Relevant bibliographies by topics / Protein kinases

Academic literature on the topic 'Protein kinases'

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Published: 4 June 2021
Last updated: 29 July 2024

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Journal articles on the topic "Protein kinases"

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Frost, J. A., S. Xu, M. R. Hutchison, S. Marcus, and M. H. Cobb. "Actions of Rho family small G proteins and p21-activated protein kinases on mitogen-activated protein kinase family members." Molecular and Cellular Biology 16, no. 7 (July 1996): 3707–13. http://dx.doi.org/10.1128/mcb.16.7.3707.

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The mitogen-activated protein (MAP) kinases are a family of serine/threonine kinases that are regulated by distinct extracellular stimuli. The currently known members include extracellular signal-regulated protein kinase 1 (ERK1), ERK2, the c-Jun N-terminal kinase/stress-activated protein kinases (JNK/SAPKs), and p38 MAP kinases. We find that overexpression of the Ste20-related enzymes p21-activated kinase 1 (PAK1) and PAK2 in 293 cells is sufficient to activate JNK/SAPK and to a lesser extent p38 MAP kinase but not ERK2. Rat MAP/ERK kinase kinase 1 can stimulate the activity of each of these MAP kinases. Although neither activated Rac nor the PAKs stimulate ERK2 activity, overexpression of either dominant negative Rac2 or the N-terminal regulatory domain of PAK1 inhibits Ras-mediated activation of ERK2, suggesting a permissive role for Rac in the control of the ERK pathway. Furthermore, constitutively active Rac2, Cdc42hs, and RhoA synergize with an activated form of Raf to increase ERK2 activity. These findings reveal a previously unrecognized connection between Rho family small G proteins and the ERK pathway.
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Jurcik, Jan, Barbara Sivakova, Ingrid Cipakova, Tomas Selicky, Erika Stupenova, Matus Jurcik, Michaela Osadska, Peter Barath, and Lubos Cipak. "Phosphoproteomics Meets Chemical Genetics: Approaches for Global Mapping and Deciphering the Phosphoproteome." International Journal of Molecular Sciences 21, no. 20 (October 15, 2020): 7637. http://dx.doi.org/10.3390/ijms21207637.

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Protein kinases are important enzymes involved in the regulation of various cellular processes. To function properly, each protein kinase phosphorylates only a limited number of proteins among the thousands present in the cell. This provides a rapid and dynamic regulatory mechanism that controls biological functions of the proteins. Despite the importance of protein kinases, most of their substrates remain unknown. Recently, the advances in the fields of protein engineering, chemical genetics, and mass spectrometry have boosted studies on identification of bona fide substrates of protein kinases. Among the various methods in protein kinase specific substrate identification, genetically engineered protein kinases and quantitative phosphoproteomics have become promising tools. Herein, we review the current advances in the field of chemical genetics in analog-sensitive protein kinase mutants and highlight selected strategies for identifying protein kinase substrates and studying the dynamic nature of protein phosphorylation.
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Hurley, Rebecca L., Kristin A. Anderson, Jeanne M. Franzone, Bruce E. Kemp, Anthony R. Means, and Lee A. Witters. "The Ca2+/Calmodulin-dependent Protein Kinase Kinases Are AMP-activated Protein Kinase Kinases." Journal of Biological Chemistry 280, no. 32 (June 24, 2005): 29060–66. http://dx.doi.org/10.1074/jbc.m503824200.

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Wang, Pengcheng, Chuan-Chih Hsu, Yanyan Du, Peipei Zhu, Chunzhao Zhao, Xing Fu, Chunguang Zhang, et al. "Mapping proteome-wide targets of protein kinases in plant stress responses." Proceedings of the National Academy of Sciences 117, no. 6 (January 28, 2020): 3270–80. http://dx.doi.org/10.1073/pnas.1919901117.

