Relevant bibliographies by topics / Protein kinase; Phosphatase; Kinetics

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Protein kinase; Phosphatase; Kinetics'

Author: Grafiati
Published: 4 June 2021
Last updated: 15 February 2022

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Journal articles on the topic "Protein kinase; Phosphatase; Kinetics"

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Kretschmer, M., W. Schellenberger, A. Otto, R. Kessler, and E. Hofmann. "Fructose-2,6-bisphosphatase and 6-phosphofructo-2-kinase are separable in yeast." Biochemical Journal 246, no. 3 (September 15, 1987): 755–59. http://dx.doi.org/10.1042/bj2460755.

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Fructose-2,6-bisphosphatase was purified from yeast and separated from 6-phosphofructo-2-kinase and alkaline phosphatase. The enzyme released Pi from the 2-position of fructose 2,6-bisphosphate and formed fructose 6-phosphate in stoichiometric amounts. The enzyme displays hyperbolic kinetics towards fructose 2,6-bisphosphate, with a Km value of 0.3 microM. It is strongly inhibited by fructose 6-phosphate. The inhibition is counteracted by L-glycerol 3-phosphate. Phosphorylation of the enzyme by cyclic-AMP-dependent protein kinase causes inactivation, which is reversible by the action of protein phosphatase 2A.
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BAJPAI, Anil, and Zacharie BRAHMI. "Regulation of natural killer cell-mediated cytotoxicity by serine/threonine phosphatases: identification of a calyculin A-sensitive serine/threonine kinase." Biochemical Journal 320, no. 1 (November 15, 1996): 153–59. http://dx.doi.org/10.1042/bj3200153.

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We have recently reported that Ser/Thr phosphatases play a key role in regulating natural killer (NK) cell lytic activity and that calyculin A and okadaic acid affect this activity differently [Bajpai and Brahmi (1994) J. Biol. Chem. 269, 18864–18869]. Here, we investigate a mechanism that might account for this differential action of calyculin A and okadaic acid on NK cells. Calyculin A specifically inhibited the lytic activity of YT-INDY, an NK-like cell line, and hyperphosphorylated 60 and 78 kDa proteins. The kinetics of appearance of these two proteins was correlated with the loss of lytic activity. In contrast, okadaic acid did not significantly affect either of these activities. The 78 kDa protein is localized in the cytosolic compartment whereas the 60 kDa protein is distributed equally between the membrane and the cytosolic fractions. Both proteins display a kinase activity and are phosphorylated mainly at serine and threonine residues but not at tyrosine residues. The activation of these kinases is specific to calyculin A treatment; it is independent of protein kinase C, protein kinase A, Ca2+, phosphotyrosine phosphatase and protein synthesis de novo. In conclusion, we have demonstrated that calyculin A, but not okadaic acid, hyperphosphorylates two proteins with Ser/Thr kinase activity, thus explaining the differential regulation of NK cells by these two Ser/Thr phosphatase inhibitors.
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Andrade, Angel, Faviola Tavares-Carreón, Maryam Khodai-Kalaki, and Miguel A. Valvano. "Tyrosine Phosphorylation and Dephosphorylation in Burkholderia cenocepacia Affect Biofilm Formation, Growth under Nutritional Deprivation, and Pathogenicity." Applied and Environmental Microbiology 82, no. 3 (November 20, 2015): 843–56. http://dx.doi.org/10.1128/aem.03513-15.

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ABSTRACTBurkholderia cenocepacia, a member of theB. cepaciacomplex (Bcc), is an opportunistic pathogen causing serious chronic infections in patients with cystic fibrosis. Tyrosine phosphorylation has emerged as an important posttranslational modification modulating the physiology and pathogenicity of Bcc bacteria. Here, we investigated the predicted bacterial tyrosine kinases BCAM1331 and BceF and the low-molecular-weight protein tyrosine phosphatases BCAM0208, BceD, and BCAL2200 ofB. cenocepaciaK56-2. We show that BCAM1331, BceF, BCAM0208, and BceD contribute to biofilm formation, while BCAL2200 is required for growth under nutrient-limited conditions. Multiple deletions of either tyrosine kinase or low-molecular-weight protein tyrosine phosphatase genes resulted in the attenuation ofB. cenocepaciaintramacrophage survival and reduced pathogenicity in theGalleria mellonellalarval infection model. Experimental evidence indicates that BCAM1331 displays reduced tyrosine autophosphorylation activity compared to that of BceF. With the artificial substratep-nitrophenyl phosphate, the phosphatase activities of the three low-molecular-weight protein tyrosine phosphatases demonstrated similar kinetic parameters. However, only BCAM0208 and BceD could dephosphorylate BceF. Further, BCAL2200 became tyrosine phosphorylatedin vivoand catalyzed its autodephosphorylation. Together, our data suggest that despite having similar biochemical activities, low-molecular-weight protein tyrosine phosphatases and tyrosine kinases have both overlapping and specific roles in the physiology ofB. cenocepacia.
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Abraham, S. M., and A. R. Clark. "Dual-specificity phosphatase 1: a critical regulator of innate immune responses." Biochemical Society Transactions 34, no. 6 (October 25, 2006): 1018–23. http://dx.doi.org/10.1042/bst0341018.

