Статті в журналах з теми "Ser/Thr protein kinases"
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PHALIP, Vincent, Jian-Hong LI, and Cheng-Cai ZHANG. "HstK, a cyanobacterial protein with both a serine/threonine kinase domain and a histidine kinase domain: implication for the mechanism of signal transduction." Biochemical Journal 360, no. 3 (December 10, 2001): 639–44. http://dx.doi.org/10.1042/bj3600639.
Повний текст джерелаMizunuma, Masataka, Atsushi Kaneko, Shunta Imai, Kazuhiro Furukawa, and Yoshiro Chuman. "Methods for Identification of Substrates/Inhibitors of FCP/SCP Type Protein Ser/Thr Phosphatases." Processes 8, no. 12 (December 4, 2020): 1598. http://dx.doi.org/10.3390/pr8121598.
Повний текст джерелаSongyang, Z., K. P. Lu, Y. T. Kwon, L. H. Tsai, O. Filhol, C. Cochet, D. A. Brickey, et al. "A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1." Molecular and Cellular Biology 16, no. 11 (November 1996): 6486–93. http://dx.doi.org/10.1128/mcb.16.11.6486.
Повний текст джерелаSeok, Seung-Hyeon. "Structural Insights into Protein Regulation by Phosphorylation and Substrate Recognition of Protein Kinases/Phosphatases." Life 11, no. 9 (September 13, 2021): 957. http://dx.doi.org/10.3390/life11090957.
Повний текст джерелаBlume, Constanze, Peter M. Benz, Ulrich Walter, Joohun Ha, Bruce E. Kemp, and Thomas Renné. "AMP-activated Protein Kinase Impairs Endothelial Actin Cytoskeleton Assembly by Phosphorylating Vasodilator-stimulated Phosphoprotein." Journal of Biological Chemistry 282, no. 7 (November 2, 2006): 4601–12. http://dx.doi.org/10.1074/jbc.m608866200.
Повний текст джерелаPrasad, Jayendra, and James L. Manley. "Regulation and Substrate Specificity of the SR Protein Kinase Clk/Sty." Molecular and Cellular Biology 23, no. 12 (June 15, 2003): 4139–49. http://dx.doi.org/10.1128/mcb.23.12.4139-4149.2003.
Повний текст джерелаTHELEN, Jay J., Jan A. MIERNYK, and Douglas D. RANDALL. "Pyruvate dehydrogenase kinase from Arabidopsis thaliana: a protein histidine kinase that phosphorylates serine residues." Biochemical Journal 349, no. 1 (June 26, 2000): 195–201. http://dx.doi.org/10.1042/bj3490195.
Повний текст джерелаGangwal, Aakriti, Nitika Sangwan, Neha Dhasmana, Nishant Kumar, Chetkar Chandra Keshavam, Lalit K. Singh, Ankur Bothra, et al. "Role of serine/threonine protein phosphatase PrpN in the life cycle of Bacillus anthracis." PLOS Pathogens 18, no. 8 (August 1, 2022): e1010729. http://dx.doi.org/10.1371/journal.ppat.1010729.
Повний текст джерелаByrne, Dominic P., Safal Shrestha, Martin Galler, Min Cao, Leonard A. Daly, Amy E. Campbell, Claire E. Eyers, Elizabeth A. Veal, Natarajan Kannan, and Patrick A. Eyers. "Aurora A regulation by reversible cysteine oxidation reveals evolutionarily conserved redox control of Ser/Thr protein kinase activity." Science Signaling 13, no. 639 (July 7, 2020): eaax2713. http://dx.doi.org/10.1126/scisignal.aax2713.
Повний текст джерелаLutterbach, B., and S. R. Hann. "Hierarchical phosphorylation at N-terminal transformation-sensitive sites in c-Myc protein is regulated by mitogens and in mitosis." Molecular and Cellular Biology 14, no. 8 (August 1994): 5510–22. http://dx.doi.org/10.1128/mcb.14.8.5510-5522.1994.
