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Articoli di riviste sul tema "Intracellular pathways"

Autore: Grafiati
Pubblicato: 4 giugno 2021
Ultima modifica: 15 febbraio 2024

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1

Waligora, E. A., C. R. Fisher, N. J. Hanovice, A. Rodou, E. E. Wyckoff, and S. M. Payne. "Role of Intracellular Carbon Metabolism Pathways in Shigella flexneri Virulence." Infection and Immunity 82, no. 7 (April 14, 2014): 2746–55. http://dx.doi.org/10.1128/iai.01575-13.

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ABSTRACTShigella flexneri, which replicates in the cytoplasm of intestinal epithelial cells, can use the Embden-Meyerhof-Parnas, Entner-Doudoroff, or pentose phosphate pathway for glycolytic carbon metabolism. To determine which of these pathways is used by intracellularS. flexneri, mutants were constructed and tested in a plaque assay for the ability to invade, replicate intracellularly, and spread to adjacent epithelial cells. Mutants blocked in the Embden-Meyerhof-Parnas pathway (pfkABandpykAFmutants) invaded the cells but formed very small plaques. Loss of the Entner-Doudoroff pathway geneedaresulted in small plaques, but the doubleeda eddmutant formed normal-size plaques. This suggested that the plaque defect of theedamutant was due to buildup of the toxic intermediate 2-keto-3-deoxy-6-phosphogluconic acid rather than a specific requirement for this pathway. Loss of the pentose phosphate pathway had no effect on plaque formation, indicating that it is not critical for intracellularS. flexneri. Supplementation of the epithelial cell culture medium with pyruvate allowed the glycolysis mutants to form larger plaques than those observed with unsupplemented medium, consistent with data from phenotypic microarrays (Biolog) indicating that pyruvate metabolism was not disrupted in these mutants. Interestingly, the wild-typeS. flexnerialso formed larger plaques in the presence of supplemental pyruvate or glucose, with pyruvate yielding the largest plaques. Analysis of the metabolites in the cultured cells showed increased intracellular levels of the added compound. Pyruvate increased the growth rate ofS. flexneriin vitro, suggesting that it may be a preferred carbon source inside host cells.
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Ulevitch, Richard J., David L. Dunn, Mitchell P. Fink, and Christopher E. Taylor. "ENDOTOXIN-RELATED INTRACELLULAR PATHWAYS." Shock 6, no. 1 (July 1996): 1–2. http://dx.doi.org/10.1097/00024382-199607000-00001.

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Benitah, Salvador Aznar. "Intracellular signalling pathways and carcinogenesis." Revista de Oncología 3, no. 5 (September 2001): 274–77. http://dx.doi.org/10.1007/bf02719890.

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Nahorski, Stefan R. "Pharmacology of intracellular signalling pathways." British Journal of Pharmacology 147, S1 (January 2006): S38—S45. http://dx.doi.org/10.1038/sj.bjp.0706468.

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Sanders-Bush, Elaine. "CONTROL OF INTRACELLULAR SIGNALING PATHWAYS." Behavioural Pharmacology 10, SUPPLEMENT 1 (August 1999): S80. http://dx.doi.org/10.1097/00008877-199908001-00203.

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LACOMBE, CATHERINE, ISABELLE DUSANTER, STÉPHANIE GOBERT, ODILE MULLER, SYLVIE GISSELBRECHT, and PATRICK MAYEUX. "Intracellular Pathways Activated by Erythropoietina." Annals of the New York Academy of Sciences 718, no. 1 (February 26, 2008): 223–31. http://dx.doi.org/10.1111/j.1749-6632.1994.tb55721.x.

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Castle, D., and A. Castle. "Intracellular Transport and Secretion of Salivary Proteins." Critical Reviews in Oral Biology & Medicine 9, no. 1 (January 1998): 4–22. http://dx.doi.org/10.1177/10454411980090010301.

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Intracellular transport and secretion of salivary proteins are major activities of salivary acinar cells. While the major intracellular pathway followed by salivary proteins following their synthesis has been described previously, there is only limited understanding of how this process is regulated at the molecular level. Studies of salivary proteins, especially proline-rich proteins, expressed in an endocrine cell line have begun to provide insight regarding intermolecular interactions during transport and the role played by structural signals during intracellular sorting. Analysis of the secretion of newly synthesized salivary proteins in parotid tissue has shown that there are multiple pathways of discharge from acinar cells. While granule exocytosis is the major pathway, at least two other pathways that export salivary proteins have been found to originate from maturing secretion granules. These pathways may contribute to other acinar cell functions, including secretion of proteins in the absence of acute stimulation and support of the secretory process for fluid and electrolytes.
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8

Xu, Wen, Bei Wang, Yisong Gao, Yuxuan Cai, Jiali Zhang, Zhiyin Wu, Jiameng Wei, Chong Guo, and Chengfu Yuan. "Alkaloids Exhibit a Meaningful Function as Anticancer Agents by Restraining Cellular Signaling Pathways." Mini-Reviews in Medicinal Chemistry 22, no. 7 (April 2022): 968–83. http://dx.doi.org/10.2174/1389557521666211007114935.

