| Year |
Citation |
Score |
| 2011 |
Gergely J, Seidel JC. Conformational Changes and Molecular Dynamics of Myosin Comprehensive Physiology. 257-274. DOI: 10.1002/Cphy.Cp100109 |
0.37 |
|
| 2008 |
Gergely J. Key events in the history of calcium regulation of striated muscle. Biochemical and Biophysical Research Communications. 369: 49-51. PMID 18157939 DOI: 10.1016/J.Bbrc.2007.11.184 |
0.325 |
|
| 2007 |
Gergely J. Highlights of the history of calcium regulation of striated muscle. Advances in Experimental Medicine and Biology. 592: 11-8. PMID 17278352 DOI: 10.1007/978-4-431-38453-3_3 |
0.33 |
|
| 2006 |
Gergely J. The 34th European Muscle Conference Hortobágy, Hungary, 17-21 September 2005. Journal of Muscle Research and Cell Motility. 27: 215-20. PMID 16741829 DOI: 10.1007/S10974-006-9064-7 |
0.326 |
|
| 2002 |
Luo Y, Li B, Yang G, Gergely J, Tao T. Cross-linking between the regulatory regions of troponin-I and troponin-C abolishes the inhibitory function of troponin. Biochemistry. 41: 12891-8. PMID 12379133 DOI: 10.1021/Bi020396M |
0.432 |
|
| 2002 |
Luo Y, Leszyk J, Li B, Li Z, Gergely J, Tao T. Troponin-I interacts with the Met47 region of skeletal muscle actin. Implications for the mechanism of thin filament regulation by calcium. Journal of Molecular Biology. 316: 429-34. PMID 11866508 DOI: 10.1006/Jmbi.2001.5358 |
0.464 |
|
| 2001 |
Li Z, Gergely J, Tao T. Proximity relationships between residue 117 of rabbit skeletal troponin-I and residues in troponin-C and actin. Biophysical Journal. 81: 321-33. PMID 11423417 DOI: 10.1016/S0006-3495(01)75702-5 |
0.442 |
|
| 2000 |
GERGELY J. Muscle proteins and energy utilization. Annals of the New York Academy of Sciences. 72: 538-54. PMID 13627938 DOI: 10.1111/J.1749-6632.1959.Tb44181.X |
0.317 |
|
| 2000 |
Luo Y, Leszyk J, Li B, Gergely J, Tao T. Proximity relationships between residue 6 of troponin I and residues in troponin C: further evidence for extended conformation of troponin C in the troponin complex. Biochemistry. 39: 15306-15. PMID 11112516 DOI: 10.1021/Bi001259X |
0.388 |
|
| 2000 |
Luo Y, Wu JL, Li B, Langsetmo K, Gergely J, Tao T. Photocrosslinking of benzophenone-labeled single cysteine troponin I mutants to other thin filament proteins. Journal of Molecular Biology. 296: 899-910. PMID 10677290 DOI: 10.1006/Jmbi.1999.3495 |
0.439 |
|
| 1999 |
Tao T, Gong BJ, Grabarek Z, Gergely J. Conformational changes induced in troponin I by interaction with troponin T and actin/tropomyosin. Biochimica Et Biophysica Acta. 1450: 423-33. PMID 10395953 DOI: 10.1016/S0167-4889(99)00050-6 |
0.451 |
|
| 1999 |
Luo Y, Leszyk J, Qian Y, Gergely J, Tao T. Residues 48 and 82 at the N-terminal hydrophobic pocket of rabbit skeletal muscle troponin-C photo-cross-link to Met121 of troponin-I. Biochemistry. 38: 6678-88. PMID 10350487 DOI: 10.1021/Bi9824341 |
0.456 |
|
| 1999 |
Gergely J. Professor Ebashi's impact on the study of the regulation of striated muscle contraction. Molecular and Cellular Biochemistry. 190: 5-8. PMID 10098964 DOI: 10.1023/A:1006987223644 |
0.317 |
|
| 1998 |
GERGELY J. The relaxing factor of muscle. Annals of the New York Academy of Sciences. 81: 490-504. PMID 13827474 DOI: 10.1111/J.1749-6632.1959.Tb49330.X |
0.334 |
|
| 1998 |
Gergely J. Molecular switches in troponin. Advances in Experimental Medicine and Biology. 453: 169-76. PMID 9889827 DOI: 10.1007/978-1-4684-6039-1_20 |
0.441 |
|
| 1998 |
Leszyk J, Tao T, Nuwaysir LM, Gergely J. Identification of the photocrosslinking sites in troponin-I with 4-maleimidobenzophenone labelled mutant troponin-Cs having single cysteines at positions 158 and 21. Journal of Muscle Research and Cell Motility. 19: 479-90. PMID 9682135 DOI: 10.1023/A:1005352324741 |
0.323 |
|
| 1998 |
Luo Y, Wu JL, Gergely J, Tao T. Localization of Cys133 of rabbit skeletal troponin-I with respect to troponin-C by resonance energy transfer. Biophysical Journal. 74: 3111-9. PMID 9635764 DOI: 10.1016/S0006-3495(98)78017-8 |
