Статті в журналах з теми "PACSIN2"
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Zudeh, Giulia, Raffaella Franca, Marianna Lucafò, Erik J. Bonten, Matteo Bramuzzo, Riccardo Sgarra, Cristina Lagatolla, et al. "PACSIN2as a modulator of autophagy and mercaptopurine cytotoxicity: mechanisms in lymphoid and intestinal cells." Life Science Alliance 6, no. 3 (January 3, 2023): e202201610. http://dx.doi.org/10.26508/lsa.202201610.
Повний текст джерелаNishimura, Tamako, and Shiro Suetsugu. "Super-resolution analysis of PACSIN2 and EHD2 at caveolae." PLOS ONE 17, no. 7 (July 14, 2022): e0271003. http://dx.doi.org/10.1371/journal.pone.0271003.
Повний текст джерелаGusmira, Aini, Kazuhiro Takemura, Shin Yong Lee, Takehiko Inaba, Kyoko Hanawa-Suetsugu, Kayoko Oono-Yakura, Kazuma Yasuhara, Akio Kitao, and Shiro Suetsugu. "Regulation of caveolae through cholesterol-depletion-dependent tubulation mediated by PACSIN2." Journal of Cell Science 133, no. 19 (September 2, 2020): jcs246785. http://dx.doi.org/10.1242/jcs.246785.
Повний текст джерелаPopov, Sergei, Elena Popova, Michio Inoue, Yuanfei Wu, and Heinrich Göttlinger. "HIV-1 gag recruits PACSIN2 to promote virus spreading." Proceedings of the National Academy of Sciences 115, no. 27 (June 11, 2018): 7093–98. http://dx.doi.org/10.1073/pnas.1801849115.
Повний текст джерелаGiannini, Silvia, Markus Bender, Fred G. Pluthero, Hilary Christensen, Richard Leung, Richard W. Lo, Jan Kormann, Markus Plomann, Walter H. A. Kahr, and Hervé Falet. "Dynamin 2 (DNM2) and PACSIN2 Regulate Megakaryocyte Demarcation Membrane System Formation and Platelet Production in Concert." Blood 126, no. 23 (December 3, 2015): 419. http://dx.doi.org/10.1182/blood.v126.23.419.419.
Повний текст джерелаJönsson, Terese, Fred G. Pluthero, Antonija Jurak Begonja, Jan Kormann, Mélanie Demers, Denisa D. Wagner, Markus Plomann, John H. Hartwig, Walter H. Kahr, and Hervé Falet. "The F-BAR Protein PACSIN2 Regulates Platelet Intracellular Membrane Architecture and in Vivo Hemostatic Functions." Blood 124, no. 21 (December 6, 2014): 4154. http://dx.doi.org/10.1182/blood.v124.21.4154.4154.
Повний текст джерелаPostema, Meagan M., Nathan E. Grega-Larson, Leslie M. Meenderink, and Matthew J. Tyska. "PACSIN2-dependent apical endocytosis regulates the morphology of epithelial microvilli." Molecular Biology of the Cell 30, no. 19 (September 1, 2019): 2515–26. http://dx.doi.org/10.1091/mbc.e19-06-0352.
Повний текст джерелаBegonja, Antonija Jurak, Fred G. Pluthero, Worawit Suphamungmee, Silvia Giannini, Hilary Christensen, Richard Leung, Richard W. Lo, et al. "FlnA binding to PACSIN2 F-BAR domain regulates membrane tubulation in megakaryocytes and platelets." Blood 126, no. 1 (July 2, 2015): 80–88. http://dx.doi.org/10.1182/blood-2014-07-587600.
Повний текст джерелаSanderlin, Allen G., Cassandra Vondrak, Arianna J. Scricco, Indro Fedrigo, Vida Ahyong, and Rebecca L. Lamason. "RNAi screen reveals a role for PACSIN2 and caveolins during bacterial cell-to-cell spread." Molecular Biology of the Cell 30, no. 17 (August 2019): 2124–33. http://dx.doi.org/10.1091/mbc.e19-04-0197.
