Year |
Citation |
Score |
2023 |
Rajan S, Aguirre R, Hong Zhou Z, Hauser P, Reisler E. Drebrin Protects Assembled Actin from INF2-FFC-mediated Severing and Stabilizes Cell Protrusions. Journal of Molecular Biology. 436: 168421. PMID 38158176 DOI: 10.1016/j.jmb.2023.168421 |
0.494 |
|
2023 |
Rajan S, Yoon J, Wu H, Srapyan S, Baskar R, Ahmed G, Yang T, Grintsevich EE, Reisler E, Terman JR. Disassembly of bundled F-actin and cellular remodeling via an interplay of Mical, cofilin, and F-actin crosslinkers. Proceedings of the National Academy of Sciences of the United States of America. 120: e2309955120. PMID 37725655 DOI: 10.1073/pnas.2309955120 |
0.478 |
|
2023 |
Rajan S, Kudryashov DS, Reisler E. Actin Bundles Dynamics and Architecture. Biomolecules. 13. PMID 36979385 DOI: 10.3390/biom13030450 |
0.447 |
|
2023 |
Rajan S, Terman JR, Reisler E. MICAL-mediated oxidation of actin and its effects on cytoskeletal and cellular dynamics. Frontiers in Cell and Developmental Biology. 11: 1124202. PMID 36875759 DOI: 10.3389/fcell.2023.1124202 |
0.479 |
|
2022 |
Das S, Zhang Z, Kalvakota S, Soto R, Phillips ML, Terman JR, Reisler E. Parallel actin monomers in the 8S complex of actin-INF2. Journal of Biomolecular Structure & Dynamics. 1-10. PMID 35343388 DOI: 10.1080/07391102.2022.2050947 |
0.508 |
|
2021 |
Grintsevich EE, Ahmed G, Ginosyan AA, Wu H, Rich SK, Reisler E, Terman JR. Profilin and Mical combine to impair F-actin assembly and promote disassembly and remodeling. Nature Communications. 12: 5542. PMID 34545088 DOI: 10.1038/s41467-021-25781-3 |
0.469 |
|
2021 |
Smith H, Pinkerton N, Heisler DB, Kudryashova E, Hall AR, Karch KR, Norris A, Wysocki V, Sotomayor M, Reisler E, Vavylonis D, Kudryashov DS. the Understanding of ACD Toxicity with the Discovery of Cyclic Forms of Actin Oligomers. International Journal of Molecular Sciences. 22. PMID 33450834 DOI: 10.3390/ijms22020718 |
0.444 |
|
2020 |
Das S, Ge P, Oztug Durer ZA, Grintsevich EE, Zhou ZH, Reisler E. D-loop Dynamics and Near-Atomic-Resolution Cryo-EM Structure of Phalloidin-Bound F-Actin. Structure (London, England : 1993). PMID 32348747 DOI: 10.1016/J.Str.2020.04.004 |
0.577 |
|
2020 |
Ostrowska-Podhorodecka Z, Śliwinska M, Reisler E, Moraczewska J. Tropomyosin isoforms regulate cofilin 1 activity by modulating actin filament conformationw. Archives of Biochemistry and Biophysics. 108280. PMID 31996302 DOI: 10.1016/J.Abb.2020.108280 |
0.641 |
|
2019 |
Ginosyan AA, Grintsevich EE, Reisler E. Neuronal drebrin A directly interacts with mDia2 formin to inhibit actin assembly. Molecular Biology of the Cell. mbcE18100639. PMID 30625038 DOI: 10.1091/Mbc.E18-10-0639 |
0.574 |
|
2019 |
Kraus J, Yehl J, Kudryashova E, Reisler E, Kudryashov D, Polenova T. Investigations into the Structure and Intermolecular Interface of Human Cofilin-2 Assembled on Actin Filaments by Magic Angle Spinning NMR Biophysical Journal. 116: 456a. DOI: 10.1016/J.Bpj.2018.11.2462 |
0.393 |
|
2017 |
Grintsevich EE, Ge P, Sawaya MR, Yesilyurt HG, Terman JR, Zhou ZH, Reisler E. Catastrophic disassembly of actin filaments via Mical-mediated oxidation. Nature Communications. 8: 2183. PMID 29259197 DOI: 10.1038/S41467-017-02357-8 |
0.564 |
|
2017 |
Yehl J, Kudryashova E, Reisler E, Kudryashov D, Polenova T. Structural Analysis of Human Cofilin 2/Filamentous Actin Assemblies: Atomic-Resolution Insights from Magic Angle Spinning NMR Spectroscopy. Scientific Reports. 7: 44506. PMID 28303963 DOI: 10.1038/Srep44506 |
0.58 |
|
2017 |
Grintsevich EE, Peng G, Sawaya MR, Terman JR, Zhou ZH, Reisler E. Catastrophic depolymerization of actin filaments: structural and functional effects of Mical oxidation Nature Communications. DOI: 10.2210/Pdb5Ubo/Pdb |
0.441 |
|
2016 |
Grintsevich EE, Yesilyurt HG, Rich SK, Hung RJ, Terman JR, Reisler E. F-actin dismantling through a redox-driven synergy between Mical and cofilin. Nature Cell Biology. 18: 876-885. PMID 27454820 DOI: 10.1038/Ncb3390 |
0.571 |
|
2016 |
Grintsevich EE, Gizem Yesilyurt H, Rich SK, Hung R, Terman JR, Reisler E. Targeted Actin Disassembly by Mical and Cofilin Biophysical Journal. 110: 354a. DOI: 10.1016/J.Bpj.2015.11.1910 |
0.568 |
|
2015 |
Mikati MA, Breitsprecher D, Jansen S, Reisler E, Goode BL. Coronin Enhances Actin Filament Severing by Recruiting Cofilin to Filament Sides and Altering F-Actin Conformation. Journal of Molecular Biology. 427: 3137-47. PMID 26299936 DOI: 10.1016/J.Jmb.2015.08.011 |
0.63 |
|
2015 |
Oztug Durer ZA, McGillivary RM, Kang H, Elam WA, Vizcarra CL, Hanein D, De La Cruz EM, Reisler E, Quinlan ME. Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments. Journal of Molecular Biology. 427: 2782-98. PMID 26168869 DOI: 10.1016/J.Jmb.2015.07.005 |
0.62 |
|
2015 |
Kang H, Bradley MJ, Cao W, Zhou K, Grintsevich EE, Michelot A, Reisler E, Sindelar CV, Hochstrasser M, De La Cruz EM. Site-Specific Cation Release Drives Actin Filament Severing by Vertebrate Cofilin Biophysical Journal. 108: 24a-25a. DOI: 10.1016/j.bpj.2014.11.159 |
0.345 |
|
2014 |
Ge P, Durer ZA, Kudryashov D, Zhou ZH, Reisler E. Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Nature Structural & Molecular Biology. 21: 1075-81. PMID 25362487 DOI: 10.1038/Nsmb.2907 |
0.857 |
|
2014 |
Grintsevich EE, Reisler E. Drebrin inhibits cofilin-induced severing of F-actin. Cytoskeleton (Hoboken, N.J.). 71: 472-83. PMID 25047716 DOI: 10.1002/Cm.21184 |
0.615 |
|
2014 |
Sharma S, Grintsevich EE, Woo J, Gurel PS, Higgs HN, Reisler E, Gimzewski JK. Nanostructured self-assembly of inverted formin 2 (INF2) and F-actin-INF2 complexes revealed by atomic force microscopy. Langmuir : the Acs Journal of Surfaces and Colloids. 30: 7533-9. PMID 24915113 DOI: 10.1021/La501748X |
0.547 |
|
2014 |
Gurel PS, Ge P, Grintsevich EE, Shu R, Blanchoin L, Zhou ZH, Reisler E, Higgs HN. INF2-mediated severing through actin filament encirclement and disruption. Current Biology : Cb. 24: 156-64. PMID 24412206 DOI: 10.1016/J.Cub.2013.12.018 |
