Relevant bibliographies by topics / Proteins Cellular signal transduction

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

Academic literature on the topic 'Proteins Cellular signal transduction'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Proteins Cellular signal transduction"

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Watt, F. M., and R. Sever. "Signal transduction." Journal of Cell Science 114, no. 7 (April 1, 2001): 1247–48. http://dx.doi.org/10.1242/jcs.114.7.1247.

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We are pleased to announce the appointment of John Heath as an Editor of Journal of Cell Science. John has a background in developmental biology and has for many years been a leading figure in the field of growth factor and cytokine signalling. Our desire to appoint a new Editor is in part due to the continuing increase in the number of submissions? a consequence of our rising impact factor and author-friendly policies? and in part to our need for another expert in the field of signal transduction among the Editors. On behalf of all the Editors, we would like to welcome John to JCS; we look forward to working with him. The appointment of John Heath coincides with the start of a series of Commentaries focusing on Signal Transduction and Cellular Organization, which will be a feature of JCS throughout 2001. This series is intended to reflect our increasing understanding of the organization of signalling networks, which are no longer viewed merely as linear pathways but instead as complex webs in which scaffold-organized multiprotein complexes and subcellular localization of signalling molecules play key roles. Morgan Sheng's summary of the scaffold functions of PSD-95 in the post-synaptic density (see Cell Science at a Glance) underlines this complexity: PSD-95 is part of an extensive network of proteins that links together different classes of glutamate receptor and couples them to intracellular signalling pathways. In the first Commentary of this series (p. 1253), Bruce Mayer examines the roles of SH3 domains in signalling and discusses the overall logic governing signalling networks. On p. 1265, Graeme Milligan develops the theme by reviewing the evidence for regulation of G-protein-coupled receptor signalling through receptor oligomerization. Future articles in the series examine the importance of subcellular localization of signalling molecules such as Ca(2+), inositol phosphates and Ras, scaffold proteins such as STE5, KSR and AKAPs, and proteins such as p300/CBP and WASP that play central roles integrating signalling to produce biological output (see over). Finally, we would like to emphasize our interest in primary articles relating to this topic and take this opportunity to encourage all those working in the field of signal transduction to submit their best articles to the journal.?
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Ortegón Salas, Clara, Katharina Schneider, Christopher Horst Lillig, and Manuela Gellert. "Signal-regulated oxidation of proteins via MICAL." Biochemical Society Transactions 48, no. 2 (March 27, 2020): 613–20. http://dx.doi.org/10.1042/bst20190866.

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Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificity, redox signalling requires catalysis, just like phosphorylation signalling requires kinases and phosphatases. While reducing enzymes of both cysteinyl- and methionyl-derivates have been characterised in great detail before, the discovery and characterisation of MICAL proteins evinced the first examples of specific oxidases in signal transduction. This article provides an overview of the functions of MICAL proteins in the redox regulation of cellular functions.
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Bonventre, J. V. "Phospholipase A2 and signal transduction." Journal of the American Society of Nephrology 3, no. 2 (August 1992): 128–50. http://dx.doi.org/10.1681/asn.v32128.

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Phospholipases A2 (PLA2) comprise a family of enzymes that hydrolyze the acyl bond at the sn-2 position of phospholipids to generate free fatty acids and lysophospholipids. Different forms of PLA2 are involved in digestion, inflammation, and intercellular and intracellular signal transduction. The sn-2 position of phospholipids in mammalian cells is enriched in arachidonic acid, the precursor of eicosanoids, which have diverse physiologic and pathophysiologic effects on the kidney and other organs. Thus, the regulation of PLA2 activity has important implications for kidney function. PLA2 regulation involves: calcium, pH, protein kinases, GTP-binding proteins, inhibitory and activating proteins, metabolic product inhibition, and transcriptional control. The various roles of arachidonic acid and cyclooxygenase, lipoxygenase, and cytochrome P450 mono-oxygenase products of arachidonic acid metabolism, as intracellular messengers, in the regulation of membrane channel activities, intracellular enzyme activities, cellular calcium homeostasis, mitogenesis, differentiation, cytokine and early response gene expression are discussed.
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Finley, Rebecca S. "New Directions in the Treatment of Cancer: Inhibition of Signal Transduction." Journal of Pharmacy Practice 15, no. 1 (February 2002): 5–16. http://dx.doi.org/10.1106/cj0v-jb04-vbd4-v65d.

