Bibliografías temáticas / PKC

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Literatura académica sobre el tema "PKC"

Autor: Grafiati
Publicado: 4 de junio de 2021
Última modificación: 25 de julio de 2025

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Artículos de revistas sobre el tema "PKC"

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Muramatsu, M., K. Kaibuchi, and K. Arai. "A protein kinase C cDNA without the regulatory domain is active after transfection in vivo in the absence of phorbol ester." Molecular and Cellular Biology 9, no. 2 (1989): 831–36. http://dx.doi.org/10.1128/mcb.9.2.831-836.1989.

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We constructed mutant protein kinase C (PKC) cDNAs which expressed PKC activity in vivo in the absence of phorbol ester activation. A hybrid PKC gene, PKAC, was constructed by substituting the coding region for the N-terminal 253 amino acids of PKC alpha with the N-terminal 17 amino acids of the cyclic AMP-dependent protein kinase catalytic subunit (PKA). A truncated PKC gene, delta PKC beta, lacking the coding region for amino acid positions 6 to 159 of PKC beta was also constructed. These mutant kinase genes expressed under the control of the SR alpha promoter activated the c-fos gene enhanc
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Muramatsu, M., K. Kaibuchi, and K. Arai. "A protein kinase C cDNA without the regulatory domain is active after transfection in vivo in the absence of phorbol ester." Molecular and Cellular Biology 9, no. 2 (1989): 831–36. http://dx.doi.org/10.1128/mcb.9.2.831.

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We constructed mutant protein kinase C (PKC) cDNAs which expressed PKC activity in vivo in the absence of phorbol ester activation. A hybrid PKC gene, PKAC, was constructed by substituting the coding region for the N-terminal 253 amino acids of PKC alpha with the N-terminal 17 amino acids of the cyclic AMP-dependent protein kinase catalytic subunit (PKA). A truncated PKC gene, delta PKC beta, lacking the coding region for amino acid positions 6 to 159 of PKC beta was also constructed. These mutant kinase genes expressed under the control of the SR alpha promoter activated the c-fos gene enhanc
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3

Tremblay, Patricia G., and Marc-André Sirard. "Gene analysis of major signaling pathways regulated by gonadotropins in human ovarian granulosa tumor cells (KGN)†." Biology of Reproduction 103, no. 3 (2020): 583–98. http://dx.doi.org/10.1093/biolre/ioaa079.

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Abstract The female reproductive function largely depends on timing and coordination between follicle-stimulating hormone (FSH) and luteinizing hormone. Even though it was suggested that these hormones act on granulosa cells via shared signaling pathways, mainly protein kinases A, B, and C (PKA, PKB, and PKC), there is still very little information available on how these signaling pathways are regulated by each hormone to provide such differences in gene expression throughout folliculogenesis. To obtain a global picture of the principal upstream factors involved in PKA, PKB, and PKC signaling
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Blount, Mitsi A., Penelope Cipriani, Sara K. Redd та ін. "Activation of protein kinase Cα increases phosphorylation of the UT-A1 urea transporter at serine 494 in the inner medullary collecting duct". American Journal of Physiology-Cell Physiology 309, № 9 (2015): C608—C615. http://dx.doi.org/10.1152/ajpcell.00171.2014.

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Hypertonicity increases urea transport, as well as the phosphorylation and membrane accumulation of UT-A1, the transporter responsible for urea permeability in the inner medullary collect duct (IMCD). Hypertonicity stimulates urea transport through PKC-mediated phosphorylation. To determine whether PKC phosphorylates UT-A1, eight potential PKC phosphorylation sites were individually replaced with alanine and subsequently transfected into LLC-PK1 cells. Of the single mutants, only ablation of the S494 site dampened induction of total UT-A1 phosphorylation by the PKC activator phorbol dibutyrate
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Lacroix, M., and A. Hontela. "Regulation of acute cortisol synthesis by cAMP-dependent protein kinase and protein kinase C in a teleost species, the rainbow trout (Oncorhynchus mykiss)." Journal of Endocrinology 169, no. 1 (2001): 71–78. http://dx.doi.org/10.1677/joe.0.1690071.

