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Journal articles on the topic 'Intracellular signal transduction'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 September 2023

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1

Beeram, Muralidhar, and Amita Patnaik. "Targeting intracellular signal transduction." Hematology/Oncology Clinics of North America 16, no. 5 (October 2002): 1089–100. http://dx.doi.org/10.1016/s0889-8588(02)00054-0.

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2

Burrow, G. N., and M. Eggo. "Signal transduction and intracellular chatter." Endocrinology 135, no. 2 (August 1994): 491–92. http://dx.doi.org/10.1210/endo.135.2.8033798.

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3

Hurtley, S. M. "CELL BIOLOGY: Intracellular Signal Transduction." Science 296, no. 5567 (April 19, 2002): 433a—433. http://dx.doi.org/10.1126/science.296.5567.433a.

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4

Kobayashi, T., M. Murakami, T. Kawasaki, A. Yoshimura, and A. Kusumi. "S2L1 Single molecule analysis of intracellular signal transduction in living cells." Seibutsu Butsuri 42, supplement2 (2002): S11. http://dx.doi.org/10.2142/biophys.42.s11_1.

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5

Hidaka, Hiroyoshi. "Intracellular Signal Transduction and Cell Function." membrane 21, no. 1 (1996): 9–17. http://dx.doi.org/10.5360/membrane.21.9.

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6

SODEOKA, Mikiko. "Development of Intracellular Signal Transduction Modulators." Journal of the agricultural chemical society of Japan 78, no. 12 (2004): 1156a—1157. http://dx.doi.org/10.1271/nogeikagaku1924.78.1156a.

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7

Saito, Hideaki, Woodae Kang, and Shigeo Ikeda. "Nutrition and phagocyte intracellular signal transduction." International Congress Series 1255 (August 2003): 61–64. http://dx.doi.org/10.1016/s0531-5131(03)00653-8.

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8

Louie, Dexter S. "Cholecystokinin-Stimulated Intracellular Signal Transduction Pathways." Journal of Nutrition 124, suppl_8 (August 1, 1994): 1315S—1320S. http://dx.doi.org/10.1093/jn/124.suppl_8.1315s.

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9

Müller, Werner E. G., Durdica Ugarković, Vera Gamulin, Barbara E. Weiler, and Heinz C. Schröder. "Intracellular signal transduction pathways in sponges." Electron Microscopy Reviews 3, no. 1 (January 1990): 97–114. http://dx.doi.org/10.1016/0892-0354(90)90016-l.

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10

Klesse, Laura J., and Luis F. Parada. "Trks: Signal transduction and intracellular pathways." Microscopy Research and Technique 45, no. 4-5 (May 15, 1999): 210–16. http://dx.doi.org/10.1002/(sici)1097-0029(19990515/01)45:4/5<210::aid-jemt4>3.0.co;2-f.

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11

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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12

MENE, PAOLO, MICHAEL S. SIMONSON, and MICHAEL J. DUNN. "Eicosanoids, Mesangial Contraction, and Intracellular Signal Transduction." Tohoku Journal of Experimental Medicine 166, no. 1 (1992): 57–73. http://dx.doi.org/10.1620/tjem.166.57.

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13

Mikoshiba, Katsuhiko, Kozo Hamada, Hiroko Bannai, Kazumi Fukatsu, Hideaki Ando, Toru Matsuura, Keiko Uchida, et al. "Molecular imaging of the intracellular signal transduction." Seibutsu Butsuri 43, supplement (2003): S15. http://dx.doi.org/10.2142/biophys.43.s15_3.

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14

Kistner, Catherine, and Martin Parniske. "Evolution of signal transduction in intracellular symbiosis." Trends in Plant Science 7, no. 11 (November 2002): 511–18. http://dx.doi.org/10.1016/s1360-1385(02)02356-7.