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Protein kinases are major regulatory components in almost all cellular processes in eukaryotic cells. By adding phosphate groups, protein kinases regulate the activity, localization, protein–protein interactions, and other features of their target proteins. It is known that protein kinases are central components in plant responses to environmental stresses such as drought, high salinity, cold, and pathogen attack. However, only a few targets of these protein kinases have been identified. Moreover, how these protein kinases regulate downstream biological processes and mediate stress responses is still largely unknown. In this study, we introduce a strategy based on isotope-labeled in vitro phosphorylation reactions using in vivo phosphorylated peptides as substrate pools and apply this strategy to identify putative substrates of nine protein kinases that function in plant abiotic and biotic stress responses. As a result, we identified more than 5,000 putative target sites of osmotic stress-activated SnRK2.4 and SnRK2.6, abscisic acid-activated protein kinases SnRK2.6 and casein kinase 1-like 2 (CKL2), elicitor-activated protein kinase CDPK11 and MPK6, cold-activated protein kinase MPK6, H2O2-activated protein kinase OXI1 and MPK6, and salt-induced protein kinase SOS1 and MPK6, as well as the low-potassium-activated protein kinase CIPK23. These results provide comprehensive information on the role of these protein kinases in the control of cellular activities and could be a valuable resource for further studies on the mechanisms underlying plant responses to environmental stresses.
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Luise, M., C. Presotto, L. Senter, R. Betto, S. Ceoldo, S. Furlan, S. Salvatori, R. A. Sabbadini, and G. Salviati. "Dystrophin is phosphorylated by endogenous protein kinases." Biochemical Journal 293, no. 1 (July 1, 1993): 243–47. http://dx.doi.org/10.1042/bj2930243.

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Dystrophin, the protein coded by the gene missing in Duchenne muscular dystrophy, is assumed to be a component of the membrane cytoskeleton of skeletal muscle. Like other cytoskeletal proteins in different cell types, dystrophin bound to sarcolemma membranes was found to be phosphorylated by endogenous protein kinases. The phosphorylation of dystrophin was activated by cyclic AMP, cyclic GMP, calcium and calmodulin, and was inhibited by cyclic AMP-dependent protein kinase peptide inhibitor, mastoparan and heparin. These results suggest that membrane-bound dystrophin is a substrate of endogenous cyclic AMP- and cyclic GMP-dependent protein kinases, calcium/calmodulin-dependent kinase and casein kinase II. The possibility that dystrophin could be phosphorylated by protein kinase C is suggested by the inhibition of phosphorylation by staurosporin. On the other hand dystrophin seems not to be a substrate for protein tyrosine kinases, as shown by the lack of reaction of phosphorylated dystrophin with a monoclonal antiphosphotyrosine antibody. Sequence analysis indicates that dystrophin contains seven potential phosphorylation sites for cyclic AMP- and cyclic GMP-dependent protein kinases (all localized in the central rod domain of the molecule) as well as several sites for protein kinase C and casein kinase II. Interestingly, potential sites of phosphorylation by protein kinase C and casein kinase II are located in the proximity of the actin-binding site. These results suggest, by analogy with what has been demonstrated in the case of other cytoskeletal proteins, that the phosphorylation of dystrophin by endogenous protein kinases may modulate both self assembly and interaction of dystrophin with other cytoskeletal proteins in vivo.
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Lawrence, David S., and Jinkui Niu. "Protein Kinase InhibitorsThe Tyrosine-Specific Protein Kinases." Pharmacology & Therapeutics 77, no. 2 (February 1998): 81–114. http://dx.doi.org/10.1016/s0163-7258(97)00052-1.

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Wille, Christoph, Thomas Seufferlein, and Tim Eiseler. "Protein Kinase D family kinases." BioArchitecture 4, no. 3 (March 12, 2014): 111–15. http://dx.doi.org/10.4161/bioa.29273.

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Smith, F. Donelson, Bret K. Samelson, and John D. Scott. "Discovery of cellular substrates for protein kinase A using a peptide array screening protocol." Biochemical Journal 438, no. 1 (July 27, 2011): 103–10. http://dx.doi.org/10.1042/bj20110720.