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Innate immune responses are critically dependent on MAPK (mitogen-activated protein kinase) signalling pathways, in particular JNK (c-Jun N-terminal kinase) and p38 MAPK. Both of these kinases are negatively regulated via their dephosphorylation by DUSP1 (dual­-specificity phosphatase 1). Several pro- and anti-inflammatory stimuli converge to regulate the DUSP1 gene and to modulate the time course of its expression. In turn, the pattern of expression of DUSP1 dictates the kinetics of activation of JNK and p38 MAPK, and this influences the expression of several mediators of innate immunity. DUSP1 is therefore a central regulator of innate immunity, and its expression can profoundly affect the outcome of inflammatory challenges. We discuss possible implications for immune-mediated inflammatory diseases and their treatment.
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HATAKEYAMA, Mariko, Shuhei KIMURA, Takashi NAKA, Takuji KAWASAKI, Noriko YUMOTO, Mio ICHIKAWA, Jae-Hoon KIM, et al. "A computational model on the modulation of mitogen-activated protein kinase (MAPK) and Akt pathways in heregulin-induced ErbB signalling." Biochemical Journal 373, no. 2 (July 15, 2003): 451–63. http://dx.doi.org/10.1042/bj20021824.

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ErbB tyrosine kinase receptors mediate mitogenic signal cascade by binding a variety of ligands and recruiting the different cassettes of adaptor proteins. In the present study, we examined heregulin (HRG)-induced signal transduction of ErbB4 receptor and found that the phosphatidylinositol 3′-kinase (PI3K)-Akt pathway negatively regulated the extracellular signal-regulated kinase (ERK) cascade by phosphorylating Raf-1 on Ser259. As the time-course kinetics of Akt and ERK activities seemed to be transient and complex, we constructed a mathematical simulation model for HRG-induced ErbB4 receptor signalling to explain the dynamics of the regulation mechanism in this signal transduction cascade. The model reflected well the experimental results observed in HRG-induced ErbB4 cells and in other modes of growth hormone-induced cell signalling that involve Raf-Akt cross-talk. The model suggested that HRG signalling is regulated by protein phosphatase 2A as well as Raf-Akt cross-talk, and protein phosphatase 2A modulates the kinase activity in both the PI3K–Akt and MAPK (mitogen-activated protein kinase) pathways.
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Endo-Streeter, Stuart, Man-Kin Marco Tsui, Audrey R. Odom, Jeremy Block, and John D. York. "Structural Studies and Protein Engineering of Inositol Phosphate Multikinase." Journal of Biological Chemistry 287, no. 42 (August 15, 2012): 35360–69. http://dx.doi.org/10.1074/jbc.m112.365031.

