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Saracaloglu, Ahmet, Seniz Demiryürek, Sabit Kimyon, Alper Mete, Ebru Temiz, Gülper Nacarkahya, Oguzhan Saygili, Kıvanc Güngör i Abdullah Tuncay Demiryürek. "RHO Gene Polymorphisms in Patients with Pterygium". Proceedings 2, nr 25 (6.12.2018): 1572. http://dx.doi.org/10.3390/proceedings2251572.
Pełny tekst źródłaGuasch, Rosa M., Peter Scambler, Gareth E. Jones i Anne J. Ridley. "RhoE Regulates Actin Cytoskeleton Organization and Cell Migration". Molecular and Cellular Biology 18, nr 8 (1.08.1998): 4761–71. http://dx.doi.org/10.1128/mcb.18.8.4761.
Pełny tekst źródłaKönigs, Volker, Richard Jennings, Thomas Vogl, Markus Horsthemke, Anne C. Bachg, Yan Xu, Kay Grobe i in. "Mouse Macrophages Completely Lacking Rho Subfamily GTPases (RhoA, RhoB, and RhoC) Have Severe Lamellipodial Retraction Defects, but Robust Chemotactic Navigation and Altered Motility". Journal of Biological Chemistry 289, nr 44 (11.09.2014): 30772–84. http://dx.doi.org/10.1074/jbc.m114.563270.
Pełny tekst źródłaHan, Jian, Li Li, Jiongyu Hu, Lili Yu, Yingru Zheng, Jianxin Guo, Xiuhui Zheng, Ping Yi i Yuanguo Zhou. "Epidermal Growth Factor Stimulates Human Trophoblast Cell Migration through Rho A and Rho C Activation". Endocrinology 151, nr 4 (11.02.2010): 1732–42. http://dx.doi.org/10.1210/en.2009-0845.
Pełny tekst źródłaTsubaki, Masanobu, Shuuji Genno, Tomoya Takeda, Takuya Matsuda, Naoto Kimura, Yuuma Yamashita, Yuusuke Morii, Kazunori Shimomura i Shozo Nishida. "Rhosin Suppressed Tumor Cell Metastasis through Inhibition of Rho/YAP Pathway and Expression of RHAMM and CXCR4 in Melanoma and Breast Cancer Cells". Biomedicines 9, nr 1 (4.01.2021): 35. http://dx.doi.org/10.3390/biomedicines9010035.
Pełny tekst źródłaTseliou, Melpomeni, Ahmed Al-Qahtani, Saud Alarifi, Saad H. Alkahtani, Christos Stournaras i George Sourvinos. "The Role of RhoA, RhoB and RhoC GTPases in Cell Morphology, Proliferation and Migration in Human Cytomegalovirus (HCMV) Infected Glioblastoma Cells". Cellular Physiology and Biochemistry 38, nr 1 (2016): 94–109. http://dx.doi.org/10.1159/000438612.
Pełny tekst źródłaSaracaloglu, Ahmet, Seniz Demiryürek, Sabit Kimyon, Alper Mete, Ebru Temiz, Gülper Nacarkahya, Betül Düzen, Oguzhan Saygili, Kıvanc Güngör i Abdullah Tuncay Demiryürek. "Protein Expressions of the Small GTPase Rho Proteins in Pterygial Tissue and Leukocytes of Patients with Pterygium". Proceedings 2, nr 25 (6.12.2018): 1571. http://dx.doi.org/10.3390/proceedings2251571.
Pełny tekst źródłaJackson, Ben, Karine Peyrollier, Esben Pedersen, Astrid Basse, Richard Karlsson, Zhipeng Wang, Tine Lefever i in. "RhoA is dispensable for skin development, but crucial for contraction and directed migration of keratinocytes". Molecular Biology of the Cell 22, nr 5 (marzec 2011): 593–605. http://dx.doi.org/10.1091/mbc.e09-10-0859.
Pełny tekst źródłaRiento, Kirsi, Rosa M. Guasch, Ritu Garg, Boquan Jin i Anne J. Ridley. "RhoE Binds to ROCK I and Inhibits Downstream Signaling". Molecular and Cellular Biology 23, nr 12 (15.06.2003): 4219–29. http://dx.doi.org/10.1128/mcb.23.12.4219-4229.2003.
