Статті в журналах з теми "Protein Mediated Membrane Fusion"
Оформте джерело за APA, MLA, Chicago, Harvard та іншими стилями
Ознайомтеся з топ-50 статей у журналах для дослідження на тему "Protein Mediated Membrane Fusion".
Біля кожної праці в переліку літератури доступна кнопка «Додати до бібліографії». Скористайтеся нею – і ми автоматично оформимо бібліографічне посилання на обрану працю в потрібному вам стилі цитування: APA, MLA, «Гарвард», «Чикаго», «Ванкувер» тощо.
Також ви можете завантажити повний текст наукової публікації у форматі «.pdf» та прочитати онлайн анотацію до роботи, якщо відповідні параметри наявні в метаданих.
Переглядайте статті в журналах для різних дисциплін та оформлюйте правильно вашу бібліографію.
Stegmann, T., R. W. Doms, and A. Helenius. "Protein-Mediated Membrane Fusion." Annual Review of Biophysics and Biophysical Chemistry 18, no. 1 (June 1989): 187–211. http://dx.doi.org/10.1146/annurev.bb.18.060189.001155.
Повний текст джерелаBenhaim, Mark A., and Kelly K. Lee. "New Biophysical Approaches Reveal the Dynamics and Mechanics of Type I Viral Fusion Machinery and Their Interplay with Membranes." Viruses 12, no. 4 (April 8, 2020): 413. http://dx.doi.org/10.3390/v12040413.
Повний текст джерелаBoonstra, Sander, Jelle S. Blijleven, Wouter H. Roos, Patrick R. Onck, Erik van der Giessen, and Antoine M. van Oijen. "Hemagglutinin-Mediated Membrane Fusion: A Biophysical Perspective." Annual Review of Biophysics 47, no. 1 (May 20, 2018): 153–73. http://dx.doi.org/10.1146/annurev-biophys-070317-033018.
Повний текст джерелаKumar, Pawan, Samit Guha, and Ulf Diederichsen. "SNARE protein analog-mediated membrane fusion." Journal of Peptide Science 21, no. 8 (April 7, 2015): 621–29. http://dx.doi.org/10.1002/psc.2773.
Повний текст джерелаStiasny, Karin, and Franz X. Heinz. "Flavivirus membrane fusion." Journal of General Virology 87, no. 10 (October 1, 2006): 2755–66. http://dx.doi.org/10.1099/vir.0.82210-0.
Повний текст джерелаFu, Jiawen, Lin Zhao, Juan Yang, Heming Chen, Shinuo Cao, and Honglin Jia. "An unconventional SNARE complex mediates exocytosis at the plasma membrane and vesicular fusion at the apical annuli in Toxoplasma gondii." PLOS Pathogens 19, no. 3 (March 27, 2023): e1011288. http://dx.doi.org/10.1371/journal.ppat.1011288.
Повний текст джерелаTaylor, Gwen M., and David Avram Sanders. "The Role of the Membrane-spanning Domain Sequence in Glycoprotein-mediated Membrane Fusion." Molecular Biology of the Cell 10, no. 9 (September 1999): 2803–15. http://dx.doi.org/10.1091/mbc.10.9.2803.
Повний текст джерелаJohnson, Colin P., and Edwin R. Chapman. "Otoferlin is a calcium sensor that directly regulates SNARE-mediated membrane fusion." Journal of Cell Biology 191, no. 1 (October 4, 2010): 187–97. http://dx.doi.org/10.1083/jcb.201002089.
Повний текст джерелаKingsley, David H., Ali Behbahani, Afshin Rashtian, Gary W. Blissard, and Joshua Zimmerberg. "A Discrete Stage of Baculovirus GP64-mediated Membrane Fusion." Molecular Biology of the Cell 10, no. 12 (December 1999): 4191–200. http://dx.doi.org/10.1091/mbc.10.12.4191.