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Post-translational modification of proteins is a universal form of cellular regulation. Phosphorylation on serine, threonine, tyrosine or histidine residues by protein kinases is the most widespread and versatile form of covalent modification. Resultant changes in activity, localization or stability of phosphoproteins drives cellular events. MS and bioinformatic analyses estimate that ~30% of intracellular proteins are phosphorylated at any given time. Multiple approaches have been developed to systematically define targets of protein kinases; however, it is likely that we have yet to catalogue the full complement of the phosphoproteome. The amino acids that surround a phosphoacceptor site are substrate determinants for protein kinases. For example, basophilic enzymes such as PKA (protein kinase A), protein kinase C and calmodulin-dependent kinases recognize basic side chains preceding the target serine or threonine residues. In the present paper we describe a strategy using peptide arrays and motif-specific antibodies to identify and characterize previously unrecognized substrate sequences for protein kinase A. We found that the protein kinases PKD (protein kinase D) and MARK3 [MAP (microtubule-associated protein)-regulating kinase 3] can both be phosphorylated by PKA. Furthermore, we show that the adapter protein RIL [a product of PDLIM4 (PDZ and LIM domain protein 4)] is a PKA substrate that is phosphorylated on Ser119 inside cells and that this mode of regulation may control its ability to affect cell growth.
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Johnson, L. "Protein kinases and their therapeutic exploitation." Biochemical Society Transactions 35, no. 1 (January 22, 2007): 7–11. http://dx.doi.org/10.1042/bst0350007.

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This review focuses on the recognition properties of protein kinases at the molecular level. Phosphorylation of the substrate protein by a protein kinase can result in enzyme activation or inhibition, conformational changes that change recognition properties, or the creation of a surface with distinct binding properties. Protein kinases have become important targets for the development of inhibitors with potential therapeutic application. Various examples are considered in this review, and I discuss our own work on glycogen phosphorylase and phosphorylase kinase, and the structures of proteins involved with the cell cycle, including cyclins and cyclin-dependent kinases.
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Kracht, M., O. Truong, N. F. Totty, M. Shiroo, and J. Saklatvala. "Interleukin 1 alpha activates two forms of p54 alpha mitogen-activated protein kinase in rabbit liver." Journal of Experimental Medicine 180, no. 6 (December 1, 1994): 2017–25. http://dx.doi.org/10.1084/jem.180.6.2017.

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We have identified in rabbits two hepatic forms of T669 peptide kinases that are very strongly activated after systemic injection with the inflammatory cytokine interleukin 1 (IL-1). The T669 peptide contains a major phosphorylation site of the epidermal growth factor receptor, threonine 699 and is a substrate for mitogen-activated protein (MAP) kinases. The kinases were purified to homogeneity and corresponded to 50- and 55-kD proteins on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Amino acid sequencing of 12 tryptic peptides of both kinases identified them as p54 MAP kinase alpha. This kinase belongs to the novel family of stress-activated protein kinases. This is the first evidence of IL-1 activating a specific protein kinase in vivo.
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Dissertations / Theses on the topic "Protein kinases"

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Nguyen, Giang Huong. "A functional analysis of the human LPA₁G protein coupled receptor." Thesis, Available online, Georgia Institute of Technology, 2004:, 2004. http://etd.gatech.edu/theses/available/etd-06072004-131304/unrestricted/nguyen%5Fgiang%5Fh%5F200405%5Fms.pdf.

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Gatesman, Ammer Amanda. "PKCalpha direct cSrc activation and podosome formation through the adaptor protein AFAP-110." Morgantown, W. Va. : [West Virginia University Libraries], 2004. https://etd.wvu.edu/etd/controller.jsp?moduleName=documentdata&jsp%5FetdId=3762.

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Thesis (Ph. D.)--West Virginia University, 2004
Title from document title page. Document formatted into pages; contains vii, 350 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references (p. 322-346).
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Cowan, Richard H. "Refolding of protein kinases." Thesis, University of Warwick, 2009. http://wrap.warwick.ac.uk/3133/.