Повний текст джерелаChitu, Violeta, and E. Richard Stanley. "PACSIN2: a BAR-rier forming the megakaryocyte DMS." Blood 126, no. 1 (July 2, 2015): 5–6. http://dx.doi.org/10.1182/blood-2015-04-639450.
Повний текст джерелаCousin, Hélène, Douglas W. DeSimone, and Dominique Alfandari. "PACSIN2 regulates cell adhesion during gastrulation in Xenopus laevis." Developmental Biology 319, no. 1 (July 2008): 86–99. http://dx.doi.org/10.1016/j.ydbio.2008.04.007.
Повний текст джерелаCousin, Hélène, Alban Gaultier, Christian Bleux, Thierry Darribère, and Dominique Alfandari. "PACSIN2 Is a Regulator of the Metalloprotease/Disintegrin ADAM13." Developmental Biology 227, no. 1 (November 2000): 197–210. http://dx.doi.org/10.1006/dbio.2000.9871.
Повний текст джерелаCousin, Hélène, Alban Gaultier, Christian Bleux, Thierry Darribère, and Dominique Alfandari. "PACSIN2 Is a Regulator of the Metalloprotease/Disintegrin ADAM13." Developmental Biology 229, no. 2 (January 2001): 568. http://dx.doi.org/10.1006/dbio.2001.0128.
Повний текст джерелаKostan, Julius, Ulrich Salzer, Albina Orlova, Imre Törö, Vesna Hodnik, Yosuke Senju, Juan Zou, et al. "Direct interaction of actin filaments with F ‐ BAR protein pacsin2." EMBO reports 15, no. 11 (September 12, 2014): 1154–62. http://dx.doi.org/10.15252/embr.201439267.
Повний текст джерелаVan Duyne, Rachel, and Eric O. Freed. "HIV-1 packs in PACSIN2 for cell-to-cell spread." Proceedings of the National Academy of Sciences 115, no. 27 (June 20, 2018): 6885–87. http://dx.doi.org/10.1073/pnas.1808821115.
Повний текст джерелаStocco, Gabriele, Wenjian Yang, Kristine R. Crews, William E. Thierfelder, Giuliana Decorti, Margherita Londero, Raffaella Franca, et al. "PACSIN2 polymorphism influences TPMT activity and mercaptopurine-related gastrointestinal toxicity." Human Molecular Genetics 21, no. 21 (July 30, 2012): 4793–804. http://dx.doi.org/10.1093/hmg/dds302.
Повний текст джерелаSenju, Y., Y. Itoh, K. Takano, S. Hamada, and S. Suetsugu. "Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting." Journal of Cell Science 124, no. 12 (May 24, 2011): 2032–40. http://dx.doi.org/10.1242/jcs.086264.
Повний текст джерелаChandrasekaran, Ramyavardhanee, Anne K. Kenworthy, and D. Borden Lacy. "Clostridium difficile Toxin A Undergoes Clathrin-Independent, PACSIN2-Dependent Endocytosis." PLOS Pathogens 12, no. 12 (December 12, 2016): e1006070. http://dx.doi.org/10.1371/journal.ppat.1006070.
Повний текст джерелаFranca, Raffaella, Gabriele Stocco, Diego Favretto, Nagua Giurici, Irene del Rizzo, Franco Locatelli, Luciana Vinti, et al. "PACSIN2 rs2413739 influence on thiopurine pharmacokinetics: validation studies in pediatric patients." Pharmacogenomics Journal 20, no. 3 (December 3, 2019): 415–25. http://dx.doi.org/10.1038/s41397-019-0130-0.
Повний текст джерелаde Kreuk, Bart-Jan, Eloise C. Anthony, Dirk Geerts, and Peter L. Hordijk. "The F-BAR Protein PACSIN2 Regulates Epidermal Growth Factor Receptor Internalization." Journal of Biological Chemistry 287, no. 52 (November 5, 2012): 43438–53. http://dx.doi.org/10.1074/jbc.m112.391078.