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Inositol phosphates (IPs) regulate vital processes in eukaryotes, and their production downstream of phospholipase C activation is controlled through a network of evolutionarily conserved kinases and phosphatases. Inositol phosphate multikinase (IPMK, also called Ipk2 and Arg82) accounts for phosphorylation of IP3 to IP5, as well as production of several other IP molecules. Here, we report the structure of Arabidopsis thaliana IPMKα at 2.9 Å and find it is similar to the yeast homolog Ipk2, despite 17% sequence identity, as well as the active site architecture of human IP3 3-kinase. Structural comparison and substrate modeling were used to identify a putative basis for IPMK selectivity. To test this model, we re-engineered binding site residues predicted to have restricted substrate specificity. Using steady-state kinetics and in vivo metabolic labeling studies in modified yeast strains, we observed that K117W and K117W:K121W mutants exhibited nearly normal 6-kinase function but harbored significantly reduced 3-kinase activity. These mutants complemented conditional nutritional growth defects observed in ipmk null yeast and, remarkably, suppressed lethality observed in ipmk null flies. Our data are consistent with the hypothesis that IPMK 6-kinase activity and production of Ins(1,4,5,6)P4 are critical for cellular signaling. Overall, our studies provide new insights into the structure and function of IPMK and utilize a synthetic biological approach to redesign inositol phosphate signaling pathways.
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Zhang, Si Qing, William G. Tsiaras, Toshiyuki Araki, Gengyun Wen, Liliana Minichiello, Ruediger Klein, and Benjamin G. Neel. "Receptor-Specific Regulation of Phosphatidylinositol 3′-Kinase Activation by the Protein Tyrosine Phosphatase Shp2." Molecular and Cellular Biology 22, no. 12 (June 15, 2002): 4062–72. http://dx.doi.org/10.1128/mcb.22.12.4062-4072.2002.

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ABSTRACT Receptor tyrosine kinases (RTKs) play distinct roles in multiple biological systems. Many RTKs transmit similar signals, raising questions about how specificity is achieved. One potential mechanism for RTK specificity is control of the magnitude and kinetics of activation of downstream pathways. We have found that the protein tyrosine phosphatase Shp2 regulates the strength and duration of phosphatidylinositol 3′-kinase (PI3K) activation in the epidermal growth factor (EGF) receptor signaling pathway. Shp2 mutant fibroblasts exhibit increased association of the p85 subunit of PI3K with the scaffolding adapter Gab1 compared to that for wild-type (WT) fibroblasts or Shp2 mutant cells reconstituted with WT Shp2. Far-Western analysis suggests increased phosphorylation of p85 binding sites on Gab1. Gab1-associated PI3K activity is increased and PI3K-dependent downstream signals are enhanced in Shp2 mutant cells following EGF stimulation. Analogous results are obtained in fibroblasts inducibly expressing dominant-negative Shp2. Our results suggest that, in addition to its role as a positive component of the Ras-Erk pathway, Shp2 negatively regulates EGF-dependent PI3K activation by dephosphorylating Gab1 p85 binding sites, thereby terminating a previously proposed Gab1-PI3K positive feedback loop. Activation of PI3K-dependent pathways following stimulation by other growth factors is unaffected or decreased in Shp2 mutant cells. Thus, Shp2 regulates the kinetics and magnitude of RTK signaling in a receptor-specific manner.
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Lasa, Marina, Sonya M. Abraham, Christine Boucheron, Jeremy Saklatvala, and Andrew R. Clark. "Dexamethasone Causes Sustained Expression of Mitogen-Activated Protein Kinase (MAPK) Phosphatase 1 and Phosphatase-Mediated Inhibition of MAPK p38." Molecular and Cellular Biology 22, no. 22 (November 15, 2002): 7802–11. http://dx.doi.org/10.1128/mcb.22.22.7802-7811.2002.

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ABSTRACT The stress-activated protein kinase p38 stabilizes a number of mRNAs encoding inflammatory mediators, such as cyclooxygenase 2 (Cox-2). In HeLa cells the anti-inflammatory glucocorticoid dexamethasone destabilizes Cox-2 mRNA by inhibiting p38 function. Here we demonstrate that this effect is phosphatase dependent. Furthermore, in HeLa cells dexamethasone induced the sustained expression of mitogen-activated protein kinase phosphatase 1 (MKP-1), a potent inhibitor of p38 function. The inhibition of p38 and the induction of MKP-1 by dexamethasone occurred with similar dose dependence and kinetics. No other known p38 phosphatases were induced by dexamethasone, and other cell types which failed to express MKP-1 also failed to inhibit p38 in response to dexamethasone. The proinflammatory cytokine interleukin 1 (IL-1) induced MKP-1 expression in a p38-dependent manner and acted synergistically with dexamethasone to induce MKP-1 expression. In HeLa cells treated with IL-1 or IL-1 and dexamethasone, the dynamics of p38 activation mirrored the expression of MKP-1. These observations suggest that MKP-1 participates in a negative-feedback loop which regulates p38 function and that dexamethasone may inhibit proinflammatory gene expression in part by inducing MKP-1 expression.
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Markevich, Nick I., Jan B. Hoek, and Boris N. Kholodenko. "Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades." Journal of Cell Biology 164, no. 3 (January 26, 2004): 353–59. http://dx.doi.org/10.1083/jcb.200308060.

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Mitogen-activated protein kinase (MAPK) cascades can operate as bistable switches residing in either of two different stable states. MAPK cascades are often embedded in positive feedback loops, which are considered to be a prerequisite for bistable behavior. Here we demonstrate that in the absence of any imposed feedback regulation, bistability and hysteresis can arise solely from a distributive kinetic mechanism of the two-site MAPK phosphorylation and dephosphorylation. Importantly, the reported kinetic properties of the kinase (MEK) and phosphatase (MKP3) of extracellular signal–regulated kinase (ERK) fulfill the essential requirements for generating a bistable switch at a single MAPK cascade level. Likewise, a cycle where multisite phosphorylations are performed by different kinases, but dephosphorylation reactions are catalyzed by the same phosphatase, can also exhibit bistability and hysteresis. Hence, bistability induced by multisite covalent modification may be a widespread mechanism of the control of protein activity.
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KIM, Sung-Jin, and Ronald C. KAHN. "Insulin regulation of mitogen-activated protein kinase kinase (MEK), mitogen-activated protein kinase and casein kinase in the cell nucleus: a possible role in the regulation of gene expression." Biochemical Journal 323, no. 3 (May 1, 1997): 621–27. http://dx.doi.org/10.1042/bj3230621.

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After insulin receptor activation, many cytoplasmic enzymes, including mitogen-activated protein (MAP) kinase, MAP kinase kinase (MEK) and casein kinase II (CKII) are activated, but exactly how insulin signalling progresses to the nucleus remains poorly understood. In Chinese hamster ovary cells overexpressing human insulin receptors [CHO(Hirc)], MEK, CKII and the MAP kinases ERK I and ERK II can be detected by immunoblotting in the nucleus, as well as in the cytoplasm, in the unstimulated state. Nuclear localization of MAP kinase is also observed in 3T3-F442A adipocytes, NIH-3T3 cells and Fao hepatoma cells, whereas MEK is found in the nucleus only in Fao and CHO cells. Insulin treatment for 5–30 min induces a translocation of MEK from the cytoplasm to the nucleus, whereas the MAP kinases and CKII are not translocated into the nucleus in response to insulin during this period. However, nuclear MAP kinase and CKII activities increase by 2–3-fold within 1–10 min after stimulation with insulin. By using gel-shift assays, it has been shown that insulin also stimulates nuclear protein binding to an AP-1 site with kinetics similar to MEK translocation and MAP kinase and CKII activation. Treatment of the extracts in vitro with protein phosphatase 2A or treatment of the intact cells with 5,6-dichloro-1-β-d-ribofuranosylbenzimidazole, a cell-permeable inhibitor of CKII, almost completely blocks the insulin-induced DNA-binding activity, whereas incubation of cells with a MEK inhibitor produces only a slight decrease. These results suggest that insulin signalling results in the activation of serine kinases in the nucleus via two pathways: (1) insulin stimulates the nuclear translocation of some kinases, such as MEK, which might directly phosphorylate nuclear protein substrates or activate other nuclear kinases, and (2) insulin activates nuclear kinases without translocation. The latter is true of CKII, which seems to regulate the binding of nuclear proteins to the AP-1 site, possibly by phosphorylation of AP-1 transcription factors.
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Dissertations / Theses on the topic "Protein kinase; Phosphatase; Kinetics"

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Lee, Chung-Sheng Brian. "Studies of SpoIIAA, the anti-anti-#sigma#'F factor of Bacillus subtilis." Thesis, University of Oxford, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365810.

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Andersson, C. Evalena. "Structure-Function Studies of Enzymes from Ribose Metabolism." Doctoral thesis, Uppsala University, Department of Cell and Molecular Biology, 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3999.

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In the pentose phosphate pathway, carbohydrates such as glucose and ribose are degraded with production of reductive power and energy. Another important function is to produce essential pentoses, such as ribose 5-phosphate, which later can be used in biosynthesis of nucleic acids and cofactors.

This thesis presents structural and functional studies on three enzymes involved in ribose metabolism in Escherichia coli.

Ribokinase is an enzyme that phosphorylates ribose in the presence of ATP and magnesium, as the first step of exogenous ribose metabolism. Two important aspects of ribokinase function, not previously known, have been elucidated. Ribokinase was shown to be activated by monovalent cations, specifically potassium. Structural analysis of the monovalent ion binding site indicates that the ion has a structural rather than catalytic role; a mode of activation involving a conformational change has been suggested. Product inhibition studies suggest that ATP is the first substrate to bind the enzyme. Independent Kd measurements with the ATP analogue AMP-PCP support this. The results presented here will have implications for several enzymes in the protein family to which ribokinase belongs, in particular the medically interesting enzyme adenosine kinase.

Ribose 5-phosphate isomerases convert ribose 5-phosphate into ribulose 5-phosphate or vice versa. Structural studies on the two genetically distinct isomerases in E. coli have shown them to be fundamentally different in many aspects, including active site architecture. However, a kinetic study has demonstrated both enzymes to be efficient in terms of catalysis. Sequence searches of completed genomes show ribose 5-phosphate isomerase B to be the sole isomerase in many bacteria, although ribose 5-phosphate isomerase A is a nearly universal enzyme. All genomes contain at least one of the two enzymes. These results confirm that both enzymes must be independently capable of supporting ribose metabolism, a fact that had not previously been established.

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Lee, Gui-in. "Structure and dynamics of the receptor kinase interacting FHA domain of kinase associated protein kinase from arabidopsis." Free to MU campus, others may purchase, 2003. http://wwwlib.umi.com/cr/mo/fullcit?p3100058.

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Ding, Zhaofeng. "Kinase-interacting FHA domain of kinase associated protein phosphatase phosphopeptide interactions and NMR-detected dynamics /." Diss., Columbia, Mo. : University of Missouri-Columbia, 2007. http://hdl.handle.net/10355/4729.

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Thesis (Ph. D.)--University of Missouri-Columbia, 2007.
The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from title screen of research.pdf file (viewed on September 24, 2007) Vita. Includes bibliographical references.
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Dehghani, Hesam. "Embryonic alkaline phosphatase and protein kinase C in preimplantation mouse development." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/NQ58304.pdf.

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Gruninger, Robert J., and University of Lethbridge Faculty of Arts and Science. "Structure and mechanism of protein tyrosine phosphatase-like phytases." Thesis, Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry, c2009, 2009. http://hdl.handle.net/10133/2473.

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The structure and mechanism of the Protein Tyrosine Phosphatase-like Phytases (PTPLPs) from Selenomonas ruminantium (PhyAsr) and Mitsuokella multacida (PhyAmm) were investigated using a combination of enzyme kinetics, site-directed mutagenesis, and X-ray crystallography. I show that PTPLPs use a classical protein tyrosine phosphatase catalytic mechanism and adopt a core PTP fold. Several unique structural features of PTPLPs confer specificity for inositol phosphates. The effect of ionic strength and oxidation on the kinetics and structure of PTPLPs was investigated. The structural consequences of reversible and irreversible oxidation on PTPLPs and PTPs are compared and discussed. We determine the structural basis of substrate specificity in PTPLPs and propose a novel reaction mechanism for the hydrolysis of inositol polyphosphates by PTPLPs. Finally, the structure and function of a unique tandemly repeated phytase has been determined. We show that the active sites of the tandem repeat possess significantly different specificities for inositol polyphosphate.
xix, 148 leaves : ill. (some col.) ; 29 cm
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Sloss, Callum. "Control of subcellular distribution of the MAP kinase phosphatase, MKP-2." Thesis, University of Strathclyde, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.288715.

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Lam, Hiu-chor, and 林曉初. "Functional characterization of tyrosine phosphatase non-receptor 21, anovel modulator of ErbB4/NRG3." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2010. http://hub.hku.hk/bib/B44229288.

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Davies, Elizabeth Louise. "The role of mitogen-activated protein kinase phosphatase-1 in cardiac hypertrophy." Thesis, Imperial College London, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.391714.

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Kodituwakku, Jayanie Subhashi. "Mechanisms regulating mitogen-activated protein kinase phosphatase-2 expression in cardiac myocytes." Thesis, Imperial College London, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.429111.

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Books on the topic "Protein kinase; Phosphatase; Kinetics"

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NATO Advanced Study Institute on Cellular Regulation by Protein Phosphorylation (1990 La Londe les Maures, France). Cellular regulation by protein phosphorylation. Berlin: Springer-Verlag, 1991.

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G, Hardie D., ed. Protein phosphorylation: A practical approach. 2nd ed. London: Oxford University Press, 1999.

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Hardie, D. G. Protein Phosphorylation: A Practical Approach (Practical Approach Series). Oxford University Press, USA, 1999.

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Hardie, D. G. Protein Phosphorylation: A Practical Approach (Practical Approach Series). Oxford University Press, USA, 1999.

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Book chapters on the topic "Protein kinase; Phosphatase; Kinetics"

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Collas, Philippe, Thomas Küntziger, and Helga B. Landsverk. "Anchoring of protein kinase and phosphatase signaling units." In Protein Phosphatases, 145–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-540-40035-6_8.

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Lawan, Ahmed, and Anton M. Bennett. "Mitogen-Activated Protein Kinase Phosphatases in Metabolism." In Protein Tyrosine Phosphatase Control of Metabolism, 221–38. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-7855-3_12.

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Marks, Friedrich, Ursula Klingmüller, and Karin Müller-Decker. "Signal Transduction by Tyrosine Kinase- and Protein Phosphatase-Coupled Receptors." In Cellular Signal Processing, 249–90. Second edition. | New York, NY: Garland Science, 2017.: Garland Science, 2017. http://dx.doi.org/10.4324/9781315165479-7.

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Lebrin, Franck, Laurence Bianchini, Thierry Rabilloud, Edmond M. Chambaz, and Yves Goldberg. "CK2α — protein phosphatase 2A molecular complex: Possible interaction with the MAP kinase pathway." In A Molecular and Cellular View of Protein Kinase CK2, 207–12. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4419-8624-5_25.

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Ward, Walter H. J. "Chapter 4. The Mechanisms and Kinetics of Protein Kinase Inhibitors." In Drug Discovery, 96–125. Cambridge: Royal Society of Chemistry, 2011. http://dx.doi.org/10.1039/9781849733557-00096.

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Haccard, Olivier, and Catherine Jessus. "Greatwall Kinase, ARPP-19 and Protein Phosphatase 2A: Shifting the Mitosis Paradigm." In Results and Problems in Cell Differentiation, 219–34. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-19065-0_11.

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Hardesty, B., W. Kudlicki, S. Ch Chen, S. Fullilove, and G. Kramer. "Involvement of the Membrane Skeleton in the Regulation of the cAMP-Independent Protein Kinase and a Protein Phosphatase that Control Protein Synthesis." In Haematology and Blood Transfusion / Hämatologie und Bluttransfusion, 268–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-72624-8_57.

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Lima, Lucimey, and Suzana Cubillos. "Taurine-Stimulated Outgrowth from the Retina is Impaired by Protein Kinase C Activators and Phosphatase Inhibitors." In Advances in Experimental Medicine and Biology, 423–30. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-0117-0_52.

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Schroeder, Julian I., Martin Schwarz, and Zhen-Ming Pei. "Protein Kinase and Phosphatase Regulation During Abscisic Acid Signaling and Ion Channel Regulation in Guard Cells." In Cellular Integration of Signalling Pathways in Plant Development, 59–69. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-72117-5_6.

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Moore, Michael L., and Gregory A. Grant. "Peptide Design Considerations." In Synthetic Peptides. Oxford University Press, 2002. http://dx.doi.org/10.1093/oso/9780195132618.003.0005.