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In recent years, it has become increasingly apparent that proteins regulated by activated oncogenes or mutated tumor suppressor genes are responsible for the transformation of normal cells to malignant cells as well as for malignant characteristics such as uncontrolled cellular proliferation and the development of metastases. These proteins may be soluble factors, receptors on cell surfaces, or intracellular enzymes that produce signals that stimulate cellular development or proliferation. This process is called signal transduction .In many cases, increased amounts of these proteins have been demonstrated in cancer cells (over normal cells) and have been found to carry prognostic significance. New approaches in cancer treatment are being designed to block such proteins; this approach is termed signal transduction inhibition. !Specific protein targets that anticancer therapies have been developed to inhibit include epidermal growth factor receptors, tyrosine kinase, farnesyl transferase, and various promoters of angiogenesis.
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Hou, Shangwei, Mark F. Reynolds, Frank T. Horrigan, Stefan H. Heinemann, and Toshinori Hoshi. "Reversible Binding of Heme to Proteins in Cellular Signal Transduction." Accounts of Chemical Research 39, no. 12 (December 2006): 918–24. http://dx.doi.org/10.1021/ar040020w.

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Stacey, D. W., M. H. Tsai, C. L. Yu, and J. K. Smith. "Critical Role of Cellular ras Proteins in Proliferative Signal Transduction." Cold Spring Harbor Symposia on Quantitative Biology 53 (January 1, 1988): 871–81. http://dx.doi.org/10.1101/sqb.1988.053.01.100.

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Slemmon, J. Randall, Bingbing Feng, and Joseph A. Erhardt. "Small Proteins that Modulate Calmodulin-Dependent Signal Transduction." Molecular Neurobiology 22, no. 1-3 (2000): 099–114. http://dx.doi.org/10.1385/mn:22:1-3:099.

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Lee, Bok-Soo, Sun-Hwa Lee, Pinghui Feng, Heesoon Chang, Nam-Hyuk Cho, and Jae U. Jung. "Characterization of the Kaposi's Sarcoma-Associated Herpesvirus K1 Signalosome." Journal of Virology 79, no. 19 (October 1, 2005): 12173–84. http://dx.doi.org/10.1128/jvi.79.19.12173-12184.2005.

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ABSTRACT Kaposi's sarcoma (KS) is a multifocal angiogenic tumor and appears to be a hyperplastic disorder caused, in part, by local production of inflammatory cytokines. The K1 lymphocyte receptor-like protein of KS-associated herpesvirus (KSHV) efficiently transduces extracellular signals to elicit cellular activation events through its cytoplasmic immunoreceptor tyrosine-based activation motif (ITAM). To further delineate K1-mediated signal transduction, we purified K1 signaling complexes and identified its cellular components. Upon stimulation, the K1 ITAM was efficiently tyrosine phosphorylated and subsequently interacted with cellular Src homology 2 (SH2)-containing signaling proteins Lyn, Syk, p85, PLCγ2, RasGAP, Vav, SH2 domain-containing protein tyrosine phosphatase 1/2, and Grab2 through its phosphorylated tyrosine residues. Mutational analysis demonstrated that each tyrosine residue of K1 ITAM contributed to the interactions with cellular signaling proteins in distinctive ways. Consequently, these interactions led to the marked augmentation of cellular signal transduction activity, evidenced by the increase of cellular tyrosine phosphorylation and intracellular calcium mobilization, the activation of NF-AT and AP-1 transcription factor activities, and the production of inflammatory cytokines. These results demonstrate that KSHV K1 effectively recruits a set of cellular SH2-containing signaling molecules to form the K1 signalosome, which elicits downstream signal transduction and induces inflammatory cytokine production.
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Periyasamy, C. Periyasamy. "Analysis of Regulated Kinase Signal Network through Feedback Loops in Extra-Cellular Signal." Indonesian Journal of Electrical Engineering and Computer Science 8, no. 2 (November 1, 2017): 549. http://dx.doi.org/10.11591/ijeecs.v8.i2.pp549-551.

