243–50. http://dx.doi.org/10.1042/bj3040243.
Pełny tekst źródłaKNEBEL, Axel, Claire E. HAYDON, Nick MORRICE i Philip COHEN. "Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and −insensitive pathways". Biochemical Journal 367, nr 2 (15.10.2002): 525–32. http://dx.doi.org/10.1042/bj20020916.
Pełny tekst źródłaHarper, Mary-Ellen, i Martin D. Brand. "Hyperthyroidism stimulates mitochondrial proton leak and ATP turnover in rat hepatocytes but does not change the overall kinetics of substrate oxidation reactions". Canadian Journal of Physiology and Pharmacology 72, nr 8 (1.08.1994): 899–908. http://dx.doi.org/10.1139/y94-127.
Pełny tekst źródłaGaplovska-Kysela, Katarina, i Andrea Sevcovicova. "Phosphorylation". Cell Cycle 12, nr 5 (marzec 2013): 716. http://dx.doi.org/10.4161/cc.23910.
Pełny tekst źródłaBABY, Y., M. TSUHAKO i N. YOZA. "ChemInform Abstract: Phosphorylation of Biomolecules with Inorganic Phosphorylating Agents." ChemInform 25, nr 25 (19.08.2010): no. http://dx.doi.org/10.1002/chin.199425285.
Pełny tekst źródłaCohen, M. E., G. W. Sharp i M. Donowitz. "Suggestion of a role for calmodulin and phosphorylation in regulation of rabbit ileal electrolyte transport: effects of promethazine". American Journal of Physiology-Gastrointestinal and Liver Physiology 251, nr 5 (1.11.1986): G710—G717. http://dx.doi.org/10.1152/ajpgi.1986.251.5.g710.
Pełny tekst źródłaGeraghty, Kathryn M., Shuai Chen, Jean E. Harthill, Adel F. Ibrahim, Rachel Toth, Nick A. Morrice, Franck Vandermoere, Greg B. Moorhead, D. Grahame Hardie i Carol MacKintosh. "Regulation of multisite phosphorylation and 14-3-3 binding of AS160 in response to IGF-1, EGF, PMA and AICAR". Biochemical Journal 407, nr 2 (25.09.2007): 231–41. http://dx.doi.org/10.1042/bj20070649.
Pełny tekst źródłaSolomon, M. J., T. Lee i M. W. Kirschner. "Role of phosphorylation in p34cdc2 activation: identification of an activating kinase." Molecular Biology of the Cell 3, nr 1 (styczeń 1992): 13–27. http://dx.doi.org/10.1091/mbc.3.1.13.
Pełny tekst źródłaScheid, Michael P., Paola A. Marignani i James R. Woodgett. "Multiple Phosphoinositide 3-Kinase-Dependent Steps in Activation of Protein Kinase B". Molecular and Cellular Biology 22, nr 17 (1.09.2002): 6247–60. http://dx.doi.org/10.1128/mcb.22.17.6247-6260.2002.
Pełny tekst źródłaBenes, Cyril, i Stephen P. Soltoff. "Modulation of PKCδ tyrosine phosphorylation and activity in salivary and PC-12 cells by Src kinases". American Journal of Physiology-Cell Physiology 280, nr 6 (1.06.2001): C1498—C1510. http://dx.doi.org/10.1152/ajpcell.2001.280.6.c1498.
Pełny tekst źródłaVendelbo, M. H., A. B. Møller, J. T. Treebak, L. C. Gormsen, L. J. Goodyear, J. F. P. Wojtaszewski, J. O. L. Jørgensen, N. Møller i N. Jessen. "Sustained AS160 and TBC1D1 phosphorylations in human skeletal muscle 30 min after a single bout of exercise". Journal of Applied Physiology 117, nr 3 (1.08.2014): 289–96. http://dx.doi.org/10.1152/japplphysiol.00044.2014.
Pełny tekst źródłaGreiwe, Julia F., Thomas C. R. Miller, Julia Locke, Fabrizio Martino, Steven Howell, Anne Schreiber, Andrea Nans, John F. X. Diffley i Alessandro Costa. "Structural mechanism for the selective phosphorylation of DNA-loaded MCM double hexamers by the Dbf4-dependent kinase". Nature Structural & Molecular Biology 29, nr 1 (28.12.2021): 10–20. http://dx.doi.org/10.1038/s41594-021-00698-z.
Pełny tekst źródłaAlmagor, Lior, Ivan S. Ufimtsev, Aruna Ayer, Jingzhi Li i William I. Weis. "Structural insights into the aPKC regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2". Proceedings of the National Academy of Sciences 116, nr 22 (14.05.2019): 10804–12. http://dx.doi.org/10.1073/pnas.1821514116.
