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Items: 1 to 20 of 57

1.
Rap1 signaling in endothelial barrier control
Willem-Jan Pannekoek, Anneke Post, Johannes L Bos
Cell Adh Migr. 2014 Mar 1; 8(2): 100–107. Published online 2014 Jan 1. doi: 10.4161/cam.27352
PMCID:
PMC4049856
ArticlePDF–646K
2.
Expression of RABEX-5 and its clinical significance in prostate cancer
Hongtuan Zhang, Shang Cheng, Andi Wang, Hui Ma, Bing Yao, Can Qi, Ranlu Liu, Shiyong Qi, Yong Xu
J Exp Clin Cancer Res. 2014; 33(1): 31. Published online 2014 Apr 9. doi: 10.1186/1756-9966-33-31
PMCID:
PMC3996945
ArticlePDF–422K
3.
RABEX-5 Is Upregulated and Plays an Oncogenic Role in Gastric Cancer Development by Activating the VEGF Signaling Pathway
Shuang Wang, Aixia Lu, Xiangming Chen, Lin Wei, Jiqiang Ding
PLoS One. 2014; 9(11): e113891. Published online 2014 Nov 26. doi: 10.1371/journal.pone.0113891
PMCID:
PMC4245226
ArticlePDF–12M
4.
Molecular mechanism for Rabex-5 GEF activation by Rabaptin-5
Zhe Zhang, Tianlong Zhang, Shanshan Wang, Zhou Gong, Chun Tang, Jiangye Chen, Jianping Ding
eLife. 2014; 3: e02687. Published online 2014 Jun 23. doi: 10.7554/eLife.02687
PMCID:
PMC4102244
ArticlePDF–2.5M
5.
Integration of Transforming Growth Factor β and RAS Signaling Silences a RAB5 Guanine Nucleotide Exchange Factor and Enhances Growth Factor-Directed Cell Migration
Hailiang Hu, Marc Milstein, Joanne M. Bliss, Minh Thai, Gautam Malhotra, Lucia C. Huynh, John Colicelli
Mol Cell Biol. 2008 Mar; 28(5): 1573–1583. Published online 2007 Dec 26. doi: 10.1128/MCB.01087-07
PMCID:
PMC2258770
ArticlePDF–1.1M
6.
Functional Synergy between Rab5 Effector Rabaptin-5 and Exchange Factor Rabex-5 When Physically Associated in a Complex
Roger Lippé, Marta Miaczynska, Vladimir Rybin, Anja Runge, Marino Zerial
Mol Biol Cell. 2001 Jul; 12(7): 2219–2228. doi: 10.1091/mbc.12.7.2219
PMCID:
PMC55678
ArticlePDF–323K
7.
Spatiotemporal Regulation of the Ubiquitinated Cargo-binding Activity of Rabex-5 in the Endocytic Pathway
Yoshikatsu Aikawa, Hideki Hirakawa, Sangho Lee
J Biol Chem. 2012 Nov 23; 287(48): 40586–40597. Published online 2012 Oct 9. doi: 10.1074/jbc.M112.411793
PMCID:
PMC3504772
ArticlePDF–2.8M
8.
Structural basis for Rab GTPase activation by VPS9 domain exchange factors
Anna Delprato, David G Lambright
Nat Struct Mol Biol. Author manuscript; available in PMC 2008 Feb 25.
Published in final edited form as: Nat Struct Mol Biol. 2007 May; 14(5): 406–412. Published online 2007 Apr 22. doi: 10.1038/nsmb1232
PMCID:
PMC2254184
ArticlePDF–3.6M
9.
Rabex-5 is a lenalidomide target molecule that negatively regulates TLR-induced type 1 IFN production
David Millrine, Mami Tei, Yohannes Gemechu, Tadamitsu Kishimoto
Proc Natl Acad Sci U S A. 2016 Sep 20; 113(38): 10625–10630. Published online 2016 Sep 6. doi: 10.1073/pnas.1611751113
PMCID:
PMC5035883
ArticlePDF–1020K
10.
Feedback Regulation of Ras Signaling by Rabex-5-mediated Ubiquitination
Lizhong Xu, Veronica Lubkov, Laura J. Taylor, Dafna Bar-Sagi
Curr Biol. Author manuscript; available in PMC 2012 Sep 7.
Published in final edited form as: Curr Biol. 2010 Aug 10; 20(15): 1372–1377. Published online 2010 Jul 22. doi: 10.1016/j.cub.2010.06.051
PMCID:
PMC3436604
ArticlePDF–1.9M
11.