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Peptides have become an increasingly important class of molecules in biochemistry, medicinal chemistry, and physiology. Many naturally occurring, physiologically relevant peptides function as hormones, neurotransmitters, cytokines, and growth factors. Peptide analogs that possess agonist or antagonist activity are useful as tools to study the biochemistry, physiology, and pharmacology of these peptides, to characterize their receptor(s), and to study their biosynthesis, metabolism, and degradation. Radiolabeled analogs and analogs bearing affinity labels have been used for receptor characterization and isolation. Peptide substrates of proteases, kinases, phosphatases, and aminoacyl or glycosyl transferases are used to study enzyme kinetics, mechanism of action, and biochemical and physiological roles and to aid in the isolation of enzymes and in the design of inhibitors. Peptides are also used as synthetic antigens for the preparation of polyclonal or monoclonal antibodies targeted to specific sequences. Epitope mapping with synthetic peptides can be used to identify specific antigenic peptides for the preparation of synthetic vaccines, to determine protein sequence regions that are important for biological action, and to design small peptide mimetics of protein structure or function. A number of peptide hormones or analogs thereof, including arginine vasopressin, oxytocin, luteinizing hormone releasing hormone (LHRH), adrenocorticotropic hormone (ACTH), and calcitonin, have already found use as therapeutic agents, and many more are being investigated actively. Peptide-based inhibitors of proteolytic enzymes, such as angiotensin converting enzyme (ACE) and human immunodeficiency virus (HIV) protease, have widespread clinical use, and inhibitors of renin and elastase are also being investigated for therapeutic use. Finally, peptides designed to block the interaction of protein molecules by mimicking the combining site of one of the proteins, such as the fibrinogen receptor antagonists, show great therapeutic potential as well. With the development of solid-phase peptide synthesis by Bruce Merrifield (1963) and the optimization of supports, protecting groups, and coupling and deprotection chemistries by a large number of researchers, it has become possible to obtain useful amounts of peptides on a more or less routine basis.
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Conference papers on the topic "Protein kinase; Phosphatase; Kinetics"

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Ming Wu and Douglas A. Lawrence. "Monotonicity and bistability of calcium/calmodulin-dependent protein kinase-phosphatase activation." In 2010 American Control Conference (ACC 2010). IEEE, 2010. http://dx.doi.org/10.1109/acc.2010.5531229.

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Liu, Jianyu, Payton Stevens, and Tianyan Gao. "Abstract 3837: Protein Phosphatase PHLPP regulates protein translation and cell size through directly dephosphorylating p70 S6 kinase." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3837.

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Allen-Petersen, Brittany L., Amy S. Farrell, Zina P. Jenny, Colin J. Daniel, Zhiping Wang, Charles D. Lopez, Dale J. Christensen, Goutham Narla, Brett C. Sheppard, and Rosalie C. Sears. "Abstract B21: Protein phosphatase 2A (PP2A) activation functions synergistically with kinase inhibition in pancreatic cancer." In Abstracts: AACR Special Conference on Myc: From Biology to Therapy; January 7-10, 2015; La Jolla, CA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1557-3125.myc15-b21.

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Ammit, AJ, M. Manetsch, EE Ramsay, and Q. Ge. "Uncovering the Molecular Mechanisms Underlying Mitogen-Activated Protein Kinase Phosphatase 1 Upregulation by Corticosteroids/β2-Agonists." 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.a3909.

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Schaefer, Erik M., Susan Cornell-Kennon, and Bill Lu. "Abstract 1769: CSox-based sensors for continuous, homogeneous and quantitative monitoring of protein kinase and phosphatase activity." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-1769.

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Haagenson, Kelly K., Dongjun Peng, and Gen Sheng Wu. "Abstract 360: Tamoxifen treatment induces mitogen-activated protein kinase phosphatase-1 expression in T47D breast cancer cells." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-360.

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Schaefer, Erik M., Susan Cornell-Kennon, and Bill Lu. "Abstract 1769: CSox-based sensors for continuous, homogeneous and quantitative monitoring of protein kinase and phosphatase activity." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-1769.

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Kodack, David P., Joseph LaConti, Masaharu Noda, and Anton Wellstein. "Abstract 4018: Crosstalk between the pleiotrophin-anaplastic lymphoma kinase axis and the protein tyrosine phosphatase ζ signaling pathways." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4018.

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Qu, Zhe. "Effect of Enamel Matrix Derivative on Alkaline Phosphatase Activity in Osteoblast Cells through the Mitogen-activated Protein Kinase Pathway." In 2014 International Conference on Mechatronics, Electronic, Industrial and Control Engineering. Paris, France: Atlantis Press, 2014. http://dx.doi.org/10.2991/meic-14.2014.317.

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Newton, Robert, Elizabeth M. King, Wei Gong, Christopher F. Rider, and Neil S. Holden. "Induction Of Mitogen-Activated Protein Kinase Phosphatase (MKP) 1 By Glucocorticoids Inhibits Extracellular-Regulated Kinases (ERKs) To Suppress GM-CSF Synthesis." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4948.

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You might also be interested in the extended bibliographies on the topic 'Protein kinase; Phosphatase; Kinetics' for particular source types:
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