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<p>Signal network assumes a vital part in directing the principal cell capacities, for example, cell expansion, survival, separation and motility. Improvement and investigation of scientific model can help us gain a profound comprehension of the unpredictable conduct of ERK flag transduction organizes. This paper exhibits a computational model that offers an incorporated quantitative and dynamic reproduction of ERK flag transduction arranges, actuated by epidermal development figure. The mathematic demonstrate contains the enactment energy of the pathway, a huge number of input circles and association of platform proteins. The model gives knowledge into flag reaction connections between the authoritative of EGF to its receptor at the phone surface and actuation of downstream proteins in the flagging course. The diverse impact of positive and negative input circles of the ERK flag transduction pathway were for the most part examined, showing that criticism circles were the primary affecting variable to the swaying of ERK flag transduction pathway. The forecasts of this wavering of ERK enactment concur well with the writing. It can prompt flag floods of the downstream substrates and instigate relating natural practices.</p>
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Kramer, Markus M., Levin Lataster, Wilfried Weber, and Gerald Radziwill. "Optogenetic Approaches for the Spatiotemporal Control of Signal Transduction Pathways." International Journal of Molecular Sciences 22, no. 10 (May 18, 2021): 5300. http://dx.doi.org/10.3390/ijms22105300.

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Biological signals are sensed by their respective receptors and are transduced and processed by a sophisticated intracellular signaling network leading to a signal-specific cellular response. Thereby, the response to the signal depends on the strength, the frequency, and the duration of the stimulus as well as on the subcellular signal progression. Optogenetic tools are based on genetically encoded light-sensing proteins facilitating the precise spatiotemporal control of signal transduction pathways and cell fate decisions in the absence of natural ligands. In this review, we provide an overview of optogenetic approaches connecting light-regulated protein-protein interaction or caging/uncaging events with steering the function of signaling proteins. We briefly discuss the most common optogenetic switches and their mode of action. The main part deals with the engineering and application of optogenetic tools for the control of transmembrane receptors including receptor tyrosine kinases, the T cell receptor and integrins, and their effector proteins. We also address the hallmarks of optogenetics, the spatial and temporal control of signaling events.
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Dissertations / Theses on the topic "Proteins Cellular signal transduction"

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Brownlie, Zoe. "Regulation of signal transduction by RGS4." Connect to e-thesis, 2007. http://theses.gla.ac.uk/124/.

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Thesis (Ph.D.) - University of Glasgow, 2007.
Ph.D. thesis submitted to the Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, 2007. Includes bibliographical references.
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Rogers, Laura Ann. "Membranes as a hub for cellular signaling /." Access full-text from WCMC, 2007. http://proquest.umi.com/pqdweb?did=1481668281&sid=2&Fmt=2&clientId=8424&RQT=309&VName=PQD.

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Pat, Betty Kila. "Signal transduction pathways in renal fibrosis /." St. Lucia, Qld, 2003. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe17739.pdf.

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Lo, Kin Ho. "Activation of signal transducer and activator of transcription 3 (STAT3) by G[alpha]16 and G[alpha]14 via a c-Src/JAK-and ERK-dependent mechanism /." View abstract or full-text, 2004. http://library.ust.hk/cgi/db/thesis.pl?BICH%202004%20LO.

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Thesis (M. Phil.)--Hong Kong University of Science and Technology, 2004.
Includes bibliographical references (leaves 92-111). Also available in electronic version. Access restricted to campus users.
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Liu, Wei. "Role of axin in TGF-[beta] signaling pathway and characterization of axin mutant proteins in axinF̳u̳ mice /." View abstract or full-text, 2006. http://library.ust.hk/cgi/db/thesis.pl?BICH%202006%20LIUW.

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Ma, Chun-Wai. "Aboav-Weaire law in complex network and its applications in bioinformatics /." View abstract or full-text, 2005. http://library.ust.hk/cgi/db/thesis.pl?PHYS%202005%20MA.

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Chen, Yujie, and 陈宇杰. "Structural and functional studies of human APPL1-APPL2 BAR-PH heterodimer, APPL2 BAR-PH homodimer, and lanthionine synthetase component C-like protein 2." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2012. http://hdl.handle.net/10722/197138.