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Abstract: Alkaloids are nitrogen-containing organic compounds widely found in natural products, which play an essential role in clinical treatment. Cellular signaling pathways in tumors are a series of enzymatic reaction pathways that convert extracellular signals into intracellular signals to produce biological effects. The ordered function of cell signaling pathways is essential for tumor cell proliferation, differentiation, and programmed death. This review describes the antitumor progression mediated by various alkaloids after inhibiting classical signaling pathways; related studies are systematically retrieved and collected through PubMed. We selected the four currently most popular pathways for discussion and introduced the molecular mechanisms mediated by alkaloids in different signaling pathways, including the NF-kB signaling pathway, PI3K/AKT signaling pathway, MAPK signaling pathway, and P53 signaling pathway. The research progress of alkaloids related to tumor signal transduction pathwa
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9

Pieper, Rembert, C. R. Fisher, Moo-Jin Suh, S. T. Huang, P. Parmar, and S. M. Payne. "Analysis of the Proteome of Intracellular Shigella flexneri Reveals Pathways Important for Intracellular Growth." Infection and Immunity 81, no. 12 (October 7, 2013): 4635–48. http://dx.doi.org/10.1128/iai.00975-13.

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ABSTRACTGlobal proteomic analysis was performed withShigella flexneristrain 2457T in association with three distinct growth environments:S. flexnerigrowing in broth (in vitro),S. flexnerigrowing within epithelial cell cytoplasm (intracellular), andS. flexnerithat were cultured with, but did not invade, Henle cells (extracellular). Compared toin vitroand extracellular bacteria, intracellular bacteria had increased levels of proteins required for invasion and cell-to-cell spread, including Ipa, Mxi, and Ics proteins. Changes in metabolic pathways in response to the intracellular environment also were evident. There was an increase in glycogen biosynthesis enzymes, altered expression of sugar transporters, and a reduced amount of the carbon storage regulator CsrA. Mixed acid fermentation enzymes were highly expressed intracellularly, while tricarboxylic acid (TCA) cycle oxidoreductive enzymes and most electron transport chain proteins, except CydAB, were markedly decreased. This suggested that fermentation and the CydAB system primarily sustain energy generation intracellularly. Elevated levels of PntAB, which is responsible for NADPH regeneration, suggested a shortage of reducing factors for ATP synthesis. These metabolic changes likely reflect changes in available carbon sources, oxygen levels, and iron availability. Intracellular bacteria showed strong evidence of iron starvation. Iron acquisition systems (Iut, Sit, FhuA, and Feo) and the iron starvation, stress-associated Fe-S cluster assembly (Suf) protein were markedly increased in abundance. Mutational analysis confirmed that the mixed-acid fermentation pathway was required for wild-type intracellular growth and spread ofS. flexneri. Thus, iron stress and changes in carbon metabolism may be key factors in theS. flexneritransition from the extra- to the intracellular milieu.
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10

Frühbeck, Gema. "Intracellular signalling pathways activated by leptin." Biochemical Journal 393, no. 1 (December 12, 2005): 7–20. http://dx.doi.org/10.1042/bj20051578.

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Leptin is a versatile 16 kDa peptide hormone, with a tertiary structure resembling that of members of the long-chain helical cytokine family. It is mainly produced by adipocytes in proportion to fat size stores, and was originally thought to act only as a satiety factor. However, the ubiquitous distribution of OB-R leptin receptors in almost all tissues underlies the pleiotropism of leptin. OB-Rs belong to the class I cytokine receptor family, which is known to act through JAKs (Janus kinases) and STATs (signal transducers and activators of transcription). The OB-R gene is alternatively spliced to produce at least five isoforms. The full-length isoform, OB-Rb, contains intracellular motifs required for activation of the JAK/STAT signal transduction pathway, and is considered to be the functional receptor. Considerable evidence for systemic effects of leptin on body mass control, reproduction, angiogenesis, immunity, wound healing, bone remodelling and cardiovascular function, as well as on specific metabolic pathways, indicates that leptin operates both directly and indirectly to orchestrate complex pathophysiological processes. Consistent with leptin's pleiotropic role, its participation in and crosstalk with some of the main signalling pathways, including those involving insulin receptor substrates, phosphoinositide 3-kinase, protein kinase B, protein kinase C, extracellular-signal-regulated kinase, mitogen-activated protein kinases, phosphodiesterase, phospholipase C and nitric oxide, has been observed. The impact of leptin on several equally relevant signalling pathways extends also to Rho family GTPases in relation to the actin cytoskeleton, production of reactive oxygen species, stimulation of prostaglandins, binding to diacylglycerol kinase and catecholamine secretion, among others.
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11

