Year |
Citation |
Score |
2015 |
Yuan CC, Muthu P, Kazmierczak K, Liang J, Huang W, Irving TC, Kanashiro-Takeuchi RM, Hare JM, Szczesna-Cordary D. Constitutive phosphorylation of cardiac myosin regulatory light chain prevents development of hypertrophic cardiomyopathy in mice. Proceedings of the National Academy of Sciences of the United States of America. PMID 26124132 DOI: 10.1073/Pnas.1505819112 |
0.466 |
|
2014 |
Farman GP, Muthu P, Kazmierczak K, Szczesna-Cordary D, Moore JR. Impact of familial hypertrophic cardiomyopathy-linked mutations in the NH2 terminus of the RLC on β-myosin cross-bridge mechanics. Journal of Applied Physiology (Bethesda, Md. : 1985). 117: 1471-7. PMID 25324513 DOI: 10.1152/Japplphysiol.00798.2014 |
0.517 |
|
2014 |
Huang W, Liang J, Kazmierczak K, Muthu P, Duggal D, Farman GP, Sorensen L, Pozios I, Abraham TP, Moore JR, Borejdo J, Szczesna-Cordary D. Hypertrophic cardiomyopathy associated Lys104Glu mutation in the myosin regulatory light chain causes diastolic disturbance in mice. Journal of Molecular and Cellular Cardiology. 74: 318-29. PMID 24992035 DOI: 10.1016/J.Yjmcc.2014.06.011 |
0.688 |
|
2014 |
Muthu P, Liang J, Schmidt W, Moore JR, Szczesna-Cordary D. In vitro rescue study of a malignant familial hypertrophic cardiomyopathy phenotype by pseudo-phosphorylation of myosin regulatory light chain. Archives of Biochemistry and Biophysics. 552: 29-39. PMID 24374283 DOI: 10.1016/J.Abb.2013.12.011 |
0.523 |
|
2014 |
Yuan C, Muthu P, Kanashiro-Takeuchi R, Liang J, Rojas AI, Kazmierczak K, Hare JM, Irving T, Szczesna-Cordary D. The Structure-Function Analysis of Myosin Pseudo-Phosphorylation in Mouse Model of FHC Biophysical Journal. 106: 771a. DOI: 10.1016/J.Bpj.2013.11.4235 |
0.522 |
|
2014 |
Nagwekar J, Duggal D, Midde K, Muthu P, Huang W, Fudala R, Gryczynski I, Gryczynski Z, Szczesna-Cordary D, Borejdo J. A13T Mutation in the Regulatory Light Chain Associated with Cardiac Hypertrophy Imposes Differences in Kinetics of Healthy and Diseased Ventricles Biophysical Journal. 106: 563a. DOI: 10.1016/J.Bpj.2013.11.3128 |
0.727 |
|
2014 |
Karabina A, Muthu P, Kazmierczak K, Szczesna-Cordary D, Moore J. The Effect of Myosin Regulatory Light Chain Phosphorylation on N47K Mutant Myosin Mechanics Biophysical Journal. 106: 563a. DOI: 10.1016/J.Bpj.2013.11.3126 |
0.494 |
|
2014 |
Huang W, Liang J, Kazmierczak K, Muthu P, Yuan C, Rojas AI, Duggal D, Borejdo J, Irving TC, Szczesna-Cordary D. Familial Hypertrophic Cardiomyopathy-Linked Mutation (K104E) in the Myosin Regulatory Light Chain Affects Sarcomeric Structure and Function in Tg-Mice Biophysical Journal. 106: 33a. DOI: 10.1016/J.Bpj.2013.11.254 |
0.685 |
|
2014 |
Muthu P, Yuan C, Kazmierczak K, Liang J, Rojas AI, Szczesna-Cordary D. Elucidating the Role of Myosin Pseudo-Phosphorylation in a Novel Rescue Mouse Model of Cardiomyopathy Biophysical Journal. 106: 344a. DOI: 10.1016/J.Bpj.2013.11.1964 |
0.507 |
|
2013 |
