Статті в журналах з теми "Myosin IIs"
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Park, 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 джерелаLee, Kyoung Hwan, Guidenn Sulbarán, Shixin Yang, Ji Young Mun, Lorenzo Alamo, Antonio Pinto, Osamu Sato, et al. "Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals." Proceedings of the National Academy of Sciences 115, no. 9 (February 14, 2018): E1991—E2000. http://dx.doi.org/10.1073/pnas.1715247115.
Повний текст джерелаWylie, Steven R., and Peter D. Chantler. "Myosin IIC: A Third Molecular Motor Driving Neuronal Dynamics." Molecular Biology of the Cell 19, no. 9 (September 2008): 3956–68. http://dx.doi.org/10.1091/mbc.e07-08-0744.
Повний текст джерелаBezanilla, Magdalena, and Thomas D. Pollard. "Myosin-II Tails Confer Unique Functions inSchizosaccharomyces pombe: Characterization of a Novel Myosin-II Tail." Molecular Biology of the Cell 11, no. 1 (January 2000): 79–91. http://dx.doi.org/10.1091/mbc.11.1.79.
Повний текст джерелаWang, Aibing, Neil Billington, Robert S. Adelstein, and James R. Sellers. "Expression and Characterization of Full Length Nonmuscle Myosin IIs." Biophysical Journal 100, no. 3 (February 2011): 594a. http://dx.doi.org/10.1016/j.bpj.2010.12.3425.
Повний текст джерелаSchiffhauer, Eric S., Yixin Ren, Vicente A. Iglesias, Priyanka Kothari, Pablo A. Iglesias, and Douglas N. Robinson. "Myosin IIB assembly state determines its mechanosensitive dynamics." Journal of Cell Biology 218, no. 3 (January 17, 2019): 895–908. http://dx.doi.org/10.1083/jcb.201806058.
Повний текст джерелаKrivoshik, Andrew P., and Lloyd Barr. "Force relaxes before the fall of cytosolic calcium in the photomechanical response of rat sphincter pupillae." American Journal of Physiology-Cell Physiology 279, no. 1 (July 1, 2000): C274—C280. http://dx.doi.org/10.1152/ajpcell.2000.279.1.c274.
Повний текст джерелаMEDEIROS, N. "PRIMARY PEPTIDE SEQUENCES FROM SQUID MUSCLE AND OPTIC LOBE MYOSIN IIs: A STRATEGY TO IDENTIFY AN ORGANELLE MYOSIN." Cell Biology International 22, no. 2 (February 1998): 161–73. http://dx.doi.org/10.1006/cbir.1998.0248.
Повний текст джерелаSaha, Shekhar, Sumit K. Dey, Provas Das, and Siddhartha S. Jana. "Increased expression of nonmuscle myosin IIs is associated with 3MC-induced mouse tumor." FEBS Journal 278, no. 21 (September 19, 2011): 4025–34. http://dx.doi.org/10.1111/j.1742-4658.2011.08306.x.
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 джерелаBezanilla, Magdalena, Susan L. Forsburg, and Thomas D. Pollard. "Identification of a Second Myosin-II in Schizosaccharomyces pombe:." Molecular Biology of the Cell 8, no. 12 (December 1997): 2693–705. http://dx.doi.org/10.1091/mbc.8.12.2693.
Повний текст джерелаStaron, R. S., and D. Pette. "The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit tibialis anterior muscle." Biochemical Journal 243, no. 3 (May 1, 1987): 695–99. http://dx.doi.org/10.1042/bj2430695.
Повний текст джерелаToyoda, Taro, Azuma Kimura, Hiromi Tanaka, Tomonaga Ameku, Atsushi Mima, Yurie Hirose, Masahiro Nakamura, Akira Watanabe, and Kenji Osafune. "Rho-Associated Kinases and Non-muscle Myosin IIs Inhibit the Differentiation of Human iPSCs to Pancreatic Endoderm." Stem Cell Reports 9, no. 2 (August 2017): 419–28. http://dx.doi.org/10.1016/j.stemcr.2017.07.005.
Повний текст джерелаSimerly, Calvin, Grzegorz Nowak, Primal de Lanerolle, and Gerald Schatten. "Differential Expression and Functions of Cortical Myosin IIA and IIB Isotypes during Meiotic Maturation, Fertilization, and Mitosis in Mouse Oocytes and Embryos." Molecular Biology of the Cell 9, no. 9 (September 1998): 2509–25. http://dx.doi.org/10.1091/mbc.9.9.2509.
