Relevant bibliographies by topics / GTPasi

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'GTPasi'

Author: Grafiati
Published: 11 March 2023

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Journal articles on the topic "GTPasi"

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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.

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Since receptor-coupled G proteins increase GTP hydrolysis (GTPase) activity upon ligands binding to the receptor, a study was undertaken to determine if abscisic acid (ABA) induced such an effect. Plasma membranes isolated from etiolated maize (Zea mays L.) coleoptiles were enriched in GTPase activity relative to microsomal fractions. Vanadate was included in the assay to inhibit the high levels of vanadate sensitive low affinity GTPases present. Under these conditions, GTPase activity was enhanced by Mg2+, stimulated by mastoparan, and inhibited by GTPγS indicating the presence of either mono
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Estevez, Ana Y., Tamara Bond, and Kevin Strange. "Regulation of I Cl,swell in neuroblastoma cells by G protein signaling pathways." American Journal of Physiology-Cell Physiology 281, no. 1 (2001): C89—C98. http://dx.doi.org/10.1152/ajpcell.2001.281.1.c89.

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Guanosine 5′- O-(3-thiotriphosphate) (GTPγS) activated the I Cl,swell anion channel in N1E115 neuroblastoma cells in a swelling-independent manner. GTPγS-induced current was unaffected by ATP removal and broadly selective tyrosine kinase inhibitors, demonstrating that phosphorylation events do not regulate G protein-dependent channel activation. Pertussis toxin had no effect on GTPγS-induced current. However, cholera toxin inhibited the current ∼70%. Exposure of cells to 8-bromoadenosine 3′,5′-cyclic monophosphate did not mimic the effect of cholera toxin, and its inhibitory action was not pre
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Uno, Tomohide, Tsubasa Moriwaki, Yuri Isoyama, et al. "Rab14 from Bombyx mori (Lepidoptera: Bombycidae) shows ATPase activity." Biology Letters 6, no. 3 (2010): 379–81. http://dx.doi.org/10.1098/rsbl.2009.0878.

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Rab GTPases are essential for vesicular transport, whereas adenosine triphosphate (ATP) is the most important and versatile of the activated carriers in the cell. But there are little reports to clarify the connection between ATP and Rab GTPases. A cDNA clone (Rab14) from Bombyx mori was expressed in Escherichia coli as a glutathione S-transferase fusion protein and purified. The protein bound to [ 3 H]-GDP and [ 35 S]-GTPγS. Binding of [ 35 S]-GTPγS was inhibited by guanosine diphosphate (GDP), guanosine triphosphate (GTP) and ATP. Rab14 showed GTP- and ATP-hydrolysis activity. The Km value o
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Herrmann, 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 (2014): 470–82. http://dx.doi.org/10.1128/ec.00332-13.

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ABSTRACTMonomeric GTPases of the Rho subfamily are important mediators of polar growth and NADPH (Nox) signaling in a variety of organisms. These pathways influence the ability ofClaviceps purpureato infect host plants. GTPase regulators contribute to the nucleotide loading cycle that is essential for proper functionality of the GTPases. Scaffold proteins gather GTPase complexes to facilitate proper function. The guanine nucleotide exchange factors (GEFs) CpCdc24 and CpDock180 activate GTPase signaling by triggering nucleotide exchange of the GTPases. Here we show that CpCdc24 harbors nucleoti
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Shan, 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 (2007): 611–20. http://dx.doi.org/10.1083/jcb.200702018.

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During cotranslational protein targeting, two guanosine triphosphatase (GTPase) in the signal recognition particle (SRP) and its receptor (SR) form a unique complex in which hydrolyses of both guanosine triphosphates (GTP) are activated in a shared active site. It was thought that GTP hydrolysis drives the recycling of SRP and SR, but is not crucial for protein targeting. Here, we examined the translocation efficiency of mutant GTPases that block the interaction between SRP and SR at specific stages. Surprisingly, mutants that allow SRP–SR complex assembly but block GTPase activation severely
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Nur-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 (1992): 1437–42. http://dx.doi.org/10.1091/mbc.3.12.1437.