Pełny tekst źródłaPronk, Manon C. A., Jan S. M. van Bezu, Geerten P. van Nieuw Amerongen, Victor W. M. van Hinsbergh i Peter L. Hordijk. "RhoA, RhoB and RhoC differentially regulate endothelial barrier function". Small GTPases 10, nr 6 (26.09.2017): 466–84. http://dx.doi.org/10.1080/21541248.2017.1339767.
Pełny tekst źródłaAntoni, Angelika, Chelsea Ray, Ryan Kohn, Diana Andreyko i Jerrold Levine. "Analysis of the misregulation of RhoA and RhoH in autoimmune mice. (HUM7P.302)". Journal of Immunology 192, nr 1_Supplement (1.05.2014): 184.11. http://dx.doi.org/10.4049/jimmunol.192.supp.184.11.
Pełny tekst źródłaOcana-Morgner, Carlos, Christine Wahren i Rolf Jessberger. "SWAP-70 regulates RhoA/RhoB-dependent MHCII surface localization in dendritic cells". Blood 113, nr 7 (12.02.2009): 1474–82. http://dx.doi.org/10.1182/blood-2008-04-152587.
Pełny tekst źródłaQuinn, Kathrina, Melinda A. Brindley, Melodie L. Weller, Nikola Kaludov, Andrew Kondratowicz, Catherine L. Hunt, Patrick L. Sinn i in. "Rho GTPases Modulate Entry of Ebola Virus and Vesicular Stomatitis Virus Pseudotyped Vectors". Journal of Virology 83, nr 19 (22.07.2009): 10176–86. http://dx.doi.org/10.1128/jvi.00422-09.
Pełny tekst źródłaGiang Ho, T. T., Audrey Stultiens, Johanne Dubail, Charles M. Lapière, Betty V. Nusgens, Alain C. Colige i Christophe F. Deroanne. "RhoGDIα-dependent balance between RhoA and RhoC is a key regulator of cancer cell tumorigenesis". Molecular Biology of the Cell 22, nr 17 (wrzesień 2011): 3263–75. http://dx.doi.org/10.1091/mbc.e11-01-0020.
Pełny tekst źródłaWHEELER, A., i A. RIDLEY. "Why three Rho proteins? RhoA, RhoB, RhoC, and cell motility". Experimental Cell Research 301, nr 1 (15.11.2004): 43–49. http://dx.doi.org/10.1016/j.yexcr.2004.08.012.
Pełny tekst źródłaPinzón-Daza, Martha L., Iris C. Salaroglio, Joanna Kopecka, Ruth Garzòn, Pierre-Olivier Couraud, Dario Ghigo i Chiara Riganti. "The Cross-Talk between Canonical and Non-Canonical Wnt-Dependent Pathways Regulates P-Glycoprotein Expression in Human Blood–Brain Barrier Cells". Journal of Cerebral Blood Flow & Metabolism 34, nr 8 (4.06.2014): 1258–69. http://dx.doi.org/10.1038/jcbfm.2014.100.
Pełny tekst źródłaVega, Francisco M., Gilbert Fruhwirth, Tony Ng i Anne J. Ridley. "RhoA and RhoC have distinct roles in migration and invasion by acting through different targets". Journal of Cell Biology 193, nr 4 (16.05.2011): 655–65. http://dx.doi.org/10.1083/jcb.201011038.
Pełny tekst źródłaKovačević, Igor, Tomohisa Sakaue, Jisca Majoleé, Manon C. Pronk, Masashi Maekawa, Dirk Geerts, Mar Fernandez-Borja, Shigeki Higashiyama i Peter L. Hordijk. "The Cullin-3–Rbx1–KCTD10 complex controls endothelial barrier function via K63 ubiquitination of RhoB". Journal of Cell Biology 217, nr 3 (22.01.2018): 1015–32. http://dx.doi.org/10.1083/jcb.201606055.
Pełny tekst źródłaRIDLEY, A. J. "RhoA, RhoB and RhoC have different roles in cancer cell migration". Journal of Microscopy 251, nr 3 (12.03.2013): 242–49. http://dx.doi.org/10.1111/jmi.12025.