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APPL BAR-PH heterodimer and APPL2 BAR-PH homodimer The APPL (Adaptor protein containing PH domain, PTB domain and Leucine zipper) family are adaptor proteins with only two isoforms, APPL1 and APPL2. They bind to early endosomes with a small GTPase, Rab5, and mediate the interactions between various receptors and downstream signaling components, thus functioning in many signaling pathways evoked by adiponectin, insulin, FSH, EGF, and so on. However, evidences have shown APPL1 and APPL2 should perform some opposite functions, which cannot be simply explained by the functional differences attributed to their PTB domains. We hypothesize that the heterodimerization of APPL1 and APPL2’s BAR domains may account for their opposing functions. The crystal structure of APPL BAR-PH heterodimer was solved to resolution 2.8 Å. Its overall structure exhibits crescent shape with a larger curvature radius of 76 Å, compared to 55 Å of the APPL1 BAR-PH homodimer. And the crystal structure APPL2 BAR-PH homodimer was solve to resolution 3.3 Å. The overall structure of APPL2 BAR-PH homodimer is very similar to that of APPL BAR-PH heterodimer, but shows greater difference in curvature to the APPL1 BAR-PH homodimer structure. The concave side of APPL BAR-PH heterodimer and APPL2 BAR-PH homodimer all possess less positive charge than the APPL1 BAR-PH homodimer. Structural analysis reveals that leucine patches at the dimer interface may account for the formation of dimeric curve with certain curvature. Consequently, APPL2 BAR is able to enforce the curvature reduction to APPL1 BAR upon heterodimerization. In conclusion, the alterations of curvature and electrostasis are responsible for the modulation of endosome binding specificity and can elucidate the opposite roles of APPL1 and APPL2. LanCL2 LanCL2 is a member of Lanthionine synthetase component C-like family. In human, LanCL2 binds to lanthionine derivatives and glutathione, participating in keeping intracellular reducing state. By binding to absiscic acid (ABA), LanCL2 is indispensible for the ABA-stimulated adipogenesis, insulin release, glucose homeostasis, and inflammatory response. It is also implicated in anticancer drug resistance. All these functions underscore the importance of LanCL2 in the diseases like diabetes, inflammation, and cancer. The crystal structure of LanCL2 was solved to resolution 1.8 Å. The overall structure displays canonical double-layer α-barrel. The major differences from LanCL1 lay in the loops on the barrel top, which are implicated in various substrate bindings. A zinc-coordinating pocket was found among the loops, with conserved amino acid residues of distinct conformation. The electrostatic surface shows remarkable differences compared to that of LanCL1, suggesting that it may contribute to distinct substrate binding profile. Future implications APPL proteins and LanCL proteins are all involved in the regulation of metabolism, such as glucose uptake, fatty acid oxidation, and insulin secretion, and play roles in diseases like obesity and type 2 diabete. Structural and functional studies of these proteins can provide insights into the molecular mechanisms and clues for related therapeutic approaches.
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Physiology
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Doctor of Philosophy
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Lupi, Rosita. "Characterization of post translational modification of heterotrimeric G proteins." Thesis, Open University, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.343748.

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Philips, Brian John. "Protein interactions with the catechol estrogens 4-hydroxyestrone and 4-hydroxyestradiol in mouse tissue lysate : binding and metabolism studies /." free to MU campus, to others for purchase, 2001. http://wwwlib.umi.com/cr/mo/fullcit?p3036851.

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Alexander, Roger Parker. "Evolutionary Genomics of Methyl-accepting Chemotaxis Proteins." Diss., Georgia Institute of Technology, 2007. http://hdl.handle.net/1853/19860.