Повний текст джерелаGrothe, Tobias, Julia Nowak, Reinhard Jahn, and Peter Jomo Walla. "Selected tools to visualize membrane interactions." European Biophysics Journal 50, no. 2 (March 2021): 211–22. http://dx.doi.org/10.1007/s00249-021-01516-6.
Повний текст джерелаDiao, Jiajie, Yuji Ishitsuka, and Woo-Ri Bae. "Single-molecule FRET study of SNARE-mediated membrane fusion." Bioscience Reports 31, no. 6 (September 15, 2011): 457–63. http://dx.doi.org/10.1042/bsr20110011.
Повний текст джерелаWeber-Boyvat, Marion, Hongxia Zhao, Nina Aro, Qiang Yuan, Konstantin Chernov, Johan Peränen, Pekka Lappalainen, and Jussi Jäntti. "A conserved regulatory mode in exocytic membrane fusion revealed by Mso1p membrane interactions." Molecular Biology of the Cell 24, no. 3 (February 2013): 331–41. http://dx.doi.org/10.1091/mbc.e12-05-0415.
Повний текст джерелаHughson, Frederick M. "Molecular mechanisms of protein-mediated membrane fusion." Current Opinion in Structural Biology 5, no. 4 (August 1995): 507–13. http://dx.doi.org/10.1016/0959-440x(95)80036-0.
Повний текст джерелаWessels, Laura, and Keith Weninger. "Physical Aspects of Viral Membrane Fusion." Scientific World JOURNAL 9 (2009): 764–80. http://dx.doi.org/10.1100/tsw.2009.76.
Повний текст джерелаLiao, Maofu, and Margaret Kielian. "Functions of the Stem Region of the Semliki Forest Virus Fusion Protein during Virus Fusion and Assembly." Journal of Virology 80, no. 22 (September 13, 2006): 11362–69. http://dx.doi.org/10.1128/jvi.01679-06.
Повний текст джерелаStiasny, Karin, and Franz X. Heinz. "Effect of Membrane Curvature-Modifying Lipids on Membrane Fusion by Tick-Borne Encephalitis Virus." Journal of Virology 78, no. 16 (August 15, 2004): 8536–42. http://dx.doi.org/10.1128/jvi.78.16.8536-8542.2004.
Повний текст джерелаGui, Long, Jamie L. Ebner, Alexander Mileant, James A. Williams, and Kelly K. Lee. "Visualization and Sequencing of Membrane Remodeling Leading to Influenza Virus Fusion." Journal of Virology 90, no. 15 (May 25, 2016): 6948–62. http://dx.doi.org/10.1128/jvi.00240-16.
Повний текст джерелаMcClain, Mark S., Ping Cao, and Timothy L. Cover. "Amino-Terminal Hydrophobic Region ofHelicobacter pylori Vacuolating Cytotoxin (VacA) Mediates Transmembrane Protein Dimerization." Infection and Immunity 69, no. 2 (February 1, 2001): 1181–84. http://dx.doi.org/10.1128/iai.69.2.1181-1184.2001.
Повний текст джерелаChanel-Vos, Chantal, and Margaret Kielian. "Second-Site Revertants of a Semliki Forest Virus Fusion-Block Mutation Reveal the Dynamics of a Class II Membrane Fusion Protein." Journal of Virology 80, no. 12 (June 15, 2006): 6115–22. http://dx.doi.org/10.1128/jvi.00167-06.
Повний текст джерелаOu, Wu, and Jonathan Silver. "Stoichiometry of Murine Leukemia Virus Envelope Protein-Mediated Fusion and Its Neutralization." Journal of Virology 80, no. 24 (October 11, 2006): 11982–90. http://dx.doi.org/10.1128/jvi.01318-06.
Повний текст джерелаAhn, Anna, Don L. Gibbons, and Margaret Kielian. "The Fusion Peptide of Semliki Forest Virus Associates with Sterol-Rich Membrane Domains." Journal of Virology 76, no. 7 (April 1, 2002): 3267–75. http://dx.doi.org/10.1128/jvi.76.7.3267-3275.2002.