Повний текст джерелаO'Hara, Steven P., Gabriella B. Gajdos, Christy E. Trussoni, Patrick L. Splinter, and Nicholas F. LaRusso. "Cholangiocyte Myosin IIB Is Required for Localized Aggregation of Sodium Glucose Cotransporter 1 to Sites of Cryptosporidium parvum Cellular Invasion and Facilitates Parasite Internalization." Infection and Immunity 78, no. 7 (May 10, 2010): 2927–36. http://dx.doi.org/10.1128/iai.00077-10.
Повний текст джерелаLiu, Xiong, Neil Billington, Shi Shu, Shu-Hua Yu, Grzegorz Piszczek, James R. Sellers, and Edward D. Korn. "Effect of ATP and regulatory light-chain phosphorylation on the polymerization of mammalian nonmuscle myosin II." Proceedings of the National Academy of Sciences 114, no. 32 (July 24, 2017): E6516—E6525. http://dx.doi.org/10.1073/pnas.1702375114.
Повний текст джерелаPICARD, B., L. LEFAUCHEUR, B. FAUCONNEAU, H. REMIGNON, Y. CHEREL, E. BARREY, and J. NEDELEC. "Dossier : Caractérisation des différents types de fibres musculaires dans plusieurs espèces : production et utilisation d’anticorps monoclonaux dirigés contre les chaînes lourdes de myosine rapide IIa et IIb." INRAE Productions Animales 11, no. 2 (April 2, 1998): 145–63. http://dx.doi.org/10.20870/productions-animales.1998.11.2.3926.
Повний текст джерелаArii, Jun, Yoshitaka Hirohata, Akihisa Kato, and Yasushi Kawaguchi. "Nonmuscle Myosin Heavy Chain IIB Mediates Herpes Simplex Virus 1 Entry." Journal of Virology 89, no. 3 (November 26, 2014): 1879–88. http://dx.doi.org/10.1128/jvi.03079-14.
Повний текст джерелаPicariello, Hannah S., Rajappa S. Kenchappa, Vandana Rai, James F. Crish, Athanassios Dovas, Katarzyna Pogoda, Mariah McMahon, et al. "Myosin IIA suppresses glioblastoma development in a mechanically sensitive manner." Proceedings of the National Academy of Sciences 116, no. 31 (June 24, 2019): 15550–59. http://dx.doi.org/10.1073/pnas.1902847116.
Повний текст джерелаKolega, John. "Asymmetric Distribution of Myosin IIB in Migrating Endothelial Cells Is Regulated by a rho-dependent Kinase and Contributes to Tail Retraction." Molecular Biology of the Cell 14, no. 12 (December 2003): 4745–57. http://dx.doi.org/10.1091/mbc.e03-04-0205.
Повний текст джерелаTogo, Tatsuru, and Richard A. Steinhardt. "Nonmuscle Myosin IIA and IIB Have Distinct Functions in the Exocytosis-dependent Process of Cell Membrane Repair." Molecular Biology of the Cell 15, no. 2 (February 2004): 688–95. http://dx.doi.org/10.1091/mbc.e03-06-0430.
Повний текст джерелаWylie, Steven R., and Peter D. Chantler. "Myosin IIA Drives Neurite Retraction." Molecular Biology of the Cell 14, no. 11 (November 2003): 4654–66. http://dx.doi.org/10.1091/mbc.e03-03-0187.
Повний текст джерелаVicente-Manzanares, Miguel, Margaret A. Koach, Leanna Whitmore, Marcelo L. Lamers, and Alan F. Horwitz. "Segregation and activation of myosin IIB creates a rear in migrating cells." Journal of Cell Biology 183, no. 3 (October 27, 2008): 543–54. http://dx.doi.org/10.1083/jcb.200806030.
Повний текст джерелаMaupin, P., C. L. Phillips, R. S. Adelstein, and T. D. Pollard. "Differential localization of myosin-II isozymes in human cultured cells and blood cells." Journal of Cell Science 107, no. 11 (November 1, 1994): 3077–90. http://dx.doi.org/10.1242/jcs.107.11.3077.
Повний текст джерелаStaron, R. S., and D. Pette. "The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit soleus muscle." Biochemical Journal 243, no. 3 (May 1, 1987): 687–93. http://dx.doi.org/10.1042/bj2430687.
Повний текст джерелаDey, Sumit K., Raman K. Singh, Shyamtanu Chattoraj, Shekhar Saha, Alakesh Das, Kankan Bhattacharyya, Kaushik Sengupta, Shamik Sen, and Siddhartha S. Jana. "Differential role of nonmuscle myosin II isoforms during blebbing of MCF-7 cells." Molecular Biology of the Cell 28, no. 8 (April 15, 2017): 1034–42. http://dx.doi.org/10.1091/mbc.e16-07-0524.