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The general goal of this project was to use computational biology to understand signal transduction mechanisms in prokaryotes. Its specific focus was to characterize the cytoplasmic domain of methyl-accepting chemotaxis proteins (MCP_CD), a protein domain central to the function of chemotaxis, the most complex signaling network in prokaryotes. Chemotaxis enables cells to sense and respond to multiple external and internal stimuli by actively navigating to an optimal environment. MCP_CD is a central part of this circuit, but its coiled coil structure is difficult to analyze using traditional tools of computational biology. In this project, a new method for analysis of the domain was developed and used to gain insight into its function and evolution. Research advance 1: Characterization of the MCP_CD protein domain. Before this work, MCP_CD was known to have two distinct functional regions: the signaling region that activates the histidine kinase CheA and the methylation region where adaptation enzymes CheB and CheR store information about recent stimuli. The result of this project is classification of ~2000 MCP_CDs into twelve subfamilies. The unique mechanism of evolution of the domain has been clarified and precise boundaries of the adaptation and signaling regions determined. A new functional region, the flexible bundle subdomain, was identified and its contribution to the signaling mechanism elucidated by analysis of conserved sequence features. Conserved and variable sequence features in the adaptation and signaling subdomains led to a better understanding of the evolutionary history of the adaptation mechanism and of alternative higher-order arrangements of receptors within the membrane. Research advance 2: Development of a sensor / kinase correlation algorithm to couple diverse MCP_CD and kinase subfamilies. The receptor diversity discovered in this work is complemented by diversity in the kinases with which they interact. In this work, an algorithm was developed to associate receptor / kinase pairs which facilitated understanding of the function and evolution of chemotaxis. Research advance 3: Development of Cheops, a database of chemotaxis pathways. The Cheops (Chemotaxis operons) database presents the results of the sensor / kinase correlation algorithm and the information about receptor and kinase diversity in an integrated and intuitive way.
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Books on the topic "Proteins Cellular signal transduction"

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Graeme, Milligan, Wakelam M. J. O, and Kay J, eds. G-proteins and signal transduction. London: Biochemical Society, 1990.

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Karin, Müller-Decker, and Klingmüller Ursula, eds. Cellular signal processing. New York, NY: Garland Science, 2009.

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Signal transduction protocols. 3rd ed. New York: Humana Press, 2011.

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NATO/FEBS Summer School on Signal Transduction and Protein Phosphorylation (1986 Korgialenics School). Signal transduction and protein phosphorylation. New York: Plenum Press, 1987.

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Smith, B. G protein signaling: Methods and protocols. [Place of publication not identified]: Humana, 2010.

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NATO, Advanced Research Institute on Biological Signal Transduction (1990 Island of Spetsai Greece). Biological signal transduction. Berlin: Springer-Verlag, 1991.

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Yalovsky, Shaul. Integrated G Proteins Signaling in Plants. Berlin, Heidelberg: Springer-Verlag Berlin Heidelberg, 2010.

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Kelly, James Anthony. Aspects of signal transduction in bovine lymphatic smooth muscle cells. Dublin: University College Dublin, 1996.

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Watling, Keith J. The Sigma-RBI handbook of receptor classification and signal transduction. 4th ed. Natick, MA: Sigma-RBI, 2001.

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Karelin, A. A. Signalʹnyĭ ATF: Ėnergetika peredachi signala k rostu kletok plazmaticheskimi membranami. Moskva: Nauch.-izdatelʹskiĭ t︠s︡entr "Inzhener", 2000.

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Book chapters on the topic "Proteins Cellular signal transduction"

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Gudi, S. R. P., and J. A. Frangos. "Mechanical Signal Transduction and G proteins." In Cell Mechanics and Cellular Engineering, 294–307. New York, NY: Springer New York, 1994. http://dx.doi.org/10.1007/978-1-4613-8425-0_17.

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Gautam, N. "Defects in Signal Transduction Proteins Leading to Disease." In Introduction to Cellular Signal Transduction, 267–85. Boston, MA: Birkhäuser Boston, 1999. http://dx.doi.org/10.1007/978-1-4612-1990-3_11.

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Wensel, Theodore. "Heterotrimeric G-proteins: Structure, Regulation, and Signaling Mechanisms." In Introduction to Cellular Signal Transduction, 29–46. Boston, MA: Birkhäuser Boston, 1999. http://dx.doi.org/10.1007/978-1-4612-1990-3_3.

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Marks, Friedrich, Ursula Klingmüller, and Karin Müller-Decker. "Signal Transduction by Small G-Proteins: The Art of Molecular Targeting." In Cellular Signal Processing, 359–93. Second edition. | New York, NY: Garland Science, 2017.: Garland Science, 2017. http://dx.doi.org/10.4324/9781315165479-10.