0.419 |
|
| 1997 |
Luo Y, Wu JL, Gergely J, Tao T. Troponin T and Ca2+ dependence of the distance between Cys48 and Cys133 of troponin I in the ternary troponin complex and reconstituted thin filaments. Biochemistry. 36: 11027-35. PMID 9283095 DOI: 10.1021/Bi962461W |
0.453 |
|
| 1995 |
Kobayashi T, Grabarek Z, Gergely J, Collins JH. Extensive interactions between troponins C and I. Zero-length cross-linking of troponin I and acetylated troponin C. Biochemistry. 34: 10946-52. PMID 7662676 DOI: 10.1021/Bi00034A029 |
0.36 |
|
| 1995 |
Grabarek Z, Mabuchi Y, Gergely J. Properties of troponin C acetylated at lysine residues. Biochemistry. 34: 11872-81. PMID 7547922 DOI: 10.1021/Bi00037A027 |
0.42 |
|
| 1994 |
Kobayashi T, Tao T, Gergely J, Collins JH. Structure of the troponin complex. Implications of photocross-linking of troponin I to troponin C thiol mutants. The Journal of Biological Chemistry. 269: 5725-9. PMID 8119911 |
0.363 |
|
| 1993 |
Gergely J, Grabarek Z, Tao T, Maeda Y, Gulati J, Gordon AM. The molecular switch in troponin C Advances in Experimental Medicine and Biology. 332: 117-123. PMID 8109324 DOI: 10.1007/978-1-4615-2872-2_10 |
0.45 |
|
| 1992 |
Wang Z, Gergely J, Tao T. Characterization of the Ca(2+)-triggered conformational transition in troponin C. Proceedings of the National Academy of Sciences of the United States of America. 89: 11814-7. PMID 1465405 |
0.357 |
|
| 1992 |
Grabarek Z, Tao T, Gergely J. Molecular mechanism of troponin-C function. Journal of Muscle Research and Cell Motility. 13: 383-93. PMID 1401036 DOI: 10.1007/Bf01738034 |
0.416 |
|
| 1990 |
Wang ZY, Sarkar S, Gergely J, Tao T. Ca2(+)-dependent interactions between the C-helix of troponin-C and troponin-I. Photocross-linking and fluorescence studies using a recombinant troponin-C. The Journal of Biological Chemistry. 265: 4953-7. PMID 2180953 |
0.307 |
|
| 1990 |
Grabarek Z, Mabuchi Y, Gergely J. Structure-function relations in troponin C. chemical modification studies. Advances in Experimental Medicine and Biology. 269: 85-8. PMID 2112826 DOI: 10.1007/978-1-4684-5754-4_12 |
0.458 |
|
| 1990 |
Grabarek Z, Tan RY, Wang J, Tao T, Gergely J. Inhibition of mutant troponin C activity by an intra-domain disulphide bond. Nature. 345: 132-5. PMID 2110625 DOI: 10.1038/345132A0 |
0.375 |
|
| 1990 |
Leszyk J, Grabarek Z, Gergely J, Collins JH. Characterization of zero-length cross-links between rabbit skeletal muscle troponin C and troponin I: evidence for direct interaction between the inhibitory region of troponin I and the NH2-terminal, regulatory domain of troponin C. Biochemistry. 29: 299-304. PMID 2108719 DOI: 10.1021/Bi00453A041 |
0.428 |
|
| 1989 |
Tao T, Gowell E, Strasburg GM, Gergely J, Leavis PC. Ca2+ dependence of the distance between Cys-98 of troponin C and Cys-133 of troponin I in the ternary troponin complex. Resonance energy transfer measurements. Biochemistry. 28: 5902-8. PMID 2775740 DOI: 10.1021/Bi00440A029 |
0.41 |
|
| 1988 |
Gergely J, Grabarek Z, Leavis PC, Strasburg G, Tao T, Wang CL. Transmission of the Ca2+-regulatory signal in skeletal muscle thin filaments. Advances in Experimental Medicine and Biology. 226: 155-64. PMID 3407513 |
0.371 |
|
| 1988 |
Chen Q, Taljanidisz J, Sarkar S, Tao T, Gergely J. Cloning, sequencing and expression of a full-length rabbit fast skeletal troponin-C cDNA. Febs Letters. 228: 22-6. PMID 3277860 DOI: 10.1016/0014-5793(88)80576-3 |
0.304 |
|
| 1987 |
Sreter FA, Lopez JR, Alamo L, Mabuchi K, Gergely J. Changes in intracellular ionized Ca concentration associated with muscle fiber type transformation American Journal of Physiology - Cell Physiology. 253. PMID 2956887 DOI: 10.1152/Ajpcell.1987.253.2.C296 |
0.37 |
|
| 1986 |
