Academic literature on the topic 'GTPase'
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Journal articles on the topic "GTPase"
Irving, Helen R. "Abscisic acid induction of GTP hydrolysis in maize coleoptile plasma membranes." Functional Plant Biology 25, no. 5 (1998): 539. http://dx.doi.org/10.1071/pp98009.
Full textHerrmann, Andrea, Britta A. M. Tillmann, Janine Schürmann, Michael Bölker, and Paul Tudzynski. "Small-GTPase-Associated Signaling by the Guanine Nucleotide Exchange Factors CpDock180 and CpCdc24, the GTPase Effector CpSte20, and the Scaffold Protein CpBem1 in Claviceps purpurea." Eukaryotic Cell 13, no. 4 (January 31, 2014): 470–82. http://dx.doi.org/10.1128/ec.00332-13.
Full textHumphries, Brock A., Zhishan Wang, and Chengfeng Yang. "MicroRNA Regulation of the Small Rho GTPase Regulators—Complexities and Opportunities in Targeting Cancer Metastasis." Cancers 12, no. 5 (April 28, 2020): 1092. http://dx.doi.org/10.3390/cancers12051092.
Full textKötting, Carsten, and Klaus Gerwert. "What vibrations tell us about GTPases." Biological Chemistry 396, no. 2 (February 1, 2015): 131–44. http://dx.doi.org/10.1515/hsz-2014-0219.
Full textShan, Shu-ou, Sowmya Chandrasekar, and Peter Walter. "Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation." Journal of Cell Biology 178, no. 4 (August 6, 2007): 611–20. http://dx.doi.org/10.1083/jcb.200702018.
Full textNur-E-Kamal, M. S., and H. Maruta. "The role of Gln61 and Glu63 of Ras GTPases in their activation by NF1 and Ras GAP." Molecular Biology of the Cell 3, no. 12 (December 1992): 1437–42. http://dx.doi.org/10.1091/mbc.3.12.1437.
Full textKilloran, Ryan C., and Matthew J. Smith. "Conformational resolution of nucleotide cycling and effector interactions for multiple small GTPases determined in parallel." Journal of Biological Chemistry 294, no. 25 (May 14, 2019): 9937–48. http://dx.doi.org/10.1074/jbc.ra119.008653.
Full textKesseler, Christoph, Julian Kahr, Natalie Waldt, Nele Stroscher, Josephine Liebig, Frank Angenstein, Elmar Kirches, and Christian Mawrin. "EXTH-64. SMALL GTPASES IN MENINGIOMAS: PROLIFERATION, MIGRATION, SURVIVAL, POTENTIAL TREATMENT AND INTERACTIONS." Neuro-Oncology 22, Supplement_2 (November 2020): ii101. http://dx.doi.org/10.1093/neuonc/noaa215.418.
Full textMohamad Ansor, Nurhuda. "PLANT-DERIVED NATURAL PRODUCTS TARGETING RHO GTPASES SIGNALLING NETWORKS FOR CANCER THERAPY: A REVIEW." Journal of Health and Translational Medicine sp2023, no. 1 (June 6, 2023): 116–21. http://dx.doi.org/10.22452/jummec.sp2023no1.10.
Full textRubio, I. "Use of the Ras binding domain of c-Raf for biochemical and live-cell analysis of Ras activation." Biochemical Society Transactions 33, no. 4 (August 1, 2005): 662–63. http://dx.doi.org/10.1042/bst0330662.
Full textDissertations / Theses on the topic "GTPase"
Normandin, Caroline. "Identification et caractérisation de GTPases Activating Proteins spécifiques à la petite GTPase RAB21." Mémoire, Université de Sherbrooke, 2017. http://hdl.handle.net/11143/11544.
