Relevant bibliographies by topics / RhoGDIα

Contents

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

Academic literature on the topic 'RhoGDIα'

Author: Grafiati
Published: 10 January 2023
Last updated: 28 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'RhoGDIα.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "RhoGDIα"

1

Michaelson, David, Joseph Silletti, Gretchen Murphy, Peter D'Eustachio, Mark Rush, and Mark R. Philips. "Differential Localization of Rho Gtpases in Live Cells." Journal of Cell Biology 152, no. 1 (January 8, 2001): 111–26. http://dx.doi.org/10.1083/jcb.152.1.111.

Full text
Abstract:
Determinants of membrane targeting of Rho proteins were investigated in live cells with green fluorescent fusion proteins expressed with or without Rho-guanine nucleotide dissociation inhibitor (GDI)α. The hypervariable region determined to which membrane compartment each protein was targeted. Targeting was regulated by binding to RhoGDIα in the case of RhoA, Rac1, Rac2, and Cdc42hs but not RhoB or TC10. Although RhoB localized to the plasma membrane (PM), Golgi, and motile peri-Golgi vesicles, TC10 localized to PMs and endosomes. Inhibition of palmitoylation mislocalized H-Ras, RhoB, and TC10 to the endoplasmic reticulum. Although overexpressed Cdc42hs and Rac2 were observed predominantly on endomembrane, Rac1 was predominantly at the PM. RhoA was cytosolic even when expressed at levels in vast excess of RhoGDIα. Oncogenic Dbl stimulated translocation of green fluorescent protein (GFP)-Rac1, GFP-Cdc42hs, and GFP-RhoA to lamellipodia. RhoGDI binding to GFP-Cdc42hs was not affected by substituting farnesylation for geranylgeranylation. A palmitoylation site inserted into RhoA blocked RhoGDIα binding. Mutations that render RhoA, Cdc42hs, or Rac1, either constitutively active or dominant negative abrogated binding to RhoGDIα and redirected expression to both PMs and internal membranes. Thus, despite the common essential feature of the CAAX (prenylation, AAX tripeptide proteolysis, and carboxyl methylation) motif, the subcellular localizations of Rho GTPases, like their functions, are diverse and dynamic.
APA, Harvard, Vancouver, ISO, and other styles
2

Giang Ho, T. T., Audrey Stultiens, Johanne Dubail, Charles M. Lapière, Betty V. Nusgens, Alain C. Colige, and Christophe F. Deroanne. "RhoGDIα-dependent balance between RhoA and RhoC is a key regulator of cancer cell tumorigenesis." Molecular Biology of the Cell 22, no. 17 (September 2011): 3263–75. http://dx.doi.org/10.1091/mbc.e11-01-0020.

Full text
Abstract:
RhoGTPases are key signaling molecules regulating main cellular functions such as migration, proliferation, survival, and gene expression through interactions with various effectors. Within the RhoA-related subclass, RhoA and RhoC contribute to several steps of tumor growth, and the regulation of their expression affects cancer progression. Our aim is to investigate their respective contributions to the acquisition of an invasive phenotype by using models of reduced or forced expression. The silencing of RhoC, but not of RhoA, increased the expression of genes encoding tumor suppressors, such as nonsteroidal anti-inflammatory drug–activated gene 1 (NAG-1), and decreased migration and the anchorage-independent growth in vitro. In vivo, RhoC small interfering RNA (siRhoC) impaired tumor growth. Of interest, the simultaneous knockdown of RhoC and NAG-1 repressed most of the siRhoC-related effects, demonstrating the central role of NAG-1. In addition of being induced by RhoC silencing, NAG-1 was also largely up-regulated in cells overexpressing RhoA. The silencing of RhoGDP dissociation inhibitor α (RhoGDIα) and the overexpression of a RhoA mutant unable to bind RhoGDIα suggested that the effect of RhoC silencing is indirect and results from the up-regulation of the RhoA level through competition for RhoGDIα. This study demonstrates the dynamic balance inside the RhoGTPase network and illustrates its biological relevance in cancer progression.
APA, Harvard, Vancouver, ISO, and other styles
3

El Marzouk, Saad, Jennifer R. Schultz-Norton, Varsha S. Likhite, Ian X. McLeod, John R. Yates, and Ann M. Nardulli. "Rho GDP dissociation inhibitor α interacts with estrogen receptor α and influences estrogen responsiveness." Journal of Molecular Endocrinology 39, no. 4 (October 2007): 249–59. http://dx.doi.org/10.1677/jme-07-0055.