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Prabhakar, Uma, and Ponnal Nambi. "Ras- and Rho-Related Small Molecular Weight G-proteins: Structure and Signaling Mechanisms." In Introduction to Cellular Signal Transduction, 47–64. Boston, MA: Birkhäuser Boston, 1999. http://dx.doi.org/10.1007/978-1-4612-1990-3_4.

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Chiosi, E., A. Spina, F. Valente, and G. Illiano. "Protein Kinase C and G Proteins." In Adenine Nucleotides in Cellular Energy Transfer and Signal Transduction, 257–68. Basel: Birkhäuser Basel, 1992. http://dx.doi.org/10.1007/978-3-0348-7315-4_23.

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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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Kennelly, Peter J. "Bits for an Organic Microprocessor: Protein Phosphorylation/Dephosphorylation." In Introduction to Cellular Signal Transduction, 235–63. Boston, MA: Birkhäuser Boston, 1999. http://dx.doi.org/10.1007/978-1-4612-1990-3_10.

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Putney, James W., Arlene R. Hughes, Debra A. Horstman, and Haruo Takemura. "Inositol Phosphate Metabolism and Cellular Signal Transduction." In Calcium Protein Signaling, 37–48. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5679-0_5.

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Sotiroudis, T. G., V. G. Zevgolis, and A. E. Evangelopoulos. "Control of Cellular Activity by Protein Phosphorylation-Dephosphorylation: Phosphorylase Kinase from Bovine Stomach Smooth Muscle." In Biological Signal Transduction, 309–20. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75136-3_22.

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Conference papers on the topic "Proteins Cellular signal transduction"

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Mednieks, M. I. "Secretory proteins characteristic of environmental changes in cellular signal transduction: Expression in oral fluid." In HADRONS AND NUCLEI: First International Symposium. AIP, 2000. http://dx.doi.org/10.1063/1.1302484.

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Kaazempur-Mofrad, Mohammad R., Peter J. Mack, Helene Karcher, Javad Golji, and Roger G. Kamm. "Stress-Induced Mechanotransduction: Some Preliminaries." In ASME 2003 International Mechanical Engineering Congress and Exposition. ASMEDC, 2003. http://dx.doi.org/10.1115/imece2003-43215.

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Mechanical stimuli affect nearly every aspect of cellular function, yet the underlying mechanisms of transduction of force into biochemical signals are not clearly understood. One hypothesis is that forces transmitted via individual proteins, either at the site of cell adhesion to its surroundings or within the stress-bearing members of the cytoskeleton, cause conformational changes that change their binding affinity to other intracellular molecules. This altered equilibrium state can subsequently initiate biochemical signaling cascades of produce immediate structural changes. This paper addresses the distribution of forces within the cell resulting from specific mechanical stimuli, computed using a 3-D multi compartment, continuum, viscoelastic finite element model, and uses these to estimate the forces transmitted by individual proteins and protein complexes. These levels of force are compared to those known to produce conformational changes in cytoskeletal proteins, as speculated from magnetocytometry observations and computed by molecular dynamics.
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El-Kurdi, Mohammed S., J. Scott Van Epps, Robert J. Toth, Douglas W. Hamilton, Chuanyue Wu, Jeffrey S. Vipperman, and David A. Vorp. "Regulation of Cell Adhesion and De-Adhesion Proteins in Veins Perfused Under Arterial Conditions Ex-Vivo." In ASME 2004 International Mechanical Engineering Congress and Exposition. ASMEDC, 2004. http://dx.doi.org/10.1115/imece2004-61531.