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15

Bevan, A. Paul, Paul G. Drake, John J. M. Bergeron, and Barry I. Posner. "Intracellular signal transduction: The role of endosomes." Trends in Endocrinology & Metabolism 7, no. 1 (January 1996): 13–21. http://dx.doi.org/10.1016/1043-2760(95)00179-4.

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16

Brugge, Joan S. "Protein:protein interactions involved in intracellular signal transduction." Chemistry & Biology 1 (April 1994): xii—xiii. http://dx.doi.org/10.1016/1074-5521(94)90023-x.

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17

Yacoub, Adly, Anna Miller, Ruben W. Caron, Liang Qiao, David A. Curiel, Paul B. Fisher, Michael P. Hagan, Steven Grant, and Paul Dent. "Radiotherapy-induced signal transduction." Endocrine-Related Cancer 13, Supplement_1 (December 2006): S99—S114. http://dx.doi.org/10.1677/erc.1.01271.

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Exposure of tumor cells to ionizing radiation causes compensatory activation of multiple intracellular survival signaling pathways to maintain viability. In human carcinoma cells, radiation exposure caused an initial rapid inhibition of protein tyrosine phosphatase function and the activation of ERBB receptors and downstream signaling pathways. Radiation-induced activation of extracellular regulated kinase (ERK)1/2 promoted the cleavage and release of paracrine ligands in carcinoma cells which caused re-activation of ERBB family receptors and intracellular signaling pathways. Blocking ERBB receptor phosphorylation or ERK1/2 pathway activity using small-molecule inhibitors of kinases for a short period of time following exposure (3 h) surprisingly protected tumor cells from the toxic effects of ionizing radiation. Prolonged exposure (48–72 h) of tumor cells to inhibition of ERBB receptor/ERK1/2 function enhanced radiosensitivity. In addition to ERBB receptor signaling, expression of activated forms of RAS family members and alterations in p53 mutational status are known to regulate radiosensitivity apparently independent of ERBB receptor function; however, changes in RAS or p53 mutational status, in isogenic HCT116 cells, were also noted to modulate the expression of ERBB receptors and ERBB receptor paracrine ligands. These alterations in receptor and ligand expression correlated with changes in the ability of HCT116 cells to activate ERK1/2 and AKT after irradiation, and to survive radiation exposure. Collectively, our data in multiple human carcinoma cell lines argues that tumor cells are dynamic and rapidly adapt to any single therapeutic challenge, for example, radiation and/or genetic manipulation e.g. loss of activated RAS function, to maintain tumor cell growth and viability.

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18

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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19

Nürnberger, Thorsten, Wolfgang Wirtz, Dirk Nennstiel, Klaus Hahlbrock, Thorsten Jabs, Sabine Zimmermann, and Dierk Scheel. "Signal Perception and Intracellular Signal Transduction in Plant Pathogen Defense." Journal of Receptors and Signal Transduction 17, no. 1-3 (January 1997): 127–36. http://dx.doi.org/10.3109/10799899709036598.

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20

Hausott, Barbara, Rudolf Glueckert, Anneliese Schrott-Fischer, and Lars Klimaschewski. "Signal Transduction Regulators in Axonal Regeneration." Cells 11, no. 9 (May 4, 2022): 1537. http://dx.doi.org/10.3390/cells11091537.

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Intracellular signal transduction in response to growth factor receptor activation is a fundamental process during the regeneration of the nervous system. In this context, intracellular inhibitors of neuronal growth factor signaling have become of great interest in the recent years. Among them are the prominent signal transduction regulators Sprouty (SPRY) and phosphatase and tensin homolog deleted on chromosome 10 (PTEN), which interfere with major signaling pathways such as extracellular signal-regulated kinase (ERK) or phosphoinositide 3-kinase (PI3K)/Akt in neurons and glial cells. Furthermore, SPRY and PTEN are themselves tightly regulated by ubiquitin ligases such as c-casitas b-lineage lymphoma (c-CBL) or neural precursor cell expressed developmentally down-regulated protein 4 (NEDD4) and by different microRNAs (miRs) including miR-21 and miR-222. SPRY, PTEN and their intracellular regulators play an important role in the developing and the lesioned adult central and peripheral nervous system. This review will focus on the effects of SPRY and PTEN as well as their regulators in various experimental models of axonal regeneration in vitro and in vivo. Targeting these signal transduction regulators in the nervous system holds great promise for the treatment of neurological injuries in the future.

