Relevant bibliographies by topics / Protein kinase

Academic literature on the topic 'Protein kinase'

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Published: 4 June 2021
Last updated: 29 July 2024

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Journal articles on the topic "Protein kinase"

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Pang, Kam-Lee, Wei-Li Thong, and Siew-Eng How. "Cinnamomum Iners as Mitogen-Activated Protein Kinase Kinase (MKK1) Inhibitor." International Journal of Engineering and Technology 1, no. 4 (2009): 310–13. http://dx.doi.org/10.7763/ijet.2009.v1.61.

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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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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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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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Trojanek, Joanna B., Maria M. Klimecka, Anna Fraser, Grazyna Dobrowolska, and Grazyna Muszyńska. "Characterization of dual specificity protein kinase from maize seedlings." Acta Biochimica Polonica 51, no. 3 (September 30, 2004): 635–47. http://dx.doi.org/10.18388/abp.2004_3549.

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A protein kinase of 57 kDa, able to phosphorylate tyrosine in synthetic substrates pol(Glu4,Tyr1) and a fragment of Src tyrosine kinase, was isolated and partly purified from maize seedlings (Zea mays). The protein kinase was able to phosphorylate exogenous proteins: enolase, caseins, histones and myelin basic protein. Amino acid analysis of phosphorylated casein and enolase, as well as of phosphorylated endogenous proteins, showed that both Tyr and Ser residues were phosphorylated. Phosphotyrosine was also immunodetected in the 57 kDa protein fraction. In the protein fraction there are present 57 kDa protein kinase and enolase. This co-purification suggests that enolase can be an endogenous substrate of the kinase. The two proteins could be resolved by two-dimensional electrophoresis. Specific inhibitors of typical protein-tyrosine kinases had essentially no effect on the activity of the maize enzyme. Staurosporine, a nonspecific inhibitor of protein kinases, effectively inhibited the 57 kDa protein kinase. Also, poly L-lysine and heparin inhibited tyrosine phosphorylation by 57 kDa maize protein kinase. The substrate and inhibitor specificities of the 57 kDa maize protein kinase phosphorylating tyrosine indicate that it is a novel plant dual-specificity protein kinase.
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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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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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Yasuda, Jun, Alan J. Whitmarsh, Julie Cavanagh, Manoj Sharma, and Roger J. Davis. "The JIP Group of Mitogen-Activated Protein Kinase Scaffold Proteins." Molecular and Cellular Biology 19, no. 10 (October 1, 1999): 7245–54. http://dx.doi.org/10.1128/mcb.19.10.7245.

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ABSTRACT Activation of the c-Jun NH2-terminal kinase (JNK) group of mitogen-activated protein (MAP) kinases is mediated by a protein kinase cascade. This signaling mechanism may be coordinated by the interaction of components of the protein kinase cascade with scaffold proteins. The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates signaling by the mixed-lineage kinase (MLK)→MAP kinase kinase 7 (MKK7)→JNK pathway. The scaffold proteins JIP1 and JIP2 interact to form oligomeric complexes that accumulate in peripheral cytoplasmic projections extended at the cell surface. The JIP proteins function by aggregating components of a MAP kinase module (including MLK, MKK7, and JNK) and facilitate signal transmission by the protein kinase cascade.
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Parker, P. J., and S. J. Parkinson. "AGC protein kinase phosphorylation and protein kinase C." Biochemical Society Transactions 29, no. 6 (November 1, 2001): 860–63. http://dx.doi.org/10.1042/bst0290860.

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Protein kinase cascades feature in many signal transduction pathways. For those discussed here, a single upstream protein kinase appears to be responsible for the control of multiple downstream targets. So how is specificity introduced into these events? For the downstream kinases (substrates) described here, it would appear that specificity is determined by substrate-directed events that are permissive for phosphorylation. There are also distinctions relating to the turnover of these phosphorylations providing a further element of specificity.
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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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Dissertations / Theses on the topic "Protein kinase"

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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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Cheng, Kwan-wai. "Regulation of equilibrative nucleoside transporter-1 by protein kinase C and mitogen-activating protein kinase /." View the Table of Contents & Abstract, 2005. http://sunzi.lib.hku.hk/hkuto/record/B31494912.

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Wang, Jingwei. "Alterations in protein kinase A and protein kinase C activities and protein levels in cardiomyopathy." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape17/PQDD_0001/MQ32280.pdf.