Full textAbstract : Autophagy is defined as the lysosomal degradation and recycling of cellular constituents. At basal levels, autophagy eliminates protein aggregates or damaged organelles. In condition of stress, such as in condition of nutritional deficiency, hypoxia or cancer treatments, autophagy allow cells to adapt and survive. Therefore, autophagy is an essential system required for survival and maintenance of cellular homeostasis. It is thus essential to identify the cellular entities and mechanisms regulating this process. RAB GTPases were identified as master regulators of autophagy. These particular proteins act as molecular switches for the rapid execution of cellular responses. RABs are activated by Guanine Nucleotide Exchange Factors (GEF) whereas GTPase Activating Proteins (GAP) accelerates RAB deactivation. RAB21 is essential in the late stages of autophagy. Indeed, RAB21 is activated by nutritional deficiency, via its GEF MTMTR13, to allow trafficking of a SNARE required for autophagic flux. During starvation, RAB21 is deactivated which suggest that a GAP could negatively regulate RAB21 activity. However, to date no GAP for RAB21 has been identified. An eye modifier genetic screen in Drosophila was performed to identify potential RAB21 GAPs and some candidates were identified. As a result of this screen, the GAP TBC1D25 was identified as interacting with RAB21. Moreover, this interaction was increased by starvation. Proximity ligation assays revealed that the RAB21-TBC1D25 interaction partially localized at early endosomes. Moreover, prolonged activation of RAB5, located at early endosomes, inhibited RAB21-TBC1D25 interaction. Further experiments will be carried out to explain these results. With respect to the roles of autophagy in cancer, RAB21 was shown to be overexpressed in cells with high autophagic flux as well as in some colon cancer tumors. Importantly, the expression of Tbc1d25 in these same tumors does not appear to be increased, indicating that TBC1D25 could be an autophagic inhibitor specific to cells with a high autophagic flow. My work suggests that TBC1D25 could function as a GAP to negatively regulate RAB21 activity in condition of prolonged starvation.
Visvikis, Orane. "GTPase Rac1 et ubiquitination." Paris 5, 2007. http://www.theses.fr/2007PA05P622.
Full textThis thesis has been dedicated to the study of the regulation by ubiquitination of a signaling protein, the Rac1 GTPase. I have shown that the degradative ubiquitination of Rac1 affects poorly its splice variant Rac1b, and requires JNK activity, which is stimulated by Rac1 but not by Rac1b. In addition, I have described a non-degradative ubiquitination of Rac1, which could participate in pathogen endocytosis during bacterial infection. Searching for the enzyme responsible for specific Rac1 ubiquitination, I have identified a RING finger protein, Unkempt, as a new effector of Rac1. I have shown that this potential ubiquitin ligase, which is activated by Rac1, could be involved in the ubiquitination of BAF60b, a component of the chromatin remodeling complex SWI/SNF. Moreover, I have observed that Rac1 stimulates histone H2A mono-ubiquitination. Thus, Rac1 GTPase could be involved in novel pathways by controlling chromatin remodeling
Peurois, François. "Activation des petites GTPases à la périphérie des membranes." Thesis, Université Paris-Saclay (ComUE), 2018. http://www.theses.fr/2018SACLN037.
Full textSmall GTPases are major regulators of many cellular processes. Nucleotide exchange factors (GEF) activate small GTPases. Deregulation of the activation of small GTPases is at the origin of several diseases, such as certain diabetes and cancers. GTPases and GEFs interact together at the periphery of cell membranes. Beyond a simple place of co-localization, biological membranes have physicochemical properties directly impacting the activation of small GTPases by GEFs. This thesis project is based on three axes, 1) to propose an experimental strategy to quantitatively measure the effects of membranes in this activation 2) to establish a model of the activation at the periphery of membranes of the GEF EPAC1, a therapeutic target in heart diseases, 3) to characterize known ArfGEF inhibitory small molecules in a membrane context. The results showed that membranes modified GEF catalytic efficiency, and questioned their specificity towards small GTPases. The membranes also appear as partners for the activation of EPAC1 in cooperation with cAMP. These effects could be explained by a co-localization between GEF and GTPases on the membranes surfaces, a conformational rearrangement of the GEF induced by membranes, a modification of lateral diffusion of the GEF, or a catalytically advantageous geometry of the GEF-GTPase-membrane complex. Finally, understanding the involvement of membranes in this activation leads us to imagine new therapeutic inhibition strategies
Chan, King-chung Fred, and 陳敬忠. "Functional characterization of StAR-related lipid transfer domain containing 13 (DLC 2) RhoGAP in the nervous system." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2009. http://hub.hku.hk/bib/B43278449.
Full textChan, King-chung Fred. "Functional characterization of StAR-related lipid transfer domain containing 13 (DLC 2) RhoGAP in the nervous system." Click to view the E-thesis via HKUTO, 2009. http://sunzi.lib.hku.hk/hkuto/record/B43278449.