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21

Mehra, Arun, and Jeffrey L. Wrana. "TGF-β and the Smad signal transduction pathway." Biochemistry and Cell Biology 80, no. 5 (October 1, 2002): 605–22. http://dx.doi.org/10.1139/o02-161.

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Transforming growth factor β (TGF-β) superfamily members are important regulators of many diverse developmental and homeostatic processes and disruption of their activity has been implicated in a variety of human diseases ranging from cancer to chondrodysplasias and pulmonary hypertension. TGF-β family members signal through transmembrane SerThr kinase receptors that directly regulate the intracellular Smad pathway. Smads are a unique family of signal transduction molecules that can transmit signals directly from the cell surface receptors to the nucleus, where they regulate transcription by interacting with DNA binding partners as well as transcriptional coactivators and corepressors. In addition, more recent evidence indicates that Smads can also function both as substrates and adaptors for ubiquitin protein ligases, which mediate the targeted destruction of intracellular proteins. Smads have thus emerged as multifunctional transmitters of TGF-β family signals that play critical roles in the development and homeostasis of metazoans.Key words: TGF-β, Smads, receptors, ubiquitin ligase, signal transduction.

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22

Mene, P., M. S. Simonson, and M. J. Dunn. "Phospholipids in signal transduction of mesangial cells." American Journal of Physiology-Renal Physiology 256, no. 3 (March 1, 1989): F375—F386. http://dx.doi.org/10.1152/ajprenal.1989.256.3.f375.

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Glomerular mesangial cells respond to a variety of hormones, cytokines, and autacoids with an immediate hydrolysis of membrane phospholipids, including phosphatidylinositol, phosphatidylcholine, and phosphatidylethanolamine. Phospholipid metabolites such as inositol phosphates and diacylglycerol serve as initiating signals for subsequent intracellular events, including release of intracellular Ca2+ stores, increased conductance of the plasma membrane to various ions, changes of intracellular pH, and protein phosphorylation. The resting functional responses, including cell contraction and proliferation, are in turn regulated by simultaneous release of bioactive lipids such as eicosanoids and platelet-activating factor, which recognize receptors on both intrinsic glomerular cells and circulating, blood-borne cells. Through this complex signaling network, phospholipid metabolism plays a central regulatory role in mesangial functions in physiological conditions as well as in inflammatory or metabolic derangements of the kidney glomerulus.

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23

Menè, P., G. A. Cinotti, and F. Pugliese. "Signal transduction in mesangial cells." Journal of the American Society of Nephrology 2, no. 10 (April 1992): S100. http://dx.doi.org/10.1681/asn.v210s100.

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Phenotype, growth, and functional characteristics of glomerular mesangial "myofibroblasts" are under the control of multiple hormones, vasoactive agents, autacoids, and cytokines. Several parallel signal transduction pathways couple receptor occupancy with functional changes, including phospholipases C, A2, and D breakdown of membrane phospholipids, and adenylate/guanylate cyclase activation. Changes of cytosolic ion concentrations, cyclic nucleotide accumulation, and eicosanoid biosynthesis are currently interpreted as intracellular signals for protein kinase activation. Phosphorylation of multiple substrates by serine/threonine kinases C, A, and G or by tyrosine kinases directly coupled to receptors, is a final step in cell activation. Cross-talk between signal transduction pathways, along with the release of eicosanoids and cytokines acting as intercellular mediators, provides the potential for interactive regulation of glomerular cell functions.