Повний текст джерелаLutterbach, B., and S. R. Hann. "Hierarchical phosphorylation at N-terminal transformation-sensitive sites in c-Myc protein is regulated by mitogens and in mitosis." Molecular and Cellular Biology 14, no. 8 (August 1994): 5510–22. http://dx.doi.org/10.1128/mcb.14.8.5510.
Повний текст джерелаBIONDI, Ricardo M., and Angel R. NEBREDA. "Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions." Biochemical Journal 372, no. 1 (May 15, 2003): 1–13. http://dx.doi.org/10.1042/bj20021641.
Повний текст джерелаBaros, Seanantha S., Jonathan M. Blackburn, and Nelson C. Soares. "Phosphoproteomic Approaches to Discover Novel Substrates of Mycobacterial Ser/Thr Protein Kinases." Molecular & Cellular Proteomics 19, no. 2 (December 15, 2019): 233–44. http://dx.doi.org/10.1074/mcp.r119.001668.
Повний текст джерелаSalvi, Mauro, Luca Cesaro, and Lorenzo A. Pinna. "Variable contribution of protein kinases to the generation of the human phosphoproteome: a global weblogo analysis." BioMolecular Concepts 1, no. 2 (August 1, 2010): 185–95. http://dx.doi.org/10.1515/bmc.2010.013.
Повний текст джерелаWang, Junjun, Xinmiao Ji, Juanjuan Liu, and Xin Zhang. "Serine/Threonine Protein Kinase STK16." International Journal of Molecular Sciences 20, no. 7 (April 10, 2019): 1760. http://dx.doi.org/10.3390/ijms20071760.
Повний текст джерелаBAJPAI, Anil, and Zacharie BRAHMI. "Regulation of natural killer cell-mediated cytotoxicity by serine/threonine phosphatases: identification of a calyculin A-sensitive serine/threonine kinase." Biochemical Journal 320, no. 1 (November 15, 1996): 153–59. http://dx.doi.org/10.1042/bj3200153.
Повний текст джерелаFLEMING, Yvonne, Christopher G. ARMSTRONG, Nick MORRICE, Andrew PATERSON, Michel GOEDERT, and Philip COHEN. "Synergistic activation of stress-activated protein kinase 1/c-Jun N-terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein kinase kinase 4 (MKK4) and MKK7." Biochemical Journal 352, no. 1 (November 7, 2000): 145–54. http://dx.doi.org/10.1042/bj3520145.
Повний текст джерелаRezaei Adariani, Soheila, Marcel Buchholzer, Mohammad Akbarzadeh, Saeideh Nakhaei-Rad, Radovan Dvorsky, and Mohammad Reza Ahmadian. "Structural snapshots of RAF kinase interactions." Biochemical Society Transactions 46, no. 6 (October 31, 2018): 1393–406. http://dx.doi.org/10.1042/bst20170528.
Повний текст джерелаJENKINS, Scott M., Marcus ZINNERMAN, Craig GARNER, and Gail V. W. JOHNSON. "Modulation of tau phosphorylation and intracellular localization by cellular stress." Biochemical Journal 345, no. 2 (January 10, 2000): 263–70. http://dx.doi.org/10.1042/bj3450263.
Повний текст джерелаKnape, Matthias J., Maximilian Wallbott, Nicole C. G. Burghardt, Daniela Bertinetti, Jan Hornung, Sven H. Schmidt, Robin Lorenz, and Friedrich W. Herberg. "Molecular Basis for Ser/Thr Specificity in PKA Signaling." Cells 9, no. 6 (June 25, 2020): 1548. http://dx.doi.org/10.3390/cells9061548.
Повний текст джерелаClaywell, Ja E., and Derek J. Fisher. "CTL0511 from Chlamydia trachomatis Is a Type 2C Protein Phosphatase with Broad Substrate Specificity." Journal of Bacteriology 198, no. 13 (April 25, 2016): 1827–36. http://dx.doi.org/10.1128/jb.00025-16.