Rabex-5 Is a Rab22 Effector and Mediates a Rab22-Rab5 Signaling Cascade in Endocytosis
Huaiping Zhu, Zhimin Liang, Guangpu Li
Mol Biol Cell. 2009 Nov 15; 20(22): 4720–4729. doi: 10.1091/mbc.E09-06-0453
PMCID:
PMC2777102
ArticlePDF–1.4M
12.
Guanine nucleotide exchange factor RABGEF1 regulates keratinocyte-intrinsic signaling to maintain skin homeostasis
Thomas Marichal, Nicolas Gaudenzio, Sophie El Abbas, Riccardo Sibilano, Oliwia Zurek, Philipp Starkl, Laurent L. Reber, Dimitri Pirottin, Jinah Kim, Pierre Chambon, Axel Roers, Nadine Antoine, Yuko Kawakami, Toshiaki Kawakami, Fabrice Bureau, See-Ying Tam, Mindy Tsai, Stephen J. Galli
J Clin Invest. 2016 Dec 1; 126(12): 4497–4515. Published online 2016 Nov 7. doi: 10.1172/JCI86359
PMCID:
PMC5127679
ArticlePDF–6.9M
13.
Rabex-5 Protein Regulates the Endocytic Trafficking Pathway of Ubiquitinated Neural Cell Adhesion Molecule L1
Yoshikatsu Aikawa
J Biol Chem. 2012 Sep 21; 287(39): 32312–32323. Published online 2012 Jul 30. doi: 10.1074/jbc.M112.374322
PMCID:
PMC3463310
ArticlePDF–2.6M
14.
Dynamin- and Rab5-Dependent Endocytosis of a Ca2+-Activated K+ Channel, KCa2.3
Yajuan Gao, Claudia A. Bertuccio, Corina M. Balut, Simon C. Watkins, Daniel C. Devor
PLoS One. 2012; 7(8): e44150. Published online 2012 Aug 28. doi: 10.1371/journal.pone.0044150
PMCID:
PMC3429460
ArticlePDF–715K
15.
RabGEFs are a major determinant for specific Rab membrane targeting
Julia Blümer, Juliana Rey, Leif Dehmelt, Tomáš Mazel, Yao-Wen Wu, Philippe Bastiaens, Roger S. Goody, Aymelt Itzen
J Cell Biol. 2013 Feb 4; 200(3): 287–300. doi: 10.1083/jcb.201209113
PMCID:
PMC3563681
ArticlePDF–4.7M
16.
Roles of RabGEF1/Rabex-5 domains in regulating FcϵRI surface expression and FcϵRI-dependent responses in mast cells
Janet Kalesnikoff, Eon J. Rios, Ching-Cheng Chen, M. Alejandro Barbieri, Mindy Tsai, See-Ying Tam, Stephen J. Galli
Blood. 2007 Jun 15; 109(12): 5308–5317. Prepublished online 2007 Mar 6. doi: 10.1182/blood-2007-01-067363
PMCID:
PMC1890836
Article
17.
Genome-wide joint SNP and CNV analysis of aortic root diameter in African Americans: the HyperGEN study
Nathan E Wineinger, Amit Patki, Kristin J Meyers, Ulrich Broeckel, Charles C Gu, DC Rao, Richard B Devereux, Donna K Arnett, Hemant K Tiwari
BMC Med Genomics. 2011; 4: 4. Published online 2011 Jan 11. doi: 10.1186/1755-8794-4-4
PMCID:
PMC3027088
ArticlePDF–2.0M
18.
A single MIU motif of MINDY‐1 recognizes K48‐linked polyubiquitin chains
Yosua Adi Kristariyanto, Syed Arif Abdul Rehman, Simone Weidlich, Axel Knebel, Yogesh Kulathu
EMBO Rep. 2017 Mar; 18(3): 392–402. Published online 2017 Jan 12. doi: 10.15252/embr.201643205
PMCID:
PMC5331195
ArticlePDF–1.5M
19.
Divalent interaction of the GGAs with the Rabaptin-5–Rabex-5 complex
Rafael Mattera, Cecilia N. Arighi, Robert Lodge, Marino Zerial, Juan S. Bonifacino
EMBO J. 2003 Jan 2; 22(1): 78–88. doi: 10.1093/emboj/cdg015
PMCID:
PMC140067
ArticlePDF–417K
20.
A context-dependent and disordered ubiquitin-binding motif
Jesper E. Dreier, Andreas Prestel, João M. Martins, Sebastian S. Brøndum, Olaf Nielsen, Anna E. Garbers, Hiroaki Suga, Wouter Boomsma, Joseph M. Rogers, Rasmus Hartmann-Petersen, Birthe B. Kragelund
Cell Mol Life Sci. 2022; 79(9): 484. Published online 2022 Aug 16. doi: 10.1007/s00018-022-04486-w
PMCID:
PMC9381478
ArticlePDF–8.1M

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