Kazmierczak K, Paulino EC, Huang W, Muthu P, Liang J, Yuan CC, Rojas AI, Hare JM, Szczesna-Cordary D. Discrete effects of A57G-myosin essential light chain mutation associated with familial hypertrophic cardiomyopathy. American Journal of Physiology. Heart and Circulatory Physiology. 305: H575-89. PMID 23748425 DOI: 10.1152/Ajpheart.00107.2013 |
0.504 |
|
2013 |
Wang L, Muthu P, Szczesna-Cordary D, Kawai M. Diversity and similarity of motor function and cross-bridge kinetics in papillary muscles of transgenic mice carrying myosin regulatory light chain mutations D166V and R58Q. Journal of Molecular and Cellular Cardiology. 62: 153-63. PMID 23727233 DOI: 10.1016/J.Yjmcc.2013.05.012 |
0.484 |
|
2013 |
Wang L, Muthu P, Szczesna-Cordary D, Kawai M. Characterizations of myosin essential light chain's N-terminal truncation mutant Δ43 in transgenic mouse papillary muscles by using tension transients in response to sinusoidal length alterations. Journal of Muscle Research and Cell Motility. 34: 93-105. PMID 23397074 DOI: 10.1007/S10974-013-9337-X |
0.522 |
|
2013 |
Muthu P, Huang W, Kazmierczak K, Liang J, Rojas AI, Irving T, Szczesna-Cordary D. Structural Defects Induced by Malignant Mutations in the Regulatory Light Chain of Myosin Biophysical Journal. 104: 157a. DOI: 10.1016/J.Bpj.2012.11.887 |
0.459 |
|
2013 |
Huang W, Kazmierczak K, Muthu P, Szczesna-Cordary D. Effects of Hcm-Linked Mutations in Myosin Essential Light Chain and the Role of Serine-195 Pseudo-Phosphorylation Biophysical Journal. 104: 157a. DOI: 10.1016/J.Bpj.2012.11.886 |
0.507 |
|
2013 |
Karabina A, Muthu P, Kazmierczak K, Szczesna-Cordary D, Moore J. The Effect of Regulatory Light Chain Phosphorylation on Myosin Bearing Familial Hypertrophic Cardiomyopathy-Linked Mutations Biophysical Journal. 104: 157a. DOI: 10.1016/J.Bpj.2012.11.885 |
0.493 |
|
2012 |
Borejdo J, Szczesna-Cordary D, Muthu P, Metticolla P, Luchowski R, Gryczynski Z, Gryczynski I. Single molecule detection approach to muscle study: kinetics of a single cross-bridge during contraction of muscle. Methods in Molecular Biology (Clifton, N.J.). 875: 311-34. PMID 22573449 DOI: 10.1007/978-1-61779-806-1_17 |
0.736 |
|
2012 |
Kazmierczak K, Muthu P, Huang W, Jones M, Wang Y, Szczesna-Cordary D. Myosin regulatory light chain mutation found in hypertrophic cardiomyopathy patients increases isometric force production in transgenic mice. The Biochemical Journal. 442: 95-103. PMID 22091967 DOI: 10.1042/Bj20111145 |
0.547 |
|
2012 |
Muthu P, Kazmierczak K, Jones M, Szczesna-Cordary D. The effect of myosin RLC phosphorylation in normal and cardiomyopathic mouse hearts. Journal of Cellular and Molecular Medicine. 16: 911-9. PMID 21696541 DOI: 10.1111/J.1582-4934.2011.01371.X |
0.532 |
|
2012 |
Midde K, Dumka V, Pinto J, Muthu P, Marandos P, Gryczynski I, Gryczynski Z, Borejdo J. Myosin Cross-Bridges do not Form Precise Rigor Bonds in Hypertrophic Heart Muscle Carrying Troponin T Mutations Biophysical Journal. 102: 614a. DOI: 10.1016/j.bpj.2011.11.3347 |
0.4 |
|
2012 |
Wang L, Muthu P, Szczesna-Cordary D, Kawai M. Cross-Bridge Kinetics in Papillary Muscle Fibers from Transgenic Mice Expressing the Aspargine-47 to Lysine (N47K) Mutation in Myosin Regulatory Light Chain Biophysical Journal. 102: 614a. DOI: 10.1016/J.Bpj.2011.11.3346 |