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The vast increase in the number of protein structures identified since the first high resolution protein structure was determined has shown that there are relatively few protein folds. The study of the folding of proteins has also expanded significantly since its inception. The contact-order of residues in the native structure has been implicated as important in folding. This has raised the question of whether the common folds observed in protein structures fold via common mechanisms. The protein kinase domain is a large, pharmaceutically important and conserved protein fold, of which many examples fail to fold correctly when overexpressed as recombinant proteins in Escherichia coli. The kinase domain forms an excellent area in which to study the folding of a large conserved domain with varying sequence. To study the refolding of the kinase fold a refolding screen was created, using p38α as a model protein kinase. The results of this screen were compared to the results of refolding a further four protein kinases, AKT2, KIS, PhK and TTK to determine commonalities in the folding of protein kinases. The refolding of the five protein kinases was also examined using a fractional factorial screen which examined combinations of refolding additives. In the screening of the refolding of protein kinases no factors were idenified which were common to the refolding of all five of the tested protein kinases. The equilibrium folding of a single protein kinase, TTK, was also studied. The folding of TTK was determined to proceed via different pathways on folding and unfolding, with a co-operative unfolding pathway through a molten-globule intermediate, and a non-cooperative refolding pathway via an intermediate with different secondary structure content to the unfolding intermediate. The difference between the folding properties of protein kinases determined in the screen and through the analysis of the equilibrium folding of TTK suggest that there may not be a common protein kinase folding mechanism.
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Gold, Matthew. "Targeting AGC protein kinases." Thesis, Institute of Cancer Research (University Of London), 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.504788.

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A-kinase anchoring proteins (AKAPs) restrict the action of the broad-specificity cyclic AMP-dependent protein kinase (PKA) to discrete subcellular locations. The highresolution crystal structure of the docking and dimerisation (D/D) domain of the RIIa regulatory Bubunit of PKA in complex with the high-affinity anchoring peptide AKAP-IS explains the molecular basis of AKAP specificity for PKA regulatory subunits. AKAPIS folds into an amphipathic a-helix that engages an essentially preformed shallow groove on the surface of the RUa dimer D/D domains. Conserved AKAP aiiphatic residues dominate interactions to RUa at the predominantly hydrophobic interface, whereas polar residues are important in conferring regulatory subunit isoform specificity. Structural information for the AKAP family was previously limited to studies of the PKA-AKAP interface. To address this deficiency, a bioinformatic screen of AKAPs was performed to identify domains within AKAPs that might be suitable for structural investigation. A central domain in AKAP18 was identified, and its crystal structure was solved. The domain is structurally similar to 2H phosphoesterase enzymes, which catalyse the hydrolysis of cyclic nucleotides, with a central groove at the base of which two His-x-Thr motifs are positioned. The domain binds specifically to 5' AMP/CMP, with a dissociation constant for AMP in the physiological range, and the molecular basis for nucleotide specificity has been established. No catalytic activity was associated with the domain, so it may function as an AMP sensor. AKAP79 is a prototypical mammalian scaffold protein, which nucleates mUlti-protein kinase-phosphatase complexes, and localises at the cell membrane under the control of calmodulin. A system for expression and purification of AKAP79 has been developed enabling sufficient production of pure AKAP79 complexes for structural and biochemical investigation. Imaging of an AKAP79-PKA-calmodulin complex by negative-staining transmission electron microscopy indicates that the first three-dimen'sional reconstruction of this complex may be possible in the near future.
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Ferris, Douglas K. "Protein phosphatases and protein kinases in dictyostelium." Diss., Virginia Polytechnic Institute and State University, 1986. http://hdl.handle.net/10919/50017.