Pełny tekst źródłaHer, J. H., S. Lakhani, K. Zu, J. Vila, P. Dent, T. W. Sturgill i M. J. Weber. "Dual phosphorylation and autophosphorylation in mitogen-activated protein (MAP) kinase activation". Biochemical Journal 296, nr 1 (15.11.1993): 25–31. http://dx.doi.org/10.1042/bj2960025.
Pełny tekst źródłaHamáková, Kateřina, David Potěšil, Ondřej Bernatik, Igor Červenka, Matěj Rádsetoulal, Vitězslav Bryja i Zbyněk Zdráhal. "Semiquantitative Assessment of Dishevelled-3 Phosphorylation Status by Mass Spectrometry". Hungarian Journal of Industry and Chemistry 46, nr 1 (1.07.2018): 3–6. http://dx.doi.org/10.1515/hjic-2018-0002.
Pełny tekst źródłaMaik-Rachline, Galia, Shmuel Shaltiel i Rony Seger. "Extracellular phosphorylation converts pigment epithelium–derived factor from a neurotrophic to an antiangiogenic factor". Blood 105, nr 2 (15.01.2005): 670–78. http://dx.doi.org/10.1182/blood-2004-04-1569.
Pełny tekst źródłaAmano, Mutsuki, Yoko Kanazawa, Kei Kozawa i Kozo Kaibuchi. "Identification of the Kinase-Substrate Recognition Interface between MYPT1 and Rho-Kinase". Biomolecules 12, nr 2 (18.01.2022): 159. http://dx.doi.org/10.3390/biom12020159.
Pełny tekst źródłaLakkireddy, Dr Suresh. "MOLECULAR ADVANCEMENTS IN PROTEIN PHOSPHORYLATION METHODOLOGIES: A RAPID REVIEW". Era's Journal of Medical Research 10, nr 2 (grudzień 2023): 35–38. http://dx.doi.org/10.24041/ejmr2023.33.
Pełny tekst źródłaZheng, Yupeng, Sam John, James J. Pesavento, Jennifer R. Schultz-Norton, R. Louis Schiltz, Sonjoon Baek, Ann M. Nardulli, Gordon L. Hager, Neil L. Kelleher i Craig A. Mizzen. "Histone H1 phosphorylation is associated with transcription by RNA polymerases I and II". Journal of Cell Biology 189, nr 3 (3.05.2010): 407–15. http://dx.doi.org/10.1083/jcb.201001148.
Pełny tekst źródłaThornton, Tina, i Mercedes Rincon. "The role of p38 MAPK/GSK3β signaling in T and B lymphocytes undergoing programmed DNA recombination (111.47)". Journal of Immunology 188, nr 1_Supplement (1.05.2012): 111.47. http://dx.doi.org/10.4049/jimmunol.188.supp.111.47.
Pełny tekst źródłaSoltys, Carrie-Lynn M., Suzanne Kovacic i Jason R. B. Dyck. "Activation of cardiac AMP-activated protein kinase by LKB1 expression or chemical hypoxia is blunted by increased Akt activity". American Journal of Physiology-Heart and Circulatory Physiology 290, nr 6 (czerwiec 2006): H2472—H2479. http://dx.doi.org/10.1152/ajpheart.01206.2005.
Pełny tekst źródłaAkiyama, T., T. Saito, H. Ogawara, K. Toyoshima i T. Yamamoto. "Tumor promoter and epidermal growth factor stimulate phosphorylation of the c-erbB-2 gene product in MKN-7 human adenocarcinoma cells". Molecular and Cellular Biology 8, nr 3 (marzec 1988): 1019–26. http://dx.doi.org/10.1128/mcb.8.3.1019-1026.1988.
Pełny tekst źródłaAkiyama, T., T. Saito, H. Ogawara, K. Toyoshima i T. Yamamoto. "Tumor promoter and epidermal growth factor stimulate phosphorylation of the c-erbB-2 gene product in MKN-7 human adenocarcinoma cells." Molecular and Cellular Biology 8, nr 3 (marzec 1988): 1019–26. http://dx.doi.org/10.1128/mcb.8.3.1019.
Pełny tekst źródłaAhn, Jae Suk, Andrea Musacchio, Marina Mapelli, Jake Ni, Leonard Scinto, Ross Stein, Kenneth S. Kosik i Li-An Yeh. "Development of an Assay to Screen for Inhibitors of Tau Phosphorylation by Cdk5". Journal of Biomolecular Screening 9, nr 2 (marzec 2004): 122–31. http://dx.doi.org/10.1177/1087057103260594.
Pełny tekst źródłaVilimek, Dino, i Vincent Duronio. "Cytokine-stimulated phosphorylation of GSK-3 is primarily dependent upon PKCs, not PKB". Biochemistry and Cell Biology 84, nr 1 (1.02.2006): 20–29. http://dx.doi.org/10.1139/o05-154.