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Two distinct GAPs of 120 and 235 kDa called GAP1 and NF1 serve as attenuators of Ras, a member of GTP-dependent signal transducers, by stimulating its intrinsic guanosine triphosphatase (GTPase) activity. The GAP1 (also called Ras GAP) is highly specific for Ras and does not stimulate the intrinsic GTPase activity of Rap1 or Rho. Using GAP1C, the C-terminal GTPase activating domain (residues 720-1044) of bovine GAP1, we have shown previously that the GAP1 specificity is determined by the Ras domain (residues 61-65) where Gln61 plays the primary role. The corresponding domain (residues 1175-153
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Kötting, Carsten, and Klaus Gerwert. "What vibrations tell us about GTPases." Biological Chemistry 396, no. 2 (2015): 131–44. http://dx.doi.org/10.1515/hsz-2014-0219.

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Abstract In this review, we discuss how time-resolved Fourier transform infrared (FTIR) spectroscopy is used to understand how GTP hydrolysis is catalyzed by small GTPases and their cognate GTPase-activating proteins (GAPs). By interaction with small GTPases, GAPs regulate important signal transduction pathways and transport mechanisms in cells. The GTPase reaction terminates signaling and controls transport. Dysfunctions of GTP hydrolysis in these proteins are linked to serious diseases including cancer. Using FTIR, we resolved both the intrinsic and GAP-catalyzed GTPase reaction of the small
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Killoran, 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 (2019): 9937–48. http://dx.doi.org/10.1074/jbc.ra119.008653.

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Small GTPases alternatively bind GDP/GTP guanine nucleotides to gate signaling pathways that direct most cellular processes. Numerous GTPases are implicated in oncogenesis, particularly the three RAS isoforms HRAS, KRAS, and NRAS and the RHO family GTPase RAC1. Signaling networks comprising small GTPases are highly connected, and there is some evidence of direct biochemical cross-talk between their functional G-domains. The activation potential of a given GTPase is contingent on a codependent interaction with the nucleotide and a Mg2+ ion, which bind to individual variants with distinct affini
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Kesseler, Christoph, Julian Kahr, Natalie Waldt, et al. "EXTH-64. SMALL GTPASES IN MENINGIOMAS: PROLIFERATION, MIGRATION, SURVIVAL, POTENTIAL TREATMENT AND INTERACTIONS." Neuro-Oncology 22, Supplement_2 (2020): ii101. http://dx.doi.org/10.1093/neuonc/noaa215.418.

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Abstract PURPOSE To evaluate the role of the small GTPases RhoA, Rac1 and Cdc42 in meningiomas as therapeutic targets and their interactions in meningiomas. EXPERIMENTAL DESIGN We analyzed expression of GTPases in human meningioma samples and meningioma cell lines of various WHO grades. Malignant IOMM-Lee meningioma cells were used to generate shRNA mediated knockdowns of GTPases RhoA, Rac1 or Cdc42 and to study knockdown effects on proliferation and migration, as well as analysis of cell morphology by confocal microscopy. The same tests were used to investigate effects of the two inhibitors F
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Humphries, 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 (2020): 1092. http://dx.doi.org/10.3390/cancers12051092.

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The small Rho GTPases regulate important cellular processes that affect cancer metastasis, such as cell survival and proliferation, actin dynamics, adhesion, migration, invasion and transcriptional activation. The Rho GTPases function as molecular switches cycling between an active GTP-bound and inactive guanosine diphosphate (GDP)-bound conformation. It is known that Rho GTPase activities are mainly regulated by guanine nucleotide exchange factors (RhoGEFs), GTPase-activating proteins (RhoGAPs), GDP dissociation inhibitors (RhoGDIs) and guanine nucleotide exchange modifiers (GEMs). These Rho
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Dissertations / Theses on the topic "GTPasi"

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ZAMBERLAN, MARGHERITA. "La piccola GTPasi Rap1 interposta tra la proteina mitocondriale Opa1 e l'inibizione dell'angiogenesi." Doctoral thesis, Università degli studi di Padova, 2022. https://hdl.handle.net/11577/3460979.

