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Dissertations / Theses on the topic 'Protein kinase'

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Published: 4 June 2021

Last updated: 29 July 2024

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Braz, Julian C. "Protein Kinase Ca & p38 protein kinase In heart failure: old stories, new players /." Cincinnati, Ohio : University of Cincinnati, 2006. http://www.ohiolink.edu/etd/view.cgi?ucin1147723239.

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Thesis (Ph. D. )--University of Cincinnati, 2006.
Advisor: Dr. Jeffery D Molkentin Title from electronic thesis title page (viewed Nov. 23, 2007). Includes abstract. Includes bibliographical references.

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12

BRAZ, JULIAN C. "Protein Kinase Cα & p38 Protein Kinase In Heart Failure: Old Stories, New Players." University of Cincinnati / OhioLINK, 2006. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1147723239.

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13

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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14

Rojnuckarin, Ponlapat. "Mitogen-activated protein kinase pathways in megakaryocyte development /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/9200.

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15

Penfold, Lucy. "Investigating the roles of AMP-activated protein kinase and calcium/calmodulin-dependent protein kinase kinase β in prostate cancer." Thesis, Imperial College London, 2016. http://hdl.handle.net/10044/1/54390.

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Prostate cancer cells are characterised by rapid growth, proliferation and migration, which requires rewiring of cellular metabolism including increased lipid and protein synthesis. AMP-activated protein kinase (AMPK) is a conserved master regulator of energy homeostasis and acts to downregulate anabolism and cell growth, whilst upregulating catabolism to maintain cellular ATP levels. Whether these actions inhibit or aid cancer progression is controversial. Intriguingly, an upstream activating kinase of AMPK, calcium/calmodulin-dependent protein kinase kinase β (CaMKKβ) has recently been implicated in prostate cancer progression. A small-molecule direct activator of AMPK, 991, was used to test the effects of AMPK activation in a panel of prostate cancer cell lines. AMPK activation led to downregulation of cellular proliferation, 2D migration, invasion and lipogenesis, and upregulation of adhesion in all cell lines. However, in PC3 and 22RV1 cells AMPK activation led to an increase in migration down a chemoattractant gradient. This increase in migration was dependent on CaMKKβ and PAK1 activity. To investigate the role of AMPK and CaMKKβ in vivo the PTEN prostate cancer mouse model was used. AMPKβ1 and CaMKKβ were deleted in this model creating two novel mouse lines. Upon β1-deletion prostate cancer development was increased based on the timing of a switch in protein expression characterised in the PTEN-/- prostate upon disease progression and pathological analysis of tissue sections. In contrast, disease progression was significantly reduced upon CaMKKβ-deletion in the PTEN-/- prostate based on prostate weight, Ki-67 staining and pathological analysis. Disease progression was also inhibited in the PTEN mouse model upon treatment with a pharmacological inhibitor of CaMKKβ, STO609. These data suggest that AMPK and CaMKKβ have different roles in prostate cancer development and progression likely lie on separate pathways in this disease.

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16

Holland, Zoe. "Plasmodium falciparum protein kinase CK2." Thesis, University of Glasgow, 2008. http://theses.gla.ac.uk/606/.