Full textKeller, Laura. "Conception de nano-anticorps conformationnels comme nouveaux outils d'étude de l'activité des GTPases de la sous-famille RHOA." Thesis, Toulouse 3, 2017. http://www.theses.fr/2017TOU30005/document.
Full textRHOA small GTPase belongs to a subfamily acting as a molecular switch activating major signaling pathways that regulate cytoskeletal dynamics and a variety of cellular responses such as cell cycle progression, cytokinesis, migration and polarity. RHOA activity resides in a few percent of GTP loaded protein, which is finely tuned by a crosstalk between regulators of the GTPase cycle. Manipulating a single RHO at the expression level often induces imbalance in the activity of other RHO GTPases, suggesting that more specific tools targeting these active pools are needed to decipher RHOA functions in time and space. We decided to use single domain antibodies, also known as VHH or nanobodies, as a new tool for studying RHOA activation. We produced and screened a novel fully synthetic phage display library of humanized nanobodies (NaLi-H1) to develop conformational sensors of the GTP loaded active conformation of RHO subfamily. We obtained several high affinity nanobodies against RHOA's active form which we characterized as RHO active antibodies in vitro and RHO signaling blocking intrabodies in cellulo. These new tools will facilitate and improve our current knowledge of this peculiar protein subfamily and will be a paradigm for the study of other RHO related small GTPases
Tillement, Vanessa. "Régulation de la GTPase RHOB par phosphorylation." Toulouse 3, 2005. http://www.theses.fr/2005TOU30175.
Full textRhoB belongs to the Rho family (RhoA, RhoB and RhoC) of the low molecular weight GTPases, regulated by cycling between GDP and GTP bound state. We have shown that RhoB is also regulated by phosphorylation. On contrast to RhoA, which is phosphorylated by PKA, RhoB is specifically phosphorylated by Casein kinase 1 (CK1) and Calmodulin kinase II in vitro and in vivo. Mass spectrometry analysis has shown that CK1 phosphorylates RhoB on its C-terminal sequence on serine 185. With CK1 inhibitors we have shown that CK1-mediated phosphorylation of RhoB inhibits its binding to one of its effector, thus inhibiting its activity. Finally, preliminary results strongly suggest that RhoB phosphorylation by CK1 is implicated in the regulation of the intracellular trafficking of internalized EGF receptor
Paul, Florian [Verfasser]. "Developing quantitative GTPase affinity purification (qGAP) to identify interaction partners of Rho GTPases / Florian Paul." Berlin : Freie Universität Berlin, 2015. http://d-nb.info/1069532711/34.
Full textPaul, Florian Ernst Rudolf Benjamin [Verfasser]. "Developing quantitative GTPase affinity purification (qGAP) to identify interaction partners of Rho GTPases / Florian Paul." Berlin : Freie Universität Berlin, 2015. http://d-nb.info/1069532711/34.
Full textKoraïchi, Faten. "Etude de l'activation de la GTPase RhoB par complémentation split-GFP tripartite." Thesis, Toulouse 3, 2016. http://www.theses.fr/2016TOU30081.
Full textRhoB is a small GTPase that is rapidly activated in response to growth factors and cellular stress. It regulates fundamental biological processes such as cell migration, angiogenesis, DNA repair, apoptosis and response to anticancer therapies. Small GTPases activity is tightly regulated by their subcellular localization. However, RhoB activation had never been investigated in living cells. In this work, we have adapted and validated an innovative method of protein-protein interactions analysis using tripartite split-GFP complementation, for the sensitive and specific detection of small GTPases activation in living cells. Then, we developed an optimized cellular model by combining the tripartite split-GFP technology with an anti-GFP intrabody fluorescence-enhancer to detect the regulation of RhoB activation with high spatial resolution. This biosensor highlighted the translocation of active RhoB from endosomes to accumulate at the plasma membrane upon serum stimulation, revealing a novel membrane signaling platform of RhoB. Future studies based on this biosensor will enable the analysis of RhoB activation profile and other small GTPases upon various stimuli or in different cellular contexts, as well as the identification of the GTPases partners and activation modulators
Books on the topic "GTPase"
Manser, Ed, and Thomas Leung. GTPase Protocols. New Jersey: Humana Press, 2002. http://dx.doi.org/10.1385/1592592813.