0.539 |
|
2014 |
Kang H, Bradley MJ, McCullough BR, Grintsevich EE, Michelot A, Hochstrasser M, Reisler E, De La Cruz EM. Actin Filament Severing by Vertebrate Cofilin is Driven by Linked Cation Release Biophysical Journal. 106: 164a-165a. DOI: 10.1016/J.Bpj.2013.11.938 |
0.591 |
|
2014 |
Durer ZA, Vizcarra C, McGillivary RA, Hanein D, Reisler E, Quinlan ME. Metavinculin Induced Changes at the Actin Interprotomer Contacts and the Mechanism of Resulting Severing Biophysical Journal. 106: 164a. DOI: 10.1016/J.Bpj.2013.11.935 |
0.86 |
|
2014 |
Grintsevich EE, Gurel PS, Higgs HN, Reisler E. Drebrin is a Leaky Capper of Actin Filaments Modulating the Effects of Formins Biophysical Journal. 106: 571a. DOI: 10.1016/J.Bpj.2013.11.3165 |
0.56 |
|
2013 |
Chen CK, Benchaar SA, Phan M, Grintsevich EE, Loo RR, Loo JA, Reisler E. Cofilin-induced changes in F-actin detected via cross-linking with benzophenone-4-maleimide. Biochemistry. 52: 5503-9. PMID 23862734 DOI: 10.1021/Bi400715Z |
0.867 |
|
2013 |
Sharma S, Zhu H, Grintsevich EE, Reisler E, Gimzewski JK. Correlative nanoscale imaging of actin filaments and their complexes. Nanoscale. 5: 5692-702. PMID 23727693 DOI: 10.1039/C3Nr01039B |
0.568 |
|
2013 |
Mikati MA, Grintsevich EE, Reisler E. Drebrin-induced stabilization of actin filaments. The Journal of Biological Chemistry. 288: 19926-38. PMID 23696644 DOI: 10.1074/Jbc.M113.472647 |
0.636 |
|
2013 |
Kudryashov DS, Reisler E. ATP and ADP actin states. Biopolymers. 99: 245-56. PMID 23348672 DOI: 10.1002/Bip.22155 |
0.467 |
|
2013 |
Mikati MA, Chen CK, O'Brien DP, Reisler E. Cofilin-Actin Interactions Biophysical Journal. 104: 646a. DOI: 10.1016/J.Bpj.2012.11.3568 |
0.749 |
|
2013 |
Grintsevich EE, Reisler E. Cytoskeleton dynamics and binding factors Neuromethods. 79: 63-83. DOI: 10.1007/978-1-62703-266-7-4 |
0.423 |
|
2012 |
Kang H, Bradley MJ, McCullough BR, Pierre A, Grintsevich EE, Reisler E, De La Cruz EM. Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness. Proceedings of the National Academy of Sciences of the United States of America. 109: 16923-7. PMID 23027950 DOI: 10.1073/Pnas.1211078109 |
0.531 |
|
2012 |
Durer ZA, Kudryashov DS, Sawaya MR, Altenbach C, Hubbell W, Reisler E. Structural states and dynamics of the D-loop in actin. Biophysical Journal. 103: 930-9. PMID 23009842 DOI: 10.1016/J.Bpj.2012.07.030 |
0.832 |
|
2012 |
Sharma S, Grintsevich EE, Hsueh C, Reisler E, Gimzewski JK. Molecular cooperativity of drebrin1-300 binding and structural remodeling of F-actin. Biophysical Journal. 103: 275-83. PMID 22853905 DOI: 10.1016/J.Bpj.2012.06.006 |
0.576 |
|
2012 |
Chen CK, Sawaya MR, Phillips ML, Reisler E, Quinlan ME. Multiple forms of Spire-actin complexes and their functional consequences. The Journal of Biological Chemistry. 287: 10684-92. PMID 22334675 DOI: 10.1074/Jbc.M111.317792 |
0.713 |
|
2012 |
Galkin VE, Orlova A, Kudryashov D, Soloduhin A, Reisler E, Schröder GF, Egelman EH. Remodeling of Actin Filaments by Cofilin Biophysical Journal. 102: 238a. DOI: 10.1016/J.Bpj.2011.11.1307 |
0.617 |
|
2011 |
Galkin VE, Orlova A, Kudryashov DS, Solodukhin A, Reisler E, Schröder GF, Egelman EH. Remodeling of actin filaments by ADF/cofilin proteins. Proceedings of the National Academy of Sciences of the United States of America. 108: 20568-72. PMID 22158895 DOI: 10.1073/Pnas.1110109108 |
0.615 |
|
2011 |
Oztug Durer ZA, Kamal JK, Benchaar S, Chance MR, Reisler E. Myosin binding surface on actin probed by hydroxyl radical footprinting and site-directed labels. Journal of Molecular Biology. 414: 204-16. PMID 21986200 DOI: 10.1016/J.Jmb.2011.09.035 |
0.862 |
|
2011 |
McCullough BR, Grintsevich EE, Chen CK, Kang H, Hutchison AL, Henn A, Cao W, Suarez C, Martiel JL, Blanchoin L, Reisler E, De La Cruz EM. Cofilin-linked changes in actin filament flexibility promote severing. Biophysical Journal. 101: 151-9. PMID 21723825 DOI: 10.1016/J.Bpj.2011.05.049 |
0.706 |
|
2011 |
Muhlrad A, Grintsevich EE, Reisler E. Polycation induced actin bundles. Biophysical Chemistry. 155: 45-51. PMID 21411219 DOI: 10.1016/J.Bpc.2011.02.008 |
0.578 |
|
2011 |
Sharma S, Grintsevich EE, Phillips ML, Reisler E, Gimzewski JK. Atomic force microscopy reveals drebrin induced remodeling of f-actin with subnanometer resolution. Nano Letters. 11: 825-7. PMID 21175132 DOI: 10.1021/Nl104159V |
0.52 |
|
2011 |
Butterworth AH, Yan S, Kudryashov D, Reisler E, Polenova T. Fast Magic Angle Sample Spinning NMR Yields a View of the F-actin - Cofilin Complex with Atomic Resolution Biophysical Journal. 100: 300a. DOI: 10.1016/J.Bpj.2010.12.1836 |
0.585 |
|
2010 |
Kudryashov DS, Grintsevich EE, Rubenstein PA, Reisler E. A nucleotide state-sensing region on actin. The Journal of Biological Chemistry. 285: 25591-601. PMID 20530485 DOI: 10.1074/Jbc.M110.123869 |
0.558 |
|
2010 |
Grintsevich EE, Phillips M, Pavlov D, Phan M, Reisler E, Muhlrad A. Antiparallel dimer and actin assembly. Biochemistry. 49: 3919-27. PMID 20361759 DOI: 10.1021/Bi1002663 |
0.577 |
|
2010 |
Grintsevich EE, Galkin VE, Orlova A, Ytterberg AJ, Mikati MM, Kudryashov DS, Loo JA, Egelman EH, Reisler E. Mapping of drebrin binding site on F-actin. Journal of Molecular Biology. 398: 542-54. PMID 20347847 DOI: 10.1016/J.Jmb.2010.03.039 |
0.852 |
|
2010 |
Oztug Durer ZA, Diraviyam K, Sept D, Kudryashov DS, Reisler E. F-actin structure destabilization and DNase I binding loop: fluctuations mutational cross-linking and electron microscopy analysis of loop states and effects on F-actin. Journal of Molecular Biology. 395: 544-57. PMID 19900461 DOI: 10.1016/J.Jmb.2009.11.001 |
0.584 |
|
2009 |
Scoville D, Stamm JD, Altenbach C, Shvetsov A, Kokabi K, Rubenstein PA, Hubbell WL, Reisler E. Effects of binding factors on structural elements in F-actin. Biochemistry. 48: 370-8. PMID 19113841 DOI: 10.1021/Bi801649J |
