| Year |
Citation |
Score |
| 2023 |
Zhu L, Landim-Vieira M, Garcia MR, Pinto JR, Chalovich JM. Negative Charges Introduced Near the IT Helix of Cardiac Troponin T Stabilize the Active State of Actin Filaments. Biochemistry. PMID 37379571 DOI: 10.1021/acs.biochem.3c00279 |
0.414 |
|
| 2023 |
Lubomirov LT, Schroeter MM, Hasse V, Frohn M, Metzler D, Bust M, Pryymachuk G, Hescheler J, Grisk O, Chalovich JM, Smyth NR, Pfitzer G, Papadopoulos S. Dual thick and thin filament linked regulation of stretch- and L-NAME-induced tone in young and senescent murine basilar artery. Frontiers in Physiology. 14: 1099278. PMID 37057180 DOI: 10.3389/fphys.2023.1099278 |
0.319 |
|
| 2022 |
Zhu L, Johnson D, Chalovich JM. C-Terminal Basic Region of Troponin T Alters the Ca-Dependent Changes in Troponin I Interactions. Biochemistry. PMID 35522994 DOI: 10.1021/acs.biochem.2c00090 |
0.305 |
|
| 2021 |
Pütz S, Barthel LS, Frohn M, Metzler D, Barham M, Pryymachuk G, Trunschke O, Lubomirov LT, Hescheler J, Chalovich JM, Neiss WF, Koch M, Schroeter MM, Pfitzer G. Caldesmon ablation in mice causes umbilical herniation and alters contractility of fetal urinary bladder smooth muscle. The Journal of General Physiology. 153. PMID 34115104 DOI: 10.1085/jgp.202012776 |
0.389 |
|
| 2020 |
Scarff CA, Carrington G, Casas-Mao D, Chalovich JM, Knight PJ, Ranson NA, Peckham M. Structure of the shutdown state of myosin-2. Nature. PMID 33268888 DOI: 10.1038/s41586-020-2990-5 |
0.306 |
|
| 2020 |
Lopez Davila AJ, Zhu L, Fritz L, Kraft T, Chalovich JM. The Positively Charged C-Terminal Region of Human Skeletal Troponin T Retards Activation and Decreases Calcium Sensitivity. Biochemistry. PMID 33074652 DOI: 10.1021/acs.biochem.0c00499 |
0.404 |
|
| 2020 |
Johnson D, Landim-Vieira M, Solis-Ocampo C, Zhu L, Robinson J, Pinto JRR, Chalovich JM. Eliminating the First Inactive State and Stabilizing the Active State of the Cardiac Regulatory System Alters Behavior in Solution and in Ordered Systems. Biochemistry. PMID 32840354 DOI: 10.1021/Acs.Biochem.0C00430 |
0.539 |
|
| 2020 |
López-Dávila AJ, Chalovich JM, Zittrich S, Piep B, Matinmehr F, Málnási-Csizmadia A, Rauscher AÁ, Kraft T, Brenner B, Stehle R. Cycling Cross-Bridges Contribute to Thin Filament Activation in Human Slow-Twitch Fibers. Frontiers in Physiology. 11: 144. PMID 32265723 DOI: 10.3389/Fphys.2020.00144 |
0.467 |
|
| 2020 |
Lopez-Davila AJ, Zhu L, Fritz L, Kraft T, Chalovich JM. Basic Residues in the C-Terminal Region of Troponin T are Critical in Skeletal Muscle Regulation Biophysical Journal. 118: 495a. DOI: 10.1016/J.Bpj.2019.11.2739 |
0.363 |
|
| 2019 |
Johnson D, Zhu L, Landim-Vieira M, Pinto JR, Chalovich JM. Basic residues within the cardiac troponin T C-terminus are required for full inhibition of muscle contraction and limit activation by calcium. The Journal of Biological Chemistry. PMID 31712308 DOI: 10.1074/Jbc.Ra119.010966 |
0.537 |
|
| 2019 |
Johnson D, Zhu L, Chalovich JM. Basic Amino Acids within the C-Terminal 16 Residues of Troponin T Modulate Calcium Sensitivity and the Distribution of Actin States Biophysical Journal. 116: 466a. DOI: 10.1016/J.Bpj.2018.11.2519 |
0.348 |
|
| 2018 |
Johnson D, Angus CW, Chalovich JM. Stepwise C-Terminal Truncation of Cardiac Troponin T Alters Function at Low and Saturating Ca. Biophysical Journal. PMID 30057009 DOI: 10.1016/J.Bpj.2018.06.028 |
0.512 |
|
| 2018 |
Lopez-Davila AJ, Stehle R, Zittrich S, Piep B, Matinmehr F, Malnasi A, Rauscher A, Chalovich J, Kraft T, Brenner B. Myosin Effects on Thin Filament Activation in Slow-Twitch Human Soleus Muscle Fibers Biophysical Journal. 114: 644a. DOI: 10.1016/J.Bpj.2017.11.3478 |
0.408 |
|
| 2017 |
Baxley T, Johnson D, Pinto JR, Chalovich JM. Troponin C mutations partially stabilize the active state of regulated actin and fully stabilize the active state when paired with Δ14 TnT. Biochemistry. PMID 28530094 DOI: 10.1021/Acs.Biochem.6B01092 |
0.531 |
|
| 2017 |
Johnson D, Angus W, Chalovich JM. Step-Wise Truncation of the C-Terminal 14 Residues of Troponin T Reduces the B State of Regulated Actin and Enhances the M State Biophysical Journal. 112: 259a. DOI: 10.1016/J.Bpj.2016.11.1410 |
0.507 |
|
| 2016 |
Chalovich JM, Johnson D. Commentary: Effect of Skeletal Muscle Native Tropomyosin on the Interaction of Amoeba Actin with Heavy Meromyosin. Frontiers in Physiology. 7: 377. PMID 27629380 DOI: 10.3389/Fphys.2016.00377 |