Повний текст джерелаModregger, J., B. Ritter, B. Witter, M. Paulsson, and M. Plomann. "All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis." Journal of Cell Science 113, no. 24 (December 15, 2000): 4511–21. http://dx.doi.org/10.1242/jcs.113.24.4511.
Повний текст джерелаTirozzi, Alfonsina, Miriam Shasa Quiccione, Chiara Cerletti, Maria Benedetta Donati, Giovanni de Gaetano, Licia Iacoviello, and Alessandro Gialluisi. "A Multi-Trait Association Analysis of Brain Disorders and Platelet Traits Identifies Novel Susceptibility Loci for Major Depression, Alzheimer’s and Parkinson’s Disease." Cells 12, no. 2 (January 6, 2023): 245. http://dx.doi.org/10.3390/cells12020245.
Повний текст джерелаDumont, Vincent, Tuomas A. Tolvanen, Sara Kuusela, Hong Wang, Tuula A. Nyman, Sonja Lindfors, Jukka Tienari, et al. "PACSIN2 accelerates nephrin trafficking and is up‐regulated in diabetic kidney disease." FASEB Journal 31, no. 9 (September 2017): 3978–90. http://dx.doi.org/10.1096/fj.201601265r.
Повний текст джерелаRoberts, Rebecca L., Mary C. Wallace, Margien L. Seinen, Krupa Krishnaprasad, Angela Chew, Ian Lawrance, Ruth Prosser, et al. "PACSIN2 Does Not Influence Thiopurine-Related Toxicity In Patients With Inflammatory Bowel Disease." American Journal of Gastroenterology 109, no. 6 (June 2014): 925–27. http://dx.doi.org/10.1038/ajg.2014.89.
Повний текст джерелаRoberts, Rebecca L., Mary C. Wallace, Margien L. Seinen, Krupa Krishnaprasad, Angela Chew, Ian Lawrance, Ruth Prosser, et al. "Corrigendum: PACSIN2 Does Not Influence Thiopurine-Related Toxicity in Patients With Inflammatory Bowel Disease." American Journal of Gastroenterology 110, no. 1 (January 2015): 204. http://dx.doi.org/10.1038/ajg.2014.322.
Повний текст джерелаde Kreuk, B. J., M. Nethe, M. Fernandez-Borja, E. C. Anthony, P. J. Hensbergen, A. M. Deelder, M. Plomann, and P. L. Hordijk. "The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration." Journal of Cell Science 124, no. 14 (June 21, 2011): 2375–88. http://dx.doi.org/10.1242/jcs.080630.
Повний текст джерелаSenju, Y., E. Rosenbaum, C. Shah, S. Hamada-Nakahara, Y. Itoh, K. Yamamoto, K. Hanawa-Suetsugu, O. Daumke, and S. Suetsugu. "Phosphorylation of PACSIN2 by protein kinase C triggers the removal of caveolae from the plasma membrane." Journal of Cell Science 128, no. 15 (June 19, 2015): 2766–80. http://dx.doi.org/10.1242/jcs.167775.
Повний текст джерелаSenju, Yosuke, and Shiro Suetsugu. "Possible regulation of caveolar endocytosis and flattening by phosphorylation of F-BAR domain protein PACSIN2/Syndapin II." BioArchitecture 5, no. 5-6 (December 2, 2015): 70–77. http://dx.doi.org/10.1080/19490992.2015.1128604.
Повний текст джерелаNovikova, Svetlana E., Natalia A. Soloveva, Tatiana E. Farafonova, Olga V. Tikhonova, Pao-Chi Liao, and Victor G. Zgoda. "Proteomic Signature of Extracellular Vesicles for Lung Cancer Recognition." Molecules 26, no. 20 (October 12, 2021): 6145. http://dx.doi.org/10.3390/molecules26206145.
Повний текст джерелаMorén, Björn, Claudio Shah, Mark T. Howes, Nicole L. Schieber, Harvey T. McMahon, Robert G. Parton, Oliver Daumke, and Richard Lundmark. "EHD2 regulates caveolar dynamics via ATP-driven targeting and oligomerization." Molecular Biology of the Cell 23, no. 7 (April 2012): 1316–29. http://dx.doi.org/10.1091/mbc.e11-09-0787.
