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Artículos de revistas sobre el tema "Cellular Signaling"

Autor: Grafiati
Publicado: 4 de junio de 2021
Última modificación: 13 de febrero de 2022

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1

Toker, Alex, and Alexandra C. Newton. "Cellular Signaling." Cell 103, no. 2 (2000): 185–88. http://dx.doi.org/10.1016/s0092-8674(00)00110-0.

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2

Brownlee, Christen. "Illuminating Cellular Signaling." ACS Chemical Biology 2, no. 3 (2007): 149–51. http://dx.doi.org/10.1021/cb7000445.

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3

Gough, N. R., and L. B. Ray. "Mapping Cellular Signaling." Science Signaling 2002, no. 135 (2002): eg8-eg8. http://dx.doi.org/10.1126/stke.2002.135.eg8.

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4

Marshall, Chris, and Werner Müller-Esterl. "Spotlight on Cellular Signaling." Molecular Cell 15, no. 6 (2004): 849–52. http://dx.doi.org/10.1016/j.molcel.2004.09.014.

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5

Wheelock, Margaret J., and Keith R. Johnson. "Cadherin-mediated cellular signaling." Current Opinion in Cell Biology 15, no. 5 (2003): 509–14. http://dx.doi.org/10.1016/s0955-0674(03)00101-7.

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6

Papin, Jason, and Shankar Subramaniam. "Bioinformatics and cellular signaling." Current Opinion in Biotechnology 15, no. 1 (2004): 78–81. http://dx.doi.org/10.1016/j.copbio.2004.01.003.

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7

Kim, William J. H. "Cellular signaling in tissue regeneration." Yonsei Medical Journal 41, no. 6 (2000): 692. http://dx.doi.org/10.3349/ymj.2000.41.6.692.

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8

TUAN, ROCKY S. "CELLULAR SIGNALING IN DEVELOPMENTAL CHONDROGENESIS." Journal of Bone and Joint Surgery-American Volume 85 (2003): 137–41. http://dx.doi.org/10.2106/00004623-200300002-00019.

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9

Chen, Wen G., and Forest M. White. "Proteomic analysis of cellular signaling." Expert Review of Proteomics 1, no. 3 (2004): 343–54. http://dx.doi.org/10.1586/14789450.1.3.343.

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10

Schlessinger, J. "CELLULAR SIGNALING BY TYROSINE PHOSPHORYLATION." Biochemical Society Transactions 28, no. 5 (2000): A128. http://dx.doi.org/10.1042/bst028a128.

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11

Sheen, Jen. "Discover and Connect Cellular Signaling." Plant Physiology 154, no. 2 (2010): 562–66. http://dx.doi.org/10.1104/pp.110.161364.

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12

Brier, Matthew I., and Jonathan S. Dordick. "Remote activation of cellular signaling." Science 368, no. 6494 (2020): 936–37. http://dx.doi.org/10.1126/science.abb9122.

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13

de Groot, P. G., and R. T. Urbanus. "Cellular signaling by antiphospholipid antibodies." Journal of Thrombosis and Haemostasis 12, no. 5 (2014): 773–75. http://dx.doi.org/10.1111/jth.12540.

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14

Baskin, Laurence S. "Cellular signaling in the bladder." Frontiers in Bioscience 2, no. 4 (1997): d592–595. http://dx.doi.org/10.2741/a215.

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15

White, Forest M. "PROTEOMIC ANALYSIS OF CELLULAR SIGNALING." Shock 21, Supplement (2004): 3. http://dx.doi.org/10.1097/00024382-200403001-00010.

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16

Boulware, Michael J., and Jonathan S. Marchant. "Timing in Cellular Ca2+ Signaling." Current Biology 18, no. 17 (2008): R769—R776. http://dx.doi.org/10.1016/j.cub.2008.07.018.

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17

Pahwa, Roma, and Ishwarlal Jialal. "Cellular Signaling in Metabolic Syndrome." Metabolic Syndrome and Related Disorders 13, no. 9 (2015): 371–72. http://dx.doi.org/10.1089/met.2015.29001.jia.