Pełny tekst źródłaOgura, Masato, Junko Yamaki, Miwako K. Homma i Yoshimi Homma. "Mitochondrial c-Src regulates cell survival through phosphorylation of respiratory chain components". Biochemical Journal 447, nr 2 (26.09.2012): 281–89. http://dx.doi.org/10.1042/bj20120509.
Pełny tekst źródłaShimasaki, Kentaro, Keigo Kumagai, Shota Sakai, Toshiyuki Yamaji i Kentaro Hanada. "Hyperosmotic Stress Induces Phosphorylation of CERT and Enhances Its Tethering throughout the Endoplasmic Reticulum". International Journal of Molecular Sciences 23, nr 7 (5.04.2022): 4025. http://dx.doi.org/10.3390/ijms23074025.
Pełny tekst źródłaKurihara, Kinji, Nobuo Nakanishi, Marilyn L. Moore-Hoon i R. James Turner. "Phosphorylation of the salivary Na+-K+-2Cl− cotransporter". American Journal of Physiology-Cell Physiology 282, nr 4 (1.04.2002): C817—C823. http://dx.doi.org/10.1152/ajpcell.00352.2001.
Pełny tekst źródłaMatusiak, Magdalena, Nina Van Opdenbosch, Lieselotte Vande Walle, Jean-Claude Sirard, Thirumala-Devi Kanneganti i Mohamed Lamkanfi. "Flagellin-induced NLRC4 phosphorylation primes the inflammasome for activation by NAIP5". Proceedings of the National Academy of Sciences 112, nr 5 (20.01.2015): 1541–46. http://dx.doi.org/10.1073/pnas.1417945112.
Pełny tekst źródłaSong, Weimeng, Li Hu, Zhihui Ma, Lei Yang i Jianming Li. "Importance of Tyrosine Phosphorylation in Hormone-Regulated Plant Growth and Development". International Journal of Molecular Sciences 23, nr 12 (13.06.2022): 6603. http://dx.doi.org/10.3390/ijms23126603.
Pełny tekst źródłaTinsley, John H., Elena E. Ustinova, Wenjuan Xu i Sarah Y. Yuan. "Src-dependent, neutrophil-mediated vascular hyperpermeability and β-catenin modification". American Journal of Physiology-Cell Physiology 283, nr 6 (1.12.2002): C1745—C1751. http://dx.doi.org/10.1152/ajpcell.00230.2002.
Pełny tekst źródłaHolt, K. H., B. G. Kasson i J. E. Pessin. "Insulin stimulation of a MEK-dependent but ERK-independent SOS protein kinase." Molecular and Cellular Biology 16, nr 2 (luty 1996): 577–83. http://dx.doi.org/10.1128/mcb.16.2.577.
Pełny tekst źródłaBishop, R., R. Martinez, M. J. Weber, P. J. Blackshear, S. Beatty, R. Lim i H. R. Herschman. "Protein phosphorylation in a tetradecanoyl phorbol acetate-nonproliferative variant of 3T3 cells". Molecular and Cellular Biology 5, nr 9 (wrzesień 1985): 2231–37. http://dx.doi.org/10.1128/mcb.5.9.2231-2237.1985.
Pełny tekst źródłaBishop, R., R. Martinez, M. J. Weber, P. J. Blackshear, S. Beatty, R. Lim i H. R. Herschman. "Protein phosphorylation in a tetradecanoyl phorbol acetate-nonproliferative variant of 3T3 cells." Molecular and Cellular Biology 5, nr 9 (wrzesień 1985): 2231–37. http://dx.doi.org/10.1128/mcb.5.9.2231.
Pełny tekst źródłaDrepper, Friedel, Jacek Biernat, Senthilvelrajan Kaniyappan, Helmut E. Meyer, Eva Maria Mandelkow, Bettina Warscheid i Eckhard Mandelkow. "A combinatorial native MS and LC-MS/MS approach reveals high intrinsic phosphorylation of human Tau but minimal levels of other key modifications". Journal of Biological Chemistry 295, nr 52 (26.10.2020): 18213–25. http://dx.doi.org/10.1074/jbc.ra120.015882.
Pełny tekst źródłaL'Allemain, G., J. H. Her, J. Wu, T. W. Sturgill i M. J. Weber. "Growth factor-induced activation of a kinase activity which causes regulatory phosphorylation of p42/microtubule-associated protein kinase". Molecular and Cellular Biology 12, nr 5 (maj 1992): 2222–29. http://dx.doi.org/10.1128/mcb.12.5.2222-2229.1992.
Pełny tekst źródłaL'Allemain, G., J. H. Her, J. Wu, T. W. Sturgill i M. J. Weber. "Growth factor-induced activation of a kinase activity which causes regulatory phosphorylation of p42/microtubule-associated protein kinase." Molecular and Cellular Biology 12, nr 5 (maj 1992): 2222–29. http://dx.doi.org/10.1128/mcb.12.5.2222.
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