Full text
Abstract:
AbstractEstrogen receptor α (ERα) is a ligand-activated transcription factor that regulates expression of estrogen-responsive genes. Upon binding of the ligand-occupied ERα to estrogen response elements (EREs) in DNA, the receptor interacts with a variety of coregulatory proteins to modulate transcription of target genes. We have isolated and identified a number of proteins associated with the DNA-bound ERα. One of these proteins, Rho guanosine diphosphate (GDP) dissociation inhibitor α (RhoGDIα), is a negative regulator of the Rho family of GTP-binding proteins. In this study, we demonstrate that endogenously expressed RhoGDIα is present in the nucleus as well as the cytoplasm of MCF-7 breast cancer cells, and that RhoGDIα binds directly to ERα, alters the ERα–ERE interaction, and influences the ability of ERα to regulate transcription of a heterologous estrogen-responsive reporter plasmid in transient transfection assays as well as endogenous, estrogen-responsive genes in MCF-7 cells. Our studies suggest that, in addition to the activity of RhoGDIα in the cytoplasm, it also influences ERα signaling in the nucleus.
APA, Harvard, Vancouver, ISO, and other styles
4

Dransart, E., A. Morin, J. Cherfils, and B. Olofsson. "RhoGDI-3, a promising system to investigate the regulatory function of rhoGDIs: uncoupling of inhibitory and shuttling functions of rhoGDIs." Biochemical Society Transactions 33, no. 4 (August 1, 2005): 623–26. http://dx.doi.org/10.1042/bst0330623.

Full text
Abstract:
rhoGDIs (Rho GDP dissociation inhibitors) are postulated to regulate the activity and the localization of small G-proteins of the Rho family by a shuttling process involving extraction of Rho from donor membranes, formation of inhibitory cytosolic rhoGDI/Rho complexes, and delivery of Rho to target membranes. However, the role of rhoGDIs in site-specific membrane targeting or extraction of Rho is still poorly understood. We investigated here the in vivo functions of two mammalian rhoGDIs: the specific rhoGDI-3 and the well-studied rhoGDI-1 (rhoGDI) after structure-based mutagenesis. We identified two sites in rhoGDIs, forming conserved interactions with their Rho target, whose mutation results in the uncoupling of inhibitory and shuttling functions of rhoGDIs in vivo. Remarkably, these rhoGDI mutants were detected at Rho-induced membrane ruffles or protrusions, where they co-localized with RhoG or Cdc42, probably identifying for the first time the site of extraction of a Rho protein by a rhoGDI in vivo. We propose that these mutations act by modifying the steady-state kinetics of the shuttling process regulated by rhoGDIs, such that transient steps at the cell membranes now become detectable. They should provide valuable tools for future investigations of the dynamics of membrane extraction or delivery of Rho proteins and their regulation by cellular partners.
APA, Harvard, Vancouver, ISO, and other styles
5

