Статті в журналах з теми "Myosin mechanics"
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Surcel, 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 джерелаFarman, Gerrie P., Priya Muthu, Katarzyna Kazmierczak, Danuta Szczesna-Cordary та Jeffrey R. Moore. "Impact of familial hypertrophic cardiomyopathy-linked mutations in the NH2 terminus of the RLC on β-myosin cross-bridge mechanics". Journal of Applied Physiology 117, № 12 (15 грудня 2014): 1471–77. http://dx.doi.org/10.1152/japplphysiol.00798.2014.
Повний текст джерелаHoh, Joseph F. Y. "`Superfast' or masticatory myosin and the evolution of jaw-closing muscles of vertebrates." Journal of Experimental Biology 205, no. 15 (August 1, 2002): 2203–10. http://dx.doi.org/10.1242/jeb.205.15.2203.
Повний текст джерелаButtrick, P. M., A. Malhotra, and J. Scheuer. "Effects of systolic overload and swim training on cardiac mechanics and biochemistry in rats." Journal of Applied Physiology 64, no. 4 (April 1, 1988): 1466–71. http://dx.doi.org/10.1152/jappl.1988.64.4.1466.
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 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 джерелаBates, Genevieve, Sara Sigurdardottir, Linda Kachmar, Nedjma B. Zitouni, Andrea Benedetti, Basil J. Petrof, Dilson Rassier, and Anne-Marie Lauzon. "Molecular, cellular, and muscle strip mechanics of the mdx mouse diaphragm." American Journal of Physiology-Cell Physiology 304, no. 9 (May 1, 2013): C873—C880. http://dx.doi.org/10.1152/ajpcell.00220.2012.
Повний текст джерелаAlpert, Norman R., Christine Brosseau, Andrea Federico, Maike Krenz, Jeffrey Robbins, and David M. Warshaw. "Molecular mechanics of mouse cardiac myosin isoforms." American Journal of Physiology-Heart and Circulatory Physiology 283, no. 4 (October 1, 2002): H1446—H1454. http://dx.doi.org/10.1152/ajpheart.00274.2002.
Повний текст джерелаVeigel, Claudia, and James R. Sellers. "Mechanics of myosin V near stall." Biophysical Journal 96, no. 3 (February 2009): 138a. http://dx.doi.org/10.1016/j.bpj.2008.12.3865.
Повний текст джерелаSiththanandan, Verl B., Yasuharu Takagi, Yi Yang, Davin K. T. Hong, and James R. Sellers. "Characterization of drosophila myosin 7a mechanics." Biophysical Journal 96, no. 3 (February 2009): 141a. http://dx.doi.org/10.1016/j.bpj.2008.12.3878.
Повний текст джерелаYanagida, T., S. Esaki, A. Hikikoshi Iwane, Y. Inoue, A. Ishijima, K. Kitamura, H. Tanaka, and M. Tokunaga. "Single–motor mechanics and models of the myosin motor." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 355, no. 1396 (April 29, 2000): 441–47. http://dx.doi.org/10.1098/rstb.2000.0585.
Повний текст джерелаCaremani, Marco, and Massimo Reconditi. "Anisotropic Elasticity of the Myosin Motor in Muscle." International Journal of Molecular Sciences 23, no. 5 (February 25, 2022): 2566. http://dx.doi.org/10.3390/ijms23052566.
Повний текст джерелаHuxley, A. F. "Mechanics and models of the myosin motor." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 355, no. 1396 (April 29, 2000): 433–40. http://dx.doi.org/10.1098/rstb.2000.0584.
Повний текст джерелаBaker, Josh E. "Saturation of Actin-Myosin Kinetics and Mechanics." Biophysical Journal 120, no. 3 (February 2021): 60a. http://dx.doi.org/10.1016/j.bpj.2020.11.596.
Повний текст джерелаOhnuki, Y., Y. Kunioka, M. Ohtsuki, T. Yamada, Y. Saeki, and K. yanagisawa. "1P170 Molecular mechanics of masticatory muscle myosin." Seibutsu Butsuri 44, supplement (2004): S72. http://dx.doi.org/10.2142/biophys.44.s72_2.
Повний текст джерелаBaker, Josh E. "The collective mechanics of myosin in muscle." Biophysical Journal 96, no. 3 (February 2009): 554a. http://dx.doi.org/10.1016/j.bpj.2008.12.3638.
Повний текст джерелаGuilford, William H., and David M. Warshaw. "The molecular mechanics of smooth muscle myosin." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 119, no. 3 (March 1998): 451–58. http://dx.doi.org/10.1016/s0305-0491(98)00002-9.
Повний текст джерелаLarson, Stephanie M., Hyo J. Lee, Pei-hsuan Hung, Lauren M. Matthews, Douglas N. Robinson, and Janice P. Evans. "Cortical Mechanics and Meiosis II Completion in Mammalian Oocytes Are Mediated by Myosin-II and Ezrin-Radixin-Moesin (ERM) Proteins." Molecular Biology of the Cell 21, no. 18 (September 15, 2010): 3182–92. http://dx.doi.org/10.1091/mbc.e10-01-0066.
Повний текст джерелаKarabina, Anastasia, Priya Muthu, Katarzyna Kazmierczak, Danuta Szczesna-Cordary, and Jeffrey Moore. "The Effect of Myosin Regulatory Light Chain Phosphorylation on N47K Mutant Myosin Mechanics." Biophysical Journal 106, no. 2 (January 2014): 563a. http://dx.doi.org/10.1016/j.bpj.2013.11.3126.
Повний текст джерелаMoore, Jeffrey R., Elena B. Krementsova, Kathleen M. Trybus, and David M. Warshaw. "Myosin V exhibits a high duty cycle and large unitary displacement." Journal of Cell Biology 155, no. 4 (November 12, 2001): 625–36. http://dx.doi.org/10.1083/jcb.200103128.
Повний текст джерелаWakatsuki, T. "Mechanics of cell spreading: role of myosin II." Journal of Cell Science 116, no. 8 (March 4, 2003): 1617–25. http://dx.doi.org/10.1242/jcs.00340.
Повний текст джерелаSellers, James R., John Kendrick-Jones, and Claudia Veigel. "Single Molecule Mechanics Of Myosin Motors Under Load." Biophysical Journal 96, no. 3 (February 2009): 553a. http://dx.doi.org/10.1016/j.bpj.2008.12.3636.
Повний текст джерелаNorstrom, Melanie F., Philip A. Smithback, and Ronald S. Rock. "Unconventional Processive Mechanics of Non-muscle Myosin IIB." Journal of Biological Chemistry 285, no. 34 (May 29, 2010): 26326–34. http://dx.doi.org/10.1074/jbc.m110.123851.
Повний текст джерелаJiang, Ming Ya, and Michael P. Sheetz. "Mechanics of myosin motor: Force and step size." BioEssays 16, no. 8 (August 1994): 531–32. http://dx.doi.org/10.1002/bies.950160803.
Повний текст джерелаWang, Yihua, Katalin Ajtai, and Thomas P. Burghardt. "Cardiac and skeletal actin substrates uniquely tune cardiac myosin strain-dependent mechanics." Open Biology 8, no. 11 (November 2018): 180143. http://dx.doi.org/10.1098/rsob.180143.
Повний текст джерелаKhokhlova, Anastasia, Tatiana Myachina, Denis Volzhaninov, Xenia Butova, Anastasia Kochurova, Valentina Berg, Irina Gette, et al. "Type 1 Diabetes Impairs Cardiomyocyte Contractility in the Left and Right Ventricular Free Walls but Preserves It in the Interventricular Septum." International Journal of Molecular Sciences 23, no. 3 (February 2, 2022): 1719. http://dx.doi.org/10.3390/ijms23031719.
Повний текст джерелаSquire, John. "Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview." International Journal of Molecular Sciences 20, no. 22 (November 14, 2019): 5715. http://dx.doi.org/10.3390/ijms20225715.
Повний текст джерелаButtrick, P., C. Perla, A. Malhotra, D. Geenen, M. Lahorra, and J. Scheuer. "Effects of chronic dobutamine on cardiac mechanics and biochemistry after myocardial infarction in rats." American Journal of Physiology-Heart and Circulatory Physiology 260, no. 2 (February 1, 1991): H473—H479. http://dx.doi.org/10.1152/ajpheart.1991.260.2.h473.
Повний текст джерелаGreenberg, Michael J., Tanya R. Mealy, James D. Watt, Michelle Jones, Danuta Szczesna-Cordary, and Jeffrey R. Moore. "The molecular effects of skeletal muscle myosin regulatory light chain phosphorylation." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 297, no. 2 (August 2009): R265—R274. http://dx.doi.org/10.1152/ajpregu.00171.2009.
Повний текст джерелаToyoshima, N., N. Hirakawa, Y. Kimura, K. Okamoto, A. Ishijima, and S. Fujime. "Mechanics of Chara myosin measured by an optical tweezers." Seibutsu Butsuri 40, supplement (2000): S199. http://dx.doi.org/10.2142/biophys.40.s199_4.
Повний текст джерелаRedaelli, A., M. Soncini, and F. M. Montevecchi. "Myosin cross-bridge mechanics: geometrical determinants for continuous sliding." Journal of Biomechanics 34, no. 12 (December 2001): 1607–17. http://dx.doi.org/10.1016/s0021-9290(01)00140-3.
Повний текст джерелаFiner, Jeffrey T., Robert M. Simmons, and James A. Spudich. "Single myosin molecule mechanics: piconewton forces and nanometre steps." Nature 368, no. 6467 (March 1994): 113–19. http://dx.doi.org/10.1038/368113a0.
Повний текст джерелаLecarpentier, Y., F. X. Blanc, J. Quillard, J. L. Hébert, X. Krokidis, and C. Coirault. "Statistical mechanics of myosin molecular motors in skeletal muscles." Journal of Theoretical Biology 235, no. 3 (August 2005): 381–92. http://dx.doi.org/10.1016/j.jtbi.2005.01.018.
Повний текст джерелаCai, Shuang, Lidija Pestic-Dragovich, Martha E. O’Donnell, Ning Wang, Donald Ingber, Elliot Elson, and Primal De Lanerolle. "Regulation of cytoskeletal mechanics and cell growth by myosin light chain phosphorylation." American Journal of Physiology-Cell Physiology 275, no. 5 (November 1, 1998): C1349—C1356. http://dx.doi.org/10.1152/ajpcell.1998.275.5.c1349.
Повний текст джерелаMa, Weikang, Marcus Henze, Robert L. Anderson, Henry Gong, Fiona L. Wong, Carlos L. del Rio, and Thomas Irving. "The Super-Relaxed State and Length Dependent Activation in Porcine Myocardium." Circulation Research 129, no. 6 (September 3, 2021): 617–30. http://dx.doi.org/10.1161/circresaha.120.318647.
Повний текст джерелаEgan, Paul F., Jeffrey R. Moore, Allen J. Ehrlicher, David A. Weitz, Christian Schunn, Jonathan Cagan, and Philip LeDuc. "Robust mechanobiological behavior emerges in heterogeneous myosin systems." Proceedings of the National Academy of Sciences 114, no. 39 (September 12, 2017): E8147—E8154. http://dx.doi.org/10.1073/pnas.1713219114.
Повний текст джерелаCooke, R. "Actomyosin interaction in striated muscle." Physiological Reviews 77, no. 3 (July 1, 1997): 671–97. http://dx.doi.org/10.1152/physrev.1997.77.3.671.
Повний текст джерелаToepfer, Christopher N., Markus B. Sikkel, Valentina Caorsi, Anupama Vydyanath, Iratxe Torre, O'Neal Copeland, Alexander R. Lyon, et al. "A post-MI power struggle: adaptations in cardiac power occur at the sarcomere level alongside MyBP-C and RLC phosphorylation." American Journal of Physiology-Heart and Circulatory Physiology 311, no. 2 (August 1, 2016): H465—H475. http://dx.doi.org/10.1152/ajpheart.00899.2015.