Lee, Ting-Hein, William McKleroy, Amin Khalifeh-Soltani, Stephen Sakuma, Stanislav Lazarev, Kirsi Riento, Stephen L. Nishimura, Ben J. Nichols, and Kamran Atabai. "Functional genomic screen identifies novel mediators of collagen uptake." Molecular Biology of the Cell 25, no. 5 (March 2014): 583–93. http://dx.doi.org/10.1091/mbc.e13-07-0382.

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Tissue fibrosis occurs when matrix production outpaces matrix degradation. Degradation of collagen, the main component of fibrotic tissue, is mediated through an extracellular proteolytic pathway and intracellular pathway of cellular uptake and lysosomal digestion. Recent studies demonstrate that disruption of the intracellular pathways can exacerbate fibrosis. These pathways are poorly characterized. Here we identify novel mediators of the intracellular pathway of collagen turnover through a genome-wide RNA interference screen in Drosophila S2 cells. Screening of 7505 Drosophila genes conserved among metazoans identified 22 genes that were required for efficient internalization of type I collagen. These included proteins involved in vesicle transport, the actin cytoskeleton, and signal transduction. We show further that the flotillin genes have a conserved and central role in collagen uptake in Drosophila and human cells. Short hairpin RNA–mediated silencing of flotillins in human monocyte and fibroblasts impaired collagen uptake by promoting lysosomal degradation of the endocytic collagen receptors uPARAP/Endo180 and mannose receptor. These data provide an initial characterization of intracellular pathways of collagen turnover and identify the flotillin genes as critical regulators of this process. A better understanding of these pathways may lead to novel therapies that reduce fibrosis by increasing collagen turnover.
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12

Rechsteiner, Martin. "Ubiquitin-Mediated Pathways for Intracellular Proteolysis." Annual Review of Cell Biology 3, no. 1 (November 1987): 1–30. http://dx.doi.org/10.1146/annurev.cb.03.110187.000245.

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13

Luedde, Tom, and Christian Trautwein. "Intracellular survival pathways in the liver." Liver International 26, no. 10 (December 2006): 1163–74. http://dx.doi.org/10.1111/j.1478-3231.2006.01366.x.

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14

Richter, D. W., P. M. Lalley, O. Pierrefiche, A. Haji, A. M. Bischoff, B. Wilken, and F. Hanefeld. "Intracellular signal pathways controlling respiratory neurons." Respiration Physiology 110, no. 2-3 (November 1997): 113–23. http://dx.doi.org/10.1016/s0034-5687(97)00077-7.

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15

Diba, Hasan, Reza Seifi-Kashani, Shohreh Tavakkoli, and Saeid Malek-Mohammadi. "Polyhydroxyalkanoates (Phas), Intracellular Pathways and Properties." Current World Environment 10, Special-Issue1 (June 28, 2015): 644–49. http://dx.doi.org/10.12944/cwe.10.special-issue1.78.

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Nombela-Arrieta, César. "Intracellular signaling pathways mediating lymphocyte trafficking." Inmunología 27, no. 4 (October 2008): 192–204. http://dx.doi.org/10.1016/s0213-9626(08)70067-2.

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17

Zhang, Kai, and Bianxiao Cui. "Optogenetic control of intracellular signaling pathways." Trends in Biotechnology 33, no. 2 (February 2015): 92–100. http://dx.doi.org/10.1016/j.tibtech.2014.11.007.

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18

Hakim, Jacques. "Pharmacologic Control of Intracellular Signaling Pathways." Journal of Cardiovascular Pharmacology 25 (1995): S106—S113. http://dx.doi.org/10.1097/00005344-199500252-00023.