Pełny tekst źródłaNeisch, Amanda L., Olga Speck, Beth Stronach i Richard G. Fehon. "Rho1 regulates apoptosis via activation of the JNK signaling pathway at the plasma membrane". Journal of Cell Biology 189, nr 2 (19.04.2010): 311–23. http://dx.doi.org/10.1083/jcb.200912010.
Pełny tekst źródłaKonstantinidis, Diamantis G., Suvarnamala Pushkaran, Katie M. Giger, Ping Zhou, Paul R. Andreassen, Ursula Klingmuller, James Palis, Yi Zheng i Theodosia A. Kalfa. "RhoA Gtpase Regulates Erythroblast Cytokinesis and Enucleation By Dynamic Coordination Of The Microtubule-Actomyosin Machineries For Successful Abscission". Blood 122, nr 21 (15.11.2013): 311. http://dx.doi.org/10.1182/blood.v122.21.311.311.
Pełny tekst źródłaRafa-Zabłocka, Katarzyna, Agnieszka Zelek-Molik, Beata Tepper, Piotr Chmielarz, Grzegorz Kreiner, Michał Wilczkowski i Irena Nalepa. "Chronic restraint stress induces changes in the cerebral Galpha 12/13 and Rho-GTPase signaling network". Pharmacological Reports 73, nr 4 (11.06.2021): 1179–87. http://dx.doi.org/10.1007/s43440-021-00294-4.
Pełny tekst źródłaMichaelson, David, Joseph Silletti, Gretchen Murphy, Peter D'Eustachio, Mark Rush i Mark R. Philips. "Differential Localization of Rho Gtpases in Live Cells". Journal of Cell Biology 152, nr 1 (8.01.2001): 111–26. http://dx.doi.org/10.1083/jcb.152.1.111.
Pełny tekst źródłaASPENSTRÖM, Pontus, Åsa FRANSSON i Jan SARAS. "Rho GTPases have diverse effects on the organization of the actin filament system". Biochemical Journal 377, nr 2 (15.01.2004): 327–37. http://dx.doi.org/10.1042/bj20031041.
Pełny tekst źródłaKonstantinidis, Diamantis, Suvarnamala Pushkaran, Ursula Klingmuller, James Palis, Yi Zheng i Theodosia A. Kalfa. "Erythroid Specific RhoA Deficiency Causes Dysplastic and Inefficient Fetal Erythropoiesis with Lethal Embryonic Anemia Due to Defects in Erythroblast Cytokinesis and Enucleation". Blood 120, nr 21 (16.11.2012): 82. http://dx.doi.org/10.1182/blood.v120.21.82.82.
Pełny tekst źródłaBayer, Cynthia A., Susan R. Halsell, James W. Fristrom, Daniel P. Kiehart i Laurence von Kalm. "Genetic Interactions Between the RhoA and Stubble-stubbloid Loci Suggest a Role for a Type II Transmembrane Serine Protease in Intracellular Signaling During Drosophila Imaginal Disc Morphogenesis". Genetics 165, nr 3 (1.11.2003): 1417–32. http://dx.doi.org/10.1093/genetics/165.3.1417.
Pełny tekst źródłaBernusso, Vanessa Aline, Mariana Lazarini, João Agostinho Machado-Neto, Karin Spat Albino Barcellos i Sara Teresinha Olalla Saad. "ARHGAP21 Is Upregulated and Triggers the Modulation of Rho Gtpase Signaling Pathways during Megakaryocytic Differentiation". Blood 126, nr 23 (3.12.2015): 4760. http://dx.doi.org/10.1182/blood.v126.23.4760.4760.
Pełny tekst źródłavon Kalm, Laurence, i Corey Seavey. "Abstract 2461: The cell migration inhibitor dihydromotuporamine C regulates actin-myosin contractility and actin polymerization". Cancer Research 83, nr 7_Supplement (4.04.2023): 2461. http://dx.doi.org/10.1158/1538-7445.am2023-2461.
Pełny tekst źródłaRiento, K., P. Villalonga, R. Garg i A. Ridley. "Function and regulation of RhoE". Biochemical Society Transactions 33, nr 4 (1.08.2005): 649–51. http://dx.doi.org/10.1042/bst0330649.