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Malaria, caused by infection with intracellular protozoan parasites of the genus Plasmodium, is responsible for 300 to 600 million clinical cases annually (Snow et al., 2005), resulting in the deaths of up to three million people every year (Breman, 2001, Breman et al., 2004). There is a clear need for further research aimed at identifying novel drug targets (Ridley, 2002). Reversible phosphorylation of proteins is a major regulatory mechanism in most cellular processes, and protein kinases are considered promising drug targets, comprising as much as 30% of all protein targets under investigation (Cohen, 2002). The divergences between human and plasmodial protein kinases suggest that specific inhibition of the latter is an achievable goal (Doerig, 2004, Doerig and Meijer, 2007). This study investigates protein kinase CK2 of Plasmodium falciparum, seeking to establish by reverse genetics and biochemical approaches whether it represents a possible antimalarial drug target. Protein-kinase CK2, formerly known as Casein Kinase II, is a dual-specificity (Serine/Threonine and Tyrosine) protein kinase ubiquitously expressed in eukaryotes. It has over 300 cellular substrates catalogued to date (Meggio and Pinna, 2003). Consistent with its multiple substrates, the enzyme plays a crucial role in many cellular processes, and is essential to viability in yeast and slime mould (Padmanabha et al., 1990, Kikkawa et al., 1992). The human CK2 holoenzyme consists of two catalytic a or a’ subunits and two regulatory b subunits, and recent evidence indicates that the latter interact with several protein kinases in addition to CK2a (reviewed in (Bibby and Litchfield, 2005)), pointing to a likely role in the integration of numerous signalling pathways. A putative CK2a orthologue and two predicted CK2b subunits were identified in the P. falciparum genome (Ward et al., 2004, Anamika et al., 2005). Here we present the biochemical characterisation of the PfCK2a orthologue and both PfCK2b orthologues, and demonstrate by using a reverse genetics approach that each of the three subunits is essential for completion of the erythrocytic asexual cycle of the parasite, thereby validating the enzyme as a possible drug target. Recombinant PfCK2a possesses protein kinase activity, exhibits similar substrate and co-substrate preferences to those of CK2a subunits from other organisms, and interacts with both of the PfCK2b subunits in vitro. PfCK2a is amenable to inhibitor screening, and we report differential susceptibility between the human and P. falciparum CK2a enzymes to a small molecule inhibitor. Taken together, the data indicate that PfCK2a is an attractive, validated target for antimalarial chemotherapeutic intervention.

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17

Robinson, Karen Ann. "Protein regulators of kinase C." Thesis, University College London (University of London), 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.282756.

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18

Matthews, Sharon. "Regulation of protein kinase D." Thesis, University College London (University of London), 2000. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.716241.

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19

Davis, Alison Jane. "Kinase-anchoring proteins and the intracellular targeting of cyclic adenosine monophosphate (cAMP)-dependent protein kinase." Thesis, University of Leicester, 2007. http://hdl.handle.net/2381/29960.

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Kinase anchoring proteins (AKAPs) are a family of structurally diverse multidomain proteins classified solely by their ability to bind cAMP-dependent protein kinase/protein kinase A (PKA). We show that the prototypic AKAP, AKAP79, targets PKA to the plasma membrane. This subcellular localisation is mediated via interactions between basic regions on AKAP79 and acidic phospholipids in the plasma membrane. We show that while PKA and protein kinase C (PKC)-dependent phosphorylation of AKAP79 targeting residues has no effect on its subcellular localization, Gq-coupled receptor-driven depletion of the lipid anchor PtdIns(4,5)P2 causes release of AKAP79 from the membrane. Receptor-mediated regulation of AKAP membrane binding may be an important feedback mechanism controlling the degree of access that AKAP-bound enzymes have to membrane-associated substrates. Real-time confocal imaging failed to show significant redistribution of AKAP79 following Gq-coupled receptor activation, which may reflect only limited short-range movements.;In addition to regulated association with membrane, we also show through co-immunoprecipitation studies a direct interaction between AKAP79 and all three members of the inwardly rectifying potassium channel Kir2 family. Using a combination of deletion analysis and structural modelling we show that AKAP79 binds the Kir2 family via a novel binding motif located on the C terminus of the ion channel and not via a leucine zipper as has been reported for other AKAP-channel interactions. Interestingly, we also show using a PKA regulatory subunit overlay assays that this region of Kir2.1 is capable of isolating other, potentially novel, AKAPs from rat brain and heart homogenates.;Finally, we use whole-cell patch clamp analysis to demonstrate that cAMP-dependent modulation of Kir2.1 channel activity is significantly enhanced in the presence of AKAP79, thus confirming an important role for AKAP79 in targeting PKA to key channel phosphorylation sites.