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19

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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20

Moody, D. Branch, and Steven A. Porcelli. "Intracellular pathways of CD1 antigen presentation." Nature Reviews Immunology 3, no. 1 (January 2003): 11–22. http://dx.doi.org/10.1038/nri979.

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21

Lonez, Caroline, Michel Vandenbranden, and Jean-Marie Ruysschaert. "Cationic lipids activate intracellular signaling pathways." Advanced Drug Delivery Reviews 64, no. 15 (December 2012): 1749–58. http://dx.doi.org/10.1016/j.addr.2012.05.009.

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Mavers, Melissa, Eric M. Ruderman, and Harris Perlman. "Intracellular signal pathways: Potential for therapies." Current Rheumatology Reports 11, no. 5 (October 2009): 378–85. http://dx.doi.org/10.1007/s11926-009-0054-9.

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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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GERBER, U., C. GEE, and P. BENQUET. "Metabotropic glutamate receptors: intracellular signaling pathways." Current Opinion in Pharmacology 7, no. 1 (February 2007): 56–61. http://dx.doi.org/10.1016/j.coph.2006.08.008.

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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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Procaccini, Claudio, Mario Galgani, Veronica De Rosa, and Giuseppe Matarese. "Intracellular metabolic pathways control immune tolerance." Trends in Immunology 33, no. 1 (January 2012): 1–7. http://dx.doi.org/10.1016/j.it.2011.09.002.

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Sheldahl, Laird C., Diane C. Slusarski, Petra Pandur, Jeffrey R. Miller, Michael Kühl, and Randall T. Moon. "Dishevelled activates Ca2+ flux, PKC, and CamKII in vertebrate embryos." Journal of Cell Biology 161, no. 4 (May 26, 2003): 769–77. http://dx.doi.org/10.1083/jcb.200211094.

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Abstract (sommario):
Wnt ligands and Frizzled (Fz) receptors have been shown to activate multiple intracellular signaling pathways. Activation of the Wnt–β-catenin pathway has been described in greatest detail, but it has been reported that Wnts and Fzs also activate vertebrate planar cell polarity (PCP) and Wnt–Ca2+ pathways. Although the intracellular protein Dishevelled (Dsh) plays a dual role in both the Wnt–β-catenin and the PCP pathways, its potential involvement in the Wnt–Ca2+ pathway has not been investigated. Here we show that a Dsh deletion construct, XDshΔDIX, which is sufficient for activation of the PCP pathway, is also sufficient for activation of three effectors of the Wnt–Ca2+ pathway: Ca2+ flux, PKC, and calcium/calmodulin-dependent protein kinase II (CamKII). Furthermore, we find that interfering with endogenous Dsh function reduces the activation of PKC by Xfz7 and interferes with normal heart development. These data suggest that the Wnt–Ca2+ pathway utilizes Dsh, thereby implicating Dsh as a component of all reported Fz signaling pathways.
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Tavare, JM, LM Fletcher, and GI Welsh. "Using green fluorescent protein to study intracellular signalling." Journal of Endocrinology 170, no. 2 (August 1, 2001): 297–306. http://dx.doi.org/10.1677/joe.0.1700297.

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Subcellular compartmentalisation of signalling molecules is an important phenomenon not only in defining how a signalling pathway is activated but also in influencing the desired physiological output of that pathway (e.g. cell growth or differentiation, regulation of metabolism, cytoskeletal changes etc.). Biochemical analyses of protein and lipid compartmentalisation by, for example, subcellular fractionation presents many technical difficulties. However, this aspect of cell signalling research has seen a major revolution thanks to the cloning and availability of a variety of mutant green fluorescent protein derivatives with distinct molecular properties. Mutants with increased brightness, altered excitation and emission maxima, altered stability and differential sensitivity to pH, are now in widespread use for following the trafficking and function of proteins in living cells and for monitoring the intracellular environment. In this review we focus on some of the recent developments in the use of green fluorescent proteins for studying intracellular signalling pathways often with special reference to the actions of insulin. We also discuss the future utility of these proteins to analyse protein--protein interactions in signalling pathways using fluorescence resonance energy transfer.
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Józefiak, Agata, Magdalena Larska, Małgorzata Pomorska-Mól, and Jakub J. Ruszkowski. "The IGF-1 Signaling Pathway in Viral Infections." Viruses 13, no. 8 (July 29, 2021): 1488. http://dx.doi.org/10.3390/v13081488.