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OPA1 is a protein with pleiotropic functions ranging from the orchestration of mitochondrial fusion and cristae remodeling to transcriptional reprogramming 1, 2. Here we present two different mechanisms by which OPA1 exerts a transcriptional regulation activity in endothelial and breast cancer cells. Mitochondria are dynamic organelles that are now recognized as regulators of signal transduction able to impact on cellular genetic programs 3, 4. Increasing evidence support a fundamental role for mitochondrial shape in the orchestration of cellular transcriptional programs, but how cells sense
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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.

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L’autophagie est un processus de dégradation et de recyclage des composés cellulaires. Ce mécanisme est nécessaire que ce soit à l’état basal pour éliminer des agrégats protéiques ou des organites endommagés ou en condition de stress, tels que la carence nutritionnelle, l’hypoxie ou encore des traitements anticancéreux. De ce fait, l’autophagie est un processus essentiel à la survie ainsi qu’au maintien de l’homéostasie cellulaire. Connaître les joueurs et comprendre les mécanismes de régulation de l’autophagie sont donc importants. Les GTPases RABs sont des régulateurs importants de ce proces
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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.

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Chan, 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.

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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.

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Paul, 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.

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Bery, Nicolas. "Nouvelle stratégie de ciblage de la GTPase RhoB : développement d'intracorps conformationnels sélectifs et leur fonctionnalisation en tant qu'inhibiteurs intracellulaires de l'activité de RhoB." Toulouse 3, 2014. http://thesesups.ups-tlse.fr/2734/.

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La GTPase RhoB partage 85% d'homologie avec RhoA et RhoC. Ces protéines alternent entre deux conformations : une active liée au GTP et une inactive liée au GDP. Des dérégulations de leur expression et de leur activation sont retrouvées dans de nombreux cancers. A ce jour, aucun inhibiteur sélectif de ces GTPases n'a pu être développé afin de bloquer l'activité de l'une ou l'autre de ces Rho. Ce travail doctoral a permis de mettre au point une approche innovante ciblant sélectivement l'état activé de la protéine RhoB. Suite à la caractérisation d'une nouvelle banque d'anticorps à simple domaine
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Ghiaur, Gabriel. "The role of Rho GTPases in hematopoietic stem cell biology RhoA GTPase regulates adult HSC engraftment and Rac1 GTPases is important for embryonic HSC /." Cincinnati, Ohio : University of Cincinnati, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1204374567.

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Peurois, François. "Activation des petites GTPases à la périphérie des membranes." Thesis, Université Paris-Saclay (ComUE), 2018. http://www.theses.fr/2018SACLN037.

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Les petites GTPases sont des régulateurs majeurs de nombreux processus cellulaires. La dérégulation de l’activation des petites GTPases est à l’origine de nombreuses maladies comme, entre autres, certains diabètes et cancers. In vivo, l’activation des petites GTPases se fait par des facteurs d’échange nucléotidiques (GEF), qui interagissent avec les GTPases à la périphérie des membranes cellulaires. Au delà d’un simple lieu de co-localisation, les membranes biologiques possèdent des propriétés physico-chimiques impactant directement l’activation des petites GTPases par les GEFs. Ce projet de t
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Keller, 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.

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Les GTPases de la sous famille RHOA participent à la régulation de nombreuses voies de signalisation qui contrôlent la dynamique du cytosquelette cellulaire et une grande diversité de fonctions telles que la prolifération, la division, la migration et la polarité cellulaires. Ce sont de véritables interrupteurs moléculaires qui, en réponse à un stimulus, changent de conformation tridimensionnelle pour activer leurs protéines effectrices cibles. Elles existent donc sous deux formes, une forme inactive liant le GDP et une forme active, liant le GTP. La proportion de forme active est extrêmement
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Books on the topic "GTPasi"

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Manser, Ed, and Thomas Leung. GTPase Protocols. Humana Press, 2002. http://dx.doi.org/10.1385/1592592813.