Full textJoan, Marsh, and Goode Jamie, eds. The GTPase superfamily. Chichester: Wiley, 1993.
Find full textRush, Mark, and Peter D’Eustachio, eds. The Small GTPase Ran. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1501-2.
Full textCorda, D., H. Hamm, and A. Luini. GTPase-controlled molecular machines. Rome: Ares-Serono Symposia Publications, 1994.
Find full textHolmes, L. P. Gtpase protocols: The ras superfamily. [Place of publication not identified]: Humana, 2010.
Find full textEd, Manser, and Leung Thomas, eds. GTPase protocols: The Ras superfamily. Totowa, N.J: Humana Press, 2002.
Find full textZhang, Xin. Multistate GTPase Control Co-translational Protein Targeting. Boston, MA: Springer US, 2012. http://dx.doi.org/10.1007/978-1-4419-7808-0.
Full textMarsh, Joan, and Jamie Goode, eds. Ciba Foundation Symposium 176 - The GTPase Superfamily. Chichester, UK: John Wiley & Sons, Ltd., 1993. http://dx.doi.org/10.1002/9780470514450.
Full textA, Kahn Richard, ed. ARF family GTPases. Dordrecht: Kluwer Academic Publishers, 2003.
Find full text1949-, Balch William Edward, Der Channing J, and Hall A, eds. Regulators and effectors of small GTPases. San Diego: Academic Press, 2000.
Find full textBook chapters on the topic "GTPase"
Del Pulgar, Teresa Gómez, and Juan Carlos Lacal. "GTPase." In Encyclopedia of Cancer, 1–6. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_2533-2.
Full textDel Pulgar, Teresa Gómez, and Juan Carlos Lacal. "GTPase." In Encyclopedia of Cancer, 1968–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-46875-3_2533.
Full textPulgar, Teresa Gómez Del, and Juan Carlos Lacal. "GTPase." In Encyclopedia of Cancer, 1609–13. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_2533.
Full textKonstantinidis, Diamantis G., and Theodosia A. Kalfa. "Rac GTPase." In Encyclopedia of Signaling Molecules, 4408–14. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_597.
Full textKonstantinidis, Diamantis G., and Theodosia A. Kalfa. "Rac GTPase." In Encyclopedia of Signaling Molecules, 1–7. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4614-6438-9_597-1.
Full textDempsey, Brian R., Anne C. Rintala-Dempsey, Gary S. Shaw, Yuan Xiao Zhu, A. Keith Stewart, Jaime O. Claudio, Constance E. Runyan, et al. "Small GTPase." In Encyclopedia of Signaling Molecules, 1752. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101254.
Full textMcCormick, F. "GTPase Activating Proteins." In GTPases in Biology I, 345–59. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78267-1_23.
Full textTing, T. D., R. H. Lee, and Y. K. Ho. "The GTPase Cycle: Transducin." In GTPases in Biology II, 99–117. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78345-6_7.
Full textStevens, Ellen V., and Channing J. Der. "Overview of Rho GTPase History." In The Rho GTPases in Cancer, 3–27. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-1111-7_1.
Full textLeung, Roland, and Michael Glogauer. "Rho GTPase Techniques in Osteoclastogenesis." In Methods in Molecular Biology, 167–79. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-61779-442-1_12.
Full textConference papers on the topic "GTPase"
Na, Sungsoo. "Engineering Tools for Studying Coordination Between Biochemical and Biomechanical Activities in Cell Migration." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53709.
Full textMondal, Subhanjan, Said Goueli, and Kevin Hsiao. "Abstract C204: GTPase/GAP/GEF-Glo™: A bioluminescent system to measure GTPase, GAP, and GEF activities." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Oct 19-23, 2013; Boston, MA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1535-7163.targ-13-c204.
Full textMondal, Subhanjan, and Said A. Goueli. "Abstract B44: GTPase/GAP/GEF-Glo™: A bioluminescent system to measure GTPase, GAP, and GEF activities." In Abstracts: AACR Special Conference on RAS Oncogenes: From Biology to Therapy; February 24-27, 2014; Lake Buena Vista, FL. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1557-3125.rasonc14-b44.