Повний текст джерелаVerma, Anita, and Anthony T. Maurelli. "Identification of Two Eukaryote-Like Serine/Threonine Kinases Encoded by Chlamydia trachomatis Serovar L2 and Characterization of Interacting Partners of Pkn1." Infection and Immunity 71, no. 10 (October 2003): 5772–84. http://dx.doi.org/10.1128/iai.71.10.5772-5784.2003.
Повний текст джерелаMao, Xinguo, Yuying Li, Shoaib Ur Rehman, Lili Miao, Yanfei Zhang, Xin Chen, Chunmei Yu, Jingyi Wang, Chaonan Li, and Ruilian Jing. "The Sucrose Non-Fermenting 1-Related Protein Kinase 2 (SnRK2) Genes Are Multifaceted Players in Plant Growth, Development and Response to Environmental Stimuli." Plant and Cell Physiology 61, no. 2 (December 13, 2019): 225–42. http://dx.doi.org/10.1093/pcp/pcz230.
Повний текст джерелаHEESOM, Kate J., Matthew B. AVISON, Tricia A. DIGGLE, and Richard M. DENTON. "Insulin-stimulated kinase from rat fat cells that phosphorylates initiation factor 4E-binding protein 1 on the rapamycin-insensitive site (serine-111)." Biochemical Journal 336, no. 1 (November 15, 1998): 39–48. http://dx.doi.org/10.1042/bj3360039.
Повний текст джерелаFACCHIN, Sonia, Raffaele LOPREIATO, Silvia STOCCHETTO, Giorgio ARRIGONI, Luca CESARO, Oriano MARIN, Giovanna CARIGNANI, and Lorenzo A. PINNA. "Structure–function analysis of yeast piD261/Bud32, an atypical protein kinase essential for normal cell life." Biochemical Journal 364, no. 2 (June 1, 2002): 457–63. http://dx.doi.org/10.1042/bj20011376.
Повний текст джерелаBoo, Yong Chool, and Hanjoong Jo. "Flow-dependent regulation of endothelial nitric oxide synthase: role of protein kinases." American Journal of Physiology-Cell Physiology 285, no. 3 (September 2003): C499—C508. http://dx.doi.org/10.1152/ajpcell.00122.2003.
Повний текст джерелаTyler, Jessica S., and David I. Friedman. "Characterization of a Eukaryotic-Like Tyrosine Protein Kinase Expressed by the Shiga Toxin-Encoding Bacteriophage 933W." Journal of Bacteriology 186, no. 11 (June 1, 2004): 3472–79. http://dx.doi.org/10.1128/jb.186.11.3472-3479.2004.
Повний текст джерелаMorrison, Donna L., Jasbinder S. Sanghera, Justine Stewart, Steven L. Pelech, Cindy Sutherland, and Michael P. Walsh. "Phosphorylation and activation of smooth muscle myosin light chain kinase by MAP kinase and cyclin-dependent kinase-1." Biochemistry and Cell Biology 74, no. 4 (July 1, 1996): 549–57. http://dx.doi.org/10.1139/o96-459.
Повний текст джерелаAtkinson, Eleanor L., Jessica Iegre, Paul D. Brear, Elizabeth A. Zhabina, Marko Hyvönen, and David R. Spring. "Downfalls of Chemical Probes Acting at the Kinase ATP-Site: CK2 as a Case Study." Molecules 26, no. 7 (March 31, 2021): 1977. http://dx.doi.org/10.3390/molecules26071977.
Повний текст джерелаDESDOUITS, Frédéric, C. Julio SICILIANO, C. Angus NAIRN, Paul GREENGARD, and 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, no. 1 (February 15, 1998): 211–16. http://dx.doi.org/10.1042/bj3300211.
Повний текст джерелаMassillon, D., W. Stalmans, G. van de Werve, and M. Bollen. "Identification of the glycogenic compound 5-iodotubercidin as a general protein kinase inhibitor." Biochemical Journal 299, no. 1 (April 1, 1994): 123–28. http://dx.doi.org/10.1042/bj2990123.