Повний текст джерелаStaron, Robert S., Fredrick C. Hagerman, Robert S. Hikida, Thomas F. Murray, David P. Hostler, Mathew T. Crill, Kerry E. Ragg, and Kumika Toma. "Fiber Type Composition of the Vastus Lateralis Muscle of Young Men and Women." Journal of Histochemistry & Cytochemistry 48, no. 5 (May 2000): 623–29. http://dx.doi.org/10.1177/002215540004800506.
Повний текст джерелаBriggs, Margaret M., and Fred Schachat. "The superfast extraocular myosin (MYH13) is localized to the innervation zone in both the global and orbital layers of rabbit extraocular muscle." Journal of Experimental Biology 205, no. 20 (October 15, 2002): 3133–42. http://dx.doi.org/10.1242/jeb.205.20.3133.
Повний текст джерелаSurcel, Alexandra, Eric Schiffhauer, Dustin Thomas, Qingfeng Zhu, Robert Anders, and Douglas Robinson. "Dictyostelium Mechanics Accurately Identifies New Targetable Drug Space for Pancreatic Cancer Delineated by Myosin IIS, Filamins, and Alpha-Actinins, Collectively Comprimising the Mechanobiome." Biophysical Journal 112, no. 3 (February 2017): 338a. http://dx.doi.org/10.1016/j.bpj.2016.11.1829.
Повний текст джерелаSurcel, Alexandra, Win Pin Ng, Hoku West-Foyle, Qingfeng Zhu, Yixin Ren, Lindsay B. Avery, Agata K. Krenc, et al. "Pharmacological activation of myosin II paralogs to correct cell mechanics defects." Proceedings of the National Academy of Sciences 112, no. 5 (January 20, 2015): 1428–33. http://dx.doi.org/10.1073/pnas.1412592112.
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 джерелаBloemink, Marieke J., John C. Deacon, Daniel I. Resnicow, Leslie A. Leinwand, and Michael A. Geeves. "The Superfast Human Extraocular Myosin Is Kinetically Distinct from the Fast Skeletal IIa, IIb, and IId Isoforms." Journal of Biological Chemistry 288, no. 38 (August 1, 2013): 27469–79. http://dx.doi.org/10.1074/jbc.m113.488130.
Повний текст джерелаBrown, Jacquelyn A., Robert B. Wysolmerski, and Paul C. Bridgman. "Dorsal Root Ganglion Neurons React to Semaphorin 3A Application through a Biphasic Response that Requires Multiple Myosin II Isoforms." Molecular Biology of the Cell 20, no. 4 (February 15, 2009): 1167–79. http://dx.doi.org/10.1091/mbc.e08-01-0065.
Повний текст джерелаRedowicz, Maria Jolanta. "Myosins and pathology: genetics and biology." Acta Biochimica Polonica 49, no. 4 (December 31, 2002): 789–804. http://dx.doi.org/10.18388/abp.2002_3739.
Повний текст джерелаSestoft, L., P. Iversen, I. Nordgaard, S. Amris, T. Joen, O. Overgaard, and H. Klitgaard. "Working Capacity and Expression of Myosin Heavy Chain Isoforms in Skeletal Muscle of Chronic Alcoholic Men without Liver Disease after I Day and 4 Weeks of Alcohol Abstinence." Clinical Science 86, no. 4 (April 1, 1994): 433–40. http://dx.doi.org/10.1042/cs0860433.
Повний текст джерелаKolega, John. "The Role of Myosin II Motor Activity in Distributing Myosin Asymmetrically and Coupling Protrusive Activity to Cell Translocation." Molecular Biology of the Cell 17, no. 10 (October 2006): 4435–45. http://dx.doi.org/10.1091/mbc.e06-05-0431.
Повний текст джерелаOikonomopoulou, Ifigenia, Hitesh Patel, Paul F. Watson, and Peter D. Chantler. "Relocation of myosin and actin, kinesin and tubulin in the acrosome reaction of bovine spermatozoa." Reproduction, Fertility and Development 21, no. 2 (2009): 364. http://dx.doi.org/10.1071/rd08166.
Повний текст джерелаSato, Masaaki K., Masayuki Takahashi, and Michio Yazawa. "Two Regions of the Tail Are Necessary for the Isoform-specific Functions of Nonmuscle Myosin IIB." Molecular Biology of the Cell 18, no. 3 (March 2007): 1009–17. http://dx.doi.org/10.1091/mbc.e06-08-0706.
Повний текст джерелаWada, M., T. Okumoto, K. Toro, K. Masuda, T. Fukubayashi, K. Kikuchi, S. Niihata, and S. Katsuta. "Expression of hybrid isomyosins in human skeletal muscle." American Journal of Physiology-Cell Physiology 271, no. 4 (October 1, 1996): C1250—C1255. http://dx.doi.org/10.1152/ajpcell.1996.271.4.c1250.
Повний текст джерелаCalábria, Luciana Karen, Alice Vieira da Costa, Renato José da Silva Oliveira, Simone Ramos Deconte, Rafael Nascimento, Washington João de Carvalho, Vanessa Neves de Oliveira, et al. "Myosins Are Differentially Expressed under Oxidative Stress in Chronic Streptozotocin-Induced Diabetic Rat Brains." ISRN Neuroscience 2013 (September 24, 2013): 1–10. http://dx.doi.org/10.1155/2013/423931.
Повний текст джерелаSchiaffino, S., and C. Reggiani. "Myosin isoforms in mammalian skeletal muscle." Journal of Applied Physiology 77, no. 2 (August 1, 1994): 493–501. http://dx.doi.org/10.1152/jappl.1994.77.2.493.
Повний текст джерелаSweeney, H. L., M. J. Kushmerick, K. Mabuchi, J. Gergely, and F. A. Sreter. "Velocity of shortening and myosin isozymes in two types of rabbit fast-twitch muscle fibers." American Journal of Physiology-Cell Physiology 251, no. 3 (September 1, 1986): C431—C434. http://dx.doi.org/10.1152/ajpcell.1986.251.3.c431.
Повний текст джерелаEddinger, T. J., and R. L. Moss. "Mechanical properties of skinned single fibers of identified types from rat diaphragm." American Journal of Physiology-Cell Physiology 253, no. 2 (August 1, 1987): C210—C218. http://dx.doi.org/10.1152/ajpcell.1987.253.2.c210.
Повний текст джерелаGomez, Guillermo A., Robert W. McLachlan, Selwin K. Wu, Benjamin J. Caldwell, Elliott Moussa, Suzie Verma, Michele Bastiani та ін. "An RPTPα/Src family kinase/Rap1 signaling module recruits myosin IIB to support contractile tension at apical E-cadherin junctions". Molecular Biology of the Cell 26, № 7 (квітень 2015): 1249–62. http://dx.doi.org/10.1091/mbc.e14-07-1223.
Повний текст джерелаSandquist, Joshua C., and Anthony R. Means. "The C-Terminal Tail Region of Nonmuscle Myosin II Directs Isoform-specific Distribution in Migrating Cells." Molecular Biology of the Cell 19, no. 12 (December 2008): 5156–67. http://dx.doi.org/10.1091/mbc.e08-05-0533.
Повний текст джерелаFüchtbauer, E. M., A. M. Rowlerson, K. Götz, G. Friedrich, K. Mabuchi, J. Gergely, and H. Jockusch. "Direct correlation of parvalbumin levels with myosin isoforms and succinate dehydrogenase activity on frozen sections of rodent muscle." Journal of Histochemistry & Cytochemistry 39, no. 3 (March 1991): 355–61. http://dx.doi.org/10.1177/39.3.1825216.
Повний текст джерелаHuey, K. A., and S. C. Bodine. "Altered expression of myosin mRNA and protein in rat soleus and tibialis anterior following reinnervation." American Journal of Physiology-Cell Physiology 271, no. 6 (December 1, 1996): C2016—C2026. http://dx.doi.org/10.1152/ajpcell.1996.271.6.c2016.
Повний текст джерелаSartorius, Carol A., Brian D. Lu, Leslie Acakpo-Satchivi, Renee P. Jacobsen, William C. Byrnes, and Leslie A. Leinwand. "Myosin Heavy Chains IIa and IId Are Functionally Distinct in the Mouse." Journal of Cell Biology 141, no. 4 (May 18, 1998): 943–53. http://dx.doi.org/10.1083/jcb.141.4.943.
Повний текст джерелаSieck, G. C., W. Z. Zhan, Y. S. Prakash, M. J. Daood, and J. F. Watchko. "SDH and actomyosin ATPase activities of different fiber types in rat diaphragm muscle." Journal of Applied Physiology 79, no. 5 (November 1, 1995): 1629–39. http://dx.doi.org/10.1152/jappl.1995.79.5.1629.
Повний текст джерелаZhou, Rihong, Charles Watson, Chuanhai Fu, Xuebiao Yao, and John G. Forte. "Myosin II is present in gastric parietal cells and required for lamellipodial dynamics associated with cell activation." American Journal of Physiology-Cell Physiology 285, no. 3 (September 2003): C662—C673. http://dx.doi.org/10.1152/ajpcell.00085.2003.
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