Full textSchulze, J., L. Heinkele, M. Steffens, A. Warnecke, T. Lenarz, I. Just, and A. Rohrbeck. "Rho-GTPase und p38 vermittelte Neuroprotektion in Spiralganglienzellen." In Abstract- und Posterband – 89. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Forschung heute – Zukunft morgen. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1641056.
Full textWeber, Igor. "Oscillatory dynamics of small GTPase Rac1 in motile cells." In European Microscopy Congress 2020. Royal Microscopical Society, 2021. http://dx.doi.org/10.22443/rms.emc2020.1187.
Full textAcosta, Lehi, Aaron Rogers, Jingfu Peng, Alan Mueller, Zongzhong Tong, Donghan Shin, Jae Hyuk Yoo, et al. "Abstract 4367: The small GTPase ARF6 is necessary for melanomagenesis." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-4367.
Full textSchulze, J., L. Heinkele, M. Steffens, A. Warnecke, T. Lenarz, I. Just, and A. Rohrbeck. "Rho-GTPase and p38 mediated neuroprotection in spiral ganglion cells." In Abstract- und Posterband – 89. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Forschung heute – Zukunft morgen. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1641057.
Full textJakobs, K. H., P. Gierschik, and R. Grandt. "THE ROLE OF GTP-BINDING PROTEINS EXHIBITING GTPase ACTIVITY IN PLATELET ACTIVATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644773.
Full textPusapati, Ganesh Varma, An Rykx, Sandy Vandoninck, Johan van Lint, Guido Adler, and Thomas Seufferlein. "Abstract 296: Protein kinase D regulates Rho GTPase activity through rhotekin." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-296.
Full textOkura, Hidehiro, Brian J. Golbourn, Amanda J. Luck, Christian A. Smith, and James T. Rutka. "Abstract 4038: Role of the Rho-GTPase CDC42 in glioma migration." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4038.
Full textReports on the topic "GTPase"
Simpson, Kaylene J. Rho GTPase Involvement in Breast Cancer Migration and Invasion. Fort Belvoir, VA: Defense Technical Information Center, March 2005. http://dx.doi.org/10.21236/ada435395.
Full textSimpson, Kaylene J. Rho GTPase Involvement in Breast Cancer Migration and Invasion. Fort Belvoir, VA: Defense Technical Information Center, March 2007. http://dx.doi.org/10.21236/ada469757.
Full textYang, Zhenbiao. ROP GTPase Signaling in The Hormonal Regulation of Plant Growth. Office of Scientific and Technical Information (OSTI), May 2013. http://dx.doi.org/10.2172/1080178.
Full textKandpal, Rajendra P., and G. M. Nagaraja. Involvement of a Novel Rho GTPase Activating Protein in Breast Tumorigenesis. Fort Belvoir, VA: Defense Technical Information Center, July 2001. http://dx.doi.org/10.21236/ada404607.
Full textBand, Vimia. Human Mammary Epithelial Cell Transformation by Rho GTPase through a Novel Mechanism. Fort Belvoir, VA: Defense Technical Information Center, August 2008. http://dx.doi.org/10.21236/ada500910.
Full textKleer, Celina G. Detection of Metastatic Potential in Breast Cancer by RhoC-GTPase and WISP3 Proteins. Fort Belvoir, VA: Defense Technical Information Center, May 2005. http://dx.doi.org/10.21236/ada442688.
Full textKleer, Celina G. Detection of Metastatic Potential in Breast Cancer by RhoC-GTPase and WISP3 Proteins. Fort Belvoir, VA: Defense Technical Information Center, May 2006. http://dx.doi.org/10.21236/ada456604.
Full textKleer, Celina G. Detection of Metastatic Potential in Breast Cancer by RhoC-GTPase and WISP3 Proteins. Fort Belvoir, VA: Defense Technical Information Center, May 2004. http://dx.doi.org/10.21236/ada426448.
Full textKleer, Celina G. Detection of Metastatic Potential in Breast Cancer by RhoC-GTPase and WISP3 Proteins. Fort Belvoir, VA: Defense Technical Information Center, May 2003. http://dx.doi.org/10.21236/ada422281.
Full textKleer, Celina G. Detection of Metastatic Potential in Breast Cancer by RhoC-GTPase and WISP3 Proteins. Fort Belvoir, VA: Defense Technical Information Center, May 2007. http://dx.doi.org/10.21236/ada473395.
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