Повний текст джерелаHoekstra, M. F., N. Dhillon, G. Carmel, A. J. DeMaggio, R. A. Lindberg, T. Hunter, and J. Kuret. "Budding and fission yeast casein kinase I isoforms have dual-specificity protein kinase activity." Molecular Biology of the Cell 5, no. 8 (August 1994): 877–86. http://dx.doi.org/10.1091/mbc.5.8.877.
Повний текст джерелаvan WILLIGEN, Gijsbert, Ingeborg HERS, Gertie GORTER та Jan-Willem N. AKKERMAN. "Exposure of ligand-binding sites on platelet integrin αIIB/β3 by phosphorylation of the β3 subunit". Biochemical Journal 314, № 3 (15 березня 1996): 769–79. http://dx.doi.org/10.1042/bj3140769.
Повний текст джерелаNováková, Linda, Silvia Bezoušková, Petr Pompach, Petra Špidlová, Lenka Sasková, Jaroslav Weiser, and Pavel Branny. "Identification of Multiple Substrates of the StkP Ser/Thr Protein Kinase in Streptococcus pneumoniae." Journal of Bacteriology 192, no. 14 (May 7, 2010): 3629–38. http://dx.doi.org/10.1128/jb.01564-09.
Повний текст джерелаGuerra, Barbara, and Olaf-Georg Issinger. "Natural Compounds and Derivatives as Ser/Thr Protein Kinase Modulators and Inhibitors." Pharmaceuticals 12, no. 1 (January 1, 2019): 4. http://dx.doi.org/10.3390/ph12010004.
Повний текст джерелаFujino, Aiko, Kei Fukushima, Naoko Namiki, Tomomi Kosugi, and Midori Takimoto-Kamimura. "Structural analysis of an MK2–inhibitor complex: insight into the regulation of the secondary structure of the Gly-rich loop by TEI-I01800." Acta Crystallographica Section D Biological Crystallography 66, no. 1 (December 21, 2009): 80–87. http://dx.doi.org/10.1107/s0907444909046411.
Повний текст джерелаKlomp, Jennifer E., Vincent Huyot, Anne-Marie Ray, Kerrie B. Collins, Asrar B. Malik, and Andrei V. Karginov. "Mimicking transient activation of protein kinases in living cells." Proceedings of the National Academy of Sciences 113, no. 52 (December 12, 2016): 14976–81. http://dx.doi.org/10.1073/pnas.1609675114.
Повний текст джерелаSong, Weimeng, Li Hu, Zhihui Ma, Lei Yang, and Jianming Li. "Importance of Tyrosine Phosphorylation in Hormone-Regulated Plant Growth and Development." International Journal of Molecular Sciences 23, no. 12 (June 13, 2022): 6603. http://dx.doi.org/10.3390/ijms23126603.
Повний текст джерелаKowalsky, Allison Ho, Sim Namkoong, Eric Mettetal, Hwan-Woo Park, Dubek Kazyken, Diane C. Fingar, and Jun Hee Lee. "The GATOR2–mTORC2 axis mediates Sestrin2-induced AKT Ser/Thr kinase activation." Journal of Biological Chemistry 295, no. 7 (January 8, 2020): 1769–80. http://dx.doi.org/10.1074/jbc.ra119.010857.
Повний текст джерелаAv-Gay, Yossef, Sarwat Jamil, and Steven J. Drews. "Expression and Characterization of the Mycobacterium tuberculosis Serine/Threonine Protein Kinase PknB." Infection and Immunity 67, no. 11 (November 1, 1999): 5676–82. http://dx.doi.org/10.1128/iai.67.11.5676-5682.1999.
Повний текст джерелаWang, Cheng C., Mariano Tao, Tiequan Wei, and Philip S. Low. "Identification of the Major Casein Kinase I Phosphorylation Sites on Erythrocyte Band 3." Blood 89, no. 8 (April 15, 1997): 3019–24. http://dx.doi.org/10.1182/blood.v89.8.3019.