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The effects of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) on acute ACTH-stimulated cortisol secretion were assessed using a specific PKA inhibitor (H-89) and a PKC activator (phorbol 12-myristate 13-acetate, PMA) in dispersed head kidney cells of rainbow trout (Oncorhynchus mykiss). To investigate the sites of action of both PKA and PKC, pregnenolone (a cortisol precursor stemmed from the rate limiting step in cortisol synthesis) and 25-OH-cholesterol (an exogenous substrate that bypasses the rate limiting step) were used as substrates, with and without ACTH stimulation. In
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Itoh, Hiroyuki, Shinji Yamamura, J. Anthony Ware, et al. "Differential effects of protein kinase C on human vascular smooth muscle cell proliferation and migration." American Journal of Physiology-Heart and Circulatory Physiology 281, no. 1 (2001): H359—H370. http://dx.doi.org/10.1152/ajpheart.2001.281.1.h359.

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Vascular smooth muscle cell (SMC) migration and proliferation contribute to intimal hyperplasia, and protein kinase C (PKC) may be required for both events. In this report, we investigated the role of PKC in proliferation and migration of SMC derived from the human saphenous vein. Activation of PKC by phorbol-12,13-dibutyrate (PDBu) or (−)-indolactam [(−)-ILV] increases SMC proliferation. Downregulation of PKC activity by prolonged incubation with phorbol ester or inhibition of PKC with chelerythrine in SMC diminished agonist-stimulated proliferation. In contrast, stimulation of PKC with PDBu
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Chen, Yongyue, Guillermo A. Altenberg, and Luis Reuss. "Mechanism of activation of Xenopus CFTR by stimulation of PKC." American Journal of Physiology-Cell Physiology 287, no. 5 (2004): C1256—C1263. http://dx.doi.org/10.1152/ajpcell.00229.2004.

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PKA-mediated phosphorylation of the regulatory (R) domain plays a major role in the activation of the human cystic fibrosis transmembrane conductance regulator (hCFTR). In contrast, the effect of PKC-mediated phosphorylation is controversial, smaller than that of PKA, and dependent on the cell type. In the present study, we expressed Xenopus CFTR ( XCFTR) and hCFTR in Xenopus oocytes and examined their responses (i.e., macroscopic membrane conductance) to maximal stimulation by PKC and PKA agonists. With XCFTR, the average response to PKC was approximately sixfold that of PKA stimulation. In c
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Hou, Lili, Lei Zhu, Min Zhang, et al. "Participation of Antidiuretic Hormone (ADH) in Asthma Exacerbations Induced by Psychological Stress via PKA/PKC Signal Pathway in Airway-Related Vagal Preganglionic Neurons (AVPNs)." Cellular Physiology and Biochemistry 41, no. 6 (2017): 2230–41. http://dx.doi.org/10.1159/000475638.

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Aims: Present study was performed to examine whether ADH was implicated in psychological stress asthma and to explore the underlying molecular mechanism. Methods: We not only examined ADH levels in the cerebrospinal fluid (CSF) via radioimmunoassay, but also measured ADH receptor (ADHR) expression in airway-related vagal preganglionic neurons (AVPNs) through real-time PCR in all experimental mice. Western blotting was performed to evaluate the relationship between ADH and PKA/PKC in psychological stress asthma. Finally, the role of PKA/PKC in psychological stress asthma was analyzed. Results:
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Wartmann, M., D. A. Jans, P. J. Parker, et al. "Overexpression of the alpha-type protein kinase (PK) C in LLC-PK1 cells does not lead to a proportional increase in the induction of two 12-O-tetradecanoylphorbol-13-acetate-inducible genes." Cell Regulation 2, no. 6 (1991): 491–502. http://dx.doi.org/10.1091/mbc.2.6.491.

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Phorbol esters, by activating protein kinase C (PKC), induce the expression of the urokinase-type plasminogen activator (uPA) gene and the proto-oncogene c-fos in LLC-PK1 (PK1) porcine kidney epithelial cells. To investigate the role of PKC in the regulation of these two 12-O-tetradecanoylphorbol-13-acetate (TPA)-inducible genes, the alpha-type PKC, the predominant subtype present in the PK1 cells, was overexpressed in this cell line. Two clonal PK1 derivatives overexpressing the alpha PKC 15- and 20-fold, respectively, were established. Compared with the parental and control cells, only a mod
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Wu, D., I. J. Clarke, and C. Chen. "The role of protein kinase C in GH secretion induced by GH-releasing factor and GH-releasing peptides in cultured ovine somatotrophs." Journal of Endocrinology 154, no. 2 (1997): 219–30. http://dx.doi.org/10.1677/joe.0.1540219.