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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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Chen, Dan. "Regulation of protein kinase C by protein-protein interactions /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2003. http://wwwlib.umi.com/cr/ucsd/fullcit?p3112821.

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Benjamin, Audra Ruth. "Lung liquid homeostasis : The involvement of protein kinase A and protein tyrosine kinase." Thesis, St George's, University of London, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.511892.

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Kerkelä, R. (Risto). "Signaling pathways in myocyte hypertrophy:role of GATA4, mitogen-activated protein kinases and protein kinase C." Doctoral thesis, University of Oulu, 2003. http://urn.fi/urn:isbn:9514269950.

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Abstract Cardiac myocytes react to increased workload and hypertrophic neurohumoral stimuli by increasing protein synthesis, reinitiating expression of fetal forms of structural genes, α-skeletal actin (α-SkA) and β-myosin heavy chain (β-MHC), and by increasing expression and secretion of atrial natriuretic peptide (ANP) and B-type natriuretic peptide (BNP). Initially, the response is beneficial, but when prolonged, it leads to pathological cardiomyocyte hypertrophy. In this study, cardiomyocyte hypertrophy was initiated by hypertrophic agonists, endothelin-1 (ET-1) and phenylephrine (PE), and by increased stretching of atrial wall. Transcription factor GATA4 was studied to identify the mechanism leading to increased gene expression of BNP. In BNP promoter, GATA4 binds to cis elements mediating hypertrophic response. Eliminating GATA4 binding by using the decoy approach, basal BNP gene expression was reduced. To identify mechanisms regulating GATA4, the roles of mitogen-activated protein kinases (MAPKs) were studied. Activation of p38 MAPK increased GATA4 binding to BNP gene and led to increased GATA4 dependent BNP gene expression. p38 MAPK was required for ET-1 induced GATA4 binding, whereas extracellular signal-regulated kinase (ERK) was required for maintaining basal GATA4 binding activity. PE and ET-1 activated protein kinase C (PKC) signaling in cardiac myocytes. Antisense oligonucleotide inhibition of PKCα markedly reduced PE induced ANP secretion and ET-1 induced BNP secretion, whereas gene expression of natriuretic peptides was not affected. Antisense PKCα treatment inhibited PE induced expression of α-SkA, while increased protein synthesis or β-MHC gene expression were not affected. Sretching of the perfused rat atria increased BNP, c-fos and BNP gene expression via mechanism involving p38 MAP kinase activation of transcription factor Elk-1. In cultured neonatal rat atrial myocytes stretch induced BNP gene expression was dependent upon transcription factor Elk-1 binding sites within the BNP gene promoter. In conclusion, hypertrophic signaling in cardiac myocytes involves multiple signaling cascades. Activation of p38 MAPK is required for the development of ET-1 induced hypertrophic phenotype and GATA4 mediated BNP gene expression in cultured ventricular myocytes, and for stretch induced Elk-1 dependent BNP gene expression in atrial myocytes. PKCα is involved in PE induced hypertrophic response and PE induced switch in gene programming inducing expression of α-SkA, the fetal form of cardiac α-actin.
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Cheng, Kwan-wai, and 鄭軍偉. "Regulation of equilibrative nucleoside transporter-1 by protein kinaseC and mitogen-activating protein kinase." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2005. http://hub.hku.hk/bib/B45009983.

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Toker, I. Alex. "Purification and characterisation of protein kinase C inhibitor proteins." Thesis, University College London (University of London), 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.277909.

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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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Books on the topic "Protein kinase"

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

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V, Dekker Lodewijk, ed. Protein kinase C. 2nd ed. Georgetown, Tex: Landes Bioscience/Eurekah.com, 2004.

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

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C, Newton Alexandra, ed. Protein kinase C protocols. Totowa, N.J: Humana Press, 2003.

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Reith, Alastair D. Protein Kinase Protocols. New Jersey: Humana Press, 2000. http://dx.doi.org/10.1385/1592590594.

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Mukai, Hideyuki, ed. Protein Kinase Technologies. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-824-5.

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Pinna, Lorenzo A., ed. Protein Kinase CK2. Oxford, UK: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118482490.

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

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Dekker, Lodewijk V. Protein kinase C. 2nd ed. Georgetown, Tex., U.S.A: Landes Bioscience/Eurekah.com, 2004.

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1954-, Parker Peter J., and Dekker Lodewijk V, eds. Protein kinase C. New York: Springer, 1997.