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In the present work, the chromatographic behavior and partial characterization of 5 protein phosphatases, 6 paranitrophenyl phosphate (pnpp) phosphatases and 2 protein kinases from Dictyostelium are described. .Two of the protein phosphatases are shown to have subunit structures. All of the protein phosphatase activities described were able to dephosphorylate sites on proteins that had previously been phosphorylated by the cAMP-dependent protein kinase. Therefore it may be that these phosphatases function in vivo to antagonize the action of the cAMP-dependent protein kinase. Various pnpp phosphatase activities, varying in size, cation requirements and pH optima are described. Since many pnpp phosphatases also function with protein substrates it is possible that these activities represent protein phosphatases that function with phosphoproteins that have not been tested. Evidence for the existence of protein kinase C in Dictyostelium is presented. A histone protein kinase was found in Dictyostelium extracts that eluted from DE52 cellulose at the same salt concentration that rabbit brain protein kinase C did. In addition in one experiment clear dependency on calcium and phospholipids is shown. The purification to homogeneity, and characterization of a low molecular weight autophosphorylating protein kinase, pp20, is described. This protein kinase is a major phosphorylated protein and in addition represents at least 0.03% of the total cellular protein. The autophosphorylation reaction can be inhibited by EDTA but not by EGTA. Following inhibition by EDTA, autophosphorylation can be reactivated by the addition of Mn²⁺, Mg²⁺, or Ca²⁺. Western blotting evidence is presented that shows cross reactivity of pp20 and an 85 KDa protein that may possess casein kinase activity.
Ph. D.
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Walker, Valerie Glynis. "Pl3-kinase mediates cSrc activation and podosome formation through the adaptor protein, AFAP-110, in response to PKC[alpha] activation." Morgantown, W. Va. : [West Virginia University Libraries], 2007. https://eidr.wvu.edu/etd/documentdata.eTD?documentid=5191.

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Thesis (Ph. D.)--West Virginia University, 2007.
Title from document title page. Document formatted into pages; contains viii, 306 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.
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Holland, Pamela M. "Identification, interactions, and specificity of a novel MAP kinase kinase, MKK7 /." Thesis, Connect to this title online; UW restricted, 1999. http://hdl.handle.net/1773/9262.

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Saurin, Adrian Thomas. "Protein kinases in myocardial protection." Thesis, King's College London (University of London), 2001. https://kclpure.kcl.ac.uk/portal/en/theses/protein-kinases-in-myocardial-protection(ba5e7b96-cf59-409a-b290-f18fec8be6b1).html.

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Kaser, Matthew R. "Beryllium-sensitive nuclear protein kinases." Thesis, University of Oxford, 1987. http://ora.ox.ac.uk/objects/uuid:746dac6e-9609-42b7-a809-82ebc3dd465d.

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Much effort has been spent over the last decade in producing so called "Machine Vision" systems for use in robotics, automated inspection, assembly and numerous other fields. Because of the large amount of data involved in an image (typically ¼ MByte) and the complexity of many algorithms used, the processing times required have been far in excess of real time on a VAX-class serial processor. We review a number of image understanding algorithms that compute a globally defined "state", and show that they may be computed using simple local operations that are suited to parallel implementation. In recent years, many massively parallel machines have been designed to apply local operations rapidly across an image. We review several vision machines. We develop an algebraic analysis of the performance of a vision machine and show that, contrary to the commonly-held belief, the time taken to relay images between serial streams can exceed by far the time spent processing. We proceed to investigate the roles that a variety of pipelining techniques might play. We then present three pipelined designs for vision, one of which has been built. This is a parallel pipelined bit slice convolution processor, capable of operating at video rates. This design is examined in detail, and its performance analysed in relation to the theoretical framework of the preceeding chapters. The construction and debugging of the device, which is now operational in its hardware is detailed.
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Waskiewicz, Andrew Jan. "Mitogen-activated protein kinase : evolutionary conservation and activation of downstream kinases /." Thesis, Connect to this title online; UW restricted, 1996. http://hdl.handle.net/1773/9216.

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Books on the topic "Protein kinases"

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Robert, Woodgett James, ed. Protein kinases. Oxford: IRL Press at Oxford University Press, 1994.

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Xavier, Gabriela Da Silva. Protein kinases. Rijeka: InTech, 2012.