0.84 |
|
2009 |
Shvetsov A, Berkane E, Chereau D, Dominguez R, Reisler E. The actin-binding domain of cortactin is dynamic and unstructured and affects lateral and longitudinal contacts in F-actin. Cell Motility and the Cytoskeleton. 66: 90-8. PMID 19089942 DOI: 10.1002/Cm.20328 |
0.599 |
|
2008 |
Kudryashov DS, Durer ZA, Ytterberg AJ, Sawaya MR, Pashkov I, Prochazkova K, Yeates TO, Loo RR, Loo JA, Satchell KJ, Reisler E. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America. 105: 18537-42. PMID 19015515 DOI: 10.1073/Pnas.0808082105 |
0.837 |
|
2008 |
Sawaya MR, Kudryashov DS, Pashkov I, Adisetiyo H, Reisler E, Yeates TO. Multiple crystal structures of actin dimers and their implications for interactions in the actin filament. Acta Crystallographica. Section D, Biological Crystallography. 64: 454-65. PMID 18391412 DOI: 10.1107/S0907444908003351 |
0.558 |
|
2008 |
Grintsevich EE, Benchaar SA, Warshaviak D, Boontheung P, Halgand F, Whitelegge JP, Faull KF, Loo RR, Sept D, Loo JA, Reisler E. Mapping the cofilin binding site on yeast G-actin by chemical cross-linking. Journal of Molecular Biology. 377: 395-409. PMID 18258262 DOI: 10.1016/J.Jmb.2007.12.073 |
0.866 |
|
2008 |
Shvetsov A, Galkin VE, Orlova A, Phillips M, Bergeron SE, Rubenstein PA, Egelman EH, Reisler E. Actin hydrophobic loop 262-274 and filament nucleation and elongation. Journal of Molecular Biology. 375: 793-801. PMID 18037437 DOI: 10.1016/J.Jmb.2007.10.076 |
0.645 |
|
2008 |
Kudryashov DS, Cordero CL, Reisler E, Satchell KJ. Characterization of the enzymatic activity of the actin cross-linking domain from the Vibrio cholerae MARTX Vc toxin. The Journal of Biological Chemistry. 283: 445-52. PMID 17951576 DOI: 10.1074/Jbc.M703910200 |
0.599 |
|
2007 |
Reisler E, Egelman EH. Actin structure and function: what we still do not understand. The Journal of Biological Chemistry. 282: 36133-7. PMID 17965017 DOI: 10.1074/Jbc.R700030200 |
0.446 |
|
2007 |
Kamal JK, Benchaar SA, Takamoto K, Reisler E, Chance MR. Three-dimensional structure of cofilin bound to monomeric actin derived by structural mass spectrometry data. Proceedings of the National Academy of Sciences of the United States of America. 104: 7910-5. PMID 17470807 DOI: 10.1073/Pnas.0611283104 |
0.848 |
|
2007 |
Benchaar SA, Xie Y, Phillips M, Loo RR, Galkin VE, Orlova A, Thevis M, Muhlrad A, Almo SC, Loo JA, Egelman EH, Reisler E. Mapping the interaction of cofilin with subdomain 2 on actin. Biochemistry. 46: 225-33. PMID 17198393 DOI: 10.1021/Bi0610754 |
0.865 |
|
2007 |
Pavlov D, Muhlrad A, Cooper J, Wear M, Reisler E. Actin filament severing by cofilin. Journal of Molecular Biology. 365: 1350-8. PMID 17134718 DOI: 10.1016/J.Jmb.2006.10.102 |
0.562 |
|
2006 |
Scoville D, Stamm JD, Toledo-Warshaviak D, Altenbach C, Phillips M, Shvetsov A, Rubenstein PA, Hubbell WL, Reisler E. Hydrophobic loop dynamics and actin filament stability. Biochemistry. 45: 13576-84. PMID 17087511 DOI: 10.1021/Bi061229F |
0.835 |
|
2006 |
Sowa GZ, Cannell DS, Liu AJ, Reisler E. Polyamine-induced bundling of F-actin. The Journal of Physical Chemistry. B. 110: 22279-84. PMID 17078670 DOI: 10.1021/Jp063371W |
0.834 |
|
2006 |
Muhlrad A, Ringel I, Pavlov D, Peyser YM, Reisler E. Antagonistic effects of cofilin, beryllium fluoride complex, and phalloidin on subdomain 2 and nucleotide-binding cleft in F-actin. Biophysical Journal. 91: 4490-9. PMID 16997870 DOI: 10.1529/Biophysj.106.087767 |
0.576 |
|
2006 |
Cordero CL, Kudryashov DS, Reisler E, Satchell KJ. The Actin cross-linking domain of the Vibrio cholerae RTX toxin directly catalyzes the covalent cross-linking of actin. The Journal of Biological Chemistry. 281: 32366-74. PMID 16954226 DOI: 10.1074/Jbc.M605275200 |
0.529 |
|
2006 |
Pavlov D, Muhlrad A, Cooper J, Wear M, Reisler E. Severing of F-actin by yeast cofilin is pH-independent. Cell Motility and the Cytoskeleton. 63: 533-42. PMID 16847879 DOI: 10.1002/Cm.20142 |
0.499 |
|
2006 |
Shvetsov A, Stamm JD, Phillips M, Warshaviak D, Altenbach C, Rubenstein PA, Hideg K, Hubbell WL, Reisler E. Conformational dynamics of loop 262-274 in G- and F-actin. Biochemistry. 45: 6541-9. PMID 16700564 DOI: 10.1021/Bi052558V |
0.589 |
|
2006 |
Muhlrad A, Pavlov D, Peyser YM, Reisler E. Inorganic phosphate regulates the binding of cofilin to actin filaments. The Febs Journal. 273: 1488-96. PMID 16689934 DOI: 10.1111/J.1742-4658.2006.05169.X |
0.612 |
|
2006 |
Kudryashov DS, Galkin VE, Orlova A, Phan M, Egelman EH, Reisler E. Cofilin cross-bridges adjacent actin protomers and replaces part of the longitudinal F-actin interface. Journal of Molecular Biology. 358: 785-97. PMID 16530787 DOI: 10.1016/J.Jmb.2006.02.029 |
0.631 |
|
2006 |
Bobkov AA, Muhlrad A, Pavlov DA, Kokabi K, Yilmaz A, Reisler E. Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function. Journal of Molecular Biology. 356: 325-34. PMID 16375920 DOI: 10.1016/J.Jmb.2005.11.072 |
0.623 |
|
2005 |
Kudryashov DS, Sawaya MR, Adisetiyo H, Norcross T, Hegyi G, Reisler E, Yeates TO. The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin. Proceedings of the National Academy of Sciences of the United States of America. 102: 13105-10. PMID 16141336 DOI: 10.1073/Pnas.0506429102 |
0.538 |
|
2005 |
Guan JQ, Takamoto K, Almo SC, Reisler E, Chance MR. Structure and dynamics of the actin filament. Biochemistry. 44: 3166-75. PMID 15736927 DOI: 10.1021/Bi048021J |
0.578 |
|
2004 |
Orlova A, Shvetsov A, Galkin VE, Kudryashov DS, Rubenstein PA, Egelman EH, Reisler E. Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization. Proceedings of the National Academy of Sciences of the United States of America. 101: 17664-8. PMID 15591338 DOI: 10.1073/Pnas.0407525102 |
0.615 |
|
2004 |