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Joan, Marsh, and Goode Jamie, eds. The GTPase superfamily. Wiley, 1993.

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Rush, Mark, and Peter D’Eustachio, eds. The Small GTPase Ran. Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1501-2.

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Corda, D., H. Hamm, and A. Luini. GTPase-controlled molecular machines. Ares-Serono Symposia Publications, 1994.

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Pandey, Girdhar K., Manisha Sharma, Amita Pandey, and Thiruvenkadam Shanmugam. GTPases. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11611-2.

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Ed, Manser, and Leung Thomas, eds. GTPase protocols: The Ras superfamily. Humana Press, 2002.

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Holmes, L. P. Gtpase protocols: The ras superfamily. Humana, 2010.

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Li, Guangpu, and Nava Segev, eds. Rab GTPases. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1346-7.

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Li, Guangpu, ed. Rab GTPases. Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2569-8.

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Rivero, Francisco, ed. Rho GTPases. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-61779-442-1.

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Book chapters on the topic "GTPasi"

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Edelstein-Keshet, Leah. "Pattern Formation Inside Living Cells." In SEMA SIMAI Springer Series. Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-86236-7_5.

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AbstractWhile most of our tissues appear static, in fact, cell motion comprises an important facet of all life forms, whether in single or multicellular organisms. Amoeboid cells navigate their environment seeking nutrients, whereas collectively, streams of cells move past and through evolving tissue in the development of complex organisms. Cell motion is powered by dynamic changes in the structural proteins (actin) that make up the cytoskeleton, and regulated by a circuit of signaling proteins (GTPases) that control the cytoskeleton growth, disassembly, and active contraction. Interesting mathematical questions we have explored include (1) How do GTPases spontaneously redistribute inside a cell? How does this determine the emergent polarization and directed motion of a cell? (2) How does feedback between actin and these regulatory proteins create dynamic spatial patterns (such as waves) in the cell? (3) How do properties of single cells scale up to cell populations and multicellular tissues given interactions (adhesive, mechanical) between cells? Here I survey mathematical models studied in my group to address such questions. We use reaction-diffusion systems to model GTPase spatiotemporal phenomena in both detailed and toy models (for analytic clarity). We simulate single and multiple cells to visualize model predictions and study emergent patterns of behavior. Finally, we work with experimental biologists to address data-driven questions about specific cell types and conditions.
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Del Pulgar, Teresa Gómez, and Juan Carlos Lacal. "GTPase." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_2533-2.

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Del Pulgar, Teresa Gómez, and Juan Carlos Lacal. "GTPase." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-46875-3_2533.

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Pulgar, Teresa Gómez Del, and Juan Carlos Lacal. "GTPase." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_2533.

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Konstantinidis, Diamantis G., and Theodosia A. Kalfa. "Rac GTPase." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_597.

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Konstantinidis, Diamantis G., and Theodosia A. Kalfa. "Rac GTPase." In Encyclopedia of Signaling Molecules. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4614-6438-9_597-1.

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Dempsey, Brian R., Anne C. Rintala-Dempsey, Gary S. Shaw, et al. "Small GTPase." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101254.

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McCormick, F. "GTPase Activating Proteins." In GTPases in Biology I. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78267-1_23.

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Stefanini, Lucia, Robert H. Lee, and Wolfgang Bergmeier. "GTPases." In Platelets in Thrombotic and Non-Thrombotic Disorders. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-47462-5_20.

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Pandey, Girdhar K., Manisha Sharma, Amita Pandey, and Thiruvenkadam Shanmugam. "Overview of G Proteins (GTP-Binding Proteins) in Eukaryotes." In GTPases. Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-11611-2_1.

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Conference papers on the topic "GTPasi"

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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.