0.504 |
|
2012 |
Muthu P, Kazmierczak K, Huang W, Rojas AI, Szczesna-Cordary D. Myosin Regulatory Light Chain Phosphorylation Rescues Cardiac Dysfunction Caused by Familial Hypertrophic Cardiomyopathy-Linked Mutations Biophysical Journal. 102: 557a. DOI: 10.1016/J.Bpj.2011.11.3037 |
0.577 |
|
2012 |
Huang W, Kazmierczak K, Muthu P, Wang Y, Liang J, Rojas AI, Abraham TP, Szczesna-Cordary D. Physiological Effects of FHC-Causing K104E Mutation in the Myosin Regulatory Light Chain Biophysical Journal. 102: 557a. DOI: 10.1016/J.Bpj.2011.11.3036 |
0.52 |
|
2012 |
Schmidt WM, Muthu P, Watt J, Moore J, Szczesna-Cordary D. Regulatory Light Chain Phosphorylation Mimic S15D Causes Partial Rescue of Isometric Force Production in FHC Causing Mutation D166V Biophysical Journal. 102: 557a. DOI: 10.1016/J.Bpj.2011.11.3035 |
0.547 |
|
2011 |
Muthu P, Wang L, Yuan CC, Kazmierczak K, Huang W, Hernandez OM, Kawai M, Irving TC, Szczesna-Cordary D. Structural and functional aspects of the myosin essential light chain in cardiac muscle contraction. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 25: 4394-405. PMID 21885653 DOI: 10.1096/Fj.11-191973 |
0.547 |
|
2011 |
Midde K, Dumka V, Pinto JR, Muthu P, Marandos P, Gryczynski I, Gryczynski Z, Potter JD, Borejdo J. Myosin cross-bridges do not form precise rigor bonds in hypertrophic heart muscle carrying troponin T mutations. Journal of Molecular and Cellular Cardiology. 51: 409-18. PMID 21683708 DOI: 10.1016/J.Yjmcc.2011.06.001 |
0.765 |
|
2011 |
Kazmierczak K, Muthu P, Huang W, Rojas A, Jones M, Wang Y, Szczesna-Cordary D. The HCM-Linked Ala13thr Mutation in the Cardiac Myosin Regulatory Light Chain Increases Isometric Force Production Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2010.12.813 |
0.558 |
|
2011 |
Huang W, Muthu P, Kazmierczak K, Szczesna-Cordary D. FHC-Linked Myosin Regulatory Light Chain Mutations A13T and K104E Do Not Generate Major Structural Changes Sufficient to Affect Binding of Myosin to Actin Biophysical Journal. 100: 110a-111a. DOI: 10.1016/J.Bpj.2010.12.812 |
0.535 |
|
2011 |
Kerrick WGL, Xu Y, Muthu P, Kazmierczak K, Szczesna-Cordary D. The FHC Mutation D166V in the Cardiac Muscle Regulatory Light-Chain Causes Both a Diastolic and Systolic Dysfunction in Mouse Cardiac Muscle Performance Biophysical Journal. 100: 456a. DOI: 10.1016/J.Bpj.2010.12.2683 |
0.487 |
|
2011 |
Muthu P, Kazmierczak K, Rojas A, Wang Y, Abraham T, Szczesna-Cordary D. The Effect of Myosin RLC Phosphorylation in Healthy and Diseased Heart Biophysical Journal. 100: 361a. DOI: 10.1016/J.Bpj.2010.12.2162 |
0.551 |
|
2010 |
Borejdo J, Szczesna-Cordary D, Muthu P, Calander N. Familial hypertrophic cardiomyopathy can be characterized by a specific pattern of orientation fluctuations of actin molecules . Biochemistry. 49: 5269-77. PMID 20509708 DOI: 10.1021/Bi1006749 |
0.733 |
|
2010 |
Muthu P, Mettikolla P, Calander N, Luchowski R, Gryczynski I, Gryczynski Z, Szczesna-Cordary D, Borejdo J. Single molecule kinetics in the familial hypertrophic cardiomyopathy D166V mutant mouse heart. Journal of Molecular and Cellular Cardiology. 48: 989-98. PMID 19914255 DOI: 10.1016/J.Yjmcc.2009.11.004 |
