Relevant bibliographies by topics / RalGPS2

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

Academic literature on the topic 'RalGPS2'

Author: Grafiati
Published: 9 March 2023
Last updated: 31 July 2025

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Journal articles on the topic "RalGPS2"

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Tan, Juan, Weimin Wang, Bin Song, Yingjian Song, and Zili Meng. "Integrative Analysis of Three Novel Competing Endogenous RNA Biomarkers with a Prognostic Value in Lung Adenocarcinoma." BioMed Research International 2020 (August 4, 2020): 1–12. http://dx.doi.org/10.1155/2020/2837906.

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Increasing evidence has shown competitive endogenous RNAs (ceRNAs) play key roles in numerous cancers. Nevertheless, the ceRNA network that can predict the prognosis of lung adenocarcinoma (LUAD) is still lacking. The aim of the present study was to identify the prognostic value of key ceRNAs in lung tumorigenesis. Differentially expressed (DE) RNAs were identified between LUAD and adjacent normal samples by limma package in R using The Cancer Genome Atlas database (TCGA). Gene ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway function enrichment analysis was performed u
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D’Aloia, Alessia, Edoardo Arrigoni, Barbara Costa, et al. "RalGPS2 Interacts with Akt and PDK1 Promoting Tunneling Nanotubes Formation in Bladder Cancer and Kidney Cells Microenvironment." Cancers 13, no. 24 (2021): 6330. http://dx.doi.org/10.3390/cancers13246330.

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RalGPS2 is a Ras-independent Guanine Nucleotide Exchange Factor for RalA GTPase that is involved in several cellular processes, including cytoskeletal organization. Previously, we demonstrated that RalGPS2 also plays a role in the formation of tunneling nanotubes (TNTs) in bladder cancer 5637 cells. In particular, TNTs are a novel mechanism of cell–cell communication in the tumor microenvironment, playing a central role in cancer progression and metastasis formation. However, the molecular mechanisms involved in TNTs formation still need to be fully elucidated. Here we demonstrate that mid and
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D’Aloia, A., G. Berruti, B. Costa, et al. "RalGPS2 is involved in tunneling nanotubes formation in 5637 bladder cancer cells." Experimental Cell Research 362, no. 2 (2018): 349–61. http://dx.doi.org/10.1016/j.yexcr.2017.11.036.

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Ceriani, Michela, Cristina Scandiuzzi, Loredana Amigoni, Renata Tisi, Giovanna Berruti, and Enzo Martegani. "Functional analysis of RalGPS2, a murine guanine nucleotide exchange factor for RalA GTPase." Experimental Cell Research 313, no. 11 (2007): 2293–307. http://dx.doi.org/10.1016/j.yexcr.2007.03.016.

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Ceriani, Michela, Loredana Amigoni, Cristina Scandiuzzi, Giovanna Berruti, and Enzo Martegani. "The PH-PxxP domain of RalGPS2 promotes PC12 cells differentiation acting as a dominant negative for RalA GTPase activation." Neuroscience Research 66, no. 3 (2010): 290–98. http://dx.doi.org/10.1016/j.neures.2009.11.013.

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O. Santos, Adriana, Maria Carla Parrini, and Jacques Camonis. "RalGPS2 Is Essential for Survival and Cell Cycle Progression of Lung Cancer Cells Independently of Its Established Substrates Ral GTPases." PLOS ONE 11, no. 5 (2016): e0154840. http://dx.doi.org/10.1371/journal.pone.0154840.

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Guo, Hongjun, Siqiao Wang, Aiqing Xie, et al. "Ral GEF with the PH Domain and SH3 Binding Motif 1 Regulated by Splicing Factor Junction Plakoglobin and Pyrimidine Metabolism Are Prognostic in Uterine Carcinosarcoma." Disease Markers 2021 (October 28, 2021): 1–17. http://dx.doi.org/10.1155/2021/1484227.