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24

Schiffrin, Ernesto L. "Intracellular signal transduction for vasoactive peptides in hypertension." Canadian Journal of Physiology and Pharmacology 72, no. 8 (August 1, 1994): 954–62. http://dx.doi.org/10.1139/y94-133.

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Increased peripheral resistance is the hallmark of hypertension. It may result in part from exaggerated vascular reactivity of resistance arteries. Some changes in density of surface receptors for different vasoconstrictors and vasorelaxants have been described that could play a role in physiological findings in hypertension. Smooth muscle cells of resistance arteries have increased cytosolic free calcium concentration in some models of experimental hypertension, which may contribute to enhance vascular responses. Exaggerated response of the inositol phosphate – calcium pathway has been demonstrated after stimulation with some vasoconstrictor agents such as norepinephrine, angiotensin II, and vasopressin. In contrast, responses to the potent vasoconstrictor peptide endothelin-1 are either normal (in spontaneously hypertensive rats) or blunted (in deoxycorticosterone-salt hypertension). In the latter case, endothelin receptor density, inositol phosphate and diacylglycerol generation, and cytosolic calcium responses agree with blunted response of blood vessels. Increased basal cytosolic calcium and exaggerated sensitivity of myosin light chain to calcium may be mechanisms underlying increases in sensitivity of signal transduction in smooth muscle in some models of hypertension. However, in general, signal transduction of receptors for vasoconstrictors appears to be blunted rather than exaggerated, except for responses to angiotensin II. Altered structure of resistance arteries (remodeling) may be a mechanism that, even in presence of blunted intracellular signal transduction, may result in enhanced pressor responsiveness of blood vessels in hypertension.Key words: second messengers, phospholipases, inositol phosphates, calcium, magnesium, Na+–H+ exchange, protein kinases, cyclic nucleotides, vascular reactivity.

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25

Costa, L. G., M. Guizzetti, H. Lu, F. Bordi, A. Vitalone, B. Tita, M. Palmery, P. Valeri, and B. Silvestrini. "Intracellular signal transduction pathways as targets for neurotoxicants." Toxicology 160, no. 1-3 (March 2001): 19–26. http://dx.doi.org/10.1016/s0300-483x(00)00435-2.

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26

Ichikawa, Atsushi, Manabu Negishi, Yukihiko Sugimoto, and Shuh Narumiya. "Intracellular Signal Transduction Networks of Mouse Prostaglandin Receptors." Japanese Journal of Pharmacology 71 (1996): 14. http://dx.doi.org/10.1016/s0021-5198(19)36317-6.

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27

Schonthal, Axel H. "Role of PP2A in intracellular signal transduction pathways." Frontiers in Bioscience 3, no. 4 (1998): d1262–1273. http://dx.doi.org/10.2741/a361.

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28

Yamamoto, M., M. Yasuda, S. Shiokawa, and M. Nobunaga. "Intracellular signal transduction in proliferation of synovial cells." Clinical Rheumatology 11, no. 1 (March 1992): 92–96. http://dx.doi.org/10.1007/bf02207092.

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29

Mooibroek, Marilyn J., and Jerry H. Wang. "Integration of signal-transduction processes." Biochemistry and Cell Biology 66, no. 6 (June 1, 1988): 557–66. http://dx.doi.org/10.1139/o88-066.

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The adenylate cyclase – cAMP, phospholipase C – IP3 (inositol 1,4,5-triphosphate), and DAG (diacylglycerol) signal transduction systems are used to illustrate general principles underlying the process of information transfer during cell stimulation. Both systems consist of reaction cascades that convert the external signal to an intracellular messenger, translate the messenger to regulatory activities, and then modulate the activities of appropriate cellular proteins to result in specific cell responses. Almost all of these reactions are under second-messenger-dependent regulation, with many being regulated by multiple messengers. Such complex regulation provides ample opportunities for the fine-tuning of the signal cascades and for coordination between cascades during cell stimulation. Specific examples are used to illustrate how the cell uses different intrasystem and intersystem regulatory reactions to achieve specific responses.