0.727 |
|
2010 |
Raytman A, Joshi S, Kazmierczak K, Jones M, Muthu P, Szczesna-Cordary D. Biochemical Phenotypes Associated with the Myosin Essential Light Chain Mutations Biophysical Journal. 98: 355a. DOI: 10.1016/J.Bpj.2009.12.1919 |
0.517 |
|
2010 |
Muthu P, Kazmierczak K, Liang J, Rojas AI, Jones M, Borejdo J, Szczesna-Cordary D. Is Slower Myosin Cross-Bridge Kinetics in Tg-D166V Preparations Due to Decreased Myosin RLC Phosphorylation? Biophysical Journal. 98: 355a. DOI: 10.1016/J.Bpj.2009.12.1918 |
0.729 |
|
2008 |
Calander N, Muthu P, Gryczynski Z, Gryczynski I, Borejdo J. Fluorescence correlation spectroscopy in a reverse Kretchmann surface plasmon assisted microscope. Optics Express. 16: 13381-90. PMID 18711576 DOI: 10.1364/Oe.16.013381 |
0.603 |
|
2008 |
Borejdo J, Muthu P, Talent J, Gryczynski Z, Calander N, Akopova I, Shtoyko T, Gryczynski I. Reduction of photobleaching and photodamage in single molecule detection: observing single actin monomer in skeletal myofibrils. Journal of Biomedical Optics. 13: 034021. PMID 18601566 DOI: 10.1117/1.2938689 |
0.64 |
|
2008 |
Muthu P, Calander N, Gryczynski I, Gryczynski Z, Talent JM, Shtoyko T, Akopova I, Borejdo J. Monolayers of silver nanoparticles decrease photobleaching: application to muscle myofibrils. Biophysical Journal. 95: 3429-38. PMID 18556759 DOI: 10.1529/Biophysj.108.130799 |
0.634 |
|
2008 |
Muthu P, Talent JM, Gryczynski I, Borejdo J. Cross-bridge duty cycle in isometric contraction of skeletal myofibrils. Biochemistry. 47: 5657-67. PMID 18426224 DOI: 10.1021/Bi7023223 |
0.643 |
|
2008 |
Muthu P, Gryczynski I, Gryczynski Z, Talent JM, Akopova I, Borejdo J. Decreasing photobleaching by silver nanoparticles on metal surfaces: application to muscle myofibrils. Journal of Biomedical Optics. 13: 014023. PMID 18315381 DOI: 10.1117/1.2854120 |
0.613 |
|
2007 |
Muthu P, Gryczynski I, Gryczynski Z, Talent J, Akopova I, Jain K, Borejdo J. Decreasing photobleaching by silver island films: application to muscle. Analytical Biochemistry. 366: 228-36. PMID 17531183 DOI: 10.1016/J.Ab.2007.04.014 |
0.653 |
|
2007 |
Borejdo J, Muthu P, Talent J, Akopova I, Burghardt TP. Rotation of actin monomers during isometric contraction of skeletal muscle. Journal of Biomedical Optics. 12: 014013. PMID 17343488 DOI: 10.1117/1.2697286 |
0.686 |
|
2007 |
Gryczynski Z, Gryczynski I, Matveeva EG, Calander N, Grygorczyk R, Akopova I, Bharill S, Muthu P, Klidgar S, Borejdo J. New surface plasmons approach to Single Molecule Detection (SMD) and Fluorescence Correlation Spectroscopy (FCS) Progress in Biomedical Optics and Imaging - Proceedings of Spie. 6444. DOI: 10.1117/12.715268 |
0.586 |
|
2006 |
Borejdo J, Gryczynski Z, Calander N, Muthu P, Gryczynski I. Application of surface plasmon coupled emission to study of muscle. Biophysical Journal. 91: 2626-35. PMID 16844757 DOI: 10.1529/Biophysj.106.088369 |
0.672 |
|
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