Повний текст джерелаMartens, Sascha. "Role of C2 domain proteins during synaptic vesicle exocytosis." Biochemical Society Transactions 38, no. 1 (January 19, 2010): 213–16. http://dx.doi.org/10.1042/bst0380213.
Повний текст джерелаDuncan, Roy. "Fusogenic Reoviruses and Their Fusion-Associated Small Transmembrane (FAST) Proteins." Annual Review of Virology 6, no. 1 (September 29, 2019): 341–63. http://dx.doi.org/10.1146/annurev-virology-092818-015523.
Повний текст джерелаKobayashi, Mariko, Michael C. Bennett, Theodore Bercot, and Ila R. Singh. "Functional Analysis of Hepatitis C Virus Envelope Proteins, Using a Cell-Cell Fusion Assay." Journal of Virology 80, no. 4 (February 15, 2006): 1817–25. http://dx.doi.org/10.1128/jvi.80.4.1817-1825.2006.
Повний текст джерелаJain, Surbhi, Lori W. McGinnes, and Trudy G. Morrison. "Overexpression of Thiol/Disulfide Isomerases Enhances Membrane Fusion Directed by the Newcastle Disease Virus Fusion Protein." Journal of Virology 82, no. 24 (October 1, 2008): 12039–48. http://dx.doi.org/10.1128/jvi.01406-08.
Повний текст джерелаYang, Yiming, and Nandini Nagarajan Margam. "Structural Insights into Membrane Fusion Mediated by Convergent Small Fusogens." Cells 10, no. 1 (January 15, 2021): 160. http://dx.doi.org/10.3390/cells10010160.
Повний текст джерелаWahlberg, J. M., and H. Garoff. "Membrane fusion process of Semliki Forest virus. I: Low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cells." Journal of Cell Biology 116, no. 2 (January 15, 1992): 339–48. http://dx.doi.org/10.1083/jcb.116.2.339.
Повний текст джерелаYu, Haijia, Chong Shen, Yinghui Liu, Bridget L. Menasche, Yan Ouyang, Michael H. B. Stowell, and Jingshi Shen. "SNARE zippering requires activation by SNARE-like peptides in Sec1/Munc18 proteins." Proceedings of the National Academy of Sciences 115, no. 36 (August 20, 2018): E8421—E8429. http://dx.doi.org/10.1073/pnas.1802645115.
Повний текст джерелаLiao, Maofu, Claudia Sánchez-San Martín, Aihua Zheng, and Margaret Kielian. "In Vitro Reconstitution Reveals Key Intermediate States of Trimer Formation by the Dengue Virus Membrane Fusion Protein." Journal of Virology 84, no. 11 (March 24, 2010): 5730–40. http://dx.doi.org/10.1128/jvi.00170-10.
Повний текст джерелаYamamoto, Mizuki, Takeshi Ichinohe, Aya Watanabe, Ayako Kobayashi, Rui Zhang, Jiping Song, Yasushi Kawaguchi, Zene Matsuda, and Jun-ichiro Inoue. "The Antimalarial Compound Atovaquone Inhibits Zika and Dengue Virus Infection by Blocking E Protein-Mediated Membrane Fusion." Viruses 12, no. 12 (December 21, 2020): 1475. http://dx.doi.org/10.3390/v12121475.
Повний текст джерелаRichard, Jean-Philippe, Evgenia Leikina, Ralf Langen, William Mike Henne, Margarita Popova, Tamas Balla, Harvey T. McMahon, Michael M. Kozlov, and Leonid V. Chernomordik. "Intracellular curvature-generating proteins in cell-to-cell fusion." Biochemical Journal 440, no. 2 (November 14, 2011): 185–93. http://dx.doi.org/10.1042/bj20111243.