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Insulin-like growth factor-1 (IGF-1) and the IGF-1 receptor (IGF-1R) belong to the insulin-like growth factor family, and IGF-1 activates intracellular signaling pathways by binding specifically to IGF-1R. The interaction between IGF-1 and IGF-1R transmits a signal through a number of intracellular substrates, including the insulin receptor substrate (IRS) and the Src homology collagen (Shc) proteins, which activate two major intracellular signaling pathways: the phosphatidylinositol 3-kinase (PI3K)/AKT and mitogen-activated protein kinase (MAPK) pathways, specifically the extracellular signal-regulated kinase (ERK) pathways. The PI3K/AKT kinase pathway regulates a variety of cellular processes, including cell proliferation and apoptosis. IGF1/IGF-1R signaling also promotes cell differentiation and proliferation via the Ras/MAPK pathway. Moreover, upon IGF-1R activation of the IRS and Shc adaptor proteins, Shc stimulates Raf through the GTPase Ras to activate the MAPKs ERK1 and ERK2, phosphorylate and several other proteins, and to stimulate cell proliferation. The IGF-1 signaling pathway is required for certain viral effects in oncogenic progression and may be induced as an effect of viral infection. The mechanisms of IGF signaling in animal viral infections need to be clarified, mainly because they are involved in multifactorial signaling pathways. The aim of this review is to summarize the current data obtained from virological studies and to increase our understanding of the complex role of the IGF-1 signaling axis in animal virus infections.
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Scott, Alice, and Harry Mellor. "VEGF receptor trafficking in angiogenesis." Biochemical Society Transactions 37, no. 6 (November 19, 2009): 1184–88. http://dx.doi.org/10.1042/bst0371184.

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The intracellular trafficking of receptors provides a way to control the overall sensitivity of a cell to receptor stimulation. These sorting pathways are also used to shape the balance of signals that are generated in response to receptor activation. The major pro-angiogenic growth factor receptor is VEGFR2 (vascular endothelial growth factor 2). VEGFR2 activates a very similar set of signalling pathways to other RTKs (receptor tyrosine kinases); however, its intracellular trafficking is very different. Furthermore, VEGFR2 can form a complex with a range of different angiogenic regulators that in turn regulate the trafficking of VEGFR2 through the endosomal pathway. This regulated trafficking of VEGFR2 has important consequences for angiogenic signalling and is a clear demonstration of how the endosomal pathway plays a critical role in connecting receptor signalling pathways to cellular events.
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Slotkin, T. A., C. Lau, S. E. Lappi, and F. J. Seidler. "Can intracellular signalling pathways predict developmental abnormalities?" Biomarkers 1, no. 2 (January 1996): 115–22. http://dx.doi.org/10.3109/13547509609088679.

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Palozza, Paola, Simona Serini, and Gabriella Calviello. "Carotenoids as Modulators of Intracellular Signaling Pathways." Current Signal Transduction Therapy 1, no. 3 (September 1, 2006): 325–35. http://dx.doi.org/10.2174/157436206778226950.

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Segal, R. A., and M. E. Greenberg. "Intracellular Signaling Pathways Activated by Neuropathic Factors." Annual Review of Neuroscience 19, no. 1 (March 1996): 463–89. http://dx.doi.org/10.1146/annurev.ne.19.030196.002335.

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RASO, VIC, SIMON C. WATKINS, HENRY SLAYTER, and CATHERINE FEHRMANN. "Intracellular Pathways of Ricin A Chain Cytotoxins." Annals of the New York Academy of Sciences 507, no. 1 Biological Ap (December 1987): 172–86. http://dx.doi.org/10.1111/j.1749-6632.1987.tb45800.x.

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Pasquali, Livia, Carla L. Busceti, Federica Fulceri, Antonio Paparelli, and Francesco Fornai. "Intracellular pathways underlying the effects of lithium." Behavioural Pharmacology 21, no. 5-6 (September 2010): 473–92. http://dx.doi.org/10.1097/fbp.0b013e32833da5da.

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Fulop, T., J. M. Witkowski, A. Le Page, C. Fortin, G. Pawelec, and A. Larbi. "Intracellular signalling pathways: targets to reverse immunosenescence." Clinical & Experimental Immunology 187, no. 1 (August 3, 2016): 35–43. http://dx.doi.org/10.1111/cei.12836.

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Britton, Robert S., and Bruce R. Bacon. "Intracellular Signaling Pathways in Stellate Cell Activation." Alcoholism: Clinical and Experimental Research 23, no. 5 (May 1999): 922–25. http://dx.doi.org/10.1111/j.1530-0277.1999.tb04204.x.