Zhu, Yezi, Ramakumar Tummala, Chengfei Liu, Nagalakshmi Nadiminty, Wei Lou, Christopher P. Evans, Qinghua Zhou, and Allen C. Gao. "RhoGDIα suppresses growth and survival of prostate cancer cells." Prostate 72, no. 4 (June 16, 2011): 392–98. http://dx.doi.org/10.1002/pros.21441.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Zhu, Yezi, Chengfei Liu, Ramakumar Tummala, Nagalakshmi Nadiminty, Wei Lou, and Allen C. Gao. "RhoGDIα downregulates androgen receptor signaling in prostate cancer cells." Prostate 73, no. 15 (August 6, 2013): 1614–22. http://dx.doi.org/10.1002/pros.22615.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Wu, Fan, Peishan Hu, Dengke Li, Yan Hu, Yingjiao Qi, Bin Yin, Tao Jiang, Jiangang Yuan, Wei Han, and Xiaozhong Peng. "RhoGDIα suppresses self-renewal and tumorigenesis of glioma stem cells." Oncotarget 7, no. 38 (August 19, 2016): 61619–29. http://dx.doi.org/10.18632/oncotarget.11423.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Auguste, David, Mirela Maier, Cindy Baldwin, Lamine Aoudjit, Richard Robins, Indra R. Gupta, and Tomoko Takano. "Disease-causing mutations of RhoGDIα induce Rac1 hyperactivation in podocytes." Small GTPases 7, no. 2 (January 4, 2016): 107–21. http://dx.doi.org/10.1080/21541248.2015.1113353.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Li, Xuemin, Yandong Zhao, Panhong Liu, Xiaoqing Zhu, Minyi Chen, Huadong Wang, Daxiang Lu, and Renbin Qi. "Senegenin Inhibits Hypoxia/Reoxygenation-Induced Neuronal Apoptosis by Upregulating RhoGDIα." Molecular Neurobiology 52, no. 3 (November 4, 2014): 1561–71. http://dx.doi.org/10.1007/s12035-014-8948-6.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Kuhlmann, Nora, Sarah Wroblowski, Lukas Scislowski, and Michael Lammers. "RhoGDIα Acetylation at K127 and K141 Affects Binding toward Nonprenylated RhoA." Biochemistry 55, no. 2 (January 4, 2016): 304–12. http://dx.doi.org/10.1021/acs.biochem.5b01242.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "RhoGDIα"

1

Dransart, Estelle. "Mécanismes moléculaires des rhoGDIs : le système rhoGDI3/RhoG/TrioGEF comme modèle d'nvestigation." Paris 11, 2005. http://www.theses.fr/2005PA112108.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Aldharee, Hitham Abdulrahman. "Role of ERK3 in Regulating RhoGDI1-PAKs Signaling Axis." Wright State University / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=wright1498007023965276.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Akbarzadeh, Mohammad [Verfasser]. "Mechanism of RHOGDI: Regulation and dysregulation of RHO GTPase membrane trafficking / Mohammad Akbarzadeh." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2020. http://d-nb.info/1213971462/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Ard, Ryan. "Regulation of RhoA Activation and Actin Reorganization by Diacylglycerol Kinase." Thesis, Université d'Ottawa / University of Ottawa, 2012. http://hdl.handle.net/10393/22669.

Full text
Abstract:
Rho GTPases are critical regulators of actin cytoskeletal dynamics. The three most well characterized Rho GTPases, Rac1, RhoA and Cdc42 share a common inhibitor, RhoGDI. It is only recently becoming clear how upstream signals cause the selective release of individual Rho GTPases from RhoGDI. For example, our laboratory showed that diacylglycerol kinase zeta (DGKz), which converts diacylglycerol (DAG) to phosphatidic acid (PA), activates PAK1-mediated RhoGDI phosphorylation on Ser-101/174, causing selective Rac1 release and activation. Phosphorylation of RhoGDI on Ser-34 by PKCa has recently been demonstrated to selectively release RhoA, promoting RhoA activation. Here, I show DGKz is required for optimal RhoA activation and RhoGDI Ser-34 phosphorylation. Both were substantially reduced in DGKz-null fibroblasts and occurred independently of DGKz activity, but required a function DGKz PDZ-binding motif. In contrast, Rac1 activation required DGKz-derived PA, but not PDZ-interactions, indicating DGKz regulates these Rho GTPases by two distinct regulatory complexes. Interestingly, RhoA bound directly to the DGKz C1A domain, the same region known to bind Rac1. By direct interactions with RhoA and PKCa, DGKz was required for the efficient co-precipitation of these proteins, suggesting it is important to assemble a signalling complex that functions as a RhoA-specific RhoGDI dissociation complex. Consequently, cells lacking DGKz exhibited decreased RhoA signalling downstream and disrupted stress fibers. Moreover, DGKz loss resulted in decreased stress fiber formation following the expression of a constitutively active RhoA mutant, suggesting it is also important for RhoA function following activation. This is consistent with the ability of DGKz to bind both active and inactive RhoA conformations. Collectively, these findings suggest DGKz is central to two distinct Rho GTPase activation complexes, each having different requirements for DGKz activity and PDZ interactions, and might regulate the balance of Rac1 and RhoA activity during dynamic changes to the actin cytoskeleton.
APA, Harvard, Vancouver, ISO, and other styles
5