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Abstract The involvement of protein kinase C (PKC) in the action of GH-releasing factor (GRF) and synthetic GH-releasing peptides (GHRP-2 and GHRP-6) was investigated in ovine somatotrophs in primary culture. In partially purified sheep somatotrophs, GRF and GHRP-2 caused translocation of PKC activity from the cytosol to the cell membranes and caused GH release in a dose- and time-dependent manner. GHRP-6 did not cause PKC translocation. The PKC inhibitors, calphostin C, staurosporine and chelerythrine, partially reduced GH release in response to GRF and GHRP-2 at doses which selectively inhib
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Tesis sobre el tema "PKC"

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Plammootil, Suma Mary. "Herstellung und Etablierung von 4-Hydroxytamoxifen aktivierbaren PKC[alpha]- [PKC alpha]-, PKC[beta]1- [PKC beta1] und PKCd--Fusionsproteinen [PKC delta-Fusionsproteinen]." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=971703302.

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Snider, Adam K. "PKC gamma regulates connexin 57." Thesis, Manhattan, Kan. : Kansas State University, 2010. http://hdl.handle.net/2097/4128.

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Bahte, Svenja-Katharina Paula. "Identifikation neuer Bindungspartner von PKC- d [PKC-delta] mit Hilfe des Yeast-two-hybrid-Screens." [S.l.] : [s.n.], 2004. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=013081490&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.

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Cheng, Sam Xian Jun. "Functional significance of phosphorylation of rat renal Na+,K+-ATPase by PKA and PKC /." Stockholm, 1998. http://diss.kib.ki.se/1998/91-628-2971-8.

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Quittau-Prévostel, Corinne. "Mutant D294G de la PKC[alpha] tumorigénèse humaine : la PKC[alpha], un nouveau suppresseur de tumeur." Montpellier 1, 1997. http://www.theses.fr/1997MON1T005.

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ZINI, SILVIA. "PKC: Paffard Keatinge-Clay architetto itinerante." Doctoral thesis, Università IUAV di Venezia, 2015. http://hdl.handle.net/11578/278352.

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Worthmann, Kirstin [Verfasser]. "Die Rolle der atypischen Protein Kinase C Isoformen PKC[lambda]/[iota] und PKC[zeta] in Podozyten / Kirstin Worthmann." Hannover : Technische Informationsbibliothek und Universitätsbibliothek Hannover, 2011. http://d-nb.info/1012625508/34.

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Cabrerizo, Benito Yolanda. "Studies on a PKC-PLD-MAPK pathway." Thesis, University College London (University of London), 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.399767.

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Kostelecky, B. D. "An investigation of PKC isoform functional specificity." Thesis, University College London (University of London), 2009. http://discovery.ucl.ac.uk/18705/.

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Protein kinase C (PKC) isozymes are vital signalling proteins in many intracellular processes including cell survival, proliferation and migration. As such, changes in their expression levels have been linked to many types of cancer. The various PKC family members provoke differential responses in cancer highlighting the need for study of individual isoforms. This investigation of PKC has aimed to determine how kinase domain structure, regulatory region interactions and binding partners confer functional specificity to individual PKC isoforms. X-ray crystallographic, biochemical and biophysica
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Peel, N. R. "Dissecting compartmentalised atypical PKC controls in cell migration." Thesis, University College London (University of London), 2014. http://discovery.ucl.ac.uk/1419046/.

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Atypical Protein Kinase C (aPKC) isoforms are essential regulators of polarised cell behaviour and in migrating NRK cells translocate to the leading edge in a complex with the exocyst and KIBRA. Engineered delivery of upstream signals to the plasma membrane places leading edge ERK activation downstream of aPKC and demonstrates partial sufficiency in regulating cell migration and adhesion. This model system provides the opportunity to probe the leading edge to better understand events downstream of aPKC. Multiple screening approaches have identified cytoskeletal and translation processes as put
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Libros sobre el tema "PKC"

1

Garay, Juan A., ed. Public-Key Cryptography – PKC 2021. Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-75245-3.

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Garay, Juan A., ed. Public-Key Cryptography – PKC 2021. Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-75248-4.

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Hanaoka, Goichiro, Junji Shikata, and Yohei Watanabe, eds. Public-Key Cryptography – PKC 2022. Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-97121-2.

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Hanaoka, Goichiro, Junji Shikata, and Yohei Watanabe, eds. Public-Key Cryptography – PKC 2022. Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-97131-1.