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30

Alenzi, Faris Q. "Signal Transduction Pathway in Chronic Leukemia." Bangladesh Journal of Medical Science 16, no. 1 (January 16, 2017): 21–23. http://dx.doi.org/10.3329/bjms.v16i1.31127.

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It is becoming progressively clearer that the three RAS genes, N-. H-and K-RAS, encode 21 kDa proteins which act as intracellular switches, playing important roles in the signal transduction pathway that control cell development and maturation. These three genes are profoundly homologous, yet more recent findings indicate they have important roles in the functions various cell types playing focal roles in numerous human infections. This article briefly reviews the regulation of RAs-dependent signaling mechanisms.Bangladesh Journal of Medical Science Vol.16(1) 2017 p.21-23

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31

Williams, John A. "Signal transduction and intracellular signaling in pancreatic acinar cells." Current Opinion in Gastroenterology 11, no. 5 (September 1995): 397–401. http://dx.doi.org/10.1097/00001574-199509000-00002.

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32

Lodish, H. F., D. J. Hilton, U. Klingmuller, S. S. Watowich, and H. Wu. "The Erythropoietin Receptor: Biogenesis, Dimerization, and Intracellular Signal Transduction." Cold Spring Harbor Symposia on Quantitative Biology 60 (January 1, 1995): 93–104. http://dx.doi.org/10.1101/sqb.1995.060.01.012.

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33

Hidaka, Hiroyoshi. "Elucidation of the intracellular signal transduction by synthesized compounds." Japanese Journal of Pharmacology 73 (1997): 19. http://dx.doi.org/10.1016/s0021-5198(19)44588-5.

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34

Constantinescu, Stefan N., Saghi Ghaffari, and Harvey F. Lodish. "The Erythropoietin Receptor: Structure, Activation and Intracellular Signal Transduction." Trends in Endocrinology & Metabolism 10, no. 1 (January 1999): 18–23. http://dx.doi.org/10.1016/s1043-2760(98)00101-5.

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35

Okamoto, Koichi, and Masayuki Sekiguchi. "Synaptic receptors and intracellular signal transduction in the cerebellum." Neuroscience Research 9, no. 4 (January 1991): 213–36. http://dx.doi.org/10.1016/0168-0102(91)90023-r.

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36

Läer, Leonhard, Mirko Kloppstech, Christof Schöfl, Terrence J. Sejnowski, Georg Brabant, and Klaus Prank. "Noise enhanced hormonal signal transduction through intracellular calcium oscillations." Biophysical Chemistry 91, no. 2 (July 2001): 157–66. http://dx.doi.org/10.1016/s0301-4622(01)00167-3.

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37

Nakabayashi, Jun, and Akira Sasaki. "Optimal phosphorylation step number of intracellular signal-transduction pathway." Journal of Theoretical Biology 233, no. 3 (April 2005): 413–21. http://dx.doi.org/10.1016/j.jtbi.2004.10.022.

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38

Im, Gun-Il. "Intracellular Signal Transduction Pathways and Transcription Factors for Osteogenesis." Journal of the Korean Rheumatism Association 15, no. 1 (2008): 1. http://dx.doi.org/10.4078/jkra.2008.15.1.1.

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39

SHARMA, B. K., S. JAIN, and N. K. GANGULY. "Intracellular Signal Transduction in T Cells in Takayasu's Arteritis." Annals of the New York Academy of Sciences 793, no. 1 Myocardial Pr (September 1996): 453–55. http://dx.doi.org/10.1111/j.1749-6632.1996.tb33540.x.