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20

Cherezova, Lidia Nikolayevna. "Determining the effects of phosphorylation on AFAP-110 function." Morgantown, W. Va. : [West Virginia University Libraries], 2002. http://etd.wvu.edu/templates/showETD.cfm?recnum=2492.

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Thesis (M.S.)--West Virginia University, 2002.
Title from document title page. Document formatted into pages; contains v, 105 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.

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21

Chan, Ka-wai, and 陳嘉威. "Characterization of a physiological 62-kDa protein substrate for ganglioside-stimulated protein kinase in central nervous systemmyelin." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2004. http://hub.hku.hk/bib/B30595575.

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22

Maitra, Sushmit. "The AU-rich element mRNA decay-promoting activity of BRF1 is regulated by mitogen-activated protein kinase activated protein kinase 2." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2008. https://www.mhsl.uab.edu/dt/2008r/maitra.pdf.

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23

Dettori, Rosalia Angela [Verfasser], and Albrecht [Akademischer Betreuer] Piiper. "Regulation of the interaction between protein kinase C-related protein kinase 2 (PRK2) and its upstream kinase, 3-phosphoinositide-dependent protein kinase 1 (PDK1) / Rosalia Angela Dettori. Betreuer: Albrecht Piiper." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2011. http://d-nb.info/1051285267/34.

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24

Dettori, Rosalia Angela [Verfasser], and Albrecht [Akademischer Betreuer] Piiper. "Regulation of the interaction between protein kinase C-related protein kinase 2(PRK2) and its upstream kinase, 3-phosphoinositide-dependent protein kinase 1 (PDK1) / Rosalia Angela Dettori ; Betreuer: Albrecht Piiper." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2017. http://d-nb.info/1131628934/34.

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25

Streicher, John Michael. "The role of mitogen activated protein kinase activated protein kinase-2 in regulating p38 mitogen activated protein kinase induced cyclooxygenase-2 induction and heart failure." Diss., Restricted to subscribing institutions, 2009. http://proquest.umi.com/pqdweb?did=1872200951&sid=6&Fmt=2&clientId=1564&RQT=309&VName=PQD.

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26

Yap, Jessica. "Identification of Plasmodium falciparum protein kinase substrates and interacting proteins." Honors in the Major Thesis, University of Central Florida, 2012. http://digital.library.ucf.edu/cdm/ref/collection/ETH/id/644.

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Characterization of PfPKA and PfPK5 substrates, as well as the proteins they interact with, will help us to develop innovative therapies targeting binding sites.; Malaria is a devastating disease that results in almost one million deaths annually. Most of the victims are children under the age of five in Sub-Saharan Africa. Malaria parasite strains throughout developing countries are continually building resistance to available drugs. Current therapies such as mefloquine, chloroquine, as well as artemisinin are becoming less effective, and this underscores the urgency for therapeutics directed against novel drug targets. In order to identify new drug targets, the molecular biology of the malaria parasite Plasmodium needs to be elucidated. Plasmodium exhibits a unique cell cycle in which it undergoes multiple rounds of DNA synthesis and mitosis without cytokinesis. Thus, cell cycle regulatory proteins are likely to be promising pathogen-specific drug targets. It is expected that fluctuating activity of key proteins, such as protein kinases, play an essential role in regulating the noncanonical life cycle of Plasmodium. Consequently, malarial kinases are a prime target for therapy. One way to better understand the role of malarial kinases in Plasmodium cell cycle regulation is to identify putative protein kinase substrates and interacting proteins. Two malarial kinases that have been implicated in regulating malaria parasite cell cycle stages were investigated in this study: P. falciparum CDK-like Protein Kinase 5 (PfPK5) and cAMP-Dependent Protein Kinase A (PfPKA). A transgenic P. falciparum line was created for the expression of epitope-tagged PfPK5 for pull-down analysis. Phospho-substrate antibodies were used to identify physiological substrates of both PfPK5 and PfPKA. Immunoblotting with these antibodies identified several potential substrates. Identities of the PfPKA physiological substrates were determined from the global P. falciparum phosphoproteome dataset that has recently been generated in our laboratory.
B.S.
Bachelors
Burnett School of Biomedical Sciences
Molecular and Microbiology