BRUNET, NICOLAS. "Etude des proteines rho et de leurs regulateurs dans les voies de signalisation intracellulaire : - un regulateur original, la proteine rhogdi-3-." Paris 11, 2001. http://www.theses.fr/2001PA112197.

Full text
Abstract:
Les petites proteines g de la superfamille ras se comportent dans la cellule comme de veritables commutateurs moleculaires en oscillant entre une conformation inactive liee au gdp, et une conformation active liee au gtp. C'est l'integration d'un stimulus extracellulaire activateur qui permet le passage d'un etat a l'autre pour la transduction du signal. L'activation a une duree determinee dans le temps et dans l'espace cellulaire. L'orchestration des differentes interactions qui ont lieu entre les petites proteines g et leurs regulateurs est absolument cruciale pour mettre en place une reponse cellulaire specifique. Dans le cas des proteines de la famille rho, une autre famille de proteines regulatrices intervient en plus des gef et des gap : les proteines rhogdi. Les rhogdi regulent le cycle gtp/gdp et le cycle d'association/dissociation des proteines rho aux membranes. L'activation de la proteine rho implique que la stimulation de l'echange nucleotidique par le gef soit coordonnee a la dissociation de la proteine rhogdi. L'articulation de ces deux evenements est tres mal connue. Dans cette optique, l'etude de la proteine rhogdi-3 a ete entreprise. Nous avons montre que la proteine rhogdi-3 est une gdi non conventionnelle qui se distingue de ses deux isoformes par une association aux membranes de l'appareil de golgi. L'extremite n-terminale hydrophobe de la proteine rhogdi-3 est necessaire et suffisante pour cette localisation. De plus, rhogdi-3 regule negativement et specifiquement l'activite de la proteine rhog dans les cellules hela. Il a aussi ete mis en evidence l'existence d'un complexe cytoplasmique entre ces deux proteines et la capacite de rhogdi-3 a extraire rhog des membranes pour former un pool de complexes inactifs. L'ensemble de ces resultats nous conduit a faire l'hypothese que la proteine rhogdi-3 pourrait participer au recyclage de la proteine rhog inactive de la membrane plasmique vers l'appareil de golgi ou elle serait activee par le facteur d'echange trio.
APA, Harvard, Vancouver, ISO, and other styles
6

Newcombe, Anthony Richard. "The biochemical role of the small G protein Rac1 in cell signalling pathways : interaction with RhoGDI and the phagocyte NADPH oxidase component, p67'p'h'o'x." Thesis, University College London (University of London), 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342224.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Chan, Hsiang-Yu, and 詹翔嵎. "Biochemical and functional studies of RhoGDIα methylation by PRMT6." Thesis, 2016. http://ndltd.ncl.edu.tw/handle/hxyahx.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Tseng, Chun-Hsien, and 曾俊賢. "Investigating the effect of arginine methylation on RhoGDIα function." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/fvw29b.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Hsu, Kai-Hsuan, and 許楷瑄. "Investigating the molecular mechanisms through which RhoGDIα regulates megakaryocyte differentiation in K562 cells." Thesis, 2015. http://ndltd.ncl.edu.tw/handle/5u7p5a.