Повний текст джерелаSenju, Yosuke, and Shiro Suetsugu. "3P197 The role of F-BAR protein pacsin2 in the formation of caveolae(Cell biology,The 48th Annual Meeting of the Biophysical Society of Japan)." Seibutsu Butsuri 50, supplement2 (2010): S179. http://dx.doi.org/10.2142/biophys.50.s179_5.
Повний текст джерелаShimada, Atsushi, Kazunori Takano, Mikako Shirouzu, Kyoko Hanawa-Suetsugu, Takaho Terada, Kiminori Toyooka, Takashi Umehara, Masaki Yamamoto, Shigeyuki Yokoyama, and Shiro Suetsugu. "Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II." FEBS Letters 584, no. 6 (February 24, 2010): 1111–18. http://dx.doi.org/10.1016/j.febslet.2010.02.058.
Повний текст джерелаGong, Yan, Yuebo Zhang, Biao Li, Yu Xiao, Qinghua Zeng, Kang Xu, Yehui Duan, Jianhua He, and Haiming Ma. "Insight into Liver lncRNA and mRNA Profiling at Four Developmental Stages in Ningxiang Pig." Biology 10, no. 4 (April 8, 2021): 310. http://dx.doi.org/10.3390/biology10040310.
Повний текст джерелаJónsson, Terese, Antonija Jurak Begonja, Jan Kormann, Barbara Merkl, Fred Pluthero, Walter H. Kahr, John H. Hartwig, Markus Plomann, and Hervé Falet. "The F-BAR Protein PACSIN 2 Specifically Coats the Anastomosing Intracellular Membrane Systems of Platelets and Megakaryocytes,." Blood 118, no. 21 (November 18, 2011): 3261. http://dx.doi.org/10.1182/blood.v118.21.3261.3261.
Повний текст джерелаBai, Xiaoyun, Geng Meng, and Xiaofeng Zheng. "Cloning, purification, crystallization and preliminary X-ray diffraction analysis of mouse PACSIN 3 protein." Acta Crystallographica Section F Structural Biology and Crystallization Communications 68, no. 2 (January 25, 2012): 159–62. http://dx.doi.org/10.1107/s1744309111049116.
Повний текст джерелаJones, T., W. Yang, W. Evans, and M. Relling. "Using hapmap tools to predict oncology-related phenotypes: TPMT activity vs hapmap SNPs." Journal of Clinical Oncology 24, no. 18_suppl (June 20, 2006): 13035. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.13035.
Повний текст джерелаBillcliff, Peter G., Christopher J. Noakes, Zenobia B. Mehta, Guanhua Yan, LokHang Mak, Rudiger Woscholski, and Martin Lowe. "OCRL1 engages with the F-BAR protein pacsin 2 to promote biogenesis of membrane-trafficking intermediates." Molecular Biology of the Cell 27, no. 1 (January 2016): 90–107. http://dx.doi.org/10.1091/mbc.e15-06-0329.
Повний текст джерелаRahman, Md Habibur, Silong Peng, Xiyuan Hu, Chen Chen, Md Rezanur Rahman, Shahadat Uddin, Julian M. W. Quinn, and Mohammad Ali Moni. "A Network-Based Bioinformatics Approach to Identify Molecular Biomarkers for Type 2 Diabetes that Are Linked to the Progression of Neurological Diseases." International Journal of Environmental Research and Public Health 17, no. 3 (February 6, 2020): 1035. http://dx.doi.org/10.3390/ijerph17031035.
Повний текст джерелаCuajungco, Math P., Christian Grimm, Kazuo Oshima, Dieter D'hoedt, Bernd Nilius, Arjen R. Mensenkamp, René J. M. Bindels, Markus Plomann, and Stefan Heller. "PACSINs Bind to the TRPV4 Cation Channel." Journal of Biological Chemistry 281, no. 27 (April 20, 2006): 18753–62. http://dx.doi.org/10.1074/jbc.m602452200.