Pełny tekst źródłaHo, T. T. Giang, Sofia D. Merajver, Charles M. Lapière, Betty V. Nusgens i Christophe F. Deroanne. "RhoA-GDP Regulates RhoB Protein Stability". Journal of Biological Chemistry 283, nr 31 (4.06.2008): 21588–98. http://dx.doi.org/10.1074/jbc.m710033200.
Pełny tekst źródłaO'Connor, Kathleen L., Min Chen i L. Nicole Towers. "Integrin α6β4 cooperates with LPA signaling to stimulate Rac through AKAP-Lbc-mediated RhoA activation". American Journal of Physiology-Cell Physiology 302, nr 3 (luty 2012): C605—C614. http://dx.doi.org/10.1152/ajpcell.00095.2011.
Pełny tekst źródłaZaritsky, Assaf, Yun-Yu Tseng, M. Angeles Rabadán, Shefali Krishna, Michael Overholtzer, Gaudenz Danuser i Alan Hall. "Diverse roles of guanine nucleotide exchange factors in regulating collective cell migration". Journal of Cell Biology 216, nr 6 (16.05.2017): 1543–56. http://dx.doi.org/10.1083/jcb.201609095.
Pełny tekst źródłaShi, Geng-Xian, Won Seok Yang, Ling Jin, Michelle L. Matter i Joe W. Ramos. "RSK2 drives cell motility by serine phosphorylation of LARG and activation of Rho GTPases". Proceedings of the National Academy of Sciences 115, nr 2 (26.12.2017): E190—E199. http://dx.doi.org/10.1073/pnas.1708584115.
Pełny tekst źródłaLeung, T., X. Q. Chen, E. Manser i L. Lim. "The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton." Molecular and Cellular Biology 16, nr 10 (październik 1996): 5313–27. http://dx.doi.org/10.1128/mcb.16.10.5313.
Pełny tekst źródłaMarcos-Ramiro, Beatriz, Diego García-Weber, Susana Barroso, Jorge Feito, María C. Ortega, Eva Cernuda-Morollón, Natalia Reglero-Real i in. "RhoB controls endothelial barrier recovery by inhibiting Rac1 trafficking to the cell border". Journal of Cell Biology 213, nr 3 (2.05.2016): 385–402. http://dx.doi.org/10.1083/jcb.201504038.
Pełny tekst źródłaArthur, William T., Shawn M. Ellerbroek, Channing J. Der, Keith Burridge i Krister Wennerberg. "XPLN, a Guanine Nucleotide Exchange Factor for RhoA and RhoB, But Not RhoC". Journal of Biological Chemistry 277, nr 45 (6.09.2002): 42964–72. http://dx.doi.org/10.1074/jbc.m207401200.
Pełny tekst źródłaVignal, E., A. Blangy, M. Martin, C. Gauthier-Rouvière i P. Fort. "Kinectin Is a Key Effector of RhoG Microtubule-Dependent Cellular Activity". Molecular and Cellular Biology 21, nr 23 (1.12.2001): 8022–34. http://dx.doi.org/10.1128/mcb.21.23.8022-8034.2001.
Pełny tekst źródłaShields, Sarah-Kim, Catalin Nicola i Chandan Chakraborty. "Rho Guanosine 5′-Triphosphatases Differentially Regulate Insulin-Like Growth Factor I (IGF-I) Receptor-Dependent and -Independent Actions of IGF-II on Human Trophoblast Migration". Endocrinology 148, nr 10 (1.10.2007): 4906–17. http://dx.doi.org/10.1210/en.2007-0476.
Pełny tekst źródłaKilic, Ertugrul, Ayman ElAli, Ülkan Kilic, Zeyun Guo, Milas Ugur, Unal Uslu, Claudio L. Bassetti, Martin E. Schwab i Dirk M. Hermann. "Role of Nogo-A in Neuronal Survival in the Reperfused Ischemic Brain". Journal of Cerebral Blood Flow & Metabolism 30, nr 5 (20.01.2010): 969–84. http://dx.doi.org/10.1038/jcbfm.2009.268.