Повний текст джерелаSalsman, Jayme, Deniz Top, Julie Boutilier, and Roy Duncan. "Extensive Syncytium Formation Mediated by the Reovirus FAST Proteins Triggers Apoptosis-Induced Membrane Instability." Journal of Virology 79, no. 13 (July 1, 2005): 8090–100. http://dx.doi.org/10.1128/jvi.79.13.8090-8100.2005.
Повний текст джерелаBruns, Caroline, J. Michael McCaffery, Amy J. Curwin, Juan M. Duran, and Vivek Malhotra. "Biogenesis of a novel compartment for autophagosome-mediated unconventional protein secretion." Journal of Cell Biology 195, no. 6 (December 5, 2011): 979–92. http://dx.doi.org/10.1083/jcb.201106098.
Повний текст джерелаSu, B., G. L. Waneck, R. A. Flavell, and A. L. Bothwell. "The glycosyl phosphatidylinositol anchor is critical for Ly-6A/E-mediated T cell activation." Journal of Cell Biology 112, no. 3 (February 1, 1991): 377–84. http://dx.doi.org/10.1083/jcb.112.3.377.
Повний текст джерелаArnold, Matthew Grant, Pratikshya Adhikari, Baobin Kang, and Hao Xu (徐昊). "Munc18a clusters SNARE-bearing liposomes prior to trans-SNARE zippering." Biochemical Journal 474, no. 19 (September 25, 2017): 3339–54. http://dx.doi.org/10.1042/bcj20170494.
Повний текст джерелаSato, Miyuki, Keiko Saegusa, Katsuya Sato, Taichi Hara, Akihiro Harada, and Ken Sato. "Caenorhabditis elegans SNAP-29 is required for organellar integrity of the endomembrane system and general exocytosis in intestinal epithelial cells." Molecular Biology of the Cell 22, no. 14 (July 15, 2011): 2579–87. http://dx.doi.org/10.1091/mbc.e11-04-0279.
Повний текст джерелаDubé, Mathieu, Loïc Etienne, Maximilian Fels, and Margaret Kielian. "Calcium-Dependent Rubella Virus Fusion Occurs in Early Endosomes." Journal of Virology 90, no. 14 (April 27, 2016): 6303–13. http://dx.doi.org/10.1128/jvi.00634-16.
Повний текст джерелаZaitseva, Elena, Aditya Mittal, Diane E. Griffin, and Leonid V. Chernomordik. "Class II fusion protein of alphaviruses drives membrane fusion through the same pathway as class I proteins." Journal of Cell Biology 169, no. 1 (April 4, 2005): 167–77. http://dx.doi.org/10.1083/jcb.200412059.
Повний текст джерелаDawe, Sandra, Jennifer A. Corcoran, Eileen K. Clancy, Jayme Salsman, and Roy Duncan. "Unusual Topological Arrangement of Structural Motifs in the Baboon Reovirus Fusion-Associated Small Transmembrane Protein." Journal of Virology 79, no. 10 (May 15, 2005): 6216–26. http://dx.doi.org/10.1128/jvi.79.10.6216-6226.2005.
Повний текст джерелаMahal, Lara K., Sonia M. Sequeira, Jodi M. Gureasko, and Thomas H. Söllner. "Calcium-independent stimulation of membrane fusion and SNAREpin formation by synaptotagmin I." Journal of Cell Biology 158, no. 2 (July 15, 2002): 273–82. http://dx.doi.org/10.1083/jcb.200203135.
Повний текст джерелаJeetendra, E., Clinton S. Robison, Lorraine M. Albritton, and Michael A. Whitt. "The Membrane-Proximal Domain of Vesicular Stomatitis Virus G Protein Functions as a Membrane Fusion Potentiator and Can Induce Hemifusion." Journal of Virology 76, no. 23 (December 1, 2002): 12300–12311. http://dx.doi.org/10.1128/jvi.76.23.12300-12311.2002.