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40

Wong, Chun Kwok, Jiping Zhang, Wai Ki Ip, and Christopher Wai Kei Lam. "INTRACELLULAR SIGNAL TRANSDUCTION IN EOSINOPHILS AND ITS CLINICAL SIGNIFICANCE." Immunopharmacology and Immunotoxicology 24, no. 2 (January 2002): 165–86. http://dx.doi.org/10.1081/iph-120003748.

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41

Wynn, Michelle L., Megan Egbert, Nikita Consul, Jungsoo Chang, Zhi-Fen Wu, Sofia D. Meravjer, and Santiago Schnell. "Inferring Intracellular Signal Transduction Circuitry from Molecular Perturbation Experiments." Bulletin of Mathematical Biology 80, no. 5 (April 28, 2017): 1310–44. http://dx.doi.org/10.1007/s11538-017-0270-9.

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42

Isakov, Noah, Wolfgang Scholz, and Amnon Altman. "Signal transduction and intracellular events in T-lymphocyte activation." Immunology Today 7, no. 9 (September 1986): 271–77. http://dx.doi.org/10.1016/0167-5699(86)90009-5.

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43

Finkel, Toren. "Signal transduction by reactive oxygen species." Journal of Cell Biology 194, no. 1 (July 11, 2011): 7–15. http://dx.doi.org/10.1083/jcb.201102095.

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Although historically viewed as purely harmful, recent evidence suggests that reactive oxygen species (ROS) function as important physiological regulators of intracellular signaling pathways. The specific effects of ROS are modulated in large part through the covalent modification of specific cysteine residues found within redox-sensitive target proteins. Oxidation of these specific and reactive cysteine residues in turn can lead to the reversible modification of enzymatic activity. Emerging evidence suggests that ROS regulate diverse physiological parameters ranging from the response to growth factor stimulation to the generation of the inflammatory response, and that dysregulated ROS signaling may contribute to a host of human diseases.

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44

Dumont, J. E., S. Dremier, I. Pirson, and C. Maenhaut. "Cross signaling, cell specificity, and physiology." American Journal of Physiology-Cell Physiology 283, no. 1 (July 1, 2002): C2—C28. http://dx.doi.org/10.1152/ajpcell.00581.2001.

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The literature on intracellular signal transduction presents a confusing picture: every regulatory factor appears to be regulated by all signal transduction cascades and to regulate all cell processes. This contrasts with the known exquisite specificity of action of extracellular signals in different cell types in vivo. The confusion of the in vitro literature is shown to arise from several causes: the inevitable artifacts inherent in reductionism, the arguments used to establish causal effect relationships, the use of less than adequate models (cell lines, transfections, acellular systems, etc.), and the implicit assumption that networks of regulations are universal whereas they are in fact cell and stage specific. Cell specificity results from the existence in any cell type of a unique set of proteins and their isoforms at each level of signal transduction cascades, from the space structure of their components, from their combinatorial logic at each level, from the presence of modulators of signal transduction proteins and of modulators of modulators, from the time structure of extracellular signals and of their transduction, and from quantitative differences of expression of similar sets of factors.

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45

PUEBLA, HECTOR. "CONTROLLING INTRACELLULAR CALCIUM OSCILLATIONS AND WAVES." Journal of Biological Systems 13, no. 02 (June 2005): 173–90. http://dx.doi.org/10.1142/s021833900500146x.

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Biological systems perform complex signal transduction at the cellular level. Intracellular calcium ( Ca 2+) plays a significant role in signal transduction from receptors at the cell membrane to enzymes and genes controlling the complex biochemical network of the cell. Intracellular Ca 2+ shows a rich behavior of nonlinear dynamics including excitability, oscillations and nonlinear waves. In this work, a feedback control approach is introduced to control intracellular calcium dynamics of both well-mixed cell (calcium oscillations) and distributed (nonlinear waves) parameter models using an external control input that causes an influx of Ca 2+ to the signaling calcium pathway. Numerical simulations shows the effectiveness of the feedback control laws proposed.