Pełny tekst źródłaOnishi, Masayuki, Nolan Ko, Ryuichi Nishihama i John R. Pringle. "Distinct roles of Rho1, Cdc42, and Cyk3 in septum formation and abscission during yeast cytokinesis". Journal of Cell Biology 202, nr 2 (22.07.2013): 311–29. http://dx.doi.org/10.1083/jcb.201302001.
Pełny tekst źródłaNishizuka, Makoto, Rina Komada i Masayoshi Imagawa. "Knockdown of RhoE Expression Enhances TGF-β-Induced EMT (epithelial-to-mesenchymal transition) in Cervical Cancer HeLa Cells". International Journal of Molecular Sciences 20, nr 19 (22.09.2019): 4697. http://dx.doi.org/10.3390/ijms20194697.
Pełny tekst źródłaGarg, Ritu, Kirsi Riento, Nicholas Keep, Jonathan D. H. Morris i Anne J. Ridley. "N-terminus-mediated dimerization of ROCK-I is required for RhoE binding and actin reorganization". Biochemical Journal 411, nr 2 (27.03.2008): 407–14. http://dx.doi.org/10.1042/bj20071342.
Pełny tekst źródłaBilodeau, Diane, Sylvie Lamy, Richard R. Desrosiers, Denis Gingras i Richard Béliveau. "Regulation of Rho protein binding to membranes by rhoGDI: inhibition of releasing activity by physiological ionic conditions". Biochemistry and Cell Biology 77, nr 1 (1.03.1999): 59–69. http://dx.doi.org/10.1139/o99-004.
Pełny tekst źródłaVillalonga, Priam, Rosa M. Guasch, Kirsi Riento i Anne J. Ridley. "RhoE Inhibits Cell Cycle Progression and Ras-Induced Transformation". Molecular and Cellular Biology 24, nr 18 (15.09.2004): 7829–40. http://dx.doi.org/10.1128/mcb.24.18.7829-7840.2004.
Pełny tekst źródłaOinuma, Izumi, Kana Kawada, Kiyoka Tsukagoshi i Manabu Negishi. "Rnd1 and Rnd3 targeting to lipid raft is required for p190 RhoGAP activation". Molecular Biology of the Cell 23, nr 8 (15.04.2012): 1593–604. http://dx.doi.org/10.1091/mbc.e11-11-0900.
Pełny tekst źródłaTroeger, Anja, Amy J. Johnson, Jenna Wood, William G. Blum, Leslie A. Andritsos, John C. Byrd i David A. Williams. "RhoH is critical for cell-microenvironment interactions in chronic lymphocytic leukemia in mice and humans". Blood 119, nr 20 (17.05.2012): 4708–18. http://dx.doi.org/10.1182/blood-2011-12-395939.
Pełny tekst źródłaMeriane, Mayya, Pierre Roux, Michael Primig, Philippe Fort i Cécile Gauthier-Rouvière. "Critical Activities of Rac1 and Cdc42Hs in Skeletal Myogenesis: Antagonistic Effects of JNK and p38 Pathways". Molecular Biology of the Cell 11, nr 8 (sierpień 2000): 2513–28. http://dx.doi.org/10.1091/mbc.11.8.2513.
Pełny tekst źródłaHuang, Qingqing, Jiarong Xie i Jayaraman Seetharaman. "Crystal Structure of Schizosaccharomyces pombe Rho1 Reveals Its Evolutionary Relationship with Other Rho GTPases". Biology 11, nr 11 (7.11.2022): 1627. http://dx.doi.org/10.3390/biology11111627.
Pełny tekst źródłaSeccia, Teresa M., Matteo Rigato, Verdiana Ravarotto i Lorenzo A. Calò. "ROCK (RhoA/Rho Kinase) in Cardiovascular–Renal Pathophysiology: A Review of New Advancements". Journal of Clinical Medicine 9, nr 5 (2.05.2020): 1328. http://dx.doi.org/10.3390/jcm9051328.
Pełny tekst źródłaXing, Lei, Xiaodi Yao, Kathryn R. Williams i Gary J. Bassell. "Negative regulation of RhoA translation and signaling by hnRNP-Q1 affects cellular morphogenesis". Molecular Biology of the Cell 23, nr 8 (15.04.2012): 1500–1509. http://dx.doi.org/10.1091/mbc.e11-10-0867.
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