Повний текст джерелаSumoy, Lauro, Raquel Pluvinet, Nuria Andreu, Xavier Estivill, and Mònica Escarceller. "PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-syndapin-FAP52 gene family." Gene 262, no. 1-2 (January 2001): 199–205. http://dx.doi.org/10.1016/s0378-1119(00)00531-x.
Повний текст джерелаGoh, Shih Lin, Qi Wang, Laura J. Byrnes, and Holger Sondermann. "Versatile Membrane Deformation Potential of Activated Pacsin." PLoS ONE 7, no. 12 (December 7, 2012): e51628. http://dx.doi.org/10.1371/journal.pone.0051628.
Повний текст джерелаRoach, William, and Markus Plomann. "PACSIN3 overexpression increases adipocyte glucose transport through GLUT1." Biochemical and Biophysical Research Communications 355, no. 3 (April 2007): 745–50. http://dx.doi.org/10.1016/j.bbrc.2007.02.025.
Повний текст джерелаEngevik, Amy C., Izumi Kaji, Meagan M. Postema, James J. Faust, Anne R. Meyer, Janice A. Williams, Gillian N. Fitz, Matthew J. Tyska, Jean M. Wilson, and James R. Goldenring. "Loss of myosin Vb promotes apical bulk endocytosis in neonatal enterocytes." Journal of Cell Biology 218, no. 11 (September 27, 2019): 3647–62. http://dx.doi.org/10.1083/jcb.201902063.
Повний текст джерелаGrimm-Günter, Eva-Maria S., Mark Milbrandt, Barbara Merkl, Mats Paulsson, and Markus Plomann. "PACSIN proteins bind tubulin and promote microtubule assembly." Experimental Cell Research 314, no. 10 (June 2008): 1991–2003. http://dx.doi.org/10.1016/j.yexcr.2008.03.015.
Повний текст джерелаAlet, Claire. "Quand entreprises et ONG se pacsent." Alternatives Économiques 248, no. 6 (June 1, 2006): 42. http://dx.doi.org/10.3917/ae.248.0042.
Повний текст джерелаHan, Gwan Hee, Hanbyoul Cho, Hee Yun, and Jae-Hoon Kim. "PACSIN3 is a novel biomarker for platinum resistance BRCA mutated platinum resistance epithelial ovarian cancer." Journal of Clinical Oncology 40, no. 16_suppl (June 1, 2022): e17540-e17540. http://dx.doi.org/10.1200/jco.2022.40.16_suppl.e17540.
Повний текст джерелаHan, Gwan Hee, Hanbyoul Cho, Hee Yun, and Jae-Hoon Kim. "PACSIN3 is a novel biomarker for platinum resistance BRCA mutated platinum resistance epithelial ovarian cancer." Journal of Clinical Oncology 40, no. 16_suppl (June 1, 2022): e17540-e17540. http://dx.doi.org/10.1200/jco.2022.40.16_suppl.e17540.
Повний текст джерелаHansen, C. G., G. Howard, and B. J. Nichols. "Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis." Journal of Cell Science 124, no. 16 (August 1, 2011): 2777–85. http://dx.doi.org/10.1242/jcs.084319.
Повний текст джерелаHalbach, Arndt, Matthias Mörgelin, Maria Baumgarten, Mark Milbrandt, Mats Paulsson, and Markus Plomann. "PACSIN 1 forms tetramers via its N-terminal F-BAR domain." FEBS Journal 274, no. 3 (January 10, 2007): 773–82. http://dx.doi.org/10.1111/j.1742-4658.2006.05622.x.
Повний текст джерелаEdeling, Melissa A., Subramaniam Sanker, Takaki Shima, P. K. Umasankar, Stefan Höning, Hye Y. Kim, Lance A. Davidson, et al. "Structural Requirements for PACSIN/Syndapin Operation during Zebrafish Embryonic Notochord Development." PLoS ONE 4, no. 12 (December 3, 2009): e8150. http://dx.doi.org/10.1371/journal.pone.0008150.
Повний текст джерела