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Francesc, Posas, and Nebreda Angel R, eds. Stress-activated protein kinases. New York: Springer, 2008.

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M, Kreis, and Walker J. C, eds. Plant protein kinases. San Diego: Academic Press, 2000.

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Fabbro, Doriano, and Frank McCormick, eds. Protein Tyrosine Kinases. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1592599621.

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Hardie, D. G. Protein kinase factsbook. London: Academic Press, 1995.

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1933-, Kuo J. F., ed. Protein kinase C. New York: Oxford University Press, 1994.

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1953-, Lester David S., and Epand Richard M. 1937-, eds. Protein kinase C: Current concepts and future perspectives. New York: Ellis Horwood, 1992.

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Robert, Woodgett James, ed. Protein kinase functions. 2nd ed. Oxford: Oxford University Press, 2000.

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Chi-Kuang, Huang, and Shaʼafi Ramadan I. 1938-, eds. Protein kinases in blood cell function. Boca Raton, Fla: CRC Press, 1993.

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Book chapters on the topic "Protein kinases"

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Wong, Alice. "Protein Kinases." In Encyclopedia of Cancer, 1–4. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_6621-3.

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Belyi, Yuri F. "Protein Kinases." In Intracellular Parasitism of Microorganisms, 75–91. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-22047-4_8.

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Plevani, Paolo. "Protein Kinases." In Encyclopedia of Systems Biology, 1778. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_722.

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Wong, Alice. "Protein Kinases." In Encyclopedia of Cancer, 3822–24. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-46875-3_6621.

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Gupta, G. S. "Protein Kinases." In Proteomics of Spermatogenesis, 439–92. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-27655-6_19.

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Cuevas, Bruce D. "Mitogen-Activated Protein Kinase Kinase Kinases." In Encyclopedia of Cancer, 1–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_7192-1.

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Cuevas, Bruce D. "Mitogen-Activated Protein Kinase Kinase Kinases." In Encyclopedia of Cancer, 2872–76. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-662-46875-3_7192.

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Pearson, Mark, Carlos García-Echeverría, and Doriano Fabbro. "Protein Tyrosine Kinases as Targets for Cancer and Other Indications." In Protein Tyrosine Kinases, 1–29. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:001.

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García-Echeverría, Carlos. "Inhibitors of Signaling Interfaces." In Protein Tyrosine Kinases, 31–52. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:031.

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Finan, Peter M., and Stephen G. Ward. "PI3-Kinase Inhibition." In Protein Tyrosine Kinases, 53–69. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:053.

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Conference papers on the topic "Protein kinases"

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Zorina, A. A. "Protein kinases in cyanobacteria." In IX Congress of society physiologists of plants of Russia "Plant physiology is the basis for creating plants of the future". Kazan University Press, 2019. http://dx.doi.org/10.26907/978-5-00130-204-9-2019-182.

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Komolov, Konstantin, Daniela K. Laurinavichyute, Anshul Bhardwaj, and Jeffrey L. Benovic. "Calcium-dependent regulation of G protein-coupled receptor kinases." In ASPET 2023 Annual Meeting Abstracts. American Society for Pharmacology and Experimental Therapeutics, 2023. http://dx.doi.org/10.1124/jpet.122.242570.

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Beljkas, Milan, Jelena Rebić, Milica Radan, Teodora Đikić, Slavica Oljačić, and Katarina Nikolic. "3D-Quantitative Structure-Activity Relationship and design of novel Rho-associated protein kinases-1 (ROCK1) inhibitors." In 2nd International Conference on Chemo and Bioinformatics. Institute for Information Technologies, University of Kragujevac, 2023. http://dx.doi.org/10.46793/iccbi23.584b.