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27

Dutil, Erica M. "Phosphorylation of protein kinase C by the phosphoinositide-dependent kinase /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2000. http://wwwlib.umi.com/cr/ucsd/fullcit?p9961757.

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28

Mills, Julia. "Regulation of amyloid precursor protein catabolism in vitro, the role of mitogen-activated protein kinase and protein kinase C." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/nq27201.pdf.

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29

Hurst, Denise. "AMP-activated protein kinase kinase activity and phosphorylation of AMP-activated protein kinase in contracting muscle of sedentary and endurance trained rats." Diss., CLICK HERE for online access, 2007. http://contentdm.lib.byu.edu/ETD/image/etd2014.pdf.

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30

Young, Stephen W. "The insulin receptor tyrosine kinase and the activation of the map kinase cascade : interactions with the protein kinase C and protein kinase A signalling pathways." Thesis, University of Bristol, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.238958.

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31

Smart, Nicola. "Studies on the mechanism of protein kinase C down-regulation." Thesis, Royal Veterinary College (University of London), 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.391675.

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32

Kotwaliwale, Chitra V. "Regulation and functions of the Ipl1/aurora protein kinase /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/5081.

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33

Lala, Hitesh Nagin. "Subcloning of calcium-dependent protein kinase related kinase homologues in arabidopsis thaliana." Thesis, Georgia Institute of Technology, 1997. http://hdl.handle.net/1853/25343.

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34

Nurimba, Margaret. "Roles of SR protein kinase Dsk1 and LAMMER kinase Kic1 in mRNA processing in fission yeast, Schizosaccharomyces pombe." Scholarship @ Claremont, 2014. http://scholarship.claremont.edu/scripps_theses/305.

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Protein kinases comprise a fundamental class of cell function regulators that modify proteins by transferring phosphate groups from a nucleoside triphosphate such as ATP to specific amino acid residues on target proteins, altering protein conformation, function, and activity. As such, protein kinases are major regulators of many biological processes, including gene expression, which consists of the transfer of hereditary information in two major processing steps, transcription of DNA into a complementary precursor RNA transcript (pre-mRNA) and its subsequent translated into protein by the ribosome, where it can then go on to perform various processes in the cell. One particular family of protein kinases, otherwise known as serine/arginine protein-specific protein kinases (SRPKs), is conserved throughout eukaryotes and has been shown to be important in regulating gene expression, yet their roles in the gene expression pathway have yet to be elucidated. SRPK are known to phosphorylate serine/arginine (SR) splicing factor proteins, which are involved in mRNA splice site recognition and recruitment of splicing machinery. Members of the LAMMER kinase subfamily of SRPKs have also been shown to be required for efficient pre-mRNA splicing and important for mediating cellular progression through the cell cycle. To determine what other roles SRPKs play in mRNA processing, it is of use to study the homologous SRPK and LAMMER kinases in fission yeast, S. pombe, Dsk1 and Kic1, respectively. S. pombe provides a genetically valuable model for studying kinase function in RNA processing as both RNA processing machinery and SRPKs are conserved through higher eukaryotes. Using a novel green fluorescent protein tagging system based on properties of the MS2 bacteriophage genome, we are able to label specific mRNA transcripts of interest and visualize their locations in the cell using fluorescence microscopy. By visualizing the mRNA trafficking patterns of intron-containing and intronless mRNA transcripts, we show for the first time that deletions of the Dsk1 and Kic1 genes result in the nuclear retention of mRNA, such that Dsk1 and Kic1 are distinctly involved in mRNA export out of the nucleus.

