Статті в журналах з теми "Non muscle myosin II A"
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Watanabe, T., H. Hosoya, and S. Yonemura. "1P205 Live imaging of Non-muscle myosin II in epithelial cells." Seibutsu Butsuri 45, supplement (2005): S83. http://dx.doi.org/10.2142/biophys.45.s83_1.
Повний текст джерелаUbukawa, Kumi, Yong-Mei Guo, Masayuki Takahashi, Makoto Hirokawa, Yoshihiro Michishita, Miho Nara, Hiroyuki Tagawa, et al. "Enucleation of human erythroblasts involves non-muscle myosin IIB." Blood 119, no. 4 (January 26, 2012): 1036–44. http://dx.doi.org/10.1182/blood-2011-06-361907.
Повний текст джерелаDasbiswas, Kinjal, Shiqiong Hu, Frank Schnorrer, Samuel A. Safran, and Alexander D. Bershadsky. "Ordering of myosin II filaments driven by mechanical forces: experiments and theory." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1747 (April 9, 2018): 20170114. http://dx.doi.org/10.1098/rstb.2017.0114.
Повний текст джерелаWrighton, Katharine H. "Non-muscle myosin II in kidney morphogenesis." Nature Reviews Nephrology 13, no. 7 (May 30, 2017): 384. http://dx.doi.org/10.1038/nrneph.2017.77.
Повний текст джерелаLevinson, Howard, Blaine Mischen, Bruce Klitzman, Detlev Erdmann, and L. Scott Levin. "Non muscle myosin II regulates contractile phenotypes." Journal of the American College of Surgeons 205, no. 3 (September 2007): S60—S61. http://dx.doi.org/10.1016/j.jamcollsurg.2007.06.148.
Повний текст джерелаMaciver, Sutherland K. "Myosin II function in non-muscle cells." BioEssays 18, no. 3 (March 1996): 179–82. http://dx.doi.org/10.1002/bies.950180304.
Повний текст джерелаPorro, Chiara, Antonio Pennella, Maria Antonietta Panaro, and Teresa Trotta. "Functional Role of Non-Muscle Myosin II in Microglia: An Updated Review." International Journal of Molecular Sciences 22, no. 13 (June 22, 2021): 6687. http://dx.doi.org/10.3390/ijms22136687.
Повний текст джерелаTakubo, T., S. Wakui, K. Daigo, K. Kurokata, T. Ohashi, K. Katayama, and M. Hino. "Expression of non-muscle type myosin heavy polypeptide 9 (MYH9) in mammalian cells." European Journal of Histochemistry 47, no. 4 (June 26, 2009): 345. http://dx.doi.org/10.4081/845.
Повний текст джерелаJuanes-García, Alba, Clara Llorente-González, and Miguel Vicente-Manzanares. "Molecular control of non-muscle myosin II assembly." Oncotarget 7, no. 5 (January 18, 2016): 5092–93. http://dx.doi.org/10.18632/oncotarget.6936.
Повний текст джерелаWan, Xiaohu. "Counting Molecules in Non-Muscle Myosin II Filaments." Biophysical Journal 108, no. 2 (January 2015): 322a. http://dx.doi.org/10.1016/j.bpj.2014.11.1750.
Повний текст джерелаGrinnell, F., and C. H. Ho. "Non-muscle myosin II heavy chain has a cryptic cell-adhesion domain." Biochemical Journal 309, no. 2 (July 15, 1995): 569–74. http://dx.doi.org/10.1042/bj3090569.
Повний текст джерелаKolega, J. "Cytoplasmic dynamics of myosin IIA and IIB: spatial ‘sorting’ of isoforms in locomoting cells." Journal of Cell Science 111, no. 15 (August 1, 1998): 2085–95. http://dx.doi.org/10.1242/jcs.111.15.2085.
Повний текст джерелаJohnson, Chloe A., Jake E. McGreig, Sarah T. Jeanfavre, Jonathan Walklate, Carlos D. Vera, Marta Farré, Daniel P. Mulvihill, et al. "Identification of sequence changes in myosin II that adjust muscle contraction velocity." PLOS Biology 19, no. 6 (June 10, 2021): e3001248. http://dx.doi.org/10.1371/journal.pbio.3001248.
Повний текст джерелаDaneshparvar, Nadia, Dianne W. Taylor, Thomas S. O’Leary, Hamidreza Rahmani, Fatemeh Abbasiyeganeh, Michael J. Previs, and Kenneth A. Taylor. "CryoEM structure of Drosophila flight muscle thick filaments at 7 Å resolution." Life Science Alliance 3, no. 8 (July 27, 2020): e202000823. http://dx.doi.org/10.26508/lsa.202000823.
Повний текст джерелаPark, Inju, Cecil Han, Sora Jin, Boyeon Lee, Heejin Choi, Jun Tae Kwon, Dongwook Kim, et al. "Myosin regulatory light chains are required to maintain the stability of myosin II and cellular integrity." Biochemical Journal 434, no. 1 (January 27, 2011): 171–80. http://dx.doi.org/10.1042/bj20101473.
Повний текст джерелаEliott, S., P. H. Vardy, and K. L. Williams. "The distribution of myosin II in Dictyostelium discoideum slug cells." Journal of Cell Biology 115, no. 5 (December 1, 1991): 1267–74. http://dx.doi.org/10.1083/jcb.115.5.1267.
Повний текст джерелаKim, Jong-Hee, and LaDora V. Thompson. "Non-weight bearing-induced muscle weakness: the role of myosin quantity and quality in MHC type II fibers." American Journal of Physiology-Cell Physiology 307, no. 2 (July 15, 2014): C190—C194. http://dx.doi.org/10.1152/ajpcell.00076.2014.
Повний текст джерелаAgarwal, Priti, and Ronen Zaidel-Bar. "Diverse roles of non-muscle myosin II contractility in 3D cell migration." Essays in Biochemistry 63, no. 5 (September 24, 2019): 497–508. http://dx.doi.org/10.1042/ebc20190026.
Повний текст джерелаVerkhovsky, A. B., and G. G. Borisy. "Non-sarcomeric mode of myosin II organization in the fibroblast lamellum." Journal of Cell Biology 123, no. 3 (November 1, 1993): 637–52. http://dx.doi.org/10.1083/jcb.123.3.637.
Повний текст джерелаMatsui, Tsubasa S., Roland Kaunas, Makoto Kanzaki, Masaaki Sato, and Shinji Deguchi. "Non-muscle myosin II induces disassembly of actin stress fibres independently of myosin light chain dephosphorylation." Interface Focus 1, no. 5 (August 3, 2011): 754–66. http://dx.doi.org/10.1098/rsfs.2011.0031.
Повний текст джерелаNewell-Litwa, K. A., R. Horwitz, and M. L. Lamers. "Non-muscle myosin II in disease: mechanisms and therapeutic opportunities." Disease Models & Mechanisms 8, no. 12 (November 5, 2015): 1495–515. http://dx.doi.org/10.1242/dmm.022103.
Повний текст джерелаWest-Foyle, Hoku, Priyanka Kothari, Jonathan Osborne, and Douglas N. Robinson. "14-3-3 proteins tune non-muscle myosin II assembly." Journal of Biological Chemistry 293, no. 18 (March 16, 2018): 6751–61. http://dx.doi.org/10.1074/jbc.m117.819391.
Повний текст джерелаSchewkunow, Vitali, Karan P. Sharma, Gerold Diez, Anna H. Klemm, Pal C. Sharma, and Wolfgang H. Goldmann. "Thermodynamic evidence of non-muscle myosin II–lipid-membrane interaction." Biochemical and Biophysical Research Communications 366, no. 2 (February 2008): 500–505. http://dx.doi.org/10.1016/j.bbrc.2007.11.170.
Повний текст джерелаVerkhovsky, A. B., T. M. Svitkina, and G. G. Borisy. "Polarity sorting of actin filaments in cytochalasin-treated fibroblasts." Journal of Cell Science 110, no. 15 (August 1, 1997): 1693–704. http://dx.doi.org/10.1242/jcs.110.15.1693.
Повний текст джерелаWang, Kui, Zhifang Yang, Xiaohui Chen, Shunxiao Liu, Xiang Li, Liuhao Wang, Hao Yu, and Hongwei Zhang. "Characterization and analysis of myosin gene family in the whitefly (<i>Bemisia tabaci</i>)." AIMS Molecular Science 9, no. 2 (2022): 91–106. http://dx.doi.org/10.3934/molsci.2022006.
Повний текст джерелаJavier-Torrent, Míriam, and Carlos A. Saura. "Conventional and Non-Conventional Roles of Non-Muscle Myosin II-Actin in Neuronal Development and Degeneration." Cells 9, no. 9 (August 19, 2020): 1926. http://dx.doi.org/10.3390/cells9091926.
Повний текст джерелаMoura, Pedro L., Bethan R. Hawley, Tosti J. Mankelow, Rebecca E. Griffiths, Johannes G. G. Dobbe, Geert J. Streekstra, David J. Anstee, Timothy J. Satchwell, and Ashley M. Toye. "Non-muscle myosin II drives vesicle loss during human reticulocyte maturation." Haematologica 103, no. 12 (August 3, 2018): 1997–2007. http://dx.doi.org/10.3324/haematol.2018.199083.
Повний текст джерелаBetapudi, Venkaiah, Linda Hsi, Kristi L. Allen, Belinda Willard, and Keith R. McCrae. "Non-Muscle Myosin II Mediates Microparticle Release From Endothelial Cells Activated by Antiphospholipid Antibodies,." Blood 118, no. 21 (November 18, 2011): 3343. http://dx.doi.org/10.1182/blood.v118.21.3343.3343.
Повний текст джерелаKondo, Tomo, Kozue Hamao, Keiju Kamijo, Hiroshi Kimura, Makiko Morita, Masayuki Takahashi, and Hiroshi Hosoya. "Enhancement of myosin II/actin turnover at the contractile ring induces slower furrowing in dividing HeLa cells." Biochemical Journal 435, no. 3 (April 13, 2011): 569–76. http://dx.doi.org/10.1042/bj20100837.
Повний текст джерелаMarcucci, Lorenzo, Hiroki Fukunaga, Toshio Yanagida, and Mitsuhiro Iwaki. "The Synergic Role of Actomyosin Architecture and Biased Detachment in Muscle Energetics: Insights in Cross Bridge Mechanism beyond the Lever-Arm Swing." International Journal of Molecular Sciences 22, no. 13 (June 29, 2021): 7037. http://dx.doi.org/10.3390/ijms22137037.
Повний текст джерелаBond, Lisa M., Hemma Brandstaetter, James R. Sellers, John Kendrick-Jones, and Folma Buss. "Myosin motor proteins are involved in the final stages of the secretory pathways." Biochemical Society Transactions 39, no. 5 (September 21, 2011): 1115–19. http://dx.doi.org/10.1042/bst0391115.
Повний текст джерелаVicente-Manzanares, Miguel, Xuefei Ma, Robert S. Adelstein, and Alan Rick Horwitz. "Non-muscle myosin II takes centre stage in cell adhesion and migration." Nature Reviews Molecular Cell Biology 10, no. 11 (November 2009): 778–90. http://dx.doi.org/10.1038/nrm2786.
Повний текст джерелаSnell, Nicole E. "Triple FRET Imaging of Non-Muscle Myosin II Localization in Migrating Cells." Biophysical Journal 112, no. 3 (February 2017): 267a. http://dx.doi.org/10.1016/j.bpj.2016.11.1449.
Повний текст джерелаChattoraj, Shyamtanu, Shekhar Saha, Debdatta Halder, Siddhartha S. Jana, and Kankan Bhattacharyya. "Structural Oscillations of Non-muscle Myosin II-C2: Time Resolved Confocal Microscopy." ChemistrySelect 2, no. 3 (January 23, 2017): 953–58. http://dx.doi.org/10.1002/slct.201601963.
Повний текст джерелаWang, Aibing, Xuefei Ma, Mary Anne Conti, and Robert S. Adelstein. "Distinct and redundant roles of the non-muscle myosin II isoforms and functional domains." Biochemical Society Transactions 39, no. 5 (September 21, 2011): 1131–35. http://dx.doi.org/10.1042/bst0391131.
Повний текст джерелаChaudoir, B. M., P. A. Kowalczyk, and R. L. Chisholm. "Regulatory light chain mutations affect myosin motor function and kinetics." Journal of Cell Science 112, no. 10 (May 15, 1999): 1611–20. http://dx.doi.org/10.1242/jcs.112.10.1611.
Повний текст джерелаHirota, Yuki, Alice Meunier, Shihhui Huang, Togo Shimozawa, Yasuyuki S. Kida, Masashi Inoue, Tsubasa Ito, et al. "Planar cell polarity of multiciliated ependymal cells regulated by non-muscle myosin II." Neuroscience Research 68 (January 2010): e364. http://dx.doi.org/10.1016/j.neures.2010.07.1614.
Повний текст джерелаNie, Wei, Ming-tzo Wei, H. Daniel Ou-Yang, Sabrina Jedlicka, and Dimitrios Vavylonis. "Dynamics of Non-Muscle Myosin II Organization into Stress Fibers and Contractile Networks." Biophysical Journal 104, no. 2 (January 2013): 140a. http://dx.doi.org/10.1016/j.bpj.2012.11.799.
Повний текст джерелаLiu, Zhenan, Elke Van Rossen, Jean-Pierre Timmermans, Albert Geerts, Leo A. van Grunsven, and Hendrik Reynaert. "Distinct roles for non-muscle myosin II isoforms in mouse hepatic stellate cells." Journal of Hepatology 54, no. 1 (January 2011): 132–41. http://dx.doi.org/10.1016/j.jhep.2010.06.020.
Повний текст джерелаHo, Wei-Ting, Jung-Shen Chang, San-Fang Chou, Wei-Lun Hwang, Po-Jen Shih, Shu-Wen Chang, Muh-Hwa Yang, Tzuu-Shuh Jou, and I.-Jong Wang. "Targeting non-muscle myosin II promotes corneal endothelial migration through regulating lamellipodial dynamics." Journal of Molecular Medicine 97, no. 9 (July 13, 2019): 1345–57. http://dx.doi.org/10.1007/s00109-019-01818-5.
Повний текст джерелаKovari, Daniel T., Wenbin Wei, Jan-Simon Toro, Ruth E. Fogg, Karen Porter, and Jennifer E. Curtis. "Frustrated Phagocytic Spreading Dynamics End in Distinct Non-Muscle Myosin II Dependent Contraction." Biophysical Journal 110, no. 3 (February 2016): 621a. http://dx.doi.org/10.1016/j.bpj.2015.11.3330.
Повний текст джерелаLee, Stacey, and Sanjay Kumar. "Actomyosin stress fiber mechanosensing in 2D and 3D." F1000Research 5 (September 7, 2016): 2261. http://dx.doi.org/10.12688/f1000research.8800.1.
Повний текст джерелаPetrof, B. J., A. M. Kelly, N. A. Rubinstein, and A. I. Pack. "Effect of hypothyroidism on myosin heavy chain expression in rat pharyngeal dilator muscles." Journal of Applied Physiology 73, no. 1 (July 1, 1992): 179–87. http://dx.doi.org/10.1152/jappl.1992.73.1.179.
Повний текст джерелаJana, Siddhartha S., Kye-Young Kim, Jian Mao, Sachiyo Kawamoto, James R. Sellers, and Robert S. Adelstein. "An Alternatively Spliced Isoform of Non-muscle Myosin II-C Is Not Regulated by Myosin Light Chain Phosphorylation." Journal of Biological Chemistry 284, no. 17 (February 23, 2009): 11563–71. http://dx.doi.org/10.1074/jbc.m806574200.
Повний текст джерелаHabicht, Juri, Ashley Mooneyham, Asumi Hoshino, Mihir Shetty, Xiaonan Zhang, Edith Emmings, Qing Yang, Courtney Coombes, Melissa K. Gardner, and Martina Bazzaro. "UNC-45A breaks the microtubule lattice independently of its effects on non-muscle myosin II." Journal of Cell Science 134, no. 1 (December 1, 2020): jcs248815. http://dx.doi.org/10.1242/jcs.248815.
Повний текст джерелаSingh, Kuldeep, Anne B. Kim, and Kathleen G. Morgan. "Non‐muscle myosin II regulates aortic stiffness through effects on specific focal adhesion proteins and the non‐muscle cortical cytoskeleton." Journal of Cellular and Molecular Medicine 25, no. 5 (February 6, 2021): 2471–83. http://dx.doi.org/10.1111/jcmm.16170.
Повний текст джерелаChen, Ping, De-qiang Xu, Sheng-li Xu, He Xiao, Sheng-hong Wan, Xing-huan Wang, Michael E. DiSanto, and Xin-hua Zhang. "Blebbistatin modulates prostatic cell growth and contrapctility through myosin II signaling." Clinical Science 132, no. 20 (October 19, 2018): 2189–205. http://dx.doi.org/10.1042/cs20180294.
Повний текст джерелаAguilar-Cuenca, Rocío, Clara Llorente-González, Jessica R. Chapman, Vanessa C. Talayero, Marina Garrido-Casado, Cristina Delgado-Arévalo, María Millán-Salanova, et al. "Tyrosine Phosphorylation of the Myosin Regulatory Light Chain Controls Non-muscle Myosin II Assembly and Function in Migrating Cells." Current Biology 30, no. 13 (July 2020): 2446–58. http://dx.doi.org/10.1016/j.cub.2020.04.057.
Повний текст джерелаWendt, T., D. Taylor, K. Trybus, and K. Taylor. "3-D Electron Crystallography Reveals the “Off” State of Smooth Muscle Myosin." Microscopy and Microanalysis 6, S2 (August 2000): 86–87. http://dx.doi.org/10.1017/s143192760003292x.
Повний текст джерелаZeng, Q., D. Lagunoff, R. Masaracchia, Z. Goeckeler, G. Cote, and R. Wysolmerski. "Endothelial cell retraction is induced by PAK2 monophosphorylation of myosin II." Journal of Cell Science 113, no. 3 (February 1, 2000): 471–82. http://dx.doi.org/10.1242/jcs.113.3.471.
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