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Uterine carcinosarcoma (UCS) is a highly invasive malignant tumor that originated from the uterine epithelium. Many studies suggested that the abnormal changes of alternative splicing (AS) of pre-mRNA are related to the occurrence and metastasis of the tumor. This study investigates the mechanism of alternative splicing events (ASEs) in the tumorigenesis and metastasis of UCS. RNA-seq of UCS samples and alternative splicing event (ASE) data of UCS samples were downloaded from The Cancer Genome Atlas (TCGA) and TCGASpliceSeq databases, several times. Firstly, we performed the Cox regression ana
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Kikuchi, A., S. D. Demo, Z. H. Ye, Y. W. Chen, and L. T. Williams. "ralGDS family members interact with the effector loop of ras p21." Molecular and Cellular Biology 14, no. 11 (1994): 7483–91. http://dx.doi.org/10.1128/mcb.14.11.7483-7491.1994.

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Using a yeast two-hybrid system, we identified a novel protein which interacts with ras p21. This protein shares 69% amino acid homology with ral guanine nucleotide dissociation stimulator (ralGDS), a GDP/GTP exchange protein for ral p24. We designated this protein RGL, for ralGDS-like. Using the yeast two-hybrid system, we found that an effector loop mutant of ras p21 was defective in interacting with the ras p21-interacting domain of RGL, suggesting that this domain binds to ras p21 through the effector loop of ras p21. Since ralGDS contained a region highly homologous with the ras p21-inter
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Kikuchi, A., S. D. Demo, Z. H. Ye, Y. W. Chen, and L. T. Williams. "ralGDS family members interact with the effector loop of ras p21." Molecular and Cellular Biology 14, no. 11 (1994): 7483–91. http://dx.doi.org/10.1128/mcb.14.11.7483.

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Using a yeast two-hybrid system, we identified a novel protein which interacts with ras p21. This protein shares 69% amino acid homology with ral guanine nucleotide dissociation stimulator (ralGDS), a GDP/GTP exchange protein for ral p24. We designated this protein RGL, for ralGDS-like. Using the yeast two-hybrid system, we found that an effector loop mutant of ras p21 was defective in interacting with the ras p21-interacting domain of RGL, suggesting that this domain binds to ras p21 through the effector loop of ras p21. Since ralGDS contained a region highly homologous with the ras p21-inter
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Rondaij, Mariska G., Ruben Bierings, Ellen L. van Agtmaal, et al. "Guanine exchange factor RalGDS mediates exocytosis of Weibel-Palade bodies from endothelial cells." Blood 112, no. 1 (2008): 56–63. http://dx.doi.org/10.1182/blood-2007-07-099309.

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Abstract The small GTP-binding protein Ral has been implicated in regulated exocytosis via its interaction with the mammalian exocyst complex. We have previously demonstrated that Ral is involved in exocytosis of Weibel-Palade bodies (WPBs). Little is known about intracellular signaling pathways that promote activation of Ral in response to ligand binding of G protein–coupled receptors. Here we show that RNAi-mediated knockdown of RalGDS, an exchange factor for Ral, results in inhibition of thrombin- and epinephrine-induced exocytosis of WPBs, while overexpression of RalGDS promotes exocytosis
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Dissertations / Theses on the topic "RalGPS2"

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D'ALOIA, ALESSIA. "RalGPS2 interacts with LST1 and supports tunneling nanotubes formation in human bladder cancer cells." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2017. http://hdl.handle.net/10281/158357.

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RalGPS2 è uno scambiatore appartenente alla famiglia RalGPS, composto da un dominio catalitico Cdc25-like nella regione N-terminale, un motivo PxxP nella regione centrale, e un dominio di omologia alla Pleckstrina (PH) nella regione C-terminale. E’ stato precedentemente dimostrato che RalGPS2 attiva in “vivo” la GTPasi RalA, mentre la regione PH-PxxP si comporta da dominante negativo per l’attività di RalA in cellule NIH3T3 e PC12. Inoltre, se è overespresso RalGPS2 causa cambiamenti morfologici consistenti nelle cellule HEK293, suggerendo che esso possa avere effetti sul citoscheletro. Tutto
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Giddings, Barton William 1963. "Characterization of a mammalian exchange factor, ralGDS." Thesis, Massachusetts Institute of Technology, 1994. http://hdl.handle.net/1721.1/33522.