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35

Beeton, Carolyn Ann. "Functional differences of class 1a PI 3-kinase heterodimers." Thesis, University College London (University of London), 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.322073.

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36

Brancho, Deborah Marie. "Regulation and Function of Stress-Activated Protein Kinase Signal Transduction Pathways: A Dissertation." eScholarship@UMMS, 2005. https://escholarship.umassmed.edu/gsbs_diss/101.

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The c-Jun NH2-terminal kinase (JNK) group and the p38 group of mitogen-activated protein kinases (MAPK) are stress-activated protein kinases that regulate cell proliferation, differentiation, development, and apoptosis. These protein kinases are involved in a signal transduction cascade that includes a MAP kinase (MAPK), a MAP kinase kinase (MAP2K), and a MAP kinase kinase kinase (MAP3K). MAPK are phosphorylated and activated by the MAP2K, which are phosphorylated and activated by various MAP3K. The work presented in this dissertation focuses on understanding the regulation and function of the JNK and p38 MAPK pathways. Two different strategies were utilized. First, I used molecular and biochemical techniques to examine how MAP2K and MAP3K mediate signaling specificity and to define their role in the MAPK pathway. Second, I used gene targeted disruption studies to determine the in vivo role ofMAP2K and MAP3K in MAPK activation. I specifically used these approaches to examine: (1) docking interactions between p38 MAPK and MAP2K [MKK3 and MKK6 (Chapter II)]; (2) the differential activation of p38 MAPK by MAP2K [MKK3, MKK4, and MKK6 (Chapter III)]; and (3) the selective involvement of the mixed lineage kinase (MLK) group of MAP3K in JNK and p38 MAPK activation (Chapter IV and Appendix). In addition, I analyzed the role of the MKK3 and MKK6 MAP2K in cell proliferation and the role of the MLK MAP3K in adipocyte differentiation (Chapter III and Chapter IV). Together, these data provide insight into the regulation and function of the stress-activated MAPK signal transduction pathways.

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37

Chen, Mingzi. "Mos regulation in activating the MAP kinase pathway /." Thesis, Connect to this title online; UW restricted, 1997. http://hdl.handle.net/1773/9195.

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38

Luhovy, Artem. "The activation of protein kinase SLK." Thesis, McGill University, 2011. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=97038.

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The inappropriate expression, localization, or activation of kidney protein kinases may precipitate renal dysplasia or cystic diseases. The expression and activation of the Ste20-like kinase, SLK, is increased during renal development and recovery from ischemic acute renal failure (ARF). Activation of SLK promotes apoptosis and, during development and healing, SLK may regulate cell growth. Alternatively, in glomerular diseases, the activation of SLK and apoptosis of glomerular epithelial cells (GEC) may be harmful and lead to sclerotic glomerular injury. The overall aim of the project is to elucidate the regulation of SLK activity in order to better understand the role of SLK in kidney development and injury. It is proposed that activation of SLK may be due to upregulation of expression, which may then favor homodimerization and autophosphorylation. Serine and threonine residues were mutated in the putative activation segment of the SLK catalytic domain. Wild type (WT) and mutant proteins were expressed in COS-1 cells or GEC. Compared with SLK WT, the S189A mutant and the T183A/S189A double mutant showed trivial in vitro kinase activity, while kinase activity was reduced significantly by the T183A mutation. Expression of SLK WT increased activation-specific phosphorylation of c-Jun N-terminal kinase (JNK) and p38 kinase, reflecting enhanced signaling via stress kinase pathways. In contrast, activation of JNK by SLK T183A, S189A, and T183A/S189A and p38 by T183A/S189A was impaired. Similarly, expression of SLK WT stimulated activator protein-1 (AP1) reporter activity, but activation of AP1 by the three SLK mutants was ineffective. To test if homodimerization of SLK affects phosphorylation, the cDNA encoding the SLK catalytic domain (amino acids 1-373) was fused with a cDNA for a modified FK506 binding protein, Fv (SLK-Fv). After transfection, addition of AP20187 (an FK506 analog) induced regulated dimerization of SLK-Fv. AP20187-stimulated dimerization enhanced the kinase activity of SLK-Fv WT. In contrast, kinase activities of SLK-Fv T183A/S189A and activation site mutants E79A, K63R, T193A were weak, and were not enhanced after dimerization. Surprisingly, phosphomimetic mutants of SLK-Fv, including T183D, T183E, S189D, and S189E showed weak kinase activity, which was unaffected by dimerization. Co-transfection of SLK and T183A/S189A failed to silence the kinase activity of the WT in an in vitro kinase assay. Finally, apoptosis and late apoptosis were increased after expression of SLK-Fv WT, but not T183A/S189A. Thus, phosphorylation of T183, S189 and T193 plays a key role in the activation and signaling of SLK and could represent a target for novel therapeutic approaches to renal injury.
Une expression, une localisation ou une activation inappropriée des protéines kinases rénales peut provoquer une dysplasie rénale ou une maladie cystique prématurée. L'expression et l'activation de la protéine Ste20-like kinase (SLK) sont plus élevées pendant le développement des reins et durant la guérison d'une insuffisance rénale ischémique aiguë. Une activation de la protéine SLK entraîne l'apoptose des cellules in vitro et in vivo. Au cours du développement et de la régénérescence cellulaire, SLK peut réguler la croissance cellulaire. Par contre, dans les glomérulonéphrites, l'activation de la SLK et une apoptose des cellules épithéliales glomérulaires (GEC) peuvent être dommageables et peuvent provoquer des lésions glomérulaires sclérotiques. L'objectif de ce projet est d'élucider la régulation de l'activité de la SLK dans le but de mieux comprendre son rôle dans le développement et les lésions ou maladies glomérulaires rénales. Ce projet postule que l'activation de la protéine SLK peut être due à une régulation à la hausse de l'expression, qui peut alors favoriser une homodimérisation et une autophosphorylation. Pour étudier le rôle de la phosphorylation dans la régulation de l'activation, les résidus sérine (S189) et thréonine (T183) ont été mutés dans le segment putatif du domaine catalytique de la SLK. Deux mutants simples (T183A et S189A) et un double mutant (T183A/S189A) ont été créés. La forme sauvage (WT) et les mutants de la SLK ont été exprimés dans les cellules cos-1 et GEC. SLK WT phosphorylais la protéine basique de myéline (MBP) contrairement aux mutants S189A et T183A/S189A qui montraient une activité kinase in vitro non significative. La mutation T183A diminuait la phosphorylation de MBP significativement. L'analyse des voies de signalisation de la kinase N-terminal c-jun (JNK) et de la p38 par la SLK a été étudiée sachant que l'expression de la SLK WT stimule la phosphorylation de la JNK et de la p38. Tant que T183A/S189A n'a pas pu activer la JNK et la p38, les mutants T183A et S189A ont activé la JNK à un degré moindre que la SLK WT. Ces résultats démontrent que la phosphorylation de T183 et de S189 est importante pour l'activation de la SLK. De façon similaire, l'expression de la SLK WT a stimulé l'activation de la protéine activatrice 1 (AP1), un facteur de transcription de la famille c-fos et c-Jun, tandis que les trois mutants ont été incapables de stimuler AP1. Pour déterminer si l'homodimérisation de la SLK affecte la phosphorylation, l'ADN complémentaire de la SLK codant le domaine catalytique (1-373) a été fusionné avec l'ADN complémentaire d'une protéine modifiée qui s'attache à des molécules FK506 (Fv), pour créer SLK-Fv. Après la transfection, l'addition du AP20187, un analogue de FK506, induit la dimérisation de la SLK-Fv. La dimérisation occasionnée par l'AP20187 a augmenté l'activité catalytique de la SLK-Fv. Par contre, tous les mutants Fv fusionnés T183A/S189A, E79A, K63R et T193A démontraient une activité catalytique faible, que la dimérisation n'a pas pu augmenter. Ce qui est particulièrement intéressant, les mutants phosphomimétiques T183D, T183E, S189D et S189E montraient aussi une activité catalytique faible qui n'a pas été affectée par la dimérisation. Finalement, l'apoptose et la nécrose sont accrues suite à une surexpression de la SLK-Fv WT, mais pas avec le mutant T183A/S189A-Fv. Ainsi, les acides aminés K63 et E79 et la phosphorylation de T183, S189 et T193 jouent un rôle important dans la régulation de la SLK et pourraient être ciblés par des approches thérapeutiques pour le traitement des néphropathies.

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39

Stafford, Margaret Jackson. "Protein kinase C in platelet signalling." Thesis, University of Oxford, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.275204.

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40

Murphy, John Anthony. "The protein kinase C of glia." Thesis, University of York, 1989. http://etheses.whiterose.ac.uk/9762/.

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41

Ressurreicao, Margarida de Azevedo Gomes de Carvalho. "Protein kinase signalling in Schistosoma mansoni." Thesis, Kingston University, 2013. http://eprints.kingston.ac.uk/28771/.

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The present study focused on protein kinase C (pKC), extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein kinase (p38 MAPK) signalling in the human parasite Schistosoma mansoni, with a focus on life-stages which are human infective and dependent (cercariae, schistosomules and adult worms). Western blotting with anti-phospho antibodies, detected two phosphorylated PKC 081 kDa and ~ 116 kDa) and two phosphorylated ERK (~43 kDa and ~48 kDa) isotypes predicted in the S. mansoni genome in addition to the previously identified ~78 kDa PKC and ~42 kDa p38 MAPK (Ludtmann et al., 2009; Ressurreíçâo et al., 20lla,b). Additionally, an unusually large ~132 kDa PKC-like protein was detected that is not predicted in the genome. These proteins possessed enzymatic activities, responded to conventional activators and inhtbitors, and their activation profile was dissimilar between life-stages suggesting isotype distinct roles in each developmental stage. In vitro challenge with praziquantel stimulated activity of specific PKC and ERK isotypes, showing a putative involvement in the mode of action of this anthelmintic drug. In situ localization revealed the activated kinases associated with several regions including tegument, sensory, neuromuscular and reproductive structures; additionally, phosphorylated ERK was associated with the excretory system. PKC, ERK and p38 MAPK function was assessed through pharmacological and environmental assays. PKC and ERK were found to playa role in pairing, motility, ventral sucker attachment and egg output of adult worms and motility of schistosomules. Maintenance of unpaired adult worms in different sex ratio environments resulted in changes in PKC, ERK and p38 MAPK activity (both in male and females) showing importance in transduction of chemotatic and/or thigmotatic stimuli. Light and temperature changes affected kinase activity in cercariae mainly at the cercariae sensory papillae and parasite surface. Moreover, combined linoleic acid (LA) and CFDA-SE based assays developed for induction and monitoring of cercarial gland release showed that PKC, ERK and p38 MAPK are involved in mechanisms that underpin cercariae host detection/penetration and that pharmacological inhibition of these enzymes partially blocked LA induced release, while the PKC activator accelerated it. In schistosomules, epidermal growth factor and insulin stimulated ERK and PKC activity whereas insulin-like growth factor I and mouse red blood cells up¬regulated PKC activity only suggesting association with parasite nutrition and host-parasite communication. Internalization of fluorescently labelled transferrin via the schistosomule tegument was delayed with PKC inhibitors suggesting a role in transferrin uptake. Taken together, these data contribute significantly to our understanding of cell signalling in schistosomes and how such signalling regulates parasite function, and should open up new avenues of investigation for development of anti-schistosome drugs.