Повний текст джерелаHuang, Xiaofang, Xin Zhou, Xiaoyu Hu, Amit S. Joshi, Xiangyang Guo, Yushan Zhu, Quan Chen, William A. Prinz, and Junjie Hu. "Sequences flanking the transmembrane segments facilitate mitochondrial localization and membrane fusion by mitofusin." Proceedings of the National Academy of Sciences 114, no. 46 (November 1, 2017): E9863—E9872. http://dx.doi.org/10.1073/pnas.1708782114.
Повний текст джерелаMendonsa, Rima, and JoAnne Engebrecht. "Phosphatidylinositol-4,5-Bisphosphate and Phospholipase D-Generated Phosphatidic Acid Specify SNARE-Mediated Vesicle Fusion for Prospore Membrane Formation." Eukaryotic Cell 8, no. 8 (June 5, 2009): 1094–105. http://dx.doi.org/10.1128/ec.00076-09.
Повний текст джерелаYamamoto, Mizuki, Shutoku Matsuyama, Xiao Li, Makoto Takeda, Yasushi Kawaguchi, Jun-ichiro Inoue, and Zene Matsuda. "Identification of Nafamostat as a Potent Inhibitor of Middle East Respiratory Syndrome Coronavirus S Protein-Mediated Membrane Fusion Using the Split-Protein-Based Cell-Cell Fusion Assay." Antimicrobial Agents and Chemotherapy 60, no. 11 (August 22, 2016): 6532–39. http://dx.doi.org/10.1128/aac.01043-16.
Повний текст джерелаWeber, Thomas, Francesco Parlati, James A. McNew, Robert J. Johnston, Benedikt Westermann, Thomas H. Söllner та James E. Rothman. "Snarepins Are Functionally Resistant to Disruption by Nsf and αSNAP". Journal of Cell Biology 149, № 5 (29 травня 2000): 1063–72. http://dx.doi.org/10.1083/jcb.149.5.1063.
Повний текст джерелаKlupp, Barbara G., Ralf Nixdorf, and Thomas C. Mettenleiter. "Pseudorabies Virus Glycoprotein M Inhibits Membrane Fusion." Journal of Virology 74, no. 15 (August 1, 2000): 6760–68. http://dx.doi.org/10.1128/jvi.74.15.6760-6768.2000.
Повний текст джерелаShmulevitz, Maya, Jayme Salsman, and Roy Duncan. "Palmitoylation, Membrane-Proximal Basic Residues, and Transmembrane Glycine Residues in the Reovirus p10 Protein Are Essential for Syncytium Formation." Journal of Virology 77, no. 18 (September 15, 2003): 9769–79. http://dx.doi.org/10.1128/jvi.77.18.9769-9779.2003.
Повний текст джерелаAdrien, Vladimir, Hugo Fumat, Cédric Tessier, Philippe Nuss, and David Tareste. "T202. THE EFFECT OF ANTIPSYCHOTIC DRUGS ON MEMBRANE FUSION: AN IN VITRO STUDY." Schizophrenia Bulletin 46, Supplement_1 (April 2020): S308—S309. http://dx.doi.org/10.1093/schbul/sbaa029.762.
Повний текст джерелаChan, Ka Man Carmen, Ashley L. Arthur, Johannes Morstein, Meiyan Jin, Abrar Bhat, Dörte Schlesinger, Sungmin Son, Donté A. Stevens, David G. Drubin, and Daniel A. Fletcher. "Evolutionarily related small viral fusogens hijack distinct but modular actin nucleation pathways to drive cell-cell fusion." Proceedings of the National Academy of Sciences 118, no. 1 (December 21, 2020): e2007526118. http://dx.doi.org/10.1073/pnas.2007526118.
Повний текст джерелаYu, Haijia, Yinghui Liu, Daniel R. Gulbranson, Alex Paine, Shailendra S. Rathore, and Jingshi Shen. "Extended synaptotagmins are Ca2+-dependent lipid transfer proteins at membrane contact sites." Proceedings of the National Academy of Sciences 113, no. 16 (April 4, 2016): 4362–67. http://dx.doi.org/10.1073/pnas.1517259113.
Повний текст джерела