Muhlrad A, Kudryashov D, Michael Peyser Y, Bobkov AA, Almo SC, Reisler E. Cofilin induced conformational changes in F-actin expose subdomain 2 to proteolysis. Journal of Molecular Biology. 342: 1559-67. PMID 15364581 DOI: 10.1016/J.Jmb.2004.08.010 |
0.542 |
|
2004 |
Kudryashov DS, Phillips M, Reisler E. Formation and destabilization of actin filaments with tetramethylrhodamine-modified actin. Biophysical Journal. 87: 1136-45. PMID 15298916 DOI: 10.1529/Biophysj.104.042242 |
0.598 |
|
2004 |
Bobkov AA, Muhlrad A, Shvetsov A, Benchaar S, Scoville D, Almo SC, Reisler E. Cofilin (ADF) affects lateral contacts in F-actin. Journal of Molecular Biology. 337: 93-104. PMID 15001354 DOI: 10.1016/J.Jmb.2004.01.014 |
0.823 |
|
2003 |
Galkin VE, Orlova A, VanLoock MS, Shvetsov A, Reisler E, Egelman EH. ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments. The Journal of Cell Biology. 163: 1057-66. PMID 14657234 DOI: 10.1083/Jcb.200308144 |
0.596 |
|
2003 |
Guan JQ, Almo SC, Reisler E, Chance MR. Structural reorganization of proteins revealed by radiolysis and mass spectrometry: G-actin solution structure is divalent cation dependent. Biochemistry. 42: 11992-2000. PMID 14556630 DOI: 10.1021/Bi034914K |
0.482 |
|
2003 |
Kudryashov DS, Reisler E. Solution properties of tetramethylrhodamine-modified G-actin. Biophysical Journal. 85: 2466-75. PMID 14507709 DOI: 10.1016/S0006-3495(03)74669-4 |
0.522 |
|
2003 |
Nitao LK, Loo RR, O'Neall-Hennessey E, Loo JA, Szent-Györgyi AG, Reisler E. Conformation and dynamics of the SH1-SH2 helix in scallop myosin. Biochemistry. 42: 7663-74. PMID 12820875 DOI: 10.1021/Bi027312U |
0.814 |
|
2003 |
Muhlrad A, Peyser YM, Nili M, Ajtai K, Reisler E, Burghardt TP. Chemical decoupling of ATPase activation and force production from the contractile cycle in myosin by steric hindrance of lever-arm movement. Biophysical Journal. 84: 1047-56. PMID 12547786 DOI: 10.1016/S0006-3495(03)74921-2 |
0.489 |
|
2003 |
Pavlov D, Gerson JH, Yu T, Tobacman LS, Homsher E, Reisler E. The regulation of subtilisin-cleaved actin by tropomyosin/troponin. The Journal of Biological Chemistry. 278: 5517-22. PMID 12468534 DOI: 10.1074/Jbc.M210889200 |
0.856 |
|
2002 |
Bobkov AA, Muhlrad A, Kokabi K, Vorobiev S, Almo SC, Reisler E. Structural effects of cofilin on longitudinal contacts in F-actin. Journal of Molecular Biology. 323: 739-50. PMID 12419261 DOI: 10.1016/S0022-2836(02)01008-2 |
0.609 |
|
2002 |
Nitao LK, Yeates TO, Reisler E. Conformational dynamics of the SH1-SH2 helix in the transition states of myosin subfragment-1. Biophysical Journal. 83: 2733-41. PMID 12414706 DOI: 10.1016/S0006-3495(02)75283-1 |
0.796 |
|
2002 |
Wong WW, Gerson JH, Rubenstein PA, Reisler E. Thin filament regulation and ionic interactions between the N-terminal region in actin and troponin. Biophysical Journal. 83: 2726-32. PMID 12414705 DOI: 10.1016/S0006-3495(02)75282-X |
0.836 |
|
2002 |
Shvetsov A, Musib R, Phillips M, Rubenstein PA, Reisler E. Locking the hydrophobic loop 262-274 to G-actin surface by a disulfide bridge prevents filament formation. Biochemistry. 41: 10787-93. PMID 12196017 DOI: 10.1021/Bi020205F |
0.599 |
|
2002 |
Doyle TC, Reisler E. Insights into actomyosin interactions from actin mutations. Results and Problems in Cell Differentiation. 36: 31-49. PMID 11892282 DOI: 10.1007/978-3-540-46558-4_4 |
0.389 |
|
2002 |
Kim E, Bobkova E, Hegyi G, Muhlrad A, Reisler E. Actin cross-linking and inhibition of the actomyosin motor. Biochemistry. 41: 86-93. PMID 11772006 DOI: 10.1021/Bi0113824 |
0.541 |
|
2001 |
Wong WW, Doyle TC, Cheung P, Olson TM, Reisler E. Functional studies of yeast actin mutants corresponding to human cardiomyopathy mutations. Journal of Muscle Research and Cell Motility. 22: 665-74. PMID 12222827 DOI: 10.1023/A:1016354308436 |
0.717 |
|
2001 |
Reynoso JR, Bobkov A, Muhlrad A, Reisler E. Solution properties of full length and truncated forms of myosin subfragment 1 from Dictyostelium discoideum. Journal of Muscle Research and Cell Motility. 22: 657-64. PMID 12222826 DOI: 10.1023/A:1016306409345 |
0.485 |
|
2001 |
Orlova A, Galkin VE, VanLoock MS, Kim E, Shvetsov A, Reisler E, Egelman EH. Probing the structure of F-actin: cross-links constrain atomic models and modify actin dynamics. Journal of Molecular Biology. 312: 95-106. PMID 11545588 DOI: 10.1006/Jmbi.2001.4945 |
0.592 |
|
2001 |
Green NS, Reisler E, Houk KN. Quantitative evaluation of the lengths of homobifunctional protein cross-linking reagents used as molecular rulers. Protein Science : a Publication of the Protein Society. 10: 1293-304. PMID 11420431 DOI: 10.1110/Ps.51201 |
0.344 |
|
2001 |
Gerson JH, Kim E, Muhlrad A, Reisler E. Tropomyosin-troponin regulation of actin does not involve subdomain 2 motions. The Journal of Biological Chemistry. 276: 18442-9. PMID 11278830 DOI: 10.1074/Jbc.M011070200 |
0.842 |
|
2001 |
Doyle TC, Hansen JE, Reisler E. Tryptophan fluorescence of yeast actin resolved via conserved mutations. Biophysical Journal. 80: 427-34. PMID 11159413 DOI: 10.1016/S0006-3495(01)76025-0 |
0.531 |
|
2000 |
Eli-Berchoer L, Hegyi G, Patthy A, Reisler E, Muhlrad A. Effect of intramolecular cross-linking between glutamine-41 and lysine-50 on actin structure and function. Journal of Muscle Research and Cell Motility. 21: 405-14. PMID 11129431 DOI: 10.1023/A:1005649604515 |
0.644 |
|
2000 |
Kim E, Reisler E. Intermolecular dynamics and function in actin filaments. Biophysical Chemistry. 86: 191-201. PMID 11026684 DOI: 10.1016/S0301-4622(00)00143-5 |
0.622 |
|
2000 |
Bobkov AA, Reisler E. Is SH1-SH2-cross-linked myosin subfragment 1 a structural analog of the weakly-bound state of myosin? Biophysical Journal. 79: 460-7. PMID 10866971 DOI: 10.1016/S0006-3495(00)76307-7 |
0.418 |
|
2000 |
Kim E, Wriggers W, Phillips M, Kokabi K, Rubenstein PA, Reisler E. Cross-linking constraints on F-actin structure. Journal of Molecular Biology. 299: 421-9. PMID 10860749 DOI: 10.1006/Jmbi.2000.3727 |
0.564 |
|
2000 |