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42

Hocevar, Barbara Ann. "Characterization of nuclear protein kinase C." Case Western Reserve University School of Graduate Studies / OhioLINK, 1993. http://rave.ohiolink.edu/etdc/view?acc_num=case1057177248.

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43

Kumar, Varun. "Protein Kinase C Signaling in Neurodegeneration." Kent State University / OhioLINK, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=kent1455721051.

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44

Edwards, Amelia S. "Interdomain regulation of protein kinase C /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 1998. http://wwwlib.umi.com/cr/ucsd/fullcit?p9901441.

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45

Dennis, Patrick B. (Patrick Brian). "Autophosphorylation and Autoactivation of an S6/H4 Kinase Isolated From Human Placenta." Thesis, University of North Texas, 1994. https://digital.library.unt.edu/ark:/67531/metadc279364/.

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A number of protein kinases have been shown to undergo autophosphorylation, but few have demonstrated a coordinate increase or decrease in enzymatic activity as a result. Described here is a novel S6 kinase isolated from human placenta which autoactivates through autophosphorylation in vitro. This S6/H4 kinase, purified in an inactive state, was shown to be a protein of Mr of 60,000 as estimated by SDS-PAGE and could catalyze the phosphorylation of the synthetic peptide S6-21, the histone H4, and myelin basic protein. Mild digestion of the inactive S6/H4 kinase with trypsin was necessary, but not sufficient, to activate the kinase fully

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46

Hynes, Andrews Mark. "Rx-kinase and protein kinase C in superoxide production from neutrophils." Thesis, University College London (University of London), 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.267858.

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47

Foukas, Lazaros. "Defining the physiological role of phosphatidylinositol 3-kinase protein kinase activity." Thesis, University College London (University of London), 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.397223.

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48

Brown, Jacob D. "Liver Kinase B1/AMP-Activated Protein Kinase Signaling in the Diaphragm." BYU ScholarsArchive, 2010. https://scholarsarchive.byu.edu/etd/2543.

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The Liver Kinase B1 (LKB1)/AMP-Activated Protein Kinase (AMPK) signaling pathway is a major regulator of skeletal muscle metabolic processes. During exercise, LKB1-mediated phosphorylation of AMPK leads to its activation, promoting mitochondrial biogenesis and glucose transport, among other effects. The roles of LKB1 and AMPK have not been fully characterized in the diaphragm. Two methods of AMPK activation were used to characterize LKB1/AMPK signaling in diaphragms from muscle-specific LKB1 knockout (KO) and littermate control (C) mice: (1) acute injection of 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) and (2) 5-min direct electrical stimulation (ES) of the diaphragm. Diaphragms were excised 60 minutes post-AICAR injection and immediately after ES. AMPK phosphorylation increased with AICAR and ES in C but not KO mice. Acetyl CoA carboxylase (ACC) phosphorylation increased with AICAR in C but not KO mice, but increased in both genotypes with ES. While the majority of mitochondrial enzyme levels were lower in KO diaphragms, uncoupling protein 3 (UCP-3) levels were not different between genotypes. A IIx to IIb fiber type switch was observed in KO diaphragms. While in vitro peak force generation was similar between genotypes, KO diaphragms fatigued more quickly and had an impaired ability to recover. In conclusion, LKB1 regulates AMPK phosphorylation, mitochondrial enzyme expression, fiber type distribution, as well as recovery of the diaphragm from fatigue.

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49

Goodman, Alan Gabriel. "P58IPK, the cellular eIF2alpha kinase inhibitor, promotes viral mRNA translation and limits host death during influenza virus infection /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/8082.

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50

Baisden, Joseph M. "AFAP-110 is a cSrc activator." Morgantown, W. Va. : [West Virginia University Libraries], 2003. http://etd.wvu.edu/templates/showETD.cfm?recnum=2766.

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Thesis (Ph. D.)--West Virginia University, 2003.
Title from document title page. Document formatted into pages; contains v, 149 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.

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