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46

Li, Jing, Ke Quan, Yanjing Yang, Xiaohai Yang, Xiangxian Meng, Jin Huang, and Kemin Wang. "Engineering DNAzyme cascade for signal transduction and amplification." Analyst 145, no. 5 (2020): 1925–32. http://dx.doi.org/10.1039/c9an02003a.

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47

Adjei, Alex A., and Manuel Hidalgo. "Intracellular Signal Transduction Pathway Proteins As Targets for Cancer Therapy." Journal of Clinical Oncology 23, no. 23 (August 10, 2005): 5386–403. http://dx.doi.org/10.1200/jco.2005.23.648.

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Circulating cytokines, hormones, and growth factors control all aspects of cell proliferation, differentiation, angiogenesis, apoptosis, and senescence. These chemical signals are propagated from the cell surface to intracellular processes via sequential kinase signaling, arranged in modules that exhibit redundancy and cross talk. This signal transduction system comprising growth factors, transmembrane receptor proteins, and cytoplasmic secondary messengers is often exploited to optimize tumor growth and metastasis in malignancies. Thus, it represents an attractive target for cancer therapy. This review will summarize current knowledge of selected intracellular signaling networks and their role in cancer therapy. The focus will be on pathways for which inhibitory agents are currently undergoing clinical testing. Original data for inclusion in this review were identified through a MEDLINE search of the literature. All papers from 1966 through March 2005 were identified by the following search terms: “signal transduction,” “intracellular signaling,” “kinases,” “proliferation,” “growth factors,” and “cancer therapy.” All original research and review papers related to the role of intracellular signaling in oncogenesis and therapeutic interventions relating to abnormal cell signaling were identified. This search was supplemented by a manual search of the Proceedings of the Annual Meetings of the American Association for Cancer Research, American Society of Clinical Oncology, and the American Association for Cancer Research (AARC) –European Organisation for Research and Treatment of Cancer (EORTC) –National Cancer Institute (NCI) Symposium on New Anticancer Drugs.

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48

Lindemann, B. "Sweet and Salty: Transduction in Taste." Physiology 10, no. 4 (August 1, 1995): 166–70. http://dx.doi.org/10.1152/physiologyonline.1995.10.4.166.

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Abstract:

Signal pathways in taste receptor cells reach from apical events, like binding of a tastant to a receptor, through intracellular processes and basolateral regenerative ion channel activity to the release of transmitter. The responses are now being investigated with patch clamping, monitoring of intracellular messengers including Ca2+, and molecular cloning.

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49

Bergeron, John J. M., G. M. Di Guglielmo, Patricia C. Baass, François Authier, and Barry I. Posner. "Endosomes, receptor tyrosine kinase internalization and signal transduction." Bioscience Reports 15, no. 6 (December 1, 1995): 411–18. http://dx.doi.org/10.1007/bf01204345.

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Upon the binding of insulin or epidermal growth factor to their cognate receptors on the liver parenchymal plasmalemma, signal transduction and receptor internalization are near co-incident. Indeed, the rapidity and extent; of ligand mediated receptor internalization into endosomes in liver as well as other organs predicts that signal transduction is regulated at this intracellular locus. Although internalization has been thought as a mechanism to attenuate ligand mediated signal transduction responses, detailed studies of internalized receptors in isolated liver endosomes suggest an alternative scenario whereby selective signal transduction pathways can be accessed at this locus.

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50

Scott, John D., and Tony Pawson. "Cell Signaling in Space and Time: Where Proteins Come Together and When They’re Apart." Science 326, no. 5957 (November 26, 2009): 1220–24. http://dx.doi.org/10.1126/science.1175668.

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Abstract:

Signal transduction can be defined as the coordinated relay of messages derived from extracellular cues to intracellular effectors. More simply put, information received on the cell surface is processed across the plasma membrane and transmitted to intracellular targets. This requires that the activators, effectors, enzymes, and substrates that respond to cellular signals come together when they need to.

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