Full text
Abstract:
碩士
國立陽明大學
生物藥學研究所
103
Megakaryocytes (MK) are derived from bipotent megakaryocyte/erythroid progenitors (MEP) of the myeloid lineage and are the sole source of circulating platelets which play a vital role in stopping bleeding. K562 is a human bipotent myeloleukemia cell line and has been used as a cell model for studying MK differentiation. Previous studies in this lab have shown that the p38α MAPK pathway negatively regulates MK differentiation. The molecular events upstream of p38α are yet to be elucidated. 　　Members of small GTPase Rho family are known to act upstream of MAPK pathways. The Rho GDP-dissociation factor α (RhoGDIα) acts to inhibit the activity of Rho GTPases. Our previous results showed that overexpression of RhoGDIα stimulated and knockdown of RhoGDIα suppressed PMA-induced MK differentiation. My results showed that RhoGDIα-overexpressing stable clones suppressed p38 activation, which is in agreement with our previous observation that knockdown of RhoGDIα enhanced p38 activation confirming that RhoGDIα negatively regulated p38 activation. It was reported that Arg 111, 152 and 180 of RhoGDIα are methylated. Our previous results showed that the R111/152/180K triple mutant failed to promote MK differentiation. My study with R111/152/180-expressing stable clones showed that not only MK was suppressed but also p38 activation was increased suggesting Arg 111/152/180 played a role in regulating p38 activation and MK differentiation. 　　I further investigated the potential downstream target of RhoGDIα. By ectopic expression, I showed that the constitutively active Rac1 not only suppressed differentiation but also displayed a significant dominant-negative effect whereas the constitutively active forms of RhoA did not affect differentiation. These results suggest that RhoGDIα may act through suppressing the activity of Rac1.
APA, Harvard, Vancouver, ISO, and other styles
10

Liao, Min-Chiao, and 廖敏喬. "Down-regulation of RhoGDIα expression by TCF-4 and beta-catenin in hepatocellular carcinoma." Thesis, 2009. http://ndltd.ncl.edu.tw/handle/25414296876790569799.

Full text
Abstract:
碩士
輔英科技大學
醫事技術系碩士班
97
In Taiwan, hepatocellular carcinoma ranks as the first and the second leading causes of death for male and female cancer patients, respectively. Recently, inappropriate activation of Wnt signaling pathway has been implicated in the development of HCC. Therefore, this study focused on searching for TCF-4 and beta-catenin regulated proteins. TCF-4 and β-catenin were transfected in Huh7. Our study found that TCF-4 and β-catenin down-regulated RhoGDIα expression in HCC by proteomic method. Furthermore, the levels of RhoGDIα expression in HCC tissue and peritumorous non-neoplastic liver tissue were determined by RT-PCR. The results indicated that RhoGDIα expression is down-regulated in human HCC compared with peritumorous non-neoplastic liver tissues. The functional analysis of RhoGDIα in tumor cell was defined further by apoptosis assay, MTT assay, migration and invasion assay. Ectopic expression of RhoGDIα altered tumor cell survival, apoptosis and migration. The results suggest that down-regulation of RhoGDIα expression plays a significant role in the progress of hepatocellular carcinoma.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "RhoGDIα"

1

Davies, Candice Lynn. Tini and Rhogi, Yogini and Yogi: An Introduction to Kids' Yoga and Dharmadinos. Lulu Press, Inc., 2015.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

Davies, Candice Lynn. Tini and Rhogi, Yogini and Yogi: An Introduction to Kids' Yoga and Dharmadinos. Lulu Press, Inc., 2015.

Find full text
APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "RhoGDIα"