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Cell migration is achieved by the dynamic feedback interactions between traction forces generated by the cell and exerted onto the underlying extracellular matrix (ECM), and intracellular mechano-chemical signaling pathways, e.g., Rho GTPase (RhoA, Rac1, and Cdc42) activities [1,2,3]. These components are differentially distributed within a cell, and thus the coordination between tractions and mechanotransduction (i.e, RhoA and Rac1 activities) must be implemented at a precise spatial and temporal order to achieve optimized, directed cell migration [4,5]. Recent studies have shown that focal a
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Mondal, 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.

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Mondal, 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.

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Schulze, J., L. Heinkele, M. Steffens, et al. "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.

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Authi, K. S., B. J. Evenden та N. Crawford. "ACTION OF GTPγS [GUANOSINE 5∲-0-(3-THIOPHOSPHATE)] ON SAPONIN-PERMEABILISED PLATELETS: INVOLVEMENT OF 'G' PROTEINS IN PLATELET ACTIVATION". У XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644514.

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Certain ligand-receptor interactions at cell surfaces lead to the phospholipase-C (PLC) hydrolysis of phosphatidyl inositol (4.5) bisphosphate (PIP2). The products serve as intracellular second messengers, e.g. inositol (1.4.5) trisphosphate (IP3) releases Ca2+ from intracellular stores and diacylglycerol activates protein kinase-C. From studies using GTP and analogues (e.g. GTPγS) there is evidence of a key role for a guanine nucleotide binding protein(s) as a link between receptors and PIP2 hydrolysis. We report the actions of GTPγS on washed human platelets permeabilised with saponin (12-14
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Weber, 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.

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Jakobs, 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.

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Activation of platelets by agonists acting via cell surface-located receptors apparently involves as an early event in transmembrane signalling an interaction of the agonist-occupied receptor with a guanine nucleotide-binding regulatory protein (G-protein). The activated G-protein, then, transduces the information to the effector molecule, being responsible for the changes in intracellular second messengers. At least two changes in intracellular signal molecules are often found to be associated with platelet activation by agonists, i.e., increases in inositol trisphosphate and diacylglycerol l
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Acosta, Lehi, Aaron Rogers, Jingfu Peng, 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.

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Schulze, J., L. Heinkele, M. Steffens, et al. "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.

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Pusapati, 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.

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Reports on the topic "GTPasi"

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Simpson, Kaylene J. Rho GTPase Involvement in Breast Cancer Migration and Invasion. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada435395.

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Simpson, Kaylene J. Rho GTPase Involvement in Breast Cancer Migration and Invasion. Defense Technical Information Center, 2007. http://dx.doi.org/10.21236/ada469757.

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Yang, Zhenbiao. ROP GTPase Signaling in The Hormonal Regulation of Plant Growth. Office of Scientific and Technical Information (OSTI), 2013. http://dx.doi.org/10.2172/1080178.

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Kandpal, Rajendra P., and G. M. Nagaraja. Involvement of a Novel Rho GTPase Activating Protein in Breast Tumorigenesis. Defense Technical Information Center, 2001. http://dx.doi.org/10.21236/ada404607.

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Band, Vimia. Human Mammary Epithelial Cell Transformation by Rho GTPase through a Novel Mechanism. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada500910.

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Kleer, Celina G. Detection of Metastatic Potential in Breast Cancer by RhoC-GTPase and WISP3 Proteins. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada442688.

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Kleer, Celina G. Detection of Metastatic Potential in Breast Cancer by RhoC-GTPase and WISP3 Proteins. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada456604.

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Kleer, Celina G. Detection of Metastatic Potential in Breast Cancer by RhoC-GTPase and WISP3 Proteins. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada426448.

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Kleer, Celina G. Detection of Metastatic Potential in Breast Cancer by RhoC-GTPase and WISP3 Proteins. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada422281.

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Kleer, Celina G. Detection of Metastatic Potential in Breast Cancer by RhoC-GTPase and WISP3 Proteins. Defense Technical Information Center, 2007. http://dx.doi.org/10.21236/ada473395.

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