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Book chapters on the topic "Protein kinase"

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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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Ward, Tony Milford. "Protein Kinase." In Proteins and Tumour Markers May 1995, 1363. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0681-8_72.

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Baker, Julien S., Fergal Grace, Lon Kilgore, David J. Smith, Stephen R. Norris, Andrew W. Gardner, Robert Ringseis, et al. "Protein Kinase." In Encyclopedia of Exercise Medicine in Health and Disease, 732. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2920.

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Schomburg, Dietmar, and Dörte Stephan. "Protein kinase." In Enzyme Handbook 13, 763–70. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59176-1_148.

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Gewies, Andreas, Jürgen Ruland, Alexey Kotlyarov, Matthias Gaestel, Shiri Procaccia, Rony Seger, Shin Yasuda, et al. "Mitogen-Activated Protein Kinase Kinase Kinase Kinase 1." In Encyclopedia of Signaling Molecules, 1082. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100818.

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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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Gewies, Andreas, Jürgen Ruland, Alexey Kotlyarov, Matthias Gaestel, Shiri Procaccia, Rony Seger, Shin Yasuda, et al. "Mitogen-Activated Protein Kinase Kinase Kinase 11." In Encyclopedia of Signaling Molecules, 1081. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100814.

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Gewies, Andreas, Jürgen Ruland, Alexey Kotlyarov, Matthias Gaestel, Shiri Procaccia, Rony Seger, Shin Yasuda, et al. "Mitogen-Activated Protein Kinase Kinase Kinase 12." In Encyclopedia of Signaling Molecules, 1081. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100816.

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Gewies, Andreas, Jürgen Ruland, Alexey Kotlyarov, Matthias Gaestel, Shiri Procaccia, Rony Seger, Shin Yasuda, et al. "Mitogen-Activated Protein Kinase Kinase Kinase 8." In Encyclopedia of Signaling Molecules, 1081. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100817.

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Conference papers on the topic "Protein kinase"

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Timmons, Sheila, and Jack Hawiger. "REGULATION OF PLATELET RECEPTORS FOR FIBRINOGEN AND VON WILLEBRAND FACTOR BY PROTEIN KINASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644674.

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Positive and negative regulation of platelet receptors for adhesive proteins, fibrinogen (F) and von Willebrand Factor (vWF) determines whether binding of these ligands will or will not take place. We have shown previously that ADP stimulates and cyclic AMP inhibits binding of F and vWF to human platelets. Now we show that positive regulation of F and vWF binding to platelets via the glycoprotein 11b/1111a complex is dependent on platelet Protein Kinase C, a calcium- and phospholipid-dependent enzyme. A potent activator of Protein Kinase C, phorbol-12-myristoyl-13-acetate (PMA) induced saturable and specific binding of F and vWF which was inhibited by synthetic peptides, gamma chain .dodecapeptide (gamma 400-411) and RGDS. The phosphorylation of 47kDa protein (P47), a marker of Protein Kinase C activation in platelets, preceded binding of F and vWF induced with PMA as well as with ADP and thrombin. Sphingosine, an inhibitor of Protein Kinase C, blocked binding of F and vWF to platelets stimulated with PMA, ADP, and thrombin. Inhibition of binding was concentration-dependent and it was accompanied by inhibition of platelet aggregation. Thus, stimulation of Protein Kinase C is required for exposure of platelet receptors for adhesive proteins whereas inhibition of Protein Kinase C prevents receptorexposure. Protein Kinase C fulfills the role of an intraplatelet signal transducer, regulating receptors for adhesive proteins, and constitutes a target for pharmacologic modulation of the adhesive interactions of platelets.
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Ranjit, Sabina, Jingwen Zhu, Tomoka Gose, Amanda Nourse, Vishwajeeth Pagala, Yao Wang, Aaron Pitre, et al. "Protein Kinase A Activation Promotes ABCC4 Protein Network Assembly." In ASPET 2024 Annual Meeting Abstract. American Society for Pharmacology and Experimental Therapeutics, 2024. http://dx.doi.org/10.1124/jpet.431.952760.

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Safaei, Javad, Jan Manuch, Arvind Gupta, Ladislav Stacho, and Steven Pelech. "Prediction of human protein kinase substrate specificities." In 2010 IEEE International Conference on Bioinformatics and Biomedicine (BIBM 2010). IEEE, 2010. http://dx.doi.org/10.1109/bibm.2010.5706573.

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Gosal, Gurinder Pal Singh, Natarajan Kannan, and Krys J. Kochut. "ProKinO: A Framework for Protein Kinase Ontology." In 2011 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2011. http://dx.doi.org/10.1109/bibm.2011.125.