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18

Teh, Jessica L. F., and Suzie Chen. "Glutamatergic signaling in cellular transformation." Pigment Cell & Melanoma Research 25, no. 3 (2012): 331–42. http://dx.doi.org/10.1111/j.1755-148x.2012.00983.x.

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19

Torres, Vicente E., and Albert C. M. Ong. "Cellular signaling in PKD: foreword." Cellular Signalling 71 (July 2020): 109625. http://dx.doi.org/10.1016/j.cellsig.2020.109625.

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20

Pryciak, Peter M. "Designing New Cellular Signaling Pathways." Chemistry & Biology 16, no. 3 (2009): 249–54. http://dx.doi.org/10.1016/j.chembiol.2009.01.011.

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21

Martin, Nadine, and David Bernard. "Calcium signaling and cellular senescence." Cell Calcium 70 (March 2018): 16–23. http://dx.doi.org/10.1016/j.ceca.2017.04.001.

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22

Boscher, Cecile, James W. Dennis, and Ivan R. Nabi. "Glycosylation, galectins and cellular signaling." Current Opinion in Cell Biology 23, no. 4 (2011): 383–92. http://dx.doi.org/10.1016/j.ceb.2011.05.001.

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23

Ren, Jian-Lin, Jin-Shui Pan, Ya-Pi Lu, Peiqing Sun, and Jiahuai Han. "Inflammatory signaling and cellular senescence." Cellular Signalling 21, no. 3 (2009): 378–83. http://dx.doi.org/10.1016/j.cellsig.2008.10.011.

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24

Gregory, TD. "Inositol lipids in cellular signaling." Biochemical Education 16, no. 2 (1988): 117. http://dx.doi.org/10.1016/0307-4412(88)90105-7.

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25

Mekahli, D., Jan B. Parys, G. Bultynck, L. Missiaen, and H. De Smedt. "Polycystins and cellular Ca2+ signaling." Cellular and Molecular Life Sciences 70, no. 15 (2012): 2697–712. http://dx.doi.org/10.1007/s00018-012-1188-x.

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26

Michel, Thomas, and Paul M. Vanhoutte. "Cellular signaling and NO production." Pflügers Archiv - European Journal of Physiology 459, no. 6 (2010): 807–16. http://dx.doi.org/10.1007/s00424-009-0765-9.

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27

Ding, Xianting, Peter O. Krutzik, Amir Ali Ghaffari, et al. "Cellular Signaling Analysis shows antiviral, ribavirin-mediated ribosomal signaling modulation." Antiviral Research 171 (November 2019): 104598. http://dx.doi.org/10.1016/j.antiviral.2019.104598.

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28

., ,. "Dynamics of cellular NO-cGMP signaling." Frontiers in Bioscience 10, no. 1-3 (2005): 1868. http://dx.doi.org/10.2741/1666.

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29

Lammi, Mikko. "Cellular Signaling in Cartilage Tissue Engineering." Current Signal Transduction Therapy 2, no. 1 (2007): 41–48. http://dx.doi.org/10.2174/157436207779317155.

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30

Slinger, Erik, Ellen Langemeijer, Marco Siderius, Henry F. Vischer, and Martine J. Smit. "Herpesvirus-encoded GPCRs rewire cellular signaling." Molecular and Cellular Endocrinology 331, no. 2 (2011): 179–84. http://dx.doi.org/10.1016/j.mce.2010.04.007.

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31

Morton, David B., and P. Jeanette Simpson. "Cellular signaling in eclosion hormone action." Journal of Insect Physiology 48, no. 1 (2002): 1–13. http://dx.doi.org/10.1016/s0022-1910(01)00157-3.

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32

Babcock, Donner F., and Bertil Hille. "Mitochondrial oversight of cellular Ca2+ signaling." Current Opinion in Neurobiology 8, no. 3 (1998): 398–404. http://dx.doi.org/10.1016/s0959-4388(98)80067-6.

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33

WILKINSON, SOPHIE. "Big Science Takes On Cellular Signaling." Chemical & Engineering News 78, no. 42 (2000): 24. http://dx.doi.org/10.1021/cen-v078n042.p024.

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34

Jerius, Hilde, Arthur Beall, David Woodrum, Aaron Epstein, and Colleen Brophy. "Thrombin-induced vasospasm: Cellular signaling mechanisms." Surgery 123, no. 1 (1998): 46–50. http://dx.doi.org/10.1016/s0039-6060(98)70227-2.

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35

Ramchandran, Ramam, S. Ananth Karumanchi, Jun-ichi Hanai, Seth L. Alper, and Vikas P. Sukhatme. "Cellular Actions and Signaling by Endostatin." Critical Reviews™ in Eukaryotic Gene Expression 12, no. 3 (2002): 17. http://dx.doi.org/10.1615/critreveukargeneexpr.v12.i3.20.

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36

Ramchandran, Ramam, S. Ananth Karumanchi, Jun-ichi Hanai, Seth L. Alper, and Vikas P. Sukhatme. "Cellular Actions and Signaling by Endostatin." Critical Reviews? in Eukaryotic Gene Expression 12, no. 3 (2002): 175–92. http://dx.doi.org/10.1615/critreveukaryotgeneexpr.v12.i3.20.

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37

Li, Haisheng, Yang Wei, Yuanjie Huang, Qiang Cai, and Junping Du. "Visual analytics of cellular signaling data." Multimedia Tools and Applications 78, no. 20 (2018): 29447–61. http://dx.doi.org/10.1007/s11042-018-6966-5.

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38

Iwanaga, Tsuyoshi, Ryouhei Tsutsumi, Jun Noritake, Yuko Fukata, and Masaki Fukata. "Dynamic protein palmitoylation in cellular signaling." Progress in Lipid Research 48, no. 3-4 (2009): 117–27. http://dx.doi.org/10.1016/j.plipres.2009.02.001.

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39

Nick, P. "Plant immunity – cellular aspects of signaling." Protoplasma 230, no. 1-2 (2007): V. http://dx.doi.org/10.1007/s00709-007-0252-0.

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40

Cheng, Xiaolin, and Jeremy C. Smith. "Biological Membrane Organization and Cellular Signaling." Chemical Reviews 119, no. 9 (2019): 5849–80. http://dx.doi.org/10.1021/acs.chemrev.8b00439.

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41

Hunyady, László. "Cellular signaling in health and disease." Molecular and Cellular Endocrinology 353, no. 1-2 (2012): 1–2. http://dx.doi.org/10.1016/j.mce.2012.01.012.

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42

Kim, Hong Pyo, Stefan W. Ryter, and Augustine M. K. Choi. "CO AS A CELLULAR SIGNALING MOLECULE." Annual Review of Pharmacology and Toxicology 46, no. 1 (2006): 411–49. http://dx.doi.org/10.1146/annurev.pharmtox.46.120604.141053.

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43

Zhang, Jixiang, Xiaoli Wang, Vikash Vikash, et al. "ROS and ROS-Mediated Cellular Signaling." Oxidative Medicine and Cellular Longevity 2016 (2016): 1–18. http://dx.doi.org/10.1155/2016/4350965.

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Resumen
It has long been recognized that an increase of reactive oxygen species (ROS) can modify the cell-signaling proteins and have functional consequences, which successively mediate pathological processes such as atherosclerosis, diabetes, unchecked growth, neurodegeneration, inflammation, and aging. While numerous articles have demonstrated the impacts of ROS on various signaling pathways and clarify the mechanism of action of cell-signaling proteins, their influence on the level of intracellular ROS, and their complex interactions among multiple ROS associated signaling pathways, the systemic summary is necessary. In this review paper, we particularly focus on the pattern of the generation and homeostasis of intracellular ROS, the mechanisms and targets of ROS impacting on cell-signaling proteins (NF-κB, MAPKs, Keap1-Nrf2-ARE, and PI3K-Akt), ion channels and transporters (Ca2+and mPTP), and modifying protein kinase and Ubiquitination/Proteasome System.
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44

Karpen, J. W. "The Fourth Dimension in Cellular Signaling." Science 293, no. 5538 (2001): 2204–5. http://dx.doi.org/10.1126/science.293.5538.2204.

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45

de Graauw, Marjo, Paul Hensbergen, and Bob van de Water. "Phospho-proteomic analysis of cellular signaling." ELECTROPHORESIS 27, no. 13 (2006): 2676–86. http://dx.doi.org/10.1002/elps.200600018.

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46

Gow, Andrew J., and Harry Ischiropoulos. "Nitric oxide chemistry and cellular signaling." Journal of Cellular Physiology 187, no. 3 (2001): 277–82. http://dx.doi.org/10.1002/jcp.1085.

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47

Adams, Levi, Maria C. Franco, and Alvaro G. Estevez. "Reactive nitrogen species in cellular signaling." Experimental Biology and Medicine 240, no. 6 (2015): 711–17. http://dx.doi.org/10.1177/1535370215581314.

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48

KOSIK, K. S., W. Q. QIU, and S. GREENBERG. "Cellular Signaling Pathways and Cytoskeletal Organization." Annals of the New York Academy of Sciences 777, no. 1 (1996): 114–20. http://dx.doi.org/10.1111/j.1749-6632.1996.tb34409.x.

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49

Wen, X., H. H. Lin, and D. K. Ann. "Salivary Cellular Signaling and Gene Regulation." Advances in Dental Research 14, no. 1 (2000): 76–80. http://dx.doi.org/10.1177/08959374000140011201.

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Protein tyrosine kinase and protein serine kinase activation has been implicated in the regulation of salivary cell proliferation and differentiation. Aberrant expression and alterations of certain tyrosine or serine kinases, such as Raf or erbB2, are known to trigger salivary tumor development (Li et al., 1997; Cho et al., 1999). It has been estimated that there are about 1000 to 2000 protein kinases in the mammalian genome, with 100 to 200 of them ( i.e., 10%) being tyrosine kinase (Hanks and Hunter, 1995). At present, there are approximately 85 different tyrosine kinases identified in the GenBank database. Based on the relatively slow rate of discovery in the past few years, 100 is a better approximation of the total number of tyrosine kinases encoded by each mammalian genome. It is reasonable to assume that there are about 30 to 50 tyrosine kinases expressed in a given cell at a given differentiation/proliferation stage. This number is large enough to provide a characteristic tissue-specific tyrosine kinase expression profile, but small enough to be identified in a simple screening. The hope for tyrosine kinases as differentiation or proliferation markers rests with the possibility for the identification and characterization of a differentiation/proliferation stage-specific expression pattern in salivary cells. Several ligands that transmit signal through receptor tyrosine kinases and/or Ras/Raf/ERK kinases have been extensively studied in salivary cells. This review focuses mainly on the signaling pathways activated bv Raf and Etk.
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50

Barbour, Jayne Alexandra, and Nigel Turner. "Mitochondrial Stress Signaling Promotes Cellular Adaptations." International Journal of Cell Biology 2014 (2014): 1–12. http://dx.doi.org/10.1155/2014/156020.

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Mitochondrial dysfunction has been implicated in the aetiology of many complex diseases, as well as the ageing process. Much of the research on mitochondrial dysfunction has focused on how mitochondrial damage may potentiate pathological phenotypes. The purpose of this review is to draw attention to the less well-studied mechanisms by which the cell adapts to mitochondrial perturbations. This involves communication of stress to the cell and successful induction of quality control responses, which include mitophagy, unfolded protein response, upregulation of antioxidant and DNA repair enzymes, morphological changes, and if all else fails apoptosis. The mitochondrion is an inherently stressful environment and we speculate that dysregulation of stress signaling or an inability to switch on these adaptations during times of mitochondrial stress may underpin mitochondrial dysfunction and hence amount to pathological states over time.
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