Повний текст джерелаAlomair, Lamya, Sabeena Mustafa, Mohsin Saleet Jafri, Wardah Alharbi, Abdulrhman Aljouie, Fahad Almsned, Mohammed Alawad, Yahya Abdulfattah Bokhari, and Mamoon Rashid. "Molecular Dynamics Simulations to Decipher the Role of Phosphorylation of SARS-CoV-2 Nonstructural Proteins (nsps) in Viral Replication." Viruses 14, no. 11 (November 2, 2022): 2436. http://dx.doi.org/10.3390/v14112436.
Повний текст джерелаXing, Jun, Jon M. Kornhauser, Zhengui Xia, Elizabeth A. Thiele, and Michael E. Greenberg. "Nerve Growth Factor Activates Extracellular Signal-Regulated Kinase and p38 Mitogen-Activated Protein Kinase Pathways To Stimulate CREB Serine 133 Phosphorylation." Molecular and Cellular Biology 18, no. 4 (April 1, 1998): 1946–55. http://dx.doi.org/10.1128/mcb.18.4.1946.
Повний текст джерелаZhou, Peifu, Dennis Wong, Wu Li, Jianping Xie, and Yossef Av-Gay. "Phosphorylation of Mycobacterium tuberculosis protein tyrosine kinase A PtkA by Ser/Thr protein kinases." Biochemical and Biophysical Research Communications 467, no. 2 (November 2015): 421–26. http://dx.doi.org/10.1016/j.bbrc.2015.09.124.
Повний текст джерелаMukhopadhyay, Subhendu, Vinayak Kapatral, Wenbin Xu, and A. M. Chakrabarty. "Characterization of a Hank’s Type Serine/Threonine Kinase and Serine/Threonine Phosphoprotein Phosphatase inPseudomonas aeruginosa." Journal of Bacteriology 181, no. 21 (November 1, 1999): 6615–22. http://dx.doi.org/10.1128/jb.181.21.6615-6622.1999.
Повний текст джерелаChen, R. H., C. Sarnecki, and J. Blenis. "Nuclear localization and regulation of erk- and rsk-encoded protein kinases." Molecular and Cellular Biology 12, no. 3 (March 1992): 915–27. http://dx.doi.org/10.1128/mcb.12.3.915-927.1992.
Повний текст джерелаChen, R. H., C. Sarnecki, and J. Blenis. "Nuclear localization and regulation of erk- and rsk-encoded protein kinases." Molecular and Cellular Biology 12, no. 3 (March 1992): 915–27. http://dx.doi.org/10.1128/mcb.12.3.915.
Повний текст джерелаWang, Luyao, Ying Gui, Bingye Yang, Wenpan Dong, Peiling Xu, Fangjie Si, Wei Yang, et al. "Mitogen-Activated Protein Kinases Associated Sites of Tobacco Repression of Shoot Growth Regulates Its Localization in Plant Cells." International Journal of Molecular Sciences 23, no. 16 (August 11, 2022): 8941. http://dx.doi.org/10.3390/ijms23168941.
Повний текст джерелаNádvorník, Richard, Tomáš Vomastek, Jiří Janeček, Zuzana Techniková, and Pavel Branny. "Pkg2, a Novel Transmembrane Protein Ser/Thr Kinase of Streptomyces granaticolor." Journal of Bacteriology 181, no. 1 (January 1, 1999): 15–23. http://dx.doi.org/10.1128/jb.181.1.15-23.1999.
Повний текст джерелаKarthigeyan, Dhanasekan, Arnab Bose, Ramachandran Boopathi, Vinay Jaya Rao, Hiroki Shima, Narendra Bharathy, Kazuhiko Igarashi, Reshma Taneja, Arun Kumar Trivedi, and Tapas K. Kundu. "Aurora kinase A-mediated phosphorylation of mPOU at a specific site drives skeletal muscle differentiation." Journal of Biochemistry 167, no. 2 (October 30, 2019): 195–201. http://dx.doi.org/10.1093/jb/mvz088.
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