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Rozinek, Sarah C., Robert J. Thomas, and Lorenzo Brancaleon. "Photoinduced structural changes to protein kinase A." In SPIE BiOS, edited by E. Duco Jansen, Robert J. Thomas, Gerald J. Wilmink, and Bennett L. Ibey. SPIE, 2014. http://dx.doi.org/10.1117/12.2038561.

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Reykhardt, Boris A., and Peter D. Shabanov. "Neuroprotective effects of protein kinase CK2 modulators." In II Международная конференция, посвящеенная 100- летию И.А. Држевецкой. СКФУ, 2022. http://dx.doi.org/10.38006/9612-62-6.2022.271.275.

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Paniagua-Morales, Oscar, Laura Johnston, Leonid Serebreni, Gigi Liu, Paul Hassoun, and Mahendra Damarla. "Abstract 1350: Mitogen activated protein kinase activated protein kinase 2 (MK2) signaling in non-small cell lung carcinoma." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-1350.

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Verhamme, F., H. P. Van Eeckhoutte, T. Buyle-Huybrecht, G. G. Brusselle, P. Vandenabeele, T. Vanden Berghe, and K. R. Bracke. "Expression of Receptor Interacting Protein Kinase-3 and Mixed Lineage Kinase Domain-Like Protein in Patients with COPD." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a5363.

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Krishna, Sankar Narayan, Chi-Hao Luan, George Minasov, Ludmilla Shuvalova, Rebecca L. Farmer, Antoinette Nibbs, Karl A. Scheidt, Wayne F. Anderson, and Raymond C. Bergan. "Abstract 4751: Structure and inhibition of mitogen-activated protein kinase kinase 4 (MEK4): A prostate cancer pro-invasion protein." 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.am2012-4751.

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Parniani, Ahmad, Hasina Maredia, Rachel L. Damico, Bo S. Kim, Todd M. Kolb, Allen Myers, Paul M. Hassoun, and Mahendra Damarla. "Mitogen Activated Protein Kinase-Activated Protein Kinase 2 Deficiency Is Protective Against LPS-Mediated Apoptosis Induced Acute Lung Injury." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a3668.

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Reports on the topic "Protein kinase"

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Trewhella, J., G. A. Olah, D. A. Walsh, and R. D. Mitchell. Solution structure of the cAMP-dependent protein kinase. Office of Scientific and Technical Information (OSTI), December 1998. http://dx.doi.org/10.2172/560750.

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Burma, Sandeep. Interaction of BRCA1 with the DNA-Dependent Protein Kinase. Fort Belvoir, VA: Defense Technical Information Center, September 2005. http://dx.doi.org/10.21236/ada486717.

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Lannigan, Deborah. The Protein Kinase RSK Family - Roles in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, February 2006. http://dx.doi.org/10.21236/ada452371.

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Heidenreich, Kim A. Protein Kinase Pathways That Regulate Neuronal Survival and Death. Fort Belvoir, VA: Defense Technical Information Center, August 2004. http://dx.doi.org/10.21236/ada429843.

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Burma, Sandeep. Interaction of BRCA1 With the DNA-Dependent Protein Kinase. Fort Belvoir, VA: Defense Technical Information Center, September 2004. http://dx.doi.org/10.21236/ada432142.

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Lannigan, Deborah A. The Protein Kinase RSK Family - Roles in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, February 2005. http://dx.doi.org/10.21236/ada433888.

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Heidenreich, Kim A. Protein Kinase Pathways that Regulate Neuronal Survival and Death. Fort Belvoir, VA: Defense Technical Information Center, August 2003. http://dx.doi.org/10.21236/ada419485.

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Yang, Dejun. Structure-Based Discovery of Novel Inhibitors of Protein Kinase. Fort Belvoir, VA: Defense Technical Information Center, September 2003. http://dx.doi.org/10.21236/ada424718.

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Parker, Amanda P., Barbara S. Beckman, and Matthew Burow. Phosphatidylinositol 3-Kinase and Protein Kinase C as Molecular Determinants of Chemoresistance in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2002. http://dx.doi.org/10.21236/ada409382.

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Parker, Amanda, Barbara Beckman, and Matthew E. Burow. Phosphatidylinositol 3-Kinase and Protein Kinase C as Molecular Determinants of Chemoresistance in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2004. http://dx.doi.org/10.21236/ada431891.

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