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Hoffman, Gregory R., Peter B. Rahl, Ruth N. Collins, and Richard A. Cerione. "Conserved Structural Motifs in Intracellular Trafficking Pathways." Molecular Cell 12, no. 3 (September 2003): 615–25. http://dx.doi.org/10.1016/j.molcel.2003.08.002.

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Kawai, Kumi, and Masahide Takahashi. "Intracellular RET signaling pathways activated by GDNF." Cell and Tissue Research 382, no. 1 (August 20, 2020): 113–23. http://dx.doi.org/10.1007/s00441-020-03262-1.

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Lui, Pak-Yin, Dong-Yan Jin, and Nigel J. Stevenson. "MicroRNA: master controllers of intracellular signaling pathways." Cellular and Molecular Life Sciences 72, no. 18 (June 10, 2015): 3531–42. http://dx.doi.org/10.1007/s00018-015-1940-0.

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Matarese, G. "I25 Intracellular metabolic pathways control immune tolerance." Cytokine 59, no. 3 (September 2012): 496. http://dx.doi.org/10.1016/j.cyto.2012.06.315.

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Daniotti, Jose Luis, and Ramiro Iglesias-Bartolomé. "Metabolic pathways and intracellular trafficking of gangliosides." IUBMB Life 63, no. 7 (June 22, 2011): 513–20. http://dx.doi.org/10.1002/iub.477.

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Ito, Naoki, Urs Ruegg, and Shin’ichi Takeda. "ATP-Induced Increase in Intracellular Calcium Levels and Subsequent Activation of mTOR as Regulators of Skeletal Muscle Hypertrophy." International Journal of Molecular Sciences 19, no. 9 (September 18, 2018): 2804. http://dx.doi.org/10.3390/ijms19092804.

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Abstract (sommario):
Intracellular signaling pathways, including the mammalian target of rapamycin (mTOR) and the mitogen-activated protein kinase (MAPK) pathway, are activated by exercise, and promote skeletal muscle hypertrophy. However, the mechanisms by which these pathways are activated by physiological stimulation are not fully understood. Here we show that extracellular ATP activates these pathways by increasing intracellular Ca2+ levels ([Ca2+]i), and promotes muscle hypertrophy. [Ca2+]i in skeletal muscle was transiently increased after exercise. Treatment with ATP induced the increase in [Ca2+]i through the P2Y2 receptor/inositol 1,4,5-trisphosphate receptor pathway, and subsequent activation of mTOR in vitro. In addition, the ATP-induced increase in [Ca2+]i coordinately activated Erk1/2, p38 MAPK and mTOR that upregulated translation of JunB and interleukin-6. ATP also induced an increase in [Ca2+]i in isolated soleus muscle fibers, but not in extensor digitorum longus muscle fibers. Furthermore, administration of ATP led to muscle hypertrophy in an mTOR- and Ca2+-dependent manner in soleus, but not in plantaris muscle, suggesting that ATP specifically regulated [Ca2+]i in slow muscles. These findings suggest that ATP and [Ca2+]i are important mediators that convert mechanical stimulation into the activation of intracellular signaling pathways, and point to the P2Y receptor as a therapeutic target for treating muscle atrophy.
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Borger, Pieter, Anton Buzdin, Maksim Sorokin, Ekaterina Kachaylo, Bostjan Humar, Rolf Graf, and Pierre-Alien Clavien. "Large-Scale Profiling of Signaling Pathways Reveals a Distinct Demarcation between Normal and Extended Liver Resection." Cells 9, no. 5 (May 7, 2020): 1149. http://dx.doi.org/10.3390/cells9051149.

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Abstract (sommario):
Despite numerous studies addressing normal liver regeneration, we still lack comprehensive understanding of the biological processes underlying failed liver regeneration. Therefore, we analyzed the activity of 271 intracellular signaling pathways (ISPs) by genome wide profiling of differentially expressed RNAs in murine liver tissue biopsies after normal hepatectomy (nHx; 68% of liver removed) and extended hepatectomy (eHx; 86% of liver removed). Comprehensive, genome-wide transcriptome profiling using RNAseq was performed in liver tissue obtained from mice (sham, nHx, and eHx) harvested 1, 8, 16, 32, and 48 h after operation (n = 3 per group) and the OncoFinder toolkit was used for an unsupervised, unbiased identification of intracellular signaling pathways (ISP) activity. We observed that the normal regenerative process requires a transient activation and silencing of approximately two dozen of ISPs. After nHx, the Akt Pathway represented with 13 branches, the Chromatin Pathway and the DDR Pathways dominated. After eHx, the ATM main pathway and two of its branches (Cell Survival; G2_M Checkpoint Arrest) dominated, as well as the Hypoxia Pathways. Further, 14 ISPs demonstrated a strong inverse regulation, with the Hedgehog and the Brca1 Main Pathways as chief activators after nHx, and the ATM Pathway(G2_M Checkpoint Arrest) as the dominating constraining response after eHx.
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45

Henshall, D. C. "Apoptosis signalling pathways in seizure-induced neuronal death and epilepsy." Biochemical Society Transactions 35, no. 2 (March 20, 2007): 421–23. http://dx.doi.org/10.1042/bst0350421.