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Yung, Moti, Yevgeniy Dodis, Aggelos Kiayias, and Tal Malkin, eds. Public Key Cryptography - PKC 2006. Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/11745853.

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Nguyen, Phong Q., and David Pointcheval, eds. Public Key Cryptography – PKC 2010. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-13013-7.

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Okamoto, Tatsuaki, and Xiaoyun Wang, eds. Public Key Cryptography – PKC 2007. Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71677-8.

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Jarecki, Stanisław, and Gene Tsudik, eds. Public Key Cryptography – PKC 2009. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-00468-1.

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Lin, Dongdai, and Kazue Sako, eds. Public-Key Cryptography – PKC 2019. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-17253-4.

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Lin, Dongdai, and Kazue Sako, eds. Public-Key Cryptography – PKC 2019. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-17259-6.

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Capítulos de libros sobre el tema "PKC"

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Wang, Q. Jane. "PKC–PKD Interplay in Cancer." In Protein Kinase C in Cancer Signaling and Therapy. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_14.

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Sun, Zuoming. "PKC-θ." In Encyclopedia of Medical Immunology. Springer New York, 2014. http://dx.doi.org/10.1007/978-0-387-84828-0_45.

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Wolf, Christopher, An Braeken, and Bart Preneel. "Efficient Cryptanalysis of RSE(2)PKC and RSSE(2)PKC." In Security in Communication Networks. Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/978-3-540-30598-9_21.

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Kazanietz, Marcelo G. "Introduction: PKC and Cancer." In Protein Kinase C in Cancer Signaling and Therapy. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_11.

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Merajver, Sofia D., Devin T. Rosenthal, and Lauren Van Wassenhove. "PKC and Breast Cancer." In Protein Kinase C in Cancer Signaling and Therapy. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_17.

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Kim, Jeewon, and Marcelo G. Kazanietz. "PKC and Prostate Cancer." In Protein Kinase C in Cancer Signaling and Therapy. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_18.

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McNaughton, Peter A. "TRPV1 Modulation by PKC." In Encyclopedia of Pain. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-28753-4_4645.

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Denning, Mitchell F. "PKC Isozymes and Skin Cancer." In Protein Kinase C in Cancer Signaling and Therapy. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_16.

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Baier, G. "PKC Isotype Functions in T Lymphocytes." In Sparking Signals. Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/2789_2007_061.

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Basu, Alakananda. "PKC and Resistance to Chemotherapeutic Agents." In Protein Kinase C in Cancer Signaling and Therapy. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_21.

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Actas de conferencias sobre el tema "PKC"

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Chen, Meiling, Yuanyuan Yang, Sixu Guo, Jin Cao, Haitao Du, and Li Su. "Signcryption based on Elliptic Curve CL-PKC for Low Earth Orbit Satellite Security Networking." In 2024 IEEE 23rd International Conference on Trust, Security and Privacy in Computing and Communications (TrustCom). IEEE, 2024. https://doi.org/10.1109/trustcom63139.2024.00148.

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Kiviharju, Mikko. "Fuzzy pairings-based CL-PKC." In Proceedings of the First SAGA Conference. WORLD SCIENTIFIC, 2008. http://dx.doi.org/10.1142/9789812793430_0009.

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Nasako, Takeshi, Yasuyuki Murakami, and Masao Kasahara. "Security of Double-Sequence Knapsack PKC and Single-Sequence Knapsack PKC against Low-Density Attack." In 2009 Fourth International Conference on Computer Sciences and Convergence Information Technology. IEEE, 2009. http://dx.doi.org/10.1109/iccit.2009.283.

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Martin, DW, J. Mazer, EO Harrington, and G. Choudhary. "PKC Isoforms in Right Ventricular Hypertrophy." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a4145.

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Apostolatos, Andre H., Wishrawana S. Ratnayake, Tracess Smalley, Anisul Islam, and Mildred Acevedo-Duncan. "Abstract 2369: Transcription activators that regulate PKC-iota expression and are downstream targets of PKC-iota." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-2369.

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Hopple, Sara, Mark Bushfield, Fiona Murdoch, and D. Euan MacIntyre. "REGULATION OF PLATELET cAMP FORMATION BY PROTEIN KINASE C." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644512.