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Rho-associated coiled-coil kinases (ROCKs) are involved in essential cellular functions such as adhesion, contraction, motility, proliferation, and cell survival/apoptosis. Four ROCK inhibitors have already been approved by the FDA and are used to treat glaucoma (ripasudil and netarsudil), cerebral vasospasm (fasudil), and graft-versus-host disease (belumosudil). Recent studies have focused on exploring the role of ROCK kinase inhibitors in cancer treatment and the development of new ROCK inhibitors. The main objective of this study was to identify critical structural features relevant to the inhibition of ROCK1 using a ligand-based 3D-QSAR (3D quantitative structure-activity relationship) method. The 3D-QSAR model for ROCK1 was created and validated using internal and external validation parameters (R2, Q2, R2pred, rm 2, r/2m, rm̅̅2̅ and ∆r2m). The main structural features that correlate with the inhibition of ROCK1 were identified (e.g., heterocycle with hydrogen donor group like nitrogen atom) and further structural modifications of the ROCK1 inhibitors that contribute to increased activity were proposed (removal of the amino group of the oxadiazole, modification of the substituents of the phenyl ring).
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Zemskova, Marina Yu, Zanna Beharry, Sandeep Mahajan, and Andrew S. Kraft. "Abstract 1258: Regulation of energy metabolism and protein synthesis by the Pim protein kinases." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1258.

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Nickkholgh, Bita, Sivanandane Sittadjody, Michael B. Rothberg, and KC Balaji. "Abstract LB-243: Protein kinase D1 induces cell cycle arrest independent from check point kinases." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-lb-243.

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Moncayo, Gerald E., Michal Grzmil, Yuhua Wang, Stephan Frank, Adrian Merlo, and Hemmings A. Brian. "Abstract 1240: The role of hematopoietic protein kinases in GBM." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1240.

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Luo, Yu, Chi K. Chang, and David Kessel. "Modulation of PDT-induced apoptosis by protein kinases and phosphatases." In Photonics West '96, edited by Thomas J. Dougherty. SPIE, 1996. http://dx.doi.org/10.1117/12.237530.

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Mueller, Daniel, Frank Totzke, Thomas Weber, Marcel Pathe, Christoph Schaechtele, and Michael H. Kubbutat. "Abstract 2388: IC50 profiling against 320 protein kinases: Improving the accuracy of kinase inhibitor selectivity testing." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-2388.

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LeDuc, Philip R. "Dynamic Formation for the Mechanical Connection of Focal Adhesion Complexes to Study Localized Mechanisms of Angiogenesis Through Modeling With Cellular Automata." In ASME 2001 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2001. http://dx.doi.org/10.1115/imece2001/bed-23159.

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Abstract The mechanical connection through the formation of focal adhesion complexes (FACs) is critical in cell growth and apoptosis. The FACs act between the cells and the extracellular matrix (ECM), which in turn influences angiogenesis, the growth of new capillary blood vessels [1]. These complexes form direct connections from ECM into the cell cytoskeleton through a series of protein binding events. This linkage is critical for mechanical force sensing and mechanotransduction signaling [2]. Here, the probabilistic modeling of this complex formation is undertaken to begin to uncover the effect of the spatial distribution and temporal effects on this dynamic process. In this, the rich dynamic process of the FACs formation through the binding events of integrin, paxillin, talin, and vinculin are examined. The FACs are mediated through the clustering of transmembrane integrins, which initiate the binding cascade. This interaction has been shown to be a critical event in the activation of the mechanochemical cascade and further mediates downstream signaling of protein tyrosine kinases including focal adhesion kinase [3].
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Guo, Tiannan, Oi Lian Kon, and Siu Kwan Sze. "Abstract 578: Roles of mitochondrial protein kinases in targeted cancer therapy." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-578.

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Reports on the topic "Protein kinases"

1

Chernoff, Jonathan. Identification of Protein Kinases Required for NF2 Signaling. Fort Belvoir, VA: Defense Technical Information Center, December 2007. http://dx.doi.org/10.21236/ada494392.

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Chernoff, Jonathan. Identification of Protein Kinases Required for NF2 Signaling. Fort Belvoir, VA: Defense Technical Information Center, December 2006. http://dx.doi.org/10.21236/ada465844.