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Failure of veins employed as arterial bypass grafts via intimal hyperplasia (IH) often occurs within 5 years after implantation, requiring re-operation in 60% of all cases1. IH is characterized by de-adhesion, followed by migration of medial and adventitial smooth muscle cells (SMCs) and myofibroblasts into the intima, where they demonstrate uncontrolled proliferation. It is thought that this process may be induced by the abrupt exposure of the veins to the dynamic mechanical environment of the arterial circulation2. Veins are much thinner walled and more distensible than arteries. Therefore, the SMCs within the vein wall are exposed to significantly higher levels of stress and strain than they are accustomed2. The tissue responds to this perceived injury by thickening, which is thought to be an attempt to return the stress and strain to venous levels. However, when this response is uncontrolled it can over-compensate, leading to stenosis instead of the desired thickening or “arterialization” of the vein segment. Cellular de-adhesion, which refers to a change from a state of stronger adherence to a state of weaker adherence, is involved in the earliest response and therefore was the focus of this study. While there are many important proteins involved in the regulation of cellular adhesion, we focus our attention here to matricellular proteins, which function as adaptors and modulators of cell-matrix interactions3,4, and intracellular adhesion proteins, which have been shown to localize to cellular focal adhesion sites5,6. Tenascin-C (TN-C), thrombospondin-1,2 (TSP), and secreted protein acidic and rich in cysteine (SPARC) are matricellular proteins that exhibit highly regulated expression during development and cellular injury7. Mitogen inducible gene 2 (Mig-2) and integrin linked kinase (ILK) are intracellular proteins involved in cellular shape modulation5 and integrin-mediated signal transduction8, respectively. It is well known that many intracellular and extracellular matrix proteins are regulated by mechanical stress9,10. The purpose of this work was to explore the hypothesis that intact vein segments exposed to arterial hemodynamics will alter their expression of TN-C, TSP, SPARC, Mig-2 and ILK within 24 hours. This may induce a modulation of the level of cell adhesion, which could contribute to IH.
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Kim, Phillip, Jeeyun Lee, Xinjun Liu, Joon Oh Park, Tani Lee, Won Ki Kang, Limin Liu, et al. "Abstract 4019: Functional profiling of signal transduction pathway proteins in gastric cancer patients." 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.am10-4019.

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Lamontagne, Stephanie, Anne-Marie Fortier, Sophie Parent, Eric Asselin, and Monique Cadrin. "Abstract 1958: Interaction between keratin intermediate filament proteins K8/18 and cancer related signal transduction proteins in epithelial cells." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1958.

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Liu, Yuan-Wei, and Chun-Liang Lin. "Idea of Control Design for Cellular Signal Transduction Pathway of Ras." In International Conference on Computational Intelligence and Multimedia Applications (ICCIMA 2007). IEEE, 2007. http://dx.doi.org/10.1109/iccima.2007.267.

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Tong Wang, Jianxin Xue, Wenan Tan, and Bicheng Ye. "Learning and identifying the crucial proteins in signal transduction networks by a novel method." In 2014 9th International Conference on Computer Science & Education (ICCSE). IEEE, 2014. http://dx.doi.org/10.1109/iccse.2014.6926423.

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Lee, Tani, Jeeyun Lee, Katya Magonova, Won Ki Kang, Gulia Harvie, Robert Barham, Glen Leesman, Phillip Kim, Sharat Singh, and Sung Kim. "Abstract 1948: Functional profiling of signal transduction pathway proteins in gastric cancer (GC) patients." 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.am2011-1948.

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Uzgare, Rajneesh, Thomas Hundley, Dhanrajan Tiruchinapalli, Anna Solomon, Cheryl Horton, and Hao Chen. "Abstract 236: Characterizing cellular signal transduction cross-talk using in-cell kinase screen." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-236.

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Lapetina, Eduardo G. "THE ROLE OF INOSITIDES, PHOSPHOLIPASE C AND G-PROTEINS IN RECEPTOR TRANSDUCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644775.