1

Anselmo, Anthony N., Gary M. Bokoch, and Céline DerMardirossian. "RhoGDIs in Cancer." In The Rho GTPases in Cancer, 45–58. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-1111-7_3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Zalcman, Gérard, Olivier Dorseuil, Juan Antonio Garcia-Ranea, Gérard Gacon, and Jacques Camonis. "RhoGAPs and RhoGDIs, (His)stories of Two Families." In Progress in Molecular and Subcellular Biology, 85–113. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-58591-3_5.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Kost, Benedikt. "Regulatory and Cellular Functions of Plant RhoGAPs and RhoGDIs." In Integrated G Proteins Signaling in Plants, 27–48. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-03524-1_2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Boulter, Etienne, and Rafael Garcia-Mata. "Analysis of the Role of RhoGDI1 and Isoprenylation in the Degradation of RhoGTPases." In Methods in Molecular Biology, 97–105. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-61779-442-1_7.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Nishimura, Akiyuki, and Maurine E. Linder. "Monitoring RhoGDI Extraction of Lipid-Modified Rho GTPases from Membranes Using Click Chemistry." In Methods in Molecular Biology, 297–306. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9532-5_22.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Johnson, Jared, Richard A. Cerione, and Jon W. Erickson. "A Quantitative Fluorometric Approach for Measuring the Interaction of RhoGDI with Membranes and Rho GTPases." In Methods in Molecular Biology, 107–19. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-61779-442-1_8.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Wang, Pu, Xiaodong Wang, Peixing Wu, Jinghai Zhang, Toshinori Sato, Sadako Yamagata, and Tatsuya Yamagata. "GM3 Upregulation of Matrix Metalloproteinase-9 Possibly Through PI3K, AKT, RICTOR, RHOGDI-2, and TNF-A Pathways in Mouse Melanoma B16 Cells." In Advances in Experimental Medicine and Biology, 335–48. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-7877-6_16.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Read, Paul W., and Robert K. Nakamoto. "Expression and purification of Rho/RhoGDI complexes." In Methods in Enzymology, 15–25. Elsevier, 2000. http://dx.doi.org/10.1016/s0076-6879(00)25427-x.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

DerMardirossian, Celine M., and Gary M. Bokoch. "Phosphorylation of RhoGDI by p21‐Activated Kinase 1." In Methods in Enzymology, 80–90. Elsevier, 2006. http://dx.doi.org/10.1016/s0076-6879(06)06007-1.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Nitz, Matthew D., Michael A. Harding, and Dan Theodorescu. "Invasion and Metastasis Models for Studying RhoGDI2 in Bladder Cancer." In Methods in Enzymology, 219–33. Elsevier, 2008. http://dx.doi.org/10.1016/s0076-6879(07)00417-x.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "RhoGDIα"

1

Li, Yang, Junlan Zhu, Jingxia Li, and Chuanshu Huang. "Abstract 526: NFκB p65 overexpression promotes bladder cancer migration via FBW7-mediated degradation of RhoGDIα protein." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-526.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Grinnell, KL, and EO Harrington. "SHP2 Regulates the Pulmonary Endothelial Barrier through Modulation of RhoGDI-1 and p190RhoGAP." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2326.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Yu, Yonghui, Jinyi Liu, Dongyun Zhang, Wenjing Luo, Jianxiu Yu, Jingxia Li, Xinhai Zhang, Xue-Ru Wu, Germán R. Acosta, and Chuanshu Huang. "Abstract 2442: XIAP mediates cancer cell motility via RhoGDI-dependent regulation of cytoskeleton." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2442.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Koh, Sung A., Kyung Hee Lee, Eun Young Choi, Min Kyoung Kim, Byung Ik Jang, Si Hyung Lee, Kyeong Ok Kim, et al. "Abstract 2084: RhoGDI2 is associated with HGF-mediated tumor invasion through VEGF in stomach cancer." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2084.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Zhu, Junlan, Yang Li, Chuanshu Huang, and Haishan Huang. "Abstract 3310: Atg7 overexpression promotes bladder cancer invasionviaautophagic removal of AUF1 protein and subsequently increased RhoGDI2 mRNA stabilityin vitroandin vivo." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-3310.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Shin, Jung-Young, Xiang-Hua Zhang, Seong-Ae Yoon, Hiun Suk Chae, and Jin-Hyoung Kang. "Abstract 1582: Rho GDP dissociation inhibitor 2 (RhoGDI2) plays a functionally important role on EGFR signaling pathway in adenocarcinoma cells of lung cancer." 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.am10-1582.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Yu, Yonghui, Jinyi Liu, Dongyun Zhang, Wenjing Luo, Jianxiu Yu, Jingxia Li, Xinhai Zhang, Jingyuan Chen, and Chuanshu Huang. "Abstract 4312: E3 ligase activity of XIAP RING domain is required for XIAP-mediated cancer cell migration but not for its RhoGDI binding activity." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4312.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'RhoGDIα' for particular source types:
Journal articles Dissertations / Theses
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography