Статті в журналах з теми "Myosin Regulatory Light chain (RLC20)"
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Artamonov, Mykhaylo V., Swapnil K. Sonkusare, Miranda E. Good, Ko Momotani, Masumi Eto, Brant E. Isakson, Thu H. Le, et al. "RSK2 contributes to myogenic vasoconstriction of resistance arteries by activating smooth muscle myosin and the Na+/H+ exchanger." Science Signaling 11, no. 554 (October 30, 2018): eaar3924. http://dx.doi.org/10.1126/scisignal.aar3924.
Повний текст джерелаIhara, Eikichi, Elena Edwards, Meredith A. Borman, David P. Wilson, Michael P. Walsh, and Justin A. MacDonald. "Inhibition of zipper-interacting protein kinase function in smooth muscle by a myosin light chain kinase pseudosubstrate peptide." American Journal of Physiology-Cell Physiology 292, no. 5 (May 2007): C1951—C1959. http://dx.doi.org/10.1152/ajpcell.00434.2006.
Повний текст джерелаTsuji, Masayuki, Takao Ojima, and Kiyoyoshi Nishita. "Exchange of DTNB light chain with molluscan myosin regulatory light chain in rabbit myosin." NIPPON SUISAN GAKKAISHI 55, no. 4 (1989): 681–87. http://dx.doi.org/10.2331/suisan.55.681.
Повний текст джерелаTakashima, Seiji. "Phosphorylation of Myosin Regulatory Light Chain by Myosin Light Chain Kinase, and Muscle Contraction." Circulation Journal 73, no. 2 (2009): 208–13. http://dx.doi.org/10.1253/circj.cj-08-1041.
Повний текст джерелаAkiyama, K., G. Akopian, P. Jinadasa, T. L. Gluckman, A. Terhakopian, B. Massey, and R. J. Bing. "Myocardial Infarction and Regulatory Myosin Light Chain." Journal of Molecular and Cellular Cardiology 29, no. 10 (October 1997): 2641–52. http://dx.doi.org/10.1006/jmcc.1997.0493.
Повний текст джерелаSevrieva, Ivanka R., Birgit Brandmeier, Saraswathi Ponnam, Mathias Gautel, Malcolm Irving, Kenneth S. Campbell, Yin-Biao Sun, and Thomas Kampourakis. "Cardiac myosin regulatory light chain kinase modulates cardiac contractility by phosphorylating both myosin regulatory light chain and troponin I." Journal of Biological Chemistry 295, no. 14 (February 21, 2020): 4398–410. http://dx.doi.org/10.1074/jbc.ra119.011945.
Повний текст джерелаKamm, Kristine E., and James T. Stull. "Signaling to Myosin Regulatory Light Chain in Sarcomeres." Journal of Biological Chemistry 286, no. 12 (January 21, 2011): 9941–47. http://dx.doi.org/10.1074/jbc.r110.198697.
Повний текст джерелаJosephson, Matthew P., Laura A. Sikkink, Alan R. Penheiter, Thomas P. Burghardt, and Katalin Ajtai. "Smooth muscle myosin light chain kinase efficiently phosphorylates serine 15 of cardiac myosin regulatory light chain." Biochemical and Biophysical Research Communications 416, no. 3-4 (December 2011): 367–71. http://dx.doi.org/10.1016/j.bbrc.2011.11.044.
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 джерелаCummins, C., and P. Anderson. "Regulatory myosin light-chain genes of Caenorhabditis elegans." Molecular and Cellular Biology 8, no. 12 (December 1988): 5339–49. http://dx.doi.org/10.1128/mcb.8.12.5339-5349.1988.
Повний текст джерелаCummins, C., and P. Anderson. "Regulatory myosin light-chain genes of Caenorhabditis elegans." Molecular and Cellular Biology 8, no. 12 (December 1988): 5339–49. http://dx.doi.org/10.1128/mcb.8.12.5339.
Повний текст джерелаHuang, Jian, John M. Shelton, James A. Richardson, Kristine E. Kamm, and James T. Stull. "Myosin Regulatory Light Chain Phosphorylation Attenuates Cardiac Hypertrophy." Journal of Biological Chemistry 283, no. 28 (May 12, 2008): 19748–56. http://dx.doi.org/10.1074/jbc.m802605200.
Повний текст джерелаDonato, Megan E., Jonathan Schiavi, Alexis D. Ulerich, Frances E. Weaver, and David J. Coughlin. "Myosin regulatory light chain expression in trout muscle." Journal of Experimental Zoology Part A: Ecological Genetics and Physiology 309A, no. 2 (2008): 64–72. http://dx.doi.org/10.1002/jez.433.
Повний текст джерелаBreithaupt, Jason J., Hannah C. Pulcastro, Peter O. Awinda, David C. DeWitt, and Bertrand C. W. Tanner. "Regulatory light chain phosphorylation augments length-dependent contraction in PTU-treated rats." Journal of General Physiology 151, no. 1 (December 6, 2018): 66–76. http://dx.doi.org/10.1085/jgp.201812158.
Повний текст джерелаPost, P. L., R. L. DeBiasio, and D. L. Taylor. "A fluorescent protein biosensor of myosin II regulatory light chain phosphorylation reports a gradient of phosphorylated myosin II in migrating cells." Molecular Biology of the Cell 6, no. 12 (December 1995): 1755–68. http://dx.doi.org/10.1091/mbc.6.12.1755.
Повний текст джерелаNaqvi, Naweed I., Kelvin C. Y. Wong, Xie Tang, and Mohan K. Balasubramanian. "Type II myosin regulatory light chain relieves auto-inhibition of myosin-heavy-chain function." Nature Cell Biology 2, no. 11 (October 17, 2000): 855–58. http://dx.doi.org/10.1038/35041107.
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 джерелаChen, Chen, Tao Tao, Cheng Wen, Wei-Qi He, Yan-Ning Qiao, Yun-Qian Gao, Xin Chen, et al. "Myosin Light Chain Kinase (MLCK) Regulates Cell Migration in a Myosin Regulatory Light Chain Phosphorylation-independent Mechanism." Journal of Biological Chemistry 289, no. 41 (August 13, 2014): 28478–88. http://dx.doi.org/10.1074/jbc.m114.567446.
Повний текст джерелаDing, Peiguo, Jian Huang, Pavan K. Battiprolu, Joseph A. Hill, Kristine E. Kamm, and James T. Stull. "Cardiac Myosin Light Chain Kinase Is Necessary for Myosin Regulatory Light Chain Phosphorylation and Cardiac Performancein Vivo." Journal of Biological Chemistry 285, no. 52 (October 13, 2010): 40819–29. http://dx.doi.org/10.1074/jbc.m110.160499.
Повний текст джерелаMcDaniel, Nancy L., Christopher M. Rembold, and Richard A. Murphy. "Cyclic nucleotide dependent relaxation in vascular smooth muscle." Canadian Journal of Physiology and Pharmacology 72, no. 11 (November 1, 1994): 1380–85. http://dx.doi.org/10.1139/y94-199.
Повний текст джерелаBennett, A. J., and C. R. Bagshaw. "The mechanism of regulatory light chain dissociation from scallop myosin." Biochemical Journal 233, no. 1 (January 1, 1986): 179–86. http://dx.doi.org/10.1042/bj2330179.
Повний текст джерелаIshibashi, K., A. Evans, T. Shingu, K. Bian, and R. D. Bukoski. "Differential expression and effect of 1,25-dihydroxyvitamin D3 on myosin in arterial tree of rats." American Journal of Physiology-Cell Physiology 269, no. 2 (August 1, 1995): C443—C450. http://dx.doi.org/10.1152/ajpcell.1995.269.2.c443.
Повний текст джерелаGreenberg, M. J., K. Kazmierczak, D. Szczesna-Cordary, and J. R. Moore. "Cardiomyopathy-linked myosin regulatory light chain mutations disrupt myosin strain-dependent biochemistry." Proceedings of the National Academy of Sciences 107, no. 40 (September 20, 2010): 17403–8. http://dx.doi.org/10.1073/pnas.1009619107.
Повний текст джерелаCao, Lichuang, Chengli Hou, Qingwu Shen, Dequan Zhang, and Zhenyu Wang. "Phosphorylation of myosin regulatory light chain affects actomyosin dissociation and myosin degradation." International Journal of Food Science & Technology 54, no. 6 (February 22, 2019): 2246–55. http://dx.doi.org/10.1111/ijfs.14138.
Повний текст джерелаSATTERWHITE, LISA, LARS CISEK, JEFFRY CORDEN, and THOMAS POLLARD. "A p34cdc2-Containing Kinase Phosphorylates Myosin Regulatory Light Chain." Annals of the New York Academy of Sciences 582, no. 1 Cytokinesis (April 1990): 307. http://dx.doi.org/10.1111/j.1749-6632.1990.tb21692.x.
Повний текст джерелаGrant, James W., Rui Q. Zhong, Pat M. McEwen, and Susan L. Church. "Human nonsarcomeric 20,000 Da myosin regulatory light chain cDNA." Nucleic Acids Research 18, no. 19 (1990): 5892. http://dx.doi.org/10.1093/nar/18.19.5892.
Повний текст джерелаWang, Lu, Isabel J. Sobieszek, Chun Y. Seow, and Apolinary Sobieszek. "Purification of Myosin from Bovine Tracheal Smooth Muscle, Filament Formation and Endogenous Association of Its Regulatory Complex." Cells 12, no. 3 (February 3, 2023): 514. http://dx.doi.org/10.3390/cells12030514.
Повний текст джерелаIkebe, M., S. Reardon, J. P. Schwonek, C. R. Sanders, and R. Ikebe. "Structural requirement of the regulatory light chain of smooth muscle myosin as a substrate for myosin light chain kinase." Journal of Biological Chemistry 269, no. 45 (November 1994): 28165–72. http://dx.doi.org/10.1016/s0021-9258(18)46909-8.
Повний текст джерелаDing, Peiguo, Jian Huang, Pavan K. Battiprolu, Joseph A. Hill, Kristine E. Kamm, and James T. Stull. "Cardiac Myosin Light Chain Kinase is Essential for Myosin Regulatory Light Chain Phosphorylation and Normal Cardiac Function in vivo." Biophysical Journal 100, no. 3 (February 2011): 369a. http://dx.doi.org/10.1016/j.bpj.2010.12.2203.
Повний текст джерелаDuggal, D., J. Nagwekar, R. Rich, W. Huang, K. Midde, R. Fudala, H. Das, I. Gryczynski, D. Szczesna-Cordary, and J. Borejdo. "Effect of a myosin regulatory light chain mutation K104E on actin-myosin interactions." American Journal of Physiology-Heart and Circulatory Physiology 308, no. 10 (May 15, 2015): H1248—H1257. http://dx.doi.org/10.1152/ajpheart.00834.2014.
Повний текст джерелаKampourakis, Thomas, and Malcolm Irving. "Phosphorylation of myosin regulatory light chain controls myosin head conformation in cardiac muscle." Journal of Molecular and Cellular Cardiology 85 (August 2015): 199–206. http://dx.doi.org/10.1016/j.yjmcc.2015.06.002.
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 джерелаMackenzie, L. W., R. A. Word, M. L. Casey, and J. T. Stull. "Myosin light chain phosphorylation in human myometrial smooth muscle cells." American Journal of Physiology-Cell Physiology 258, no. 1 (January 1, 1990): C92—C98. http://dx.doi.org/10.1152/ajpcell.1990.258.1.c92.
Повний текст джерелаIchikawa, Hisashi, and Kiyoyoshi Nishita. "Binding ability of regulatory light chain in akazara hybridized myosin." NIPPON SUISAN GAKKAISHI 54, no. 10 (1988): 1823–28. http://dx.doi.org/10.2331/suisan.54.1823.
Повний текст джерелаGnanasekar, Munirathinam, Ashok M. Salunkhe, A. Krishna Mallia, Yi Xun He, and Ramaswamy Kalyanasundaram. "Praziquantel Affects the Regulatory Myosin Light Chain of Schistosoma mansoni." Antimicrobial Agents and Chemotherapy 53, no. 3 (December 22, 2008): 1054–60. http://dx.doi.org/10.1128/aac.01222-08.
Повний текст джерелаLi, Hua-Shan, Qian Lin, Jia Wu, Zhi-Hui Jiang, Jia-Bi Zhao, Jian Pan, Wei-Qi He, and Juan-Min Zha. "Myosin regulatory light chain phosphorylation is associated with leiomyosarcoma development." Biomedicine & Pharmacotherapy 92 (August 2017): 810–18. http://dx.doi.org/10.1016/j.biopha.2017.05.139.
Повний текст джерелаPauly, Daniel F. "The Slow Cardiac Myosin Regulatory Light Chain in Heart Failure." Clinical Cardiology 34, no. 1 (January 2011): 10–11. http://dx.doi.org/10.1002/clc.20867.
Повний текст джерелаWalker, John S., Lori A. Walker, Elaine F. Etter, and Richard A. Murphy. "A Dilution Immunoassay to Measure Myosin Regulatory Light Chain Phosphorylation." Analytical Biochemistry 284, no. 2 (September 2000): 173–82. http://dx.doi.org/10.1006/abio.2000.4704.
Повний текст джерелаCOLEGRAVE, Melanie, Hitesh PATEL, Gerald OFFER, and Peter D. CHANTLER. "Evaluation of the symmetric model for myosin-linked regulation: effect of site-directed mutations in the regulatory light chain on scallop myosin." Biochemical Journal 374, no. 1 (August 15, 2003): 89–96. http://dx.doi.org/10.1042/bj20030404.
Повний текст джерелаLiu, G., and P. C. Newell. "Regulation of myosin regulatory light chain phosphorylation via cyclic GMP during chemotaxis of Dictyostelium." Journal of Cell Science 107, no. 7 (July 1, 1994): 1737–43. http://dx.doi.org/10.1242/jcs.107.7.1737.
Повний текст джерелаGao, Xing, Xin Li, Zheng Li, Manting Du, and Dequan Zhang. "Dephosphorylation of myosin regulatory light chain modulates actin-myosin interaction adverse to meat tenderness." International Journal of Food Science & Technology 52, no. 6 (May 16, 2017): 1400–1407. http://dx.doi.org/10.1111/ijfs.13343.
Повний текст джерелаGreenberg, Michael J., Katarzyna Kazmierczak, Danuta Szczesna-Cordary, and Jeffrey R. Moore. "Familial Hypertrophic Cardiomyopathy Mutations of the Myosin Regulatory Light Chain Remove Myosin Load Sensitivity." Biophysical Journal 98, no. 3 (January 2010): 215a—216a. http://dx.doi.org/10.1016/j.bpj.2009.12.1163.
Повний текст джерелаKarabina, Anastasia, Katarzyna Kazmierczak, Danuta Szczesna-Cordary та Jeffrey R. Moore. "Myosin regulatory light chain phosphorylation enhances cardiac β-myosin in vitro motility under load". Archives of Biochemistry and Biophysics 580 (серпень 2015): 14–21. http://dx.doi.org/10.1016/j.abb.2015.06.014.
Повний текст джерелаLorenz, Robert R., David O. Warner, and Keith A. Jones. "Hydrogen peroxide decreases Ca2+ sensitivity in airway smooth muscle by inhibiting rMLC phosphorylation." American Journal of Physiology-Lung Cellular and Molecular Physiology 277, no. 4 (October 1, 1999): L816—L822. http://dx.doi.org/10.1152/ajplung.1999.277.4.l816.
Повний текст джерелаNayak, Arnab, Tianbang Wang, Peter Franz, Walter Steffen, Igor Chizhov, Georgios Tsiavaliaris, and Mamta Amrute-Nayak. "Single-molecule analysis reveals that regulatory light chains fine-tune skeletal myosin II function." Journal of Biological Chemistry 295, no. 20 (April 9, 2020): 7046–59. http://dx.doi.org/10.1074/jbc.ra120.012774.
Повний текст джерелаIkebe, Reiko, Sheila Reardon, Toshiaki Mitsui, and Mitsuo Ikebe. "Role of the N-terminal Region of the Regulatory Light Chain in the Dephosphorylation of Myosin by Myosin Light Chain Phosphatase." Journal of Biological Chemistry 274, no. 42 (October 15, 1999): 30122–26. http://dx.doi.org/10.1074/jbc.274.42.30122.
Повний текст джерелаTafuri, S. R., A. M. Rushforth, E. R. Kuczmarski, and R. L. Chisholm. "Dictyostelium discoideum myosin: isolation and characterization of cDNAs encoding the regulatory light chain." Molecular and Cellular Biology 9, no. 7 (July 1989): 3073–80. http://dx.doi.org/10.1128/mcb.9.7.3073-3080.1989.
Повний текст джерелаTafuri, S. R., A. M. Rushforth, E. R. Kuczmarski, and R. L. Chisholm. "Dictyostelium discoideum myosin: isolation and characterization of cDNAs encoding the regulatory light chain." Molecular and Cellular Biology 9, no. 7 (July 1989): 3073–80. http://dx.doi.org/10.1128/mcb.9.7.3073.
Повний текст джерелаOstrow, B. D., P. Chen, and R. L. Chisholm. "Expression of a myosin regulatory light chain phosphorylation site mutant complements the cytokinesis and developmental defects of Dictyostelium RMLC null cells." Journal of Cell Biology 127, no. 6 (December 15, 1994): 1945–55. http://dx.doi.org/10.1083/jcb.127.6.1945.
Повний текст джерелаCao, Lichuang, Zhenyu Wang, Dequan Zhang, Xin Li, Chengli Hou, and Chi Ren. "Phosphorylation of myosin regulatory light chain at Ser17 regulates actomyosin dissociation." Food Chemistry 356 (September 2021): 129655. http://dx.doi.org/10.1016/j.foodchem.2021.129655.
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