Nitao LK, Reisler E. Actin and temperature effects on the cross-linking of the SH1-SH2 helix in myosin subfragment 1. Biophysical Journal. 78: 3072-80. PMID 10827984 DOI: 10.1016/S0006-3495(00)76844-5 |
0.833 |
|
2000 |
Eli-Berchoer L, Reisler E, Muhlrad A. Structural implications of the chemical modification of Cys(10) on actin. Biophysical Journal. 78: 1482-9. PMID 10692333 DOI: 10.1016/S0006-3495(00)76701-4 |
0.649 |
|
2000 |
Hansen JE, Marner J, Pavlov D, Rubenstein PA, Reisler E. Structural transition at actin's N-terminus in the actomyosin cross-bridge cycle. Biochemistry. 39: 1792-9. PMID 10677229 DOI: 10.1021/Bi991873C |
0.559 |
|
1999 |
Gerson JH, Bobkova E, Homsher E, Reisler E. Role of residues 311/312 in actin-tropomyosin interaction. In vitro motility study using yeast actin mutant e311a/r312a. The Journal of Biological Chemistry. 274: 17545-50. PMID 10364188 DOI: 10.1074/Jbc.274.25.17545 |
0.849 |
|
1999 |
Wong WW, Doyle TC, Reisler E. Nonspecific weak actomyosin interactions: relocation of charged residues in subdomain 1 of actin does not alter actomyosin function. Biochemistry. 38: 1365-70. PMID 9930999 DOI: 10.1021/Bi982467G |
0.703 |
|
1999 |
Bobkova EA, Bobkov AA, Levitsky DI, Reisler E. Effects of SH1 and SH2 modifications on myosin: similarities and differences. Biophysical Journal. 76: 1001-7. PMID 9916031 DOI: 10.1016/S0006-3495(99)77264-4 |
0.539 |
|
1999 |
Hüsing N, Reisler E, Zink JI. Allosteric regulation of enzymatic reactions in a transparent inorganic sol-gel material Journal of Sol-Gel Science and Technology. 15: 57-61. DOI: 10.1023/A:1008713014152 |
0.312 |
|
1998 |
Kim E, Bobkova E, Miller CJ, Orlova A, Hegyi G, Egelman EH, Muhlrad A, Reisler E. Intrastrand cross-linked actin between Gln-41 and Cys-374. III. Inhibition of motion and force generation with myosin. Biochemistry. 37: 17801-9. PMID 9922146 DOI: 10.1021/Bi981286B |
0.612 |
|
1998 |
Kim E, Phillips M, Hegyi G, Muhlrad A, Reisler E. Intrastrand cross-linked actin between Gln-41 and Cys-374. II. Properties of cross-linked oligomers. Biochemistry. 37: 17793-800. PMID 9922145 DOI: 10.1021/Bi9812874 |
0.581 |
|
1998 |
Hegyi G, Mák M, Kim E, Elzinga M, Muhlrad A, Reisler E. Intrastrand cross-linked actin between Gln-41 and Cys-374. I. Mapping of sites cross-linked in F-actin by N-(4-azido-2-nitrophenyl) putrescine. Biochemistry. 37: 17784-92. PMID 9922144 DOI: 10.1021/Bi981285J |
0.565 |
|
1998 |
Nitao LK, Reisler E. Probing the conformational states of the SH1-SH2 helix in myosin: a cross-linking approach. Biochemistry. 37: 16704-10. PMID 9843439 DOI: 10.1021/Bi9817212 |
0.801 |
|
1997 |
Bobkov AA, Sutoh K, Reisler E. Nucleotide and actin binding properties of the isolated motor domain from Dictyostelium discoideum myosin. Journal of Muscle Research and Cell Motility. 18: 563-71. PMID 9350009 DOI: 10.1023/A:1018667319386 |
0.513 |
|
1997 |
Feng L, Kim E, Lee WL, Miller CJ, Kuang B, Reisler E, Rubenstein PA. Fluorescence probing of yeast actin subdomain 3/4 hydrophobic loop 262-274. Actin-actin and actin-myosin interactions in actin filaments. The Journal of Biological Chemistry. 272: 16829-37. PMID 9201989 DOI: 10.1074/Jbc.272.27.16829 |
0.589 |
|
1997 |
Bobkov AA, Bobkova EA, Homsher E, Reisler E. Activation of regulated actin by SH1-modified myosin subfragment 1. Biochemistry. 36: 7733-8. PMID 9201914 DOI: 10.1021/Bi963185O |
0.567 |
|
1997 |
Phan BC, Peyser YM, Reisler E, Muhlrad A. Effect of complexes of ADP and phosphate analogs on the conformation of the Cys707-Cys697 region of myosin subfragment 1. European Journal of Biochemistry / Febs. 243: 636-42. PMID 9057826 DOI: 10.1111/J.1432-1033.1997.00636.X |
0.372 |
|
1997 |
Bobkova KA, Homsher E, Reisler E. Estimation of force exerted by myosin heads in the in vitro motility assays using ppdm-cross-linked heavy meromyosin Faseb Journal. 11: A983. |
0.371 |
|
1996 |
Kim E, Miller CJ, Reisler E. Polymerization and in vitro motility properties of yeast actin: a comparison with rabbit skeletal alpha-actin. Biochemistry. 35: 16566-72. PMID 8987991 DOI: 10.1021/Bi9623892 |
0.596 |
|
1996 |
Miller CJ, Wong WW, Bobkova E, Rubenstein PA, Reisler E. Mutational analysis of the role of the N terminus of actin in actomyosin interactions. Comparison with other mutant actins and implications for the cross-bridge cycle. Biochemistry. 35: 16557-65. PMID 8987990 DOI: 10.1021/Bi962388+ |
0.76 |
|
1996 |
Kim E, Reisler E. Intermolecular coupling between loop 38-52 and the C-terminus in actin filaments. Biophysical Journal. 71: 1914-9. PMID 8889166 DOI: 10.1016/S0006-3495(96)79390-6 |
0.618 |
|
1996 |
Kim E, Miller CJ, Motoki M, Seguro K, Muhlrad A, Reisler E. Myosin-induced changes in F-actin: fluorescence probing of subdomain 2 by dansyl ethylenediamine attached to Gln-41. Biophysical Journal. 70: 1439-46. PMID 8785300 DOI: 10.1016/S0006-3495(96)79703-5 |
0.614 |
|
1996 |
Brenner B, Kraft T, DasGupta G, Reisler E. Cross-bridge binding to actin and force generation in skinned fibers of the rabbit psoas muscle in the presence of antibody fragments against the N-terminus of actin. Biophysical Journal. 70: 48-56. PMID 8770186 DOI: 10.1016/S0006-3495(96)79579-6 |
0.522 |
|
1996 |
Phan BC, Cheung P, Stafford WF, Reisler E. Complexes of myosin subfragment-1 with adenosine diphosphate and phosphate analogs: probes of active site and protein conformation. Biophysical Chemistry. 59: 341-9. PMID 8672721 DOI: 10.1016/0301-4622(95)00127-1 |
0.358 |
|
1996 |
Bobkov AA, Bobkova EA, Lin SH, Reisler E. The role of surface loops (residues 204-216 and 627-646) in the motor function of the myosin head. Proceedings of the National Academy of Sciences of the United States of America. 93: 2285-9. PMID 8637864 DOI: 10.1073/Pnas.93.6.2285 |
0.495 |
|
1996 |
Miller CJ, Doyle TC, Bobkova E, Botstein D, Reisler E. Mutational analysis of the role of hydrophobic residues in the 338-348 helix on actin in actomyosin interactions. Biochemistry. 35: 3670-6. PMID 8619986 DOI: 10.1021/Bi952645V |