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Abstract (sommario):
Delineating the molecular pathways underlying seizure-induced neuronal death may yield novel strategies for brain protection against prolonged or repetitive seizures. Glutamate-mediated excitotoxicity and necrosis is a primary contributing mechanism but seizures also activate programmed (apoptotic) cell death pathways. Apoptosis signalling pathways are typically initiated following perturbation of intracellular organelle function (intrinsic pathway) or by activated cell-surface-expressed death receptors (extrinsic pathway), with signalling cascades orchestrated in part by the Bcl-2 and caspase gene families. In this review, evidence for these pathways from experimental seizure modelling and clinical material from patients with intractable temporal lobe epilepsy is examined. Seizures cause mitochondrial dysfunction and activate intrinsic pathway components including pro-apoptotic Bcl-2 family proteins and caspases, processes that may be partly calcium-induced. The ER (endoplasmic reticulum) has emerged as a major intrinsic pathway trigger for apoptosis and its function may also be compromised following seizures and in epilepsy. The extrinsic, death-receptor-dependent pathway is also rapidly engaged following experimental seizures and in patient brain, supporting a previously unexpected apical role for a calcium-independent pathway. When considered alongside emerging functions of apoptosis-regulatory proteins in non-cell-death processes, including regulating intracellular calcium release and neuronal (re)structuring, apoptosis signalling pathways can be viewed as an important developing focus of research into how to obviate the deleterious impact of seizures on the brain.
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46

Kestler, Hans A., and Michael Kühl. "From individual Wnt pathways towards a Wnt signalling network." Philosophical Transactions of the Royal Society B: Biological Sciences 363, no. 1495 (January 11, 2008): 1333–47. http://dx.doi.org/10.1098/rstb.2007.2251.

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Abstract (sommario):
Wnt proteins play important roles during vertebrate and invertebrate development. They obviously have the ability to activate different intracellular signalling pathways. Based on the characteristic intracellular mediators used, these are commonly described as the Wnt/β-catenin, the Wnt/calcium and the Wnt/Jun N-terminal kinase pathways (also called planar cell polarity pathway). In the past, these different signalling events were mainly described as individual and independent signalling branches. Here, we discuss the possibility that Wnt proteins activate a complex intracellular signalling network rather than individual pathways and suggest a graph representation of this network. Furthermore, we discuss different ways of how to predict the specific outcome of an activation of this network in a particular cell type, which will require the use of mathematical models. We point out that the use of deterministic approaches via the application of differential equations is suitable to model only small aspects of the whole network and that more qualitative approaches are possibly a suitable starting point for the prediction of the global behaviour of such large protein interaction networks.
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47

Goldberg, Marcia B. "Actin-Based Motility of Intracellular Microbial Pathogens." Microbiology and Molecular Biology Reviews 65, no. 4 (December 1, 2001): 595–626. http://dx.doi.org/10.1128/mmbr.65.4.595-626.2001.

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SUMMARY A diverse group of intracellular microorganisms, including Listeria monocytogenes, Shigella spp., Rickettsia spp., and vaccinia virus, utilize actin-based motility to move within and spread between mammalian host cells. These organisms have in common a pathogenic life cycle that involves a stage within the cytoplasm of mammalian host cells. Within the cytoplasm of host cells, these organisms activate components of the cellular actin assembly machinery to induce the formation of actin tails on the microbial surface. The assembly of these actin tails provides force that propels the organisms through the cell cytoplasm to the cell periphery or into adjacent cells. Each of these organisms utilizes preexisting mammalian pathways of actin rearrangement to induce its own actin-based motility. Particularly remarkable is that while all of these microbes use the same or overlapping pathways, each intercepts the pathway at a different step. In addition, the microbial molecules involved are each distinctly different from the others. Taken together, these observations suggest that each of these microbes separately and convergently evolved a mechanism to utilize the cellular actin assembly machinery. The current understanding of the molecular mechanisms of microbial actin-based motility is the subject of this review.
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48

Michie, Alison M., and Juan Carlos Zúñiga-Pflücker. "InVivoDetection of Intracellular Signaling Pathways in Developing Thymocytes." Developmental Immunology 8, no. 1 (2000): 31–45. http://dx.doi.org/10.1155/2000/97820.