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Exogenous synthetic 1,2-diacylglycerols (e.g. 1,2-dioctanoylglycerol, DiC8) and 4β Phorbol esters (e.g. phorbol myristate acetate, PMA) routinely are used to probe the effects of protein Kinase C (PKC) on cellular responsiveness. Such agents act either independently or synergistically with elevated [Ca2+]i to induce platelet activation, but also inhibit agonist-induced inositol lipid metabolism and Ca2+ flux. These findings led to the concept that activated PKC can function as a bi-directional regulator of platelet reactivity. Therefore, DiCg and PMA were utilized to examine the effects of act
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Nasako, Takeshi, Yasuyuki Murakami, and Masao Kasahara. "A Note on Security of KMN PKC." In 2008 Third International Conference on Convergence and Hybrid Information Technology (ICCIT). IEEE, 2008. http://dx.doi.org/10.1109/iccit.2008.96.

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Cayrel, Pierre-Louis, and Pierre Dusart. "McEliece/Niederreiter PKC: Sensitivity to Fault Injection." In 2010 5th International Conference on Future Information Technology. IEEE, 2010. http://dx.doi.org/10.1109/futuretech.2010.5482663.

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Zuxi, Wang, and Yu Baimu. "A Probabilistic Encryption Way in Knapsack PKC." In 1st International Workshop on Cloud Computing and Information Security. Atlantis Press, 2013. http://dx.doi.org/10.2991/ccis-13.2013.33.

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Douzono, Tatsuo, Takeshi Nasako, and Yasuyuki Murakami. "Effectiveness of plaintext encoding in knapsack PKC." In 2008 International Symposium on Information Theory and Its Applications (ISITA). IEEE, 2008. http://dx.doi.org/10.1109/isita.2008.4895588.

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Informes sobre el tema "PKC"

1

Gutmann, P., and C. Bonnell. Standard Public Key Cryptography (PKC) Test Keys. RFC Editor, 2023. http://dx.doi.org/10.17487/rfc9500.

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Balaji, Kethandapatti C. MT 2A Phosphorylation by PKC Mu/PKD Influences Chemosensitivity to Cisplatin in Prostate Cancer. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada495664.

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Garg, Rachana. PKC Epsilon: A Novel Oncogenic Player in Prostate Cancer. Defense Technical Information Center, 2014. http://dx.doi.org/10.21236/ada612051.

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Garg, Rachana. PKC Epsilon: A Novel Oncogenic Player in Prostate Cancer. Defense Technical Information Center, 2013. http://dx.doi.org/10.21236/ada592838.

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Cho, Yunhi, and David Talmage. The Role of PKC in Retinoic Acid Regulation of Human Mammary Cancer Cell Proliferation. Defense Technical Information Center, 1997. http://dx.doi.org/10.21236/ada338674.

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Cho, Yunhi, and David A. Talmage. The Role of PKC in Retinoic Acid Regulation of Human Mammary Cancer Cell Proliferation. Defense Technical Information Center, 1998. http://dx.doi.org/10.21236/ada357326.

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Kazanietz, Marcelo G. Role of the Chemokine MCP-1 in Sensitization of PKC-Mediated Apoptosis in Prostate Cancer Cells. Defense Technical Information Center, 2009. http://dx.doi.org/10.21236/ada500950.

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Kazanietz, Marcelo G. Role of the Chemokine MCP-1 in Sensitization of PKC-Medicated Apoptosis in Prostate Cancer Cells. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada482340.

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Dickman, Martin B., and Oded Yarden. Role of Phosphorylation in Fungal Spore Germination. United States Department of Agriculture, 1993. http://dx.doi.org/10.32747/1993.7568761.bard.

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Spore germination is a common and fundamental event in fungal development and in many instances an essential phase of fungal infection and dissemination. Spore germination is also critical for hyperparasites to function as biocontrol agents as well as in fermentation proceses. Our common objective is to understand the mechanisms which regulated spore germination and identify factors involved in pathogenicity related prepenetration development. Our approach is to exploit the overall similarity among filamentous fungi using both a plant pathogen (Colletotricum trifolii) and a model system that i
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Lee, Yong J., S. S. Galoforo, and C. M. Berns. Differential effect of 1{alpha},25-dihydroxyvitamin D{sub 3} on Hsp28 and PKC{beta} gene expression in the phorbol ester-resistant human myeloid HL-525 leukemic cells. Office of Scientific and Technical Information (OSTI), 1997. http://dx.doi.org/10.2172/522765.

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