0.605 |
|
1995 |
Kim E, Motoki M, Seguro K, Muhlrad A, Reisler E. Conformational changes in subdomain 2 of G-actin: fluorescence probing by dansyl ethylenediamine attached to Gln-41. Biophysical Journal. 69: 2024-32. PMID 8580345 DOI: 10.1016/S0006-3495(95)80072-X |
0.451 |
|
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 |
0.75 |
|
1995 |
Miller CJ, Reisler E. Role of charged amino acid pairs in subdomain-1 of actin in interactions with myosin. Biochemistry. 34: 2694-700. PMID 7873552 DOI: 10.1021/Bi00008A037 |
0.467 |
|
1995 |
Miller CJ, Cheung P, White P, Reisler E. Actin's view of actomyosin interface. Biophysical Journal. 68: 50S-54S. PMID 7787100 |
0.397 |
|
1995 |
Vahdat A, Miller C, Phillips M, Muhlrad A, Reisler E. A novel 27/16 kDa form of subtilisin cleaved actin: structural and functional consequences of cleavage between Ser234 and Ser235. Febs Letters. 365: 149-51. PMID 7781768 DOI: 10.1016/0014-5793(95)00446-G |
0.614 |
|
1995 |
Phan BC, Cheung P, Miller CJ, Reisler E, Muhlrad A. Extensively methylated myosin subfragment-1: examination of local structure, interactions with nucleotides and actin, and ligand-induced conformational changes. Biochemistry. 33: 11286-95. PMID 7727379 DOI: 10.1021/bi00203a026 |
0.366 |
|
1994 |
Phan BC, Reisler E. Aluminum fluoride interactions with troponin C. Biophysical Journal. 65: 2511-6. PMID 8312488 DOI: 10.1016/S0006-3495(93)81305-5 |
0.379 |
|
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 |
0.787 |
|
1994 |
Adams SB, Reisler E. Sequence 18-29 on actin: antibody and spectroscopic probing of conformational changes. Biochemistry. 33: 14426-33. PMID 7981202 DOI: 10.1021/Bi00252A008 |
0.58 |
|
1994 |
Crosbie RH, Miller C, Cheung P, Goodnight T, Muhlrad A, Reisler E. Structural connectivity in actin: effect of C-terminal modifications on the properties of actin. Biophysical Journal. 67: 1957-64. PMID 7858132 DOI: 10.1016/S0006-3495(94)80678-2 |
0.804 |
|
1994 |
Duong AM, Reisler E. C-terminus on actin: spectroscopic and immunochemical examination of its role in actomyosin interactions. Advances in Experimental Medicine and Biology. 358: 59-70. PMID 7801812 DOI: 10.1007/978-1-4615-2578-3_6 |
0.343 |
|
1993 |
Reisler E. Actin molecular structure and function. Current Opinion in Cell Biology. 5: 41-7. PMID 8448029 DOI: 10.1016/S0955-0674(05)80006-7 |
0.557 |
|
1993 |
Phan BC, Faller LD, Reisler E. Kinetic and equilibrium analysis of the interactions of actomyosin subfragment-1.ADP with beryllium fluoride. Biochemistry. 32: 7712-9. PMID 8347580 DOI: 10.1021/Bi00081A016 |
0.427 |
|
1993 |
Adams S, Reisler E. Role of sequence 18-29 on actin in actomyosin interactions. Biochemistry. 32: 5051-6. PMID 7684258 DOI: 10.1021/Bi00070A012 |
0.556 |
|
1993 |
Root DD, Reisler E. The accessibility of etheno-nucleotides to collisional quenchers and the nucleotide cleft in G- and F-actin. Protein Science : a Publication of the Protein Society. 1: 1014-22. PMID 1304380 DOI: 10.1002/Pro.5560010807 |
0.583 |
|
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 |
0.781 |
|
1992 |
Chen T, Haigentz M, Reisler E. Myosin subfragment 1 and structural elements of G-actin: effects of S-1(A2) on sequences 39-52 and 61-69 in subdomain 2 of G-actin. Biochemistry. 31: 2941-6. PMID 1550820 DOI: 10.1021/Bi00126A014 |
0.478 |
|
1992 |
Phan B, Reisler E. Inhibition of myosin ATPase by beryllium fluoride. Biochemistry. 31: 4787-93. PMID 1534258 DOI: 10.1021/Bi00135A007 |
0.338 |
|
1992 |
DasGupta G, Reisler E. Actomyosin interactions in the presence of ATP and the N-terminal segment of actin. Biochemistry. 31: 1836-41. PMID 1531299 DOI: 10.1021/Bi00121A036 |
0.555 |
|
1992 |
Cheung P, Reisler E. Synthetic peptide of the sequence 632-642 on myosin subfragment 1 inhibits actomyosin ATPase activity Biochemical and Biophysical Research Communications. 189: 1143-1149. PMID 1472024 DOI: 10.1016/0006-291X(92)92323-P |
0.52 |
|
1992 |
Root DD, Reisler E. Cooperativity of thiol-modified myosin filaments. ATPase and motility assays of myosin function. Biophysical Journal. 63: 730-40. PMID 1420910 DOI: 10.1016/S0006-3495(92)81646-6 |
0.567 |
|
1992 |
Cartoux L, Chen T, DasGupta G, Chase PB, Kushmerick MJ, Reisler E. Antibody and peptide probes of interactions between the SH1-SH2 region of myosin subfragment 1 and actin's N-terminus. Biochemistry. 31: 10929-35. PMID 1420204 |
0.456 |
|
1991 |
DasGupta G, White J, Cheung P, Reisler E. Interactions between G-actin and myosin subfragment 1: immunochemical probing of the NH2-terminal segment on actin. Biochemistry. 29: 8503-8. PMID 2252908 DOI: 10.1021/Bi00488A043 |
0.584 |
|
1991 |
Chen T, Reisler E. Interactions of myosin subfragment 1 isozymes with G-actin. Biochemistry. 30: 4546-52. PMID 2021647 DOI: 10.1021/Bi00232A026 |
0.444 |
|
1991 |
DasGupta G, Reisler E. Nucleotide-induced changes in the interaction of myosin subfragment 1 with actin: detection by antibodies against the N-terminal segment of actin. Biochemistry. 30: 9961-6. PMID 1911787 DOI: 10.1021/Bi00105A021 |
0.568 |
|
1991 |
Root DD, Cheung P, Reisler E. Catalytic cooperativity induced by SH1 labeling of myosin filaments. Biochemistry. 30: 286-94. PMID 1824816 DOI: 10.1021/Bi00215A039 |
0.45 |
|
1990 |
DasGupta G, White J, Phillips M, Bulinski JC, Reisler E. Immunochemical probing of the N-terminal segment on actin: the polymerization reaction. Biochemistry. 29: 3319-24. PMID 2334693 DOI: 10.1021/Bi00465A024 |
0.561 |
|
1990 |
Schwyter DH, Kron SJ, Toyoshima YY, Spudich JA, Reisler E. Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin Journal of Cell Biology. 111: 465-470. PMID 2143196 DOI: 10.1083/Jcb.111.2.465 |
0.589 |
|
1989 |
Duong AM, Reisler E. Nucleotide-induced states of myosin subfragment 1 cross-linked to actin. Biochemistry. 28: 3502-9. PMID 2787166 DOI: 10.1021/Bi00434A053 |
0.489 |
|
1989 |
DasGupta G, Reisler E. Antibody against the amino terminus of alpha-actin inhibits actomyosin interactions in the presence of ATP. Journal of Molecular Biology. 207: 833-6. PMID 2760933 DOI: 10.1016/0022-2836(89)90249-0 |
0.53 |
|
1989 |
Schwyter D, Phillips M, Reisler E. Subtilisin-cleaved actin: polymerization and interaction with myosin subfragment 1. Biochemistry. 28: 5889-95. PMID 2673352 DOI: 10.1021/Bi00440A027 |
0.616 |
|
1989 |
Duong AM, Reisler E. Binding of myosin to actin in myofibrils during ATP hydrolysis. Biochemistry. 28: 1307-13. PMID 2523735 DOI: 10.1021/Bi00429A054 |
0.551 |
|
1988 |
Cheung P, Reisler E. The binding of heat-treated myosin subfragment 1 to actin and substructure considerations Archives of Biochemistry and Biophysics. 265: 272-278. PMID 3421705 DOI: 10.1016/0003-9861(88)90128-2 |
0.464 |
|
1988 |
Miller L, Phillips M, Reisler E. Polymerization of actin modified with fluorescein isothiocyanate. European Journal of Biochemistry. 174: 23-9. PMID 2967182 DOI: 10.1111/J.1432-1033.1988.Tb14057.X |
0.597 |
|
1987 |
Miller L, Kalnoski M, Yunossi Z, Bulinski JC, Reisler E. Antibodies directed against N-terminal residues on actin do not block acto-myosin binding. Biochemistry. 26: 6064-70. PMID 3689759 DOI: 10.1021/Bi00393A018 |
0.531 |
|
1987 |
Chen T, Liu J, Reisler E. Immunochemical probing of the N-terminus of the myosin heavy chain. Biochemical and Biophysical Research Communications. 147: 369-74. PMID 3632676 DOI: 10.1016/S0006-291X(87)80131-6 |
0.35 |
|
1987 |
Chen T, Liu J, Reisler E. Proteolysis and binding of myosin subfragment 1 to actin. Journal of Molecular Biology. 194: 565-8. PMID 3625775 DOI: 10.1016/0022-2836(87)90682-6 |
0.476 |
|
1986 |
Chen T, Applegate D, Reisler E. Cross-linking of actin to myosin subfragment 1 in the presence of nucleotides. Biochemistry. 24: 5620-5. PMID 3878158 DOI: 10.1021/Bi00341A050 |
0.483 |
|
1986 |
Reisler E, Cheung P, Borochov N. Macromolecular assemblies of myosin. Biophysical Journal. 49: 335-42. PMID 3485450 DOI: 10.1016/S0006-3495(86)83646-3 |
0.323 |
|
1986 |
Reisler E, Cheung P, Borochov N, Lake JA. Monomers, dimers, and minifilaments of vertebrate skeletal myosin in the presence of sodium pyrophosphate Biochemistry. 25: 326-332. PMID 3006755 DOI: 10.1021/Bi00350A007 |
0.336 |
|
1985 |
Miller L, Reisler E. Light chain dependent effects of actin binding on the S-1/S-2 swivel in myosin. Journal of Molecular Biology. 182: 271-9. PMID 3889349 DOI: 10.1016/0022-2836(85)90345-6 |
0.479 |
|
1985 |
Chen T, Applegate D, Reisler E. Cross-linking of actin to myosin subfragment 1: course of reaction and stoichiometry of products. Biochemistry. 24: 137-44. PMID 3846455 DOI: 10.1021/Bi00322A019 |
0.424 |
|
1984 |
Reisler E, Liu J, Cheung P. Role of magnesium binding to myosin in controlling the state of cross-bridges in skeletal rabbit muscle. Biochemistry. 22: 4954-60. PMID 6685530 DOI: 10.1021/Bi00290A012 |
0.505 |
|
1984 |
Chen T, Reisler E. Tryptic digestion of rabbit skeletal myofibrils: an enzymatic probe of myosin cross-bridges. Biochemistry. 23: 2400-7. PMID 6477873 DOI: 10.1021/Bi00306A013 |
0.441 |
|
1984 |
Applegate D, Reisler E. Protease-sensitive regions in myosin subfragment 1. Proceedings of the National Academy of Sciences of the United States of America. 80: 7109-12. PMID 6359163 DOI: 10.1073/Pnas.80.23.7109 |
0.456 |
|
1983 |
Mrakovcić-Zenic A, Reisler E. Light-chain phosphorylation and cross-bridge conformation in myosin from vertebrate skeletal muscle. Biochemistry. 22: 525-30. PMID 6838809 DOI: 10.1021/Bi00272A001 |
0.475 |
|
1983 |
Applegate D, Reisler E. Crossbridge release and alpha-helix-coil transition in myosin and rod minifilaments. Journal of Molecular Biology. 169: 455-68. PMID 6352954 DOI: 10.1016/S0022-2836(83)80061-8 |
0.332 |
|
1982 |
Cheung P, Reisler E. Effect of calcium on synthetic myosin minifilaments Biochemistry. 21: 6906-6910. PMID 7159573 DOI: 10.1021/Bi00269A044 |
0.374 |
|
1982 |
Reisler E, Cheung P, Oriol-Audit C, Lake JA. Growth of synthetic myosin filaments from myosin minifilaments Biochemistry. 21: 701-707. PMID 7074034 DOI: 10.1021/Bi00533A018 |
0.467 |
|
1982 |
Reisler E, Liu J. Conformational changes in the myosin subfragment-2. Effect of pH on synthetic rod filaments. Journal of Molecular Biology. 157: 659-69. PMID 6750134 DOI: 10.1016/0022-2836(82)90504-6 |
0.459 |
|
1982 |
Reisler E, Liu J. Interaction of myosin subfragment 1 with Cibacron Blue F3GA. Biochemistry. 20: 6745-9. PMID 6459118 DOI: 10.1021/Bi00527A001 |
0.407 |
|
1982 |
Miller L, Coppedge J, Reisler E. The reactive SH1 and SH2 cysteines in myosin subfragment 1 are cross-linked at similar rates with reagents of different length. Biochemical and Biophysical Research Communications. 106: 117-22. PMID 6213228 DOI: 10.1016/0006-291X(82)92066-6 |
0.388 |
|
1981 |
Reisler E, Smith C, Seegan G. Myosin minifilaments. Journal of Molecular Biology. 143: 129-45. PMID 7441758 DOI: 10.1016/0022-2836(80)90127-8 |
0.432 |
|
1981 |
Mrakovcić-Zenic A, Oriol-Audit C, Reisler E. On the alkali light chains of vertebrate skeletal myosin. Nucleotide binding and salt-induced conformational changes. European Journal of Biochemistry. 115: 565-70. PMID 7238521 DOI: 10.1111/J.1432-1033.1981.Tb06240.X |
0.394 |
|
1981 |
Oda S, Oriol-Audit C, Reisler E. Effects of actin and calcium ion on chymotryptic digestion of skeletal myosin and their implications to the function of light chains. Biochemistry. 19: 5614-8. PMID 7006689 DOI: 10.1021/Bi00565A024 |
0.45 |
|
1981 |
Oriol-Audit C, Lake JA, Reisler E. Structural changes in synthetic myosin minifilaments and their dissociation by adenosine triphosphate and pyrophosphate Biochemistry. 20: 679-686. PMID 6260138 DOI: 10.1021/Bi00507A002 |
0.549 |
|
1980 |
Reisler E. On the question of co-operative interaction of myosin heads with F-actin in the presence of ATP. Journal of Molecular Biology. 138: 93-107. PMID 6997492 DOI: 10.1016/S0022-2836(80)80006-4 |
0.535 |
|
1980 |
Reisler E, Liu J, Mercola M, Horwitz J. The interaction of cibacron blue F3GA with troponin and its subunits Bba - Protein Structure. 623: 243-256. PMID 6893162 DOI: 10.1016/0005-2795(80)90253-6 |
0.342 |
|
1980 |
Mrakovcić A, Oda S, Reisler E. Salt-induced conformational changes in skeletal myosin light chains, troponin-C, and parvalbumin. Biochemistry. 18: 5960-5. PMID 518878 DOI: 10.1021/Bi00593A031 |
0.365 |
|
1980 |
Zeiri L, Reisler E. Circular dichroism of complexes of NADH with self-associating bovine liver glutamate dehydrogenase. Biopolymers. 18: 2289-301. PMID 230866 DOI: 10.1002/Bip.1979.360180916 |
0.333 |
|
1978 |
Burke M, Reisler E. Effect of nucleotide binding on the proximity of the essential sulfhydryl groups of myosin. Chemical probing of movement of residues during conformational transitions. Biochemistry. 16: 5559-63. PMID 144522 DOI: 10.1021/Bi00644A026 |
0.433 |
|
1977 |
Reisler E, Haik Y, Eisenberg H. Bovine serum albumin in aqueous guanidine hydrochloride solutions. Preferential and absolute interactions and comparison with other systems Biochemistry. 16: 197-203. PMID 836784 DOI: 10.1021/Bi00621A006 |
0.574 |
|
1977 |
Eisenberg H, Josephs R, Reisler E. Scattering correction to the absorbance, wavelength dependence of the refractive index increment, and molecular weight of the bovine liver glutamate dehydrogenase oligomer and subunits. Biopolymers. 16: 2773-83. PMID 597578 DOI: 10.1002/Bip.1977.360161214 |
0.5 |
|
1977 |
Reisler E, Burke M, Harrington WF. Reactivity of essential thiols of myosin. Chemical probes of the activated state Biochemistry. 16: 5187-5191. PMID 144520 DOI: 10.1021/Bi00643A005 |
0.637 |
|
1977 |
Reisler E, Lamed R. Interaction of adipic acid dihydrazide analogue of ATP with myosin. Involvement of the essential sulfhydryl groups. Biochemistry. 16: 2532-8. PMID 16649 DOI: 10.1021/Bi00630A033 |
0.326 |
|
1976 |
Lamed R, Oplatka A, Reisler E. Affinity chromatography of heavy meromyosin subfragment-1 reacted with thiol reagents. Biochimica Et Biophysica Acta. 427: 688-95. PMID 131579 DOI: 10.1016/0005-2795(76)90212-9 |
0.344 |
|
1976 |
Eisenberg H, Josephs R, Reisler E. Bovine liver glutamate dehydrogenase. Advances in Protein Chemistry. 30: 101-81. PMID 7109 DOI: 10.1016/S0065-3233(08)60479-9 |
0.563 |
|
1975 |
Harrington WF, Reisler E, Burke M. An activation mechanism for ATP cleavage in muscle Journal of Supramolecular and Cellular Biochemistry. 3: 112-124. PMID 127882 DOI: 10.1002/Jss.400030204 |
0.611 |
|
1974 |
Reisler E, Burke M, Himmelfarb S, Harrington WF. Spatial proximity of the two essential sulfhydryl groups of myosin Biochemistry. 13: 3837-3840. PMID 4278279 DOI: 10.1021/Bi00716A001 |
0.567 |
|
1974 |
Reisler E, Burke M, Harrington WF. Cooperative role of two sulfhydryl groups in myosin adenosine triphosphatase Biochemistry. 13: 2014-2022. PMID 4275027 DOI: 10.1021/Bi00707A003 |
0.595 |
|
1973 |
Josephs R, Eisenberg H, Reisler E. Some properties of cross-linked polymers of glutamic dehydrogenase. Biochemistry. 12: 4060-7. PMID 4355550 DOI: 10.1021/Bi00745A006 |
0.567 |
|
1973 |
Burke M, Reisler E, Harrington WF. Myosin ATP hydrolysis: a mechanism involving a magnesium chelate complex Proceedings of the National Academy of Sciences of the United States of America. 70: 3793-3796. PMID 4272702 DOI: 10.1073/Pnas.70.12.3793 |
0.676 |
|
1972 |
Eisenberg H, Reisler E. Angular dependence of scattered light, rotary frictional coefficients, and distribution of sizes of associated oligomers in solutions of bovine liver glutamate dehydrogenase. Biopolymers. 10: 2363-76. PMID 5166596 DOI: 10.1002/bip.360101202 |
0.487 |
|
1972 |
Reisler E, Eisenberg H. Solubility of toluene in bovine liver glutamate dehydrogenase solutions and enhancement of enzyme association. Biochimica Et Biophysica Acta. 258: 351-7. PMID 4334530 DOI: 10.1016/0005-2744(72)90226-4 |
0.497 |
|
1972 |
Reisler E, Eisenberg H, Minton AP. Temperature and density dependence of the refractive index of pure liquids Journal of the Chemical Society, Faraday Transactions 2. 68: 1001. DOI: 10.1039/F29726801001 |
0.533 |
|
1971 |
Reisler E, Eisenberg H. Bovine liver glutamate dehydrogenase association and dependence of association on temperature. Biochemistry. 10: 2659-63. PMID 5105181 DOI: 10.1021/bi00790a001 |
0.493 |
|
1970 |
Reisler E, Eisenberg H. Studies on the viscosity of solutions of bovine liver glutamate dehydrogenase and on related hydrodynamic models; effect of toluene on enzyme association. Biopolymers. 9: 877-89. PMID 5433614 DOI: 10.1002/bip.1970.360090802 |
0.496 |
|
1970 |
Reisler E, Eisenberg H. Interpretation of equilibrium sedimentation measurements of proteins in guanidine hydrochloride solutions. Partial volumes, density increments, and the molecular weight of the subunits of rabbit muscle aldolase. Biochemistry. 8: 4572-8. PMID 5389439 DOI: 10.1021/Bi00839A051 |
0.546 |
|
1970 |
Reisler E, Pouyet J, Eisenberg H. Molecular weights, association, and frictional resistance of bovine liver glutamate dehydrogenase at low concentrations. Equilibrium and velocity sedimentation, light-scattering studies, and settling experiments with macroscopic models of the enzyme oligomer. Biochemistry. 9: 3095-102. PMID 4319828 DOI: 10.1021/Bi00817A600 |
0.549 |
|
1970 |
Eisenberg H, Reisler E. A physical model for the structure of glutamate dehydrogenase Biopolymers. 9: 113-115. DOI: 10.1002/bip.1970.360090110 |
0.508 |
|
1965 |
Reisler E, Eisenberg H. Refractive Indices and Piezo‐optic Coefficients of Deuterium Oxide, Methanol, and Other Pure Liquids The Journal of Chemical Physics. 43: 3875-3880. DOI: 10.1063/1.1696614 |
0.451 |
|
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