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Abstract:
It is now widely recognized that the activation of phospholipase C by specific agonists leads to the formation of two second messengers: (1) inositol trisphosphate, which releases Ca2+ from the endoplasmic reticulum to the cytosol and (2) 1,2- diacylglycerol, which stimulates protein kinase C. In the past few years, GTP-binding proteins have been associated with the regulation of phospholipase C. However, the identity of the GTP-binding protein involved and the type of association with phospholipase C is not yet known. It is now recognized that there are two types of phospholipase C enzymes: (a) a soluble enzyme that has been characterized in several tissues and does not preferentially hydrolyze polyphospholinositides and (b) membrane-bound enzymes that are coupled to the receptors, specifically hydrolyzing polyphosphoinositides and activated by membrane guanine nucleotide-binding proteins. Recent reports have tried to assess the involvement of GTP-binding proteins in the agonist-induced stimulation of phospholipase C, and various related aspects have been reported. These are concerned with: (a) detection of various GTP-binding proteins in platelets, (b) the effects of known inhibitors of GTP-binding proteins such as GDPgS or pertussis toxin on the agonist-induced stimulation of phospholipase C, (c) the direct effects of stimulators of GTP-binding proteins such as GTP, GTP-analogs and fluoride on phospholipase C activity, (d) the possible association of GTP-binding proteins to cytosolic phospholipase C that would then lead to degradation of the membrane-bound inositides and (e) cytosolic phospholipase C response to the activation of cell surface receptors. The emerging information has had contradictory conclusions. (1) Pretreatment of saponin-permeabilized platelets with pertussis toxin has been shown to enhance and to inhibit the thrombin-induced activation of phospholipase C. Therefore, it is not clear if a G protein that is affected by pertussis toxin in a manner similar to Gi or Go plays a central role in activation of phospholipase C. (2) Studies on the effect of GDPβ;S are also conflicting indicating that there may be GTP-independent and/or -dependent pathways for the activation of phosphoinositide hydrolysis. (3) A cytosolic phospholipase C is activated by GTP, and it has been advanced that this activity might trigger the hydrolysis of membrane-bound inositides. A cytosolic GTP-binding protein might be involved in this action, and it is speculated that an α-subunit might be released to the cytoplasm by a receptor-coupled mechanism to activate phospholipase C. However, no direct evidence exists to support this conclusion. Moreover, the exact contribution of phospholipase C from the membranes or the cytosol to inositide hydrolysis in response to cellular agonists and the relationship of those activites to membrane-bound or soluble GTP-binding proteins are unknown. Our results indicate that the stimulation of phospholipase C in platelets by GDPβS and thrombin are affected differently by GDPβS. GDPgSinhibits the formation of inositol phosphates produced by GTPγS but not that induced by thrombin. Thrombin, therefore, can directly stimulate phospholipase C without the involvement of a “stimulatory” GTP-binding protein, such as Gs, for the agonist stimulation of adenylate cyclase. However, an “inhibitory” GTP-binding protein might have some influence on thrombin-stimulated phospholipase C, since in the presence of GDPγS thrombin produces a more profound stimulation of phospholipase C.This “inhibitory” GTP-binding protein might be ADP-ribosylated by pertussis toxin because pertussis toxin can also enhance thrombin action on phospholipase C activity. Therefore, phospholipase C that responds to thrombin could be different from the one that responds to GTPγS. Cytosolic phospholipase C can be activated by GTP or GTP analogs, and the one that responds to thrombin should be coupled to the receptors present in the plasma membrane. The initial action of thrombin is to directly activate the plasma membrane-bound phospholipase C and the mechanism of this activation is probably related to the proteolytic action of thrombin or the activation of platelet proteases by thrombin. In agreement with this, trypsin can also directly activate platelet phospholipase C and, subsequently, GTPyS produces further activation of phospholipase C. If these two mechanisms are operative in platelets, the inhibition of cytosolic phospholipase C by GDPβS would allow a larger fraction of inositides for degradation of the thrombin-stimulated phospholipase C, as our results show.
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Reports on the topic "Proteins Cellular signal transduction"

1

Regan, Lynne. Signal Transduction by Designed Metal-Binding Proteins. Fort Belvoir, VA: Defense Technical Information Center, August 2003. http://dx.doi.org/10.21236/ada416956.

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Merrill, Alfred H., and Jr. Subcellular Signal Transduction Systems in the Cellular Trauma of Ischemia. Fort Belvoir, VA: Defense Technical Information Center, November 1990. http://dx.doi.org/10.21236/ada229876.

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Tyner, Angela L. A Small Scale Proteomics Approach for Identifying Proteins Regulated by the Breast Tumor Kinase BRK Signal Transduction Pathway. Fort Belvoir, VA: Defense Technical Information Center, June 2002. http://dx.doi.org/10.21236/ada406106.

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