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 джерелаWeirich, Kimberly L., Samantha Stam, Edwin Munro, and Margaret L. Gardel. "Actin bundle architecture and mechanics regulate myosin II force generation." Biophysical Journal 120, no. 10 (May 2021): 1957–70. http://dx.doi.org/10.1016/j.bpj.2021.03.026.
Повний текст джерелаShirai, K., H. Machiyama, and A. Ishijima. "Single molecule mechanics of Chara myosin : to keep motile activity." Seibutsu Butsuri 43, supplement (2003): S145. http://dx.doi.org/10.2142/biophys.43.s145_2.
Повний текст джерелаNose, H., H. Machiyama, and A. Ishijima. "3P167 Single molecule mechanics of Chara myosin : investigation of processivity." Seibutsu Butsuri 44, supplement (2004): S231. http://dx.doi.org/10.2142/biophys.44.s231_3.
Повний текст джерелаKojima, H., K. Ito, S. Kimura, K. Yamamoto, and K. Oiwa. "1P169 Single molecule mechanics of recombinant Chara myosin motor domain." Seibutsu Butsuri 45, supplement (2005): S74. http://dx.doi.org/10.2142/biophys.45.s74_1.
Повний текст джерелаDuno-Miranda, Sebastian, Shane R. Nelson, David Rasicci, Skylar M. L. Bodt, Duha Vang, Sivaraj Sivaramakrishnan, Christopher M. Yengo, and David M. Warshaw. "Molecular mechanics of E525K dilated cardiomyopathy mutant human cardiac myosin." Biophysical Journal 122, no. 3 (February 2023): 406a. http://dx.doi.org/10.1016/j.bpj.2022.11.2206.
Повний текст джерелаHai, Chi-Ming, and Hak Rim Kim. "An expanded latch-bridge model of protein kinase C-mediated smooth muscle contraction." Journal of Applied Physiology 98, no. 4 (April 2005): 1356–65. http://dx.doi.org/10.1152/japplphysiol.00834.2004.
Повний текст джерелаGreene, Peter R. "Effects of Thermal Tension Transients on the Muscle Crossbridge." Biophysical Reviews and Letters 11, no. 03 (September 2016): 117–26. http://dx.doi.org/10.1142/s1793048016500053.
Повний текст джерелаPérez-Domínguez, Sandra, Javier López-Alonso, Frank Lafont, and Manfred Radmacher. "Comparison of Rheological Properties of Healthy versus Dupuytren Fibroblasts When Treated with a Cell Contraction Inhibitor by Atomic Force Microscope." International Journal of Molecular Sciences 24, no. 3 (January 20, 2023): 2043. http://dx.doi.org/10.3390/ijms24032043.
Повний текст джерелаSonn-Segev, Adar, Anne Bernheim-Groswasser, and Yael Roichman. "Scale dependence of the mechanics of active gels with increasing motor concentration." Soft Matter 13, no. 40 (2017): 7352–59. http://dx.doi.org/10.1039/c7sm01391d.
Повний текст джерелаSamson, Shiela C., Andrew Elliott, Brian D. Mueller, Yung Kim, Keith R. Carney, Jared P. Bergman, John Blenis, and Michelle C. Mendoza. "p90 ribosomal S6 kinase (RSK) phosphorylates myosin phosphatase and thereby controls edge dynamics during cell migration." Journal of Biological Chemistry 294, no. 28 (May 28, 2019): 10846–62. http://dx.doi.org/10.1074/jbc.ra119.007431.
Повний текст джерелаLecarpentier, Edouard R., Victor A. Claes, Oumar Timbely, Abdelilah Arsalane, Jacques A. Wipff, Jean-Louis M. Hébert, Francine Y. Michel, and Yves C. Lecarpentier. "Mechanics and energetics of myosin molecular motors from nonpregnant human myometrium." Journal of Applied Physiology 111, no. 4 (October 2011): 1096–105. http://dx.doi.org/10.1152/japplphysiol.00414.2011.
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