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Döker, Rolf [Verfasser]. "NMR-spektroskopische Untersuchung von Bindungspartnern kleiner GTPasen : Bindedomänen von RalGDS und RanBP2 / vorgeleget von Rolf Döker." 2003. http://d-nb.info/967854148/34.

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Stafford, Amy Jo. "Electrostatic fields at the functional interface of the protein Ral guanine nucleotide dissociation stimulator determined by vibrational Stark effect spectroscopy." Thesis, 2011. http://hdl.handle.net/2152/ETD-UT-2011-12-4685.

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Noncovalent factors, such as shape complementarity and electrostatic driving forces, almost exclusively cause the affinity and specificity for which two or more biological macromolecules organize into a functioning complex. The human oncoprotein p21Ras (Ras) and a structurally identical but functionally distant analog, Rap1A (Rap), exhibit high selectivity and specificity when binding to downstream effector proteins that cannot be explained through structural analysis alone. Both Ras and Rap bind to Ral guanine nucleotide dissociation stimulator (RalGDS) with affinities that differ tenfold i
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Ragain, Christina Marie. "Role of local electrostatic fields in protein-protein and protein-solvent interactions determined by vibrational Stark effect spectroscopy." Thesis, 2014. http://hdl.handle.net/2152/24949.

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This examines the interplay of structure and local electrostatic fields in protein-protein and protein-solvent interactions. The partial charges of the protein amino acids and the polarization of the surrounding solvent create a complex system of electrostatic fields at protein-protein and protein-solvent interfaces. An approach incorporating vibrational Stark effect (VSE) spectroscopy, dissociation constant measurements, and molecular dynamics (MD) simulations was used to investigate the electrostatic interactions in these interfaces. Proteins p21Ras (Ras) and Rap1A (Rap) have nearly identi
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Book chapters on the topic "RalGPS2"

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Ferguson, Stephen S. G. "Methods to Investigate the Roles of β-Arrestin-Dependent RalGDS Activation in GPCR-Stimulated Membrane Blebbing." In Beta-Arrestins. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9158-7_11.

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Quilliam, Lawrence A. "Specificity and Expression of RalGPS as RalGEFs." In Regulators and Effectors of Small GTPases: Ras Family. Elsevier, 2006. http://dx.doi.org/10.1016/s0076-6879(05)07010-2.

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"Ras Association (RalGDS/AF-6) Domain Family." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_103228.

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"Ras Association (RalGDS/AF-6) Domain Family 6." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_103229.

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Bos, Johannes L. "Ras." In GTPases. Oxford University PressOxford, 2000. http://dx.doi.org/10.1093/oso/9780199637454.003.0003.

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Abstract Ras is a molecular switch that controls the transduction of signals from cell-surface receptors to intracellular targets (Fig. la). Like all GTPases, the switch mechanism consists of activation by exchange of bound GDP for GTP, and inactivation by hydrolysis of GTP into GDP. Ras achieved notoriety in the 1980s with the discovery that 15% of all human tumours contain a point mutation in one of the three Ras genes. The resulting mutant protein is unable to hydrolyse bound GTP and therefore remains constitutively in the active conformation. As a consequence, cells experience a continuous
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Conference papers on the topic "RalGPS2"

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Tian, Lu, Lo Kong Chan, Daniel Wai Hung HO, LuQing Zhao, and Irene Oi Lin NG. "Abstract 2589: Dysregulation of RalGAPA2 in hepatocellular carcinoma." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-2589.

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Perumalsamy, Lakshmi R., and Mahalingam S. "Abstract 5076: Ras association (RalGDS/AF-6) domain family member integrates with notch signaling to regulate tumor cell migration." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-5076.

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