Artículos de revistas sobre el tema "ERM PROTEINS"
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McClatchey, Andrea I. "ERM proteins". Current Biology 22, n.º 18 (septiembre de 2012): R784—R785. http://dx.doi.org/10.1016/j.cub.2012.07.057.
Texto completoMcClatchey, Andrea I. "ERM proteins at a glance". Journal of Cell Science 127, n.º 15 (20 de junio de 2014): 3199–204. http://dx.doi.org/10.1242/jcs.098343.
Texto completoClucas, J. y F. Valderrama. "ERM proteins in cancer progression". Journal of Cell Science 127, n.º 2 (13 de enero de 2014): 267–75. http://dx.doi.org/10.1242/jcs.133108.
Texto completoClucas, J. y F. Valderrama. "ERM proteins in cancer progression". Journal of Cell Science 128, n.º 6 (15 de marzo de 2015): 1253. http://dx.doi.org/10.1242/jcs.170027.
Texto completoBagchi, M., M. Katar, W. K. Lo, R. Yost, C. Hill y H. Maisel. "ERM proteins of the lens". Journal of Cellular Biochemistry 92, n.º 3 (2004): 626–30. http://dx.doi.org/10.1002/jcb.20062.
Texto completoKondo, Takahisa, Kosei Takeuchi, Yoshinori Doi, Shigenobu Yonemura, Shigekazu Nagata, Shoichiro Tsukita y Sachiko Tsukita. "ERM (Ezrin/Radixin/Moesin)-based Molecular Mechanism of Microvillar Breakdown at an Early Stage of Apoptosis". Journal of Cell Biology 139, n.º 3 (3 de noviembre de 1997): 749–58. http://dx.doi.org/10.1083/jcb.139.3.749.
Texto completoYonemura, Shigenobu, Takeshi Matsui, Shoichiro Tsukita y Sachiko Tsukita. "Rho-dependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: an essential role for polyphosphoinositides in vivo". Journal of Cell Science 115, n.º 12 (15 de junio de 2002): 2569–80. http://dx.doi.org/10.1242/jcs.115.12.2569.
Texto completoHirao, M., N. Sato, T. Kondo, S. Yonemura, M. Monden, T. Sasaki, Y. Takai, S. Tsukita y S. Tsukita. "Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway." Journal of Cell Biology 135, n.º 1 (1 de octubre de 1996): 37–51. http://dx.doi.org/10.1083/jcb.135.1.37.
Texto completoYonemura, Shigenobu, Sachiko Tsukita y Shoichiro Tsukita. "Direct Involvement of Ezrin/Radixin/Moesin (ERM)-binding Membrane Proteins in the Organization of Microvilli in Collaboration with Activated ERM Proteins". Journal of Cell Biology 145, n.º 7 (28 de junio de 1999): 1497–509. http://dx.doi.org/10.1083/jcb.145.7.1497.
Texto completoMichie, Katharine A., Adam Bermeister, Neil O. Robertson, Sophia C. Goodchild y Paul M. G. Curmi. "Two Sides of the Coin: Ezrin/Radixin/Moesin and Merlin Control Membrane Structure and Contact Inhibition". International Journal of Molecular Sciences 20, n.º 8 (23 de abril de 2019): 1996. http://dx.doi.org/10.3390/ijms20081996.
Texto completoAdyshev, Djanybek M., Steven M. Dudek, Nurgul Moldobaeva, Kyung-mi Kim, Shwu-Fan Ma, Anita Kasa, Joe G. N. Garcia y Alexander D. Verin. "Ezrin/radixin/moesin proteins differentially regulate endothelial hyperpermeability after thrombin". American Journal of Physiology-Lung Cellular and Molecular Physiology 305, n.º 3 (1 de agosto de 2013): L240—L255. http://dx.doi.org/10.1152/ajplung.00355.2012.
Texto completoTavasoli, Mahtab, Abass Al-Momany, Xin Wang, Laiji Li, John C. Edwards y Barbara J. Ballermann. "Both CLIC4 and CLIC5A activate ERM proteins in glomerular endothelium". American Journal of Physiology-Renal Physiology 311, n.º 5 (1 de noviembre de 2016): F945—F957. http://dx.doi.org/10.1152/ajprenal.00353.2016.
Texto completoChen, Emily, Meredith Shaffer, Verena Niggli y Janis Burkhardt. "Flotillins and ERM proteins function to promote uropod formation in T cells (44.10)". Journal of Immunology 184, n.º 1_Supplement (1 de abril de 2010): 44.10. http://dx.doi.org/10.4049/jimmunol.184.supp.44.10.
Texto completoRobertson, Tanner Ford, Daniel Blumenthal, Vidhi Chandra y Janis K. Burkhardt. "ERM family proteins regulate T cell signal initiation by limiting Lck activity and T cell receptor clustering." Journal of Immunology 198, n.º 1_Supplement (1 de mayo de 2017): 136.6. http://dx.doi.org/10.4049/jimmunol.198.supp.136.6.
Texto completoGloerich, Martijn, Bas Ponsioen, Marjolein J. Vliem, Zhongchun Zhang, Jun Zhao, Matthijs R. Kooistra, Leo S. Price et al. "Spatial Regulation of Cyclic AMP-Epac1 Signaling in Cell Adhesion by ERM Proteins". Molecular and Cellular Biology 30, n.º 22 (20 de septiembre de 2010): 5421–31. http://dx.doi.org/10.1128/mcb.00463-10.
Texto completoHao, Jian-Jiang, Yin Liu, Michael Kruhlak, Karen E. Debell, Barbara L. Rellahan y Stephen Shaw. "Phospholipase C–mediated hydrolysis of PIP2 releases ERM proteins from lymphocyte membrane". Journal of Cell Biology 184, n.º 3 (9 de febrero de 2009): 451–62. http://dx.doi.org/10.1083/jcb.200807047.
Texto completoLopez, James P., Jerrold R. Turner y Louis H. Philipson. "Glucose-induced ERM protein activation and translocation regulates insulin secretion". American Journal of Physiology-Endocrinology and Metabolism 299, n.º 5 (noviembre de 2010): E772—E785. http://dx.doi.org/10.1152/ajpendo.00199.2010.
Texto completoGandy, K. Alexa Orr, Daniel Canals, Mohamad Adada, Masayuki Wada, Patrick Roddy, Ashley J. Snider, Yusuf A. Hannun y Lina M. Obeid. "Sphingosine 1-phosphate induces filopodia formation through S1PR2 activation of ERM proteins". Biochemical Journal 449, n.º 3 (9 de enero de 2013): 661–72. http://dx.doi.org/10.1042/bj20120213.
Texto completoYang, Hai-Su, Kamilah Alexander, Pedro Santiago y Philip W. Hinds. "ERM Proteins and Cdk5 in Cellular Senescence". Cell Cycle 2, n.º 6 (28 de noviembre de 2003): 517–20. http://dx.doi.org/10.4161/cc.2.6.582.
Texto completoProudfit, Austin, Nabanita Bhunia, Debasis Pore, Yvonne Parker, Daniel Lindner y Neetu Gupta. "Pharmacologic Inhibition of Ezrin-Radixin-Moesin Phosphorylation is a Novel Therapeutic Strategy in Rhabdomyosarcoma". Sarcoma 2020 (9 de septiembre de 2020): 1–11. http://dx.doi.org/10.1155/2020/9010496.
Texto completoRamalho, João J., Jorian J. Sepers, Ophélie Nicolle, Ruben Schmidt, Janine Cravo, Grégoire Michaux y Mike Boxem. "C-terminal phosphorylation modulates ERM-1 localization and dynamics to control cortical actin organization and support lumen formation during Caenorhabditiselegans development". Development 147, n.º 14 (25 de junio de 2020): dev188011. http://dx.doi.org/10.1242/dev.188011.
Texto completoYonemura, Shigenobu, Motohiro Hirao, Yoshinori Doi, Nobuyuki Takahashi, Takahisa Kondo, Sachiko Tsukita y Shoichiro Tsukita. "Ezrin/Radixin/Moesin (ERM) Proteins Bind to a Positively Charged Amino Acid Cluster in the Juxta-Membrane Cytoplasmic Domain of CD44, CD43, and ICAM-2". Journal of Cell Biology 140, n.º 4 (23 de febrero de 1998): 885–95. http://dx.doi.org/10.1083/jcb.140.4.885.
Texto completoDickson, Tracey C., C. David Mintz, Deanna L. Benson y Stephen R. J. Salton. "Functional binding interaction identified between the axonal CAM L1 and members of the ERM family". Journal of Cell Biology 157, n.º 7 (17 de junio de 2002): 1105–12. http://dx.doi.org/10.1083/jcb.200111076.
Texto completoTreanor, Bebhinn, David Depoil, Andreas Bruckbauer y Facundo D. Batista. "Dynamic cortical actin remodeling by ERM proteins controls BCR microcluster organization and integrity". Journal of Experimental Medicine 208, n.º 5 (11 de abril de 2011): 1055–68. http://dx.doi.org/10.1084/jem.20101125.
Texto completoChirivino, Dafne, Laurence Del Maestro, Etienne Formstecher, Philippe Hupé, Graça Raposo, Daniel Louvard y Monique Arpin. "The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes". Molecular Biology of the Cell 22, n.º 3 (febrero de 2011): 375–85. http://dx.doi.org/10.1091/mbc.e10-09-0796.
Texto completoAsano, Shinji. "Functional Regulation of Transport Proteins by ERM (Ezrin / Radixin / Moesin) Proteins". membrane 35, n.º 6 (2010): 278–84. http://dx.doi.org/10.5360/membrane.35.278.
Texto completoKobori, Takuro, Mayuka Tameishi, Chihiro Tanaka, Yoko Urashima y Tokio Obata. "Subcellular distribution of ezrin/radixin/moesin and their roles in the cell surface localization and transport function of P-glycoprotein in human colon adenocarcinoma LS180 cells". PLOS ONE 16, n.º 5 (11 de mayo de 2021): e0250889. http://dx.doi.org/10.1371/journal.pone.0250889.
Texto completoRasmussen, Maria, R. Todd Alexander, Barbara V. Darborg, Nadja Møbjerg, Else K. Hoffmann, András Kapus y Stine F. Pedersen. "Osmotic cell shrinkage activates ezrin/radixin/moesin (ERM) proteins: activation mechanisms and physiological implications". American Journal of Physiology-Cell Physiology 294, n.º 1 (enero de 2008): C197—C212. http://dx.doi.org/10.1152/ajpcell.00268.2007.
Texto completoMatsui, Takeshi, Masato Maeda, Yoshinori Doi, Shigenobu Yonemura, Mutsuki Amano, Kozo Kaibuchi, Sachiko Tsukita y Shoichiro Tsukita. "Rho-Kinase Phosphorylates COOH-terminal Threonines of Ezrin/Radixin/Moesin (ERM) Proteins and Regulates Their Head-to-Tail Association". Journal of Cell Biology 140, n.º 3 (9 de febrero de 1998): 647–57. http://dx.doi.org/10.1083/jcb.140.3.647.
Texto completoZegers, Ingrid, Thomas Keller, Wiebke Schreiber, Joanna Sheldon, Riccardo Albertini, Søren Blirup-Jensen, Myron Johnson et al. "Characterization of the New Serum Protein Reference Material ERM-DA470k/IFCC: Value Assignment by Immunoassay". Clinical Chemistry 56, n.º 12 (1 de diciembre de 2010): 1880–88. http://dx.doi.org/10.1373/clinchem.2010.148809.
Texto completoWinckler, B., C. Gonzalez Agosti, M. Magendantz y F. Solomon. "Analysis of a cortical cytoskeletal structure: a role for ezrin-radixin-moesin (ERM proteins) in the marginal band of chicken erythrocytes". Journal of Cell Science 107, n.º 9 (1 de septiembre de 1994): 2523–34. http://dx.doi.org/10.1242/jcs.107.9.2523.
Texto completoBaeyens, Nicolas, Sandrine Horman, Didier Vertommen, Mark Rider y Nicole Morel. "Identification and functional implication of a Rho kinase-dependent moesin-EBP50 interaction in noradrenaline-stimulated artery". American Journal of Physiology-Cell Physiology 299, n.º 6 (diciembre de 2010): C1530—C1540. http://dx.doi.org/10.1152/ajpcell.00175.2010.
Texto completoCannon, J. L., P. D. Mody, K. M. Blaine, E. J. Chen, A. D. Nelson, L. J. Sayles, T. V. Moore et al. "CD43 interaction with ezrin-radixin-moesin (ERM) proteins regulates T-cell trafficking and CD43 phosphorylation". Molecular Biology of the Cell 22, n.º 7 (abril de 2011): 954–63. http://dx.doi.org/10.1091/mbc.e10-07-0586.
Texto completoMori, T., K. Kitano, S. Terawaki, R. Maesaki, Y. Fukami y T. Hakoshima. "Structural basis for CD44 recognition by ERM proteins". Acta Crystallographica Section A Foundations of Crystallography 64, a1 (23 de agosto de 2008): C233—C234. http://dx.doi.org/10.1107/s0108767308092490.
Texto completoTerawaki, Shin-ichi, Ryoko Maesaki y Toshio Hakoshima. "Structural Basis for NHERF Recognition by ERM Proteins". Structure 14, n.º 4 (abril de 2006): 777–89. http://dx.doi.org/10.1016/j.str.2006.01.015.
Texto completoLouvet-Vallée, Sophie. "ERM proteins: From cellular architecture to cell signaling". Biology of the Cell 92, n.º 5 (agosto de 2000): 305–16. http://dx.doi.org/10.1016/s0248-4900(00)01078-9.
Texto completoMangeat, Paul, Christian Roy y Marianne Martin. "ERM proteins in cell adhesion and membrane dynamics". Trends in Cell Biology 9, n.º 5 (mayo de 1999): 187–92. http://dx.doi.org/10.1016/s0962-8924(99)01544-5.
Texto completoFiévet, Bruno, Daniel Louvard y Monique Arpin. "ERM proteins in epithelial cell organization and functions". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1773, n.º 5 (mayo de 2007): 653–60. http://dx.doi.org/10.1016/j.bbamcr.2006.06.013.
Texto completoMori, Tomoyuki, Ken Kitano, Shin-ichi Terawaki, Ryoko Maesaki, Yayoi Fukami y Toshio Hakoshima. "Structural Basis for CD44 Recognition by ERM Proteins". Journal of Biological Chemistry 283, n.º 43 (27 de agosto de 2008): 29602–12. http://dx.doi.org/10.1074/jbc.m803606200.
Texto completoMintz, C. David, Ioana Carcea, Daniel G. McNickle, Tracey C. Dickson, Yongchao Ge, Stephen R. J. Salton y Deanna L. Benson. "ERM proteins regulate growth cone responses to Sema3A". Journal of Comparative Neurology 510, n.º 4 (1 de octubre de 2008): 351–66. http://dx.doi.org/10.1002/cne.21799.
Texto completoBrown, Martin J., Ruchika Nijhara, John A. Hallam, Michelle Gignac, Kenneth M. Yamada, Stanley L. Erlandsen, Jérôme Delon, Michael Kruhlak y Stephen Shaw. "Chemokine stimulation of human peripheral blood T lymphocytes induces rapid dephosphorylation of ERM proteins, which facilitates loss of microvilli and polarization". Blood 102, n.º 12 (1 de diciembre de 2003): 3890–99. http://dx.doi.org/10.1182/blood-2002-12-3807.
Texto completoHayashi, K., S. Yonemura, T. Matsui y S. Tsukita. "Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues". Journal of Cell Science 112, n.º 8 (15 de abril de 1999): 1149–58. http://dx.doi.org/10.1242/jcs.112.8.1149.
Texto completoHoshi, Yutaro, Yasuo Uchida, Takashi Kuroda, Masanori Tachikawa, Pierre-Olivier Couraud, Takashi Suzuki y Tetsuya Terasaki. "Distinct roles of ezrin, radixin and moesin in maintaining the plasma membrane localizations and functions of human blood–brain barrier transporters". Journal of Cerebral Blood Flow & Metabolism 40, n.º 7 (14 de agosto de 2019): 1533–45. http://dx.doi.org/10.1177/0271678x19868880.
Texto completoSolinet, Sara, Kazi Mahmud, Shannon F. Stewman, Khaled Ben El Kadhi, Barbara Decelle, Lama Talje, Ao Ma, Benjamin H. Kwok y Sébastien Carreno. "The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex". Journal of Cell Biology 202, n.º 2 (15 de julio de 2013): 251–60. http://dx.doi.org/10.1083/jcb.201304052.
Texto completoMcCartney, B. M. y R. G. Fehon. "Distinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumor suppressor, merlin." Journal of Cell Biology 133, n.º 4 (15 de mayo de 1996): 843–52. http://dx.doi.org/10.1083/jcb.133.4.843.
Texto completoOrian-Rousseau, Véronique, Helen Morrison, Alexandra Matzke, Thor Kastilan, Giuseppina Pace, Peter Herrlich y Helmut Ponta. "Hepatocyte Growth Factor-induced Ras Activation Requires ERM Proteins Linked to Both CD44v6 and F-Actin". Molecular Biology of the Cell 18, n.º 1 (enero de 2007): 76–83. http://dx.doi.org/10.1091/mbc.e06-08-0674.
Texto completoIwase, Akira, Ruoqian Shen, Daniel Navarro y David M. Nanus. "Direct Binding of Neutral Endopeptidase 24.11 to Ezrin/Radixin/Moesin (ERM) Proteins Competes with the Interaction of CD44 with ERM Proteins". Journal of Biological Chemistry 279, n.º 12 (2 de enero de 2004): 11898–905. http://dx.doi.org/10.1074/jbc.m212737200.
Texto completoPhang, Juanita M., Stephen J. Harrop, Anthony P. Duff, Anna V. Sokolova, Ben Crossett, James C. Walsh, Simone A. Beckham et al. "Structural characterization suggests models for monomeric and dimeric forms of full-length ezrin". Biochemical Journal 473, n.º 18 (12 de septiembre de 2016): 2763–82. http://dx.doi.org/10.1042/bcj20160541.
Texto completoHebert, A. M., B. DuBoff, J. B. Casaletto, A. B. Gladden y A. I. McClatchey. "Merlin/ERM proteins establish cortical asymmetry and centrosome position". Genes & Development 26, n.º 24 (15 de diciembre de 2012): 2709–23. http://dx.doi.org/10.1101/gad.194027.112.
Texto completoFehon, Richard G., Andrea I. McClatchey y Anthony Bretscher. "Organizing the cell cortex: the role of ERM proteins". Nature Reviews Molecular Cell Biology 11, n.º 4 (abril de 2010): 276–87. http://dx.doi.org/10.1038/nrm2866.
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