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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 (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 (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 (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 (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 (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 (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 (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 regul

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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, 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 (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 (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, et al. "Radiotherapy-induced signal transduction." Endocrine-Related Cancer 13, Supplement_1 (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 rec

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18

Watt, F. M., and R. Sever. "Signal transduction." Journal of Cell Science 114, no. 7 (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 fo

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19

Nürnberger, Thorsten, Wolfgang Wirtz, Dirk Nennstiel, et al. "Signal Perception and Intracellular Signal Transduction in Plant Pathogen Defense." Journal of Receptors and Signal Transduction 17, no. 1-3 (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 (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. Further

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21

Mehra, Arun, та Jeffrey L. Wrana. "TGF-β and the Smad signal transduction pathway". Biochemistry and Cell Biology 80, № 5 (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

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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 (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 proli

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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 (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 mu

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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 (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 demons

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25

Costa, L. G., M. Guizzetti, H. Lu, et al. "Intracellular signal transduction pathways as targets for neurotoxicants." Toxicology 160, no. 1-3 (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 (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 (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 b

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30

Alenzi, Faris Q. "Signal Transduction Pathway in Chronic Leukemia." Bangladesh Journal of Medical Science 16, no. 1 (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 (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 (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 (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 (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 (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 (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 (2002): 165–86. http://dx.doi.org/10.1081/iph-120003748.

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41

Wynn, Michelle L., Megan Egbert, Nikita Consul, et al. "Inferring Intracellular Signal Transduction Circuitry from Molecular Perturbation Experiments." Bulletin of Mathematical Biology 80, no. 5 (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 (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 (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 growt

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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 (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, et

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45

PUEBLA, HECTOR. "CONTROLLING INTRACELLULAR CALCIUM OSCILLATIONS AND WAVES." Journal of Biological Systems 13, no. 02 (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 ex

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46

Li, Jing, Ke Quan, Yanjing Yang, et al. "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 (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. T

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48

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

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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 (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 alternati

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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 (2009): 1220–24. http://dx.doi.org/10.1126/science.1175668.

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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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