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Abstract (sommario):
Information regarding the intracellular signaling processes that occur during the development of T cells has largely been obtained with the use of transgenic mouse models, which although providing invaluable information are time consuming and costly. To this end, we have developed a novel system that facilitates theInVivoanalysis of signal transduction pathways during T-lymphocyte development. This approach uses reporter-plasmids for the detection of intracellular signals mediated by the mitogen-activated protein kinase or cyclic AMP-dependent protein kinase. Reporter-plasmids are transfected into thymocytes in fetal thymic organ culture by accelerated DNA/particle bombardment (gene gun), and the activation of a signaling pathway is determined in the form of a standard luciferase assay. Importantly, this powerful technique preserves the structural integrity of the thymus, and will provide an invaluable tool to study how thymocytes respond to normal environmental stimuli encountered during differentiation within the thymic milieu. Thus, this method allows for the monitoring of signals that occur in a biological time frame, such as during differentiation, and within the natural environment of differentiating cells.
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49

Allen, Paige E., and Juan J. Martinez. "Modulation of Host Lipid Pathways by Pathogenic Intracellular Bacteria." Pathogens 9, no. 8 (July 28, 2020): 614. http://dx.doi.org/10.3390/pathogens9080614.

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Abstract (sommario):
Lipids are a broad group of molecules required for cell maintenance and homeostasis. Various intracellular pathogens have developed mechanisms of modulating and sequestering host lipid processes for a large array of functions for both bacterial and host cell survival. Among the host cell lipid functions that intracellular bacteria exploit for infection are the modulation of host plasma membrane microdomains (lipid rafts) required for efficient bacterial entry; the recruitment of specific lipids for membrane integrity of intracellular vacuoles; and the utilization of host lipid droplets for the regulation of immune responses and for energy production through fatty acid β-oxidation and oxidative phosphorylation. The majority of published studies on the utilization of these host lipid pathways during infection have focused on intracellular bacterial pathogens that reside within a vacuole during infection and, thus, have vastly different requirements for host lipid metabolites when compared to those intracellular pathogens that are released into the host cytosol upon infection. Here we summarize the mechanisms by which intracellular bacteria sequester host lipid species and compare the modulation of host lipid pathways and metabolites during host cell infection by intracellular pathogens residing in either a vacuole or within the cytosol of infected mammalian cells. This review will also highlight common and unique host pathways necessary for intracellular bacterial growth that could potentially be targeted for therapeutic intervention.
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50

Kim, Soochong, and Satya P. Kunapuli. "Negative Regulation of Gq-mediated Pathways in Platelets by G12/13 Pathways through Fyn Kinase." Journal of Biological Chemistry 286, no. 27 (May 18, 2011): 24170–79. http://dx.doi.org/10.1074/jbc.m110.212274.

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Abstract (sommario):
Platelets contain high levels of Src family kinases (SFKs), but their functional role downstream of G protein pathways has not been completely understood. We found that platelet shape change induced by selective G12/13 stimulation was potentiated by SFK inhibitors, which was abolished by intracellular calcium chelation. Platelet aggregation, secretion, and intracellular Ca2+ mobilization mediated by low concentrations of SFLLRN or YFLLRNP were potentiated by SFK inhibitors. However, 2-methylthio-ADP-induced intracellular Ca2+ mobilization and platelet aggregation were not affected by PP2, suggesting the contribution of SFKs downstream of G12/13, but not Gq/Gi, as a negative regulator to platelet activation. Moreover, PP2 potentiated YFLLRNP- and AYPGKF-induced PKC activation, indicating that SFKs downstream of G12/13 regulate platelet responses through the negative regulation of PKC activation as well as calcium response. SFK inhibitors failed to potentiate platelet responses in the presence of Gq-selective inhibitor YM254890 or in Gq-deficient platelets, indicating that SFKs negatively regulate platelet responses through modulation of Gq pathways. Importantly, AYPGKF-induced platelet aggregation and PKC activation were potentiated in Fyn-deficient but not in Lyn-deficient mice compared with wild-type littermates. We conclude that SFKs, especially Fyn, activated downstream of G12/13 negatively regulate platelet responses by inhibiting intracellular calcium mobilization and PKC activation through Gq pathways.
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