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Futcher, A. B. General Methods for Identifying Gl-phase Substrates of Cdk Protein Kinases. Fort Belvoir, VA: Defense Technical Information Center, June 1998. http://dx.doi.org/10.21236/ada366953.

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Futcher, A. B. General Methods for Identifying G1-phase Substrates of Cdk Protein Kinases. Fort Belvoir, VA: Defense Technical Information Center, June 1999. http://dx.doi.org/10.21236/ada374137.

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Futcher, A. B., and Daniel R. Marshak. General Methods for Identifying G1-Phase Substrates of Cdk Protein Kinases. Fort Belvoir, VA: Defense Technical Information Center, June 1996. http://dx.doi.org/10.21236/ada323678.

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Eddy, Sean, and Gail E. Sonenshein. Roles of ikB-alpha Protein Kinases in Activation of NF-kB in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2005. http://dx.doi.org/10.21236/ada448541.

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Romieu-Mourez, Raphaelle A. Roles of IkB-a Protein Kinases in Activation of NF-kB in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, January 2003. http://dx.doi.org/10.21236/ada412856.

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Dickman, Martin B., and Oded Yarden. Regulation of Early Events in Hyphal Elongation, Branching and Differentiation of Filamentous Fungi. United States Department of Agriculture, 2000. http://dx.doi.org/10.32747/2000.7580674.bard.

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In filamentous fungi, hyphal elongation, branching and morphogenesis are in many cases the key to successful saprophytic and pathogenic fungal proliferation. The understanding of the fungal morphogenetic response to environmental cues is in its infancy. Studies concerning the regulation of fungal growth and development (some of which have been obtained by the participating collaborators in this project) point to the fact that ser/thr protein kinases and phosphatases are (i) involved in the regulation of such processes and (ii) share common structural and functional features between saprophytes and pathogens. It is our objective to combine a pharmaceutical and a genetic approach in order to identify, characterize and functionally dissect some of the regulatory factors involved in hyphal growth, branching and differentiation. Using an immunohistochemical approach, a ser/thr protein kinase involved in hyphal elongation in both Neurospora crassa and Colletotrichum trifolii has been localized in order to identify the physical arena of regulation of hyphal elongation. The analysis of additional kinases and phosphatases (e.g. Protein kinase C, cAMP-dependent kinase, lipid-activated protein kinase, components of the type 2A protein phosphatase) as well as a RAS-related gene (an additional key participant in signal transduction) has been performed. In order to succeed in advancing the goals of this project, we have taken advantage of available elongation/branching mutants in N. crassa and continuously combined the accumulated information obtained while studying the two systems in order to dissect the elements involved in these processes. The various inhibitors/effectors analyzed can serve as a basis for modification to be used as anti-fungal compounds. Understanding the regulation of hyphal proliferation is a key requirement for identifying novel target points for either curbing fungal growth (as in the case of pathogenesis) or affecting growth patterns in various biotechnological processes. The major objective of our joint project was to advance our understanding of regulation of hyphal growth, especially during early events of fungal germination. Towards achieving this goal, we have coupled the analysis of a genetically tractable organism (N. crassa) with a plant pathogen o economic importance (C. trifolii). As the project progressed we believe that the results obtained have provided a reinforcement to our basic approach which called for combining the two fungal systems for a joint research project. On the one hand, we feel that much of the advance made was possible due to the amenability of N. crassa to genetic manipulations. The relevance of some of the initial findings obtained in Neurospora have been proven to be relevant to the plant pathogen while unique features of the pathogen have been identified in Colletotrichum. Most of the results obtained from this research project have been published. Thus, the main volume of this report is comprised of the relevant publications describing the research and results obtained.
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Edelman, Arthur. Study of Inhibitors of Neu and Related Tyrosine-Specific Protein Kinases: Implications for the Treatment of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 1998. http://dx.doi.org/10.21236/ada360940.

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Edelman, Arthur. Study of Inhibitors of Neu and Related Tyrosine-Specific Protein Kinases: Implications for the Treatment of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 1997. http://dx.doi.org/10.21236/ada338938.

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