0.589 |
|
| 2016 |
Johnson DJ, Mathur MC, Kobayashi T, Chalovich JM. The cardiomyopathy mutation, R146G TnI, stabilizes the intermediate "C" state of regulated actin at high and low free Ca2+ conditions. Biochemistry. PMID 27454189 DOI: 10.1021/Acs.Biochem.5B01359 |
0.748 |
|
| 2016 |
Zhang T, Pereyra AS, Wang ZM, Birbrair A, Reisz JA, Files DC, Purcell L, Feng X, Messi ML, Feng H, Chalovich J, Jin JP, Furdui C, Delbono O. Calpain inhibition rescues troponin T3 fragmentation, increases Cav1.1, and enhances skeletal muscle force in aging sedentary mice. Aging Cell. PMID 26892246 DOI: 10.1111/Acel.12453 |
0.409 |
|
| 2015 |
Chalovich JM, Kingsbury N, Mara A. The Kinetics of Fesselin (Avian Synaptopodin 2) Binding to Smooth Muscle Myosin is Dependent on Calcium-Calmodulin Biophysical Journal. 108: 452a. DOI: 10.1016/J.Bpj.2014.11.2466 |
0.53 |
|
| 2014 |
Baxley T, Pinto JR, Chalovich JM. Disease Causing Troponin C Mutations Have Varied Effects on Actin Regulatory States Biophysical Journal. 106: 722a. DOI: 10.1016/J.Bpj.2013.11.3991 |
0.48 |
|
| 2013 |
Kingsbury NL, Renegar RH, Chalovich JM. Avian synaptopodin 2 (fesselin) stabilizes myosin filaments and actomyosin in the presence of ATP. Biochemistry. 52: 7641-7. PMID 24083890 DOI: 10.1021/Bi401013G |
0.555 |
|
| 2013 |
Schroeter MM, Orlova A, Egelman EH, Beall B, Chalovich JM. Organization of F-actin by Fesselin (avian smooth muscle synaptopodin 2). Biochemistry. 52: 4955-61. PMID 23789719 DOI: 10.1021/Bi4005254 |
0.801 |
|
| 2013 |
Skowronsky RA, Schroeter M, Baxley T, Li Y, Chalovich JM, Spuches AM. Thermodynamics and molecular dynamics simulations of calcium binding to the regulatory site of human cardiac troponin C: evidence for communication with the structural calcium binding sites. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 18: 49-58. PMID 23111626 DOI: 10.1007/S00775-012-0948-2 |
0.435 |
|
| 2013 |
Kingsbury N, Renegar R, Schroeter MM, Chalovich JM. Avian Synaptopodin 2 (Fesselin) Inhibits Actomyosin Dissociation by ATP and Alters the Structure of Smooth Muscle Myosin Filaments Biophysical Journal. 104: 141a. DOI: 10.1016/J.Bpj.2012.11.801 |
0.557 |
|
| 2013 |
Thalhamer SE, Baxley TA, Schmidt M, Shortt KA, Lehman JM, Arthur J, Chalovich JM, Scemama J. Myopodin has a Nucleolar Localization in Several Mammalian Cell Lines Biophysical Journal. 104: 140a. DOI: 10.1016/J.Bpj.2012.11.800 |
0.426 |
|
| 2012 |
Wang H, Chalovich JM, Marriott G. Structural dynamics of troponin I during Ca2+-activation of cardiac thin filaments: a multi-site Förster resonance energy transfer study. Plos One. 7: e50420. PMID 23227172 DOI: 10.1371/Journal.Pone.0050420 |
0.491 |
|
| 2012 |
Franklin AJ, Baxley T, Kobayashi T, Chalovich JM. The C-terminus of troponin T is essential for maintaining the inactive state of regulated actin. Biophysical Journal. 102: 2536-44. PMID 22713569 DOI: 10.1016/J.Bpj.2012.04.037 |
0.569 |
|
| 2012 |
Chalovich JM. Disease causing mutations of troponin alter regulated actin state distributions. Journal of Muscle Research and Cell Motility. 33: 493-9. PMID 22678497 DOI: 10.1007/S10974-012-9305-X |
0.569 |
|
| 2012 |
Chalovich JM. Michael Bárány: a recollection. Journal of Muscle Research and Cell Motility. 33: 373-6. PMID 22539009 DOI: 10.1007/S10974-012-9295-8 |
0.374 |
|
| 2012 |
Franklin A, Baxley T, Chalovich JM. Properties of the Intermediate State of Actin-Tropomyosin-Troponin Biophysical Journal. 102: 153a. DOI: 10.1016/J.Bpj.2011.11.836 |
0.508 |
|
| 2011 |
Chalovich JM, Lutz E, Baxley T, Schroeter MM. Acrylodan-labeled smooth muscle tropomyosin reports differences in the effects of troponin and caldesmon in the transition from the active state to the inactive state. Biochemistry. 50: 6093-101. PMID 21639115 DOI: 10.1021/Bi200288C |
0.465 |
|
| 2011 |
Jung HS, Billington N, Thirumurugan K, Salzameda B, Cremo CR, Chalovich JM, Chantler PD, Knight PJ. Role of the tail in the regulated state of myosin 2. Journal of Molecular Biology. 408: 863-78. PMID 21419133 DOI: 10.1016/J.Jmb.2011.03.019 |
0.447 |
|
| 2011 |
Varughese JF, Baxley T, Chalovich JM, Li Y. A computational and experimental approach to investigate bepridil binding with cardiac troponin. The Journal of Physical Chemistry. B. 115: 2392-400. PMID 21332124 DOI: 10.1021/Jp1094504 |
0.443 |
|
| 2011 |
Mathur MC, Chase PB, Chalovich JM. Several cardiomyopathy causing mutations on tropomyosin either destabilize the active state of actomyosin or alter the binding properties of tropomyosin. Biochemical and Biophysical Research Communications. 406: 74-8. PMID 21295541 DOI: 10.1016/J.Bbrc.2011.01.112 |
0.752 |
|
| 2011 |
Lutz E, Schroeter MM, Baxley T, Chalovich JM. Kinetics of Smooth Muscle Acrylodan-Tropomyosin Transitions on Actin Biophysical Journal. 100: 113a-114a. DOI: 10.1016/J.Bpj.2010.12.829 |
0.486 |
|
| 2011 |
Chalovich JM, Baxley T, Kobayashi T, Franklin AJ. A Phosphomimetic Mutation of TnI Partially Rescues a Disease Causing Mutation of TnT Biophysical Journal. 100: 360a-361a. DOI: 10.1016/J.Bpj.2010.12.2160 |
0.432 |
|
| 2010 |
Chalovich JM, Schroeter MM. Synaptopodin family of natively unfolded, actin binding proteins: physical properties and potential biological functions. Biophysical Reviews. 2: 181-189. PMID 28510039 DOI: 10.1007/S12551-010-0040-5 |
0.469 |
|
| 2010 |
Hamden SS, Schroeter MM, Chalovich JM. Phosphorylation of caldesmon at sites between residues 627 and 642 attenuates inhibitory activity and contributes to a reduction in Ca2+-calmodulin affinity. Biophysical Journal. 99: 1861-8. PMID 20858431 DOI: 10.1016/J.Bpj.2010.07.018 |
0.764 |
|
| 2010 |
Varughese JF, Chalovich JM, Li Y. Molecular dynamics studies on troponin (TnI-TnT-TnC) complexes: insight into the regulation of muscle contraction. Journal of Biomolecular Structure & Dynamics. 28: 159-74. PMID 20645650 DOI: 10.1080/07391102.2010.10507350 |
0.356 |
|
| 2010 |
Borrego-Diaz E, Chalovich JM. Kinetics of regulated actin transitions measured by probes on tropomyosin. Biophysical Journal. 98: 2601-9. PMID 20513404 DOI: 10.1016/J.Bpj.2010.02.030 |
0.434 |
|
| 2010 |
Schroeter MM, Orlova A, Beall B, Egelman EH, Chalovich JM. Organization of F-Actin by Avian Smooth Muscle Synaptopodin 2 (Fesselin) Biophysical Journal. 98: 157a. DOI: 10.1016/J.Bpj.2009.12.843 |
0.804 |
|
| 2010 |
Hamden SS, Schroeter MM, Chalovich JM. Additional Sites are Involved in the Regulation of Caldesmon by PAK Phosphorylation Biophysical Journal. 98: 354a. DOI: 10.1016/J.Bpj.2009.12.1914 |
0.761 |
|
| 2010 |
Chalovich JM, Schroeter MM. Synaptopodin family of natively unfolded, actin binding proteins: Physical properties and potential biological functions Biophysical Reviews. 2: 181-189. DOI: 10.1007/s12551-010-0040-5 |
0.367 |
|
| 2009 |
Mathur MC, Kobayashi T, Chalovich JM. Some cardiomyopathy-causing troponin I mutations stabilize a functional intermediate actin state. Biophysical Journal. 96: 2237-44. PMID 19289050 DOI: 10.1016/J.Bpj.2008.12.3909 |
0.723 |
|
| 2009 |
Renegar RH, Chalovich JM, Leinweber BD, Zary JT, Schroeter MM. Localization of the actin-binding protein fesselin in chicken smooth muscle. Histochemistry and Cell Biology. 131: 191-6. PMID 18820943 DOI: 10.1007/S00418-008-0508-6 |
0.413 |
|
| 2009 |
Schroeter MM, Hurley D, Chalovich JM. Multiple Isoforms of Fesselin (Avian Synaptopodin 2) are expressed in Smooth, Skeletal and Heart Muscle Biophysical Journal. 96: 128a. DOI: 10.1016/J.Bpj.2008.12.573 |
0.453 |
|
| 2009 |
Mathur MC, Kobayashi T, Chalovich JM. Cardiomyopathy Causing Mutations Stabilize an Intermediate State of Thin Filaments Biophysical Journal. 96: 377a. DOI: 10.1016/J.Bpj.2008.12.2826 |
0.734 |
|
| 2008 |
Schroeter MM, Beall B, Heid HW, Chalovich JM. In vitro characterization of native mammalian smooth-muscle protein synaptopodin 2. Bioscience Reports. 28: 195-203. PMID 18588515 DOI: 10.1042/Bsr20080079 |
0.809 |
|
| 2008 |
Schroeter MM, Beall B, Heid HW, Chalovich JM. The actin binding protein, fesselin, is a member of the synaptopodin family. Biochemical and Biophysical Research Communications. 371: 582-6. PMID 18457655 DOI: 10.1016/J.Bbrc.2008.04.134 |
0.791 |
|
| 2008 |
Jung HS, Burgess SA, Billington N, Colegrave M, Patel H, Chalovich JM, Chantler PD, Knight PJ. Conservation of the regulated structure of folded myosin 2 in species separated by at least 600 million years of independent evolution. Proceedings of the National Academy of Sciences of the United States of America. 105: 6022-6. PMID 18413616 DOI: 10.1073/Pnas.0707846105 |
0.475 |
|
| 2008 |
Wang H, Mao S, Chalovich JM, Marriott G. Tropomyosin dynamics in cardiac thin filaments: a multisite forster resonance energy transfer and anisotropy study. Biophysical Journal. 94: 4358-69. PMID 18310249 DOI: 10.1529/Biophysj.107.121129 |
0.493 |
|
| 2008 |
Mathur MC, Kobayashi T, Chalovich JM. Negative charges at protein kinase C sites of troponin I stabilize the inactive state of actin. Biophysical Journal. 94: 542-9. PMID 17872964 DOI: 10.1529/Biophysj.107.113944 |
0.764 |
|
| 2007 |
Chalovich JM. Equilibrium binding of proteins to F-actin. Methods in Molecular Biology (Clifton, N.J.). 392: 1-22. PMID 17951707 DOI: 10.1007/978-1-59745-490-2_1 |
0.481 |
|
| 2007 |
Burgess SA, Yu S, Walker ML, Hawkins RJ, Chalovich JM, Knight PJ. Structures of smooth muscle myosin and heavy meromyosin in the folded, shutdown state. Journal of Molecular Biology. 372: 1165-78. PMID 17707861 DOI: 10.1016/J.Jmb.2007.07.014 |
0.419 |
|
| 2007 |
Khaymina SS, Kenney JM, Schroeter MM, Chalovich JM. Fesselin is a natively unfolded protein. Journal of Proteome Research. 6: 3648-54. PMID 17676886 DOI: 10.1021/Pr070237V |
0.386 |
|
| 2007 |
Gafurov B, Chalovich JM. Equilibrium distribution of skeletal actin-tropomyosin-troponin states, determined by pyrene-tropomyosin fluorescence. The Febs Journal. 274: 2287-99. PMID 17403044 DOI: 10.1111/J.1742-4658.2007.05765.X |
0.509 |
|
| 2006 |
Pham M, Chalovich JM. Smooth muscle alpha-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization. Journal of Muscle Research and Cell Motility. 27: 45-51. PMID 16450054 DOI: 10.1007/S10974-005-9053-2 |
0.527 |
|
| 2005 |
Schroeter MM, Chalovich JM. Fesselin binds to actin and myosin and inhibits actin-activated ATPase activity. Journal of Muscle Research and Cell Motility. 26: 183-9. PMID 16179973 DOI: 10.1007/S10974-005-9009-6 |
0.609 |
|
| 2004 |
Gafurov B, Fredricksen S, Cai A, Brenner B, Chase PB, Chalovich JM. The Delta 14 mutation of human cardiac troponin T enhances ATPase activity and alters the cooperative binding of S1-ADP to regulated actin. Biochemistry. 43: 15276-85. PMID 15568820 DOI: 10.1021/Bi048646H |
0.562 |
|
| 2004 |
Schroeter M, Chalovich JM. Ca2+-calmodulin regulates fesselin-induced actin polymerization. Biochemistry. 43: 13875-82. PMID 15504050 DOI: 10.1021/Bi0487490 |
0.524 |
|
| 2004 |
Gafurov B, Chen YD, Chalovich JM. Ca2+ and ionic strength dependencies of S1-ADP binding to actin-tropomyosin-troponin: regulatory implications. Biophysical Journal. 87: 1825-35. PMID 15345561 DOI: 10.1529/Biophysj.104.043364 |
0.566 |
|
| 2003 |
Fredricksen S, Cai A, Gafurov B, Resetar A, Chalovich JM. Influence of ionic strength, actin state, and caldesmon construct size on the number of actin monomers in a caldesmon binding site. Biochemistry. 42: 6136-48. PMID 12755616 DOI: 10.1021/Bi0274017 |
0.501 |
|
| 2003 |
Wirth A, Schroeter M, Kock-Hauser C, Manser E, Chalovich JM, de Lanerolle P, Pfitzer G. Inhibition of contraction and myosin light chain phosphorylation in guinea-pig smooth muscle by p21-activated kinase 1 Journal of Physiology. 549: 489-500. PMID 12692179 DOI: 10.1113/Jphysiol.2002.033167 |
0.45 |
|
| 2003 |
Yan B, Sen A, Chalovich JM, Chen YD. Theoretical studies on competitive binding of caldesmon and myosin S1 to actin: prediction of apparent cooperativity in equilibrium and slow-down in kinetics of S1 binding by caldesmon. Biochemistry. 42: 4208-16. PMID 12680775 DOI: 10.1021/Bi0273009 |
0.533 |
|
| 2002 |
Chalovich JM. Regulation of striated muscle contraction: a discussion. Journal of Muscle Research and Cell Motility. 23: 353-61. PMID 12630710 DOI: 10.1023/A:1022066922922 |
0.362 |
|
| 2002 |
Resetar AM, Stephens JM, Chalovich JM. Troponin-tropomyosin: an allosteric switch or a steric blocker? Biophysical Journal. 83: 1039-49. PMID 12124285 DOI: 10.1016/S0006-3495(02)75229-6 |
0.513 |
|
| 2002 |
Chalovich J, Yan B, Brenner B, Chen Y. Response to the Letter by Geeves and Lehrer Biophysical Journal. 82: 1679-1681. DOI: 10.1016/S0006-3495(02)75519-7 |
0.518 |
|
| 2001 |
Beall B, Chalovich JM. Fesselin, a synaptopodin-like protein, stimulates actin nucleation and polymerization Biochemistry. 40: 14252-14259. PMID 11714279 DOI: 10.1021/Bi011806U |
0.795 |
|
| 2001 |
Sen A, Chen YD, Yan B, Chalovich JM. Caldesmon reduces the apparent rate of binding of myosin s1 to actin-tropomyosin Biochemistry. 40: 5757-5764. PMID 11341841 DOI: 10.1021/Bi002724T |
0.521 |
|
| 2001 |
Chen YD, Yan B, Chalovich JM, Brenner B. Theoretical kinetic studies of models for binding myosin subfragment-1 to regulated actin: Hill model versus Geeves model Biophysical Journal. 80: 2338-2349. PMID 11325734 DOI: 10.1016/S0006-3495(01)76204-2 |
0.469 |
|
| 2000 |
She M, Trimble D, Yu LC, Chalovich JM. Factors contributing to troponin exchange in myofibrils and in solution. Journal of Muscle Research and Cell Motility. 21: 737-45. PMID 11392555 DOI: 10.1023/A:1010300802980 |
0.412 |
|
| 1999 |
Leinweber B, Tang JX, Stafford WF, Chalovich JM. Calponin interaction with α-actinin-actin: Evidence for a structural role for calponin Biophysical Journal. 77: 3208-3217. PMID 10585942 DOI: 10.1016/S0006-3495(99)77151-1 |
0.423 |
|
| 1999 |
Leinweber BD, Fredricksen RS, Hoffman DR, Chalovich JM. Fesselin: A novel synaptopodin-like actin binding protein from muscle tissue Journal of Muscle Research and Cell Motility. 20: 539-545. PMID 10555072 DOI: 10.1023/A:1005597306671 |
0.381 |
|
| 1999 |
Brenner B, Chalovich JM. Kinetics of thin filament activation probed by fluorescence of N- ((2(lodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazolelabeled troponin I incorporated into skinned fibers of rabbit psoas muscle: Implications for regulation of muscle contraction Biophysical Journal. 77: 2692-2708. PMID 10545369 DOI: 10.1016/S0006-3495(99)77103-1 |
0.479 |
|
| 1999 |
Brenner B, Kraft T, Yu LC, Chalovich JM. Thin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle. Biophysical Journal. 77: 2677-91. PMID 10545368 DOI: 10.1016/S0006-3495(99)77102-X |
0.494 |
|
| 1999 |
Frisbie SM, Reedy MC, Yu LC, Brenner B, Chalovich JM, Kraft T. Sarcomeric binding pattern of exogenously added intact caldesmon and its C-terminal 20-kDa fragment in skinned fibers of skeletal muscle. Journal of Muscle Research and Cell Motility. 20: 291-303. PMID 10471992 DOI: 10.1023/A:1005490405222 |
0.494 |
|
| 1998 |
Xu S, Malinchik S, Frisbie S, Gu J, Kraft T, Rapp G, Chalovich JM, Brenner B, Yu LC. X-ray diffraction studies of the cross-bridge intermediate states. Advances in Experimental Medicine and Biology. 453: 271-8; discussion 27. PMID 9889839 DOI: 10.1007/978-1-4684-6039-1_32 |
0.396 |
|
| 1998 |
Brenner B, Kraft T, Chalovich JM. Fluorescence of NBD-labelled troponin-I as a probe for the kinetics of thin filament activation in skeletal muscle fibers. Advances in Experimental Medicine and Biology. 453: 177-84; discussion 1. PMID 9889828 DOI: 10.1007/978-1-4684-6039-1_21 |
0.436 |
|
| 1998 |
Chalovich JM, Sen A, Resetar A, Leinweber B, Fredricksen RS, Lu F, Chen YD. Caldesmon: Binding to actin and myosin and effects on elementary steps in the ATPase cycle Acta Physiologica Scandinavica. 164: 427-435. PMID 9887966 DOI: 10.1046/j.1365-201X.1998.00449.x |
0.472 |
|
| 1998 |
Frisbie SM, Xu S, Chalovich JM, Yu LC. Characterizations of cross-bridges in the presence of saturating concentrations of MgAMP-PNP in rabbit permeabilized psoas muscle. Biophysical Journal. 74: 3072-82. PMID 9635761 DOI: 10.1016/S0006-3495(98)78014-2 |
0.451 |
|
| 1998 |
Sen A, Chalovich JM. Caldesmon-actin-tropomyosin contains two types of binding sites for myosin S1 Biochemistry. 37: 7526-7531. PMID 9585567 DOI: 10.1021/Bi9729256 |
0.52 |
|
| 1997 |
Heubach JF, Hartwell R, Ledwon M, Kraft T, Brenner B, Chalovich JM. Inhibition of cross-bridge binding to actin by caldesmon fragments in skinned skeletal muscle fibers Biophysical Journal. 72: 1287-1294. PMID 9138574 DOI: 10.1016/S0006-3495(97)78775-7 |
0.392 |
|
| 1997 |
Frisbie SM, Chalovich JM, Brenner B, Yu LC. Modulation of cross-bridge affinity for MgGTP by Ca2+ in skinned fibers of rabbit psoas muscle. Biophysical Journal. 72: 2255-61. PMID 9129828 DOI: 10.1016/S0006-3495(97)78869-6 |
0.457 |
|
| 1996 |
Brenner B, Xu S, Chalovich JM, Yu LC. Radial equilibrium lengths of actomyosin cross-bridges in muscle. Biophysical Journal. 71: 2751-8. PMID 8913612 DOI: 10.1016/S0006-3495(96)79468-7 |
0.386 |
|
| 1995 |
Crosbie RH, Chalovich JM, Reisler E. Flexation of caldesmon: effect of conformation on the properties of caldesmon. Journal of Muscle Research and Cell Motility. 16: 509-18. PMID 8567938 DOI: 10.1007/Bf00126435 |
0.468 |
|
| 1995 |
Resetar AM, Chalovich JM. Adenosine 5'-(γ-thiotriphosphate): An ATP analog that should be used with caution in muscle contraction studies Biochemistry. 34: 16039-16045. PMID 8519760 DOI: 10.1021/Bi00049A018 |
0.577 |
|
| 1995 |
Chalovich JM. Role of ATP in the binding of caldesmon to smooth muscle myosin Biochemistry®. 34: 6359-6365. PMID 7756264 DOI: 10.1021/Bi00019A014 |
0.501 |
|
| 1995 |
Chalovich JM, Chen YD, Dudek R, Luo H. Kinetics of binding of caldesmon to actin Journal of Biological Chemistry. 270: 9911-9916. PMID 7730374 DOI: 10.1074/Jbc.270.17.9911 |
0.508 |
|
| 1995 |
Kraft T, Chalovich JM, Yu LC, Brenner B. Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation. Biophysical Journal. 68: 2404-18. PMID 7647245 DOI: 10.1016/S0006-3495(95)80423-6 |
0.456 |
|
| 1995 |
Chalovich JM. Characterization of Calponin Binding to Actin Biochemistry. 34: 11864-11871. PMID 7547921 DOI: 10.1021/Bi00037A026 |
0.541 |
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| 1994 |
Crosbie RH, Miller C, Chalovich JM, Rubenstein PA, Reisler E. Caldesmon, N-terminal yeast actin mutants, and the regulation of actomyosin interactions. Biochemistry. 33: 3210-6. PMID 8136356 DOI: 10.1021/Bi00177A010 |
0.53 |
|
| 1994 |
Stafford WF, Chalovich JM, Graceffa P. Turkey Gizzard Caldesmon Molecular Weight and Shape Archives of Biochemistry and Biophysics. 313: 47-49. PMID 8053685 DOI: 10.1006/Abbi.1994.1356 |
0.308 |
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| 1993 |
Pfitzer G, Zeugner C, Troschka M, Chalovich JM. Caldesmon and a 20-kDa actin-binding fragment of caldesmon inhibit tension development in skinned gizzard muscle fiber bundles Proceedings of the National Academy of Sciences of the United States of America. 90: 5904-5908. PMID 8327461 DOI: 10.1073/Pnas.90.13.5904 |
0.559 |
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| 1993 |
Hemric ME, Lu FWM, Shrager R, Carey J, Chalovich JM. Reversal of caldesmon binding to myosin with calcium-calmodulin or by phosphorylating caldesmon Journal of Biological Chemistry. 268: 15305-15311. PMID 8325900 |
0.506 |
|
| 1993 |
Velaz L, Chen YD, Chalovich JM. Characterization of a caldesmon fragment that competes with myosin-ATP binding to actin Biophysical Journal. 65: 892-898. PMID 8218912 DOI: 10.1016/S0006-3495(93)81113-5 |
0.556 |
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| 1993 |
Hemric ME, Freedman MV, Chalovich JM. Inhibition of Actin Stimulation of Skeletal Muscle (A1)S-1 ATPase Activity by Caldesmon Archives of Biochemistry and Biophysics. 306: 39-43. PMID 8215419 DOI: 10.1006/Abbi.1993.1477 |
0.549 |
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| 1993 |
Pfitzer G, Fischer W, Chalovich JM, Katayama E, Sugi H, Sellers JR, Huxley. Phosphorylation-contraction coupling in smooth muscle: Role of caldesmon Advances in Experimental Medicine and Biology. 332: 195-203. PMID 8109333 DOI: 10.1007/978-1-4615-2872-2_18 |
0.496 |
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| 1992 |
Crosbie RH, Chalovich JM, Reisler E. Interaction of caldesmon and myosin subfragment 1 with the C-terminus of actin Biochemical and Biophysical Research Communications. 184: 239-245. PMID 1567431 DOI: 10.1016/0006-291X(92)91184-R |
0.479 |
|
| 1992 |
Chen YD, Chalovich JM. A mosaic multiple-binding model for the binding of caldesmon and myosin subfragment-1 to actin Biophysical Journal. 63: 1063-1070. PMID 1420925 DOI: 10.1016/S0006-3495(92)81687-9 |
0.511 |
|
| 1992 |
Chalovich JM, Bryan J, Benson CE, Velaz L. Localization and characterization of a 7.3-kDa region of caldesmon which reversibly inhibits actomyosin ATPase activity Journal of Biological Chemistry. 267: 16644-16650. PMID 1386604 |
0.497 |
|
| 1992 |
Chalovich JM. Actin mediated regulation of muscle contraction Pharmacology and Therapeutics. 55: 95-148. PMID 1289901 DOI: 10.1016/0163-7258(92)90013-P |
0.312 |
|
| 1991 |
Brenner B, Yu LC, Chalovich JM. Parallel inhibition of active force and relaxed fiber stiffness in skeletal muscle by caldesmon: implications for the pathway to force generation. Proceedings of the National Academy of Sciences of the United States of America. 88: 5739-43. PMID 2062853 DOI: 10.1073/Pnas.88.13.5739 |
0.469 |
|
| 1991 |
Crosbie R, Adams S, Chalovich JM, Reisler E. The interaction of caldesmon with the COOH terminus of actin Journal of Biological Chemistry. 266: 20001-20006. PMID 1939062 |
0.432 |
|
| 1991 |
Stein LA, Chalovich JM. Activation of skeletal S-1 ATPase activity by actin-tropomyosin-troponin: Effect of Ca++ on the fluorescence transient Biophysical Journal. 60: 399-407. PMID 1832976 DOI: 10.1016/S0006-3495(91)82065-3 |
0.518 |
|
| 1991 |
Chalovich JM, Yu LC, Brenner B. Involvement of weak binding crossbridges in force production in muscle. Journal of Muscle Research and Cell Motility. 12: 503-6. PMID 1791190 DOI: 10.1007/Bf01738438 |
0.396 |
|
| 1990 |
Hemric ME, Chalovich JM. Characterization of caldesmon binding to myosin Journal of Biological Chemistry. 265: 19672-19678. PMID 2246251 |
0.404 |
|
| 1990 |
Adams S, DasGupta G, Chalovich JM, Reisler E. Immunochemical evidence for the binding of caldesmon to the NH2-terminal segment of actin Journal of Biological Chemistry. 265: 19652-19657. PMID 2246250 |
0.442 |
|
| 1990 |
Chalovich JM, Hemric ME, Velaz L. Regulation of ATP hydrolysis by caldesmon. A novel change in the interaction of myosin with actin Annals of the New York Academy of Sciences. 599: 85-99. PMID 2221679 DOI: 10.1111/J.1749-6632.1990.Tb42367.X |
0.433 |
|
| 1990 |
Velazr L, Ingraham RH, Chalovich JM. Dissociation of the effect of caldesmon on the ATPase activity and on the binding of smooth heavy meromyosin to actin by partial digestion of caldesmon Journal of Biological Chemistry. 265: 2929-2934. PMID 2137453 |
0.465 |
|
| 1989 |
Velaz L, Hemric ME, Benson CE, Chalovich JM. The binding of caldesmon to actin and its effect on the ATPase activity of soluble myosin subfragments in the presence and absence of tropomyosin Journal of Biological Chemistry. 264: 9602-9610. PMID 2524487 |
0.461 |
|
| 1988 |
Hemric ME, Chalovich JM. Effect of caldesmon on the ATPase activity and the binding of smooth and skeletal myosin subfragments to actin Journal of Biological Chemistry. 263: 1878-1885. PMID 2962997 |
0.495 |
|
| 1988 |
Chalovich JM. Caldesmon and thin-filament regulation of muscle contraction Cell Biophysics. 12: 73-85. PMID 2453287 DOI: 10.1007/BF02918351 |
0.508 |
|
| 1987 |
Chalovich JM, Cornelius P, Benson CE. Caldesmon inhibits skeletal actomyosin subfragment-1 ATPase activity and the binding of myosin subfragment-1 to actin Journal of Biological Chemistry. 262: 5711-5716. PMID 2952642 |
0.504 |
|
| 1986 |
Greene LE, Chalovich JM, Eisenberg E. Effect of nucleotide on the binding of N,N'-p-phenylenedimaleimide-modified S-1 to unregulated and regulated actin. Biochemistry. 25: 704-9. PMID 3955026 DOI: 10.1021/Bi00351A030 |
0.464 |
|
| 1986 |
Chalovich JM, Eisenberg E. The effect of troponin-tropomyosin on the binding of heavy meromyosin to actin in the presence of ATP Journal of Biological Chemistry. 261: 5088-5093. PMID 2937784 |
0.451 |
|
| 1986 |
Chalovich JM, Fischetti VA. Crosslinking of actin filaments and inhibition of actomyosin subfragment-1 ATPase activity by streptococcal M6 protein Archives of Biochemistry and Biophysics. 245: 37-43. PMID 2936307 DOI: 10.1016/0003-9861(86)90187-6 |
0.468 |
|
| 1984 |
Schoenberg M, Brenner B, Chalovich JM, Greene LE, Eisenberg E. Cross-bridge attachment in relaxed muscle. Advances in Experimental Medicine and Biology. 170: 269-84. PMID 6741701 DOI: 10.1007/978-1-4684-4703-3_24 |
0.351 |
|
| 1984 |
Chalovich JM, Stein LA, Greene LE, Eisenberg E. Interaction of isozymes of myosin subfragment 1 with actin: effect of ionic strength and nucleotide. Biochemistry. 23: 4885-9. PMID 6238623 DOI: 10.1021/Bi00316A011 |
0.317 |
|
| 1984 |
Chalovich JM, Chantler PD, Szent-Gyorgyi AG, Eisenberg E. Regulation of molluscan actomyosin ATPase activity. The Journal of Biological Chemistry. 259: 2617-21. PMID 6230349 |
0.486 |
|
| 1983 |
Chalovich JM, Greene LE, Eisenberg E. Crosslinked myosin subfragment 1: a stable analogue of the subfragment-1.ATP complex. Proceedings of the National Academy of Sciences of the United States of America. 80: 4909-13. PMID 6576363 DOI: 10.1073/Pnas.80.16.4909 |
0.366 |
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| 1982 |
Brenner B, Schoenberg M, Chalovich JM, Greene LE, Eisenberg E. Evidence for cross-bridge attachment in relaxed muscle at low ionic strength. Proceedings of the National Academy of Sciences of the United States of America. 79: 7288-91. PMID 6961408 DOI: 10.1073/Pnas.79.23.7288 |
0.493 |
|
| 1982 |
Chalovich JM, Eisenberg E. Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin Journal of Biological Chemistry. 257: 2432-2437. PMID 6460759 |
0.436 |
|
| 1981 |
Doyle DD, Chalovich JM, Bárány M. Natural abundance 13C NMR spectra of intact muscle. Febs Letters. 131: 147-50. PMID 7286237 DOI: 10.1016/0014-5793(81)80907-6 |
0.314 |
|
| 1981 |
Hill TL, Eisenberg E, Chalovich JM. Theoretical models for cooperative steady-state ATPase activity of myosin subfragment-1 on regulated actin. Biophysical Journal. 35: 99-112. PMID 6455170 DOI: 10.1016/S0006-3495(81)84777-7 |
0.507 |
|
| 1981 |
Chalovich JM, Chock PB, Eisenberg E. Mechanism of action of troponin · tropomyosin. Inhibition of actomyosin ATPase activity without inhibition of myosin binding to actin Journal of Biological Chemistry. 256: 575-578. PMID 6450206 |
0.367 |
|
| 1980 |
Chalovich JM, Bárány M. Serine ethanolamine phosphate in avian muscular dystrophy: mechanism of accumulation in dystrophic muscle and relationship to phospholipid synthesis. Archives of Biochemistry and Biophysics. 199: 615-25. PMID 6244784 DOI: 10.1016/0003-9861(80)90319-7 |
0.392 |
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| 1979 |
Chalovich JM, Burt CT, Danon MJ, Glonek T, Bárány M. Phosphodiesters in muscular dystrophies. Annals of the New York Academy of Sciences. 317: 649-69. PMID 224750 DOI: 10.1111/J.1749-6632.1979.Tb56585.X |
0.368 |
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| Low-probability matches (unlikely to be authored by this person) |
| 1993 |
Renegar RH, Owens CR, Chalovich JM. Purification and partial characterization of relaxin and relaxin precursors from the hamster placenta Biology of Reproduction. 49: 154-161. PMID 8353182 DOI: 10.1095/Biolreprod49.1.154 |
0.291 |
|
| 1977 |
Chalovich JM, Burt CT, Cohen SM, Glonek T, Bárány M. Identification of an unknown 31P nuclear magnetic resonance from dystrophic chicken as L-serine ethanolamine phosphodiester. Archives of Biochemistry and Biophysics. 182: 683-9. PMID 900953 DOI: 10.1016/0003-9861(77)90549-5 |
0.29 |
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| 2017 |
Baxley T, Johnson D, Pinto JR, Chalovich JM. Correction to Troponin C Mutations Partially Stabilize the Active State of Regulated Actin and Fully Stabilize the Active State When Paired with Δ14 TnT. Biochemistry. PMID 29064671 DOI: 10.1021/acs.biochem.7b00963 |
0.284 |
|
| 2020 |
Johnson D, Zhu L, Vieira ML, Pinto JRD, Chalovich JM. A High Ala Mutant of the C-Terminal Region of Human Cardiac TnT Has a Large Impact on Regulation Biophysical Journal. 118: 595a. DOI: 10.1016/J.Bpj.2019.11.3218 |
0.281 |
|
| 1986 |
Brenner B, Chalovich JM, Greene LE, Eisenberg E, Schoenberg M. Stiffness of skinned rabbit psoas fibers in MgATP and MgPPi solution. Biophysical Journal. 50: 685-91. PMID 3022835 DOI: 10.1016/S0006-3495(86)83509-3 |
0.269 |
|
| 1978 |
Burt CT, Chalovich JM. Serine ethanolamine phosphodiester: a major component in chicken semen. Biochimica Et Biophysica Acta. 529: 186-8. PMID 638178 DOI: 10.1016/0005-2760(78)90118-2 |
0.25 |
|
| 1991 |
Wang CLA, Chalovich JM, Graceffa P, Lu RC, Mabuchi K, Stafford WF. A long helix from the central region of smooth muscle caldesmon Journal of Biological Chemistry. 266: 13958-13963. PMID 1856225 |
0.218 |
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| 1995 |
Brenner B, Chalovich JM, Yu LC. Distinct molecular processes associated with isometric force generation and rapid tension recovery after quick release. Biophysical Journal. 68: 106S-111S. PMID 7787051 |
0.211 |
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| 1990 |
Chalovich JM. Muscle contraction: Muscle fiber studies support solution data Trends in Biochemical Sciences. 15: 261. PMID 2382283 |
0.206 |
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| 2017 |
Chalovich JM, Kraft T, Yu LC. Obituary Bernhard Brenner. Journal of Muscle Research and Cell Motility. PMID 29147874 DOI: 10.1007/S10974-017-9488-2 |
0.184 |
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| 1993 |
Cory AH, Shibley IA, Chalovich JM, Cory JG. Deoxyguanosine-resistant leukemia L1210 cells: Loss of specific deoxyribonucleoside kinase activity Journal of Biological Chemistry. 268: 405-409. PMID 8380161 |
0.155 |
|
| 1990 |
Chalovich JM. Letters Trends in Biochemical Sciences. 15: 261. DOI: 10.1016/0968-0004(90)90049-H |
0.029 |
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| Hide low-probability matches. |