Tao T, Gergely J, Leavis P. Studies on the Interactions between the Subunits of Skeletal Muscle Troponin Using Fluorescence Quenching, Photochemical Cross-Linking, and Excitation Energy Transfer Techniques. Biophysical Journal. 49: 142-3. PMID 19431622 DOI: 10.1016/S0006-3495(86)83627-X |
0.326 |
|
| 1986 |
Grabarek Z, Leavis PC, Gergely J. Calcium binding to the low affinity sites in troponin C induces conformational changes in the high affinity domain. A possible route of information transfer in activation of muscle contraction. The Journal of Biological Chemistry. 261: 608-13. PMID 3941095 |
0.339 |
|
| 1986 |
Sweeney HL, Kushmerick MJ, Mabuchi K, Gergely J, Sréter FA. Velocity of shortening and myosin isozymes in two types of rabbit fast-twitch muscle fibers. The American Journal of Physiology. 251: C431-4. PMID 3019147 DOI: 10.1152/Ajpcell.1986.251.3.C431 |
0.328 |
|
| 1986 |
Manuck BA, Seidel JC, Gergely J. Single-headed binding of a spin-labeled-HMM-ADP complex to F-actin. Saturation transfer electron paramagnetic resonance and sedimentation studies. Biophysical Journal. 50: 221-30. PMID 3017466 DOI: 10.1016/S0006-3495(86)83456-7 |
0.38 |
|
| 1986 |
Ishiwata S, Manuck BA, Seidel JC, Gergely J. Saturation transfer electron paramagnetic resonance study of the mobility of myosin heads in myofibrils under conditions of partial dissociation. Biophysical Journal. 49: 821-8. PMID 3013329 DOI: 10.1016/S0006-3495(86)83711-0 |
0.348 |
|
| 1986 |
Wang CL, Gergely J. Modulation of the interaction between the two halves of troponin C by the other troponin subunits. European Journal of Biochemistry. 154: 225-8. PMID 3002791 DOI: 10.1111/J.1432-1033.1986.Tb09383.X |
0.411 |
|
| 1985 |
Wang CL, Leavis PC, Gergely J. Kinetic studies show that Ca2+ and Tb3+ have different binding preferences toward the four Ca2+-binding sites of calmodulin. Biochemistry. 23: 6410-5. PMID 6529556 DOI: 10.1021/Bi00321A020 |
0.354 |
|
| 1985 |
DRABIKOWSKI W, DALGARNO DC, LEVINE BA, GERGELY J, GRABAREK Z, LEAVIS PC. Solution conformation of the C‐terminal domain of skeletal troponin C: Cation, trifluoperazine and troponin I binding effects European Journal of Biochemistry. 151: 17-28. PMID 4029131 DOI: 10.1111/J.1432-1033.1985.Tb09063.X |
0.363 |
|
| 1985 |
Strasburg GM, Leavis PC, Gergely J. Troponin-C-mediated calcium-sensitive changes in the conformation of troponin I detected by pyrene excimer fluorescence. The Journal of Biological Chemistry. 260: 366-70. PMID 3965454 |
0.359 |
|
| 1984 |
Dalgarno DC, Klevit RE, Levine BA, Scott GM, Williams RJ, Gergely J, Grabarek Z, Leavis PC, Grand RJ, Drabikowski W. The nature of the trifluoperazine binding sites on calmodulin and troponin-C. Biochimica Et Biophysica Acta. 791: 164-72. PMID 6509062 DOI: 10.1016/0167-4838(84)90006-2 |
0.398 |
|
| 1984 |
Mocz G, Szilagyi L, Chen Lu R, Fabian F, Balint M, Gergely J. Effect of nucleotides, divalent cations and temperature on the tryptic susceptibility of myosin subfragment 1. European Journal of Biochemistry. 145: 221-9. PMID 6389129 DOI: 10.1111/J.1432-1033.1984.Tb08542.X |
0.337 |
|
| 1984 |
Mabuchi K, Pinter K, Mabuchi Y, Sreter F, Gergely J. Characterization of rabbit masseter muscle fibers. Muscle & Nerve. 7: 431-8. PMID 6242312 DOI: 10.1002/Mus.880070603 |
0.312 |
|
| 1983 |
Grabarek Z, Grabarek J, Leavis PC, Gergely J. Cooperative binding to the Ca2+-specific sites of troponin C in regulated actin and actomyosin. The Journal of Biological Chemistry. 258: 14098-102. PMID 6643469 |
0.331 |
|
| 1982 |
Wang CL, Aquaron RR, Leavis PC, Gergely J. Metal-binding properties of calmodulin. European Journal of Biochemistry. 124: 7-12. PMID 7084230 DOI: 10.1111/J.1432-1033.1982.Tb05900.X |
0.366 |
|
| 1981 |
Wang CL, Leavis PC, Horrocks WD, Gergely J. Binding of lanthanide ions to troponin C. Biochemistry. 20: 2439-44. PMID 7236613 DOI: 10.1021/Bi00512A012 |
0.37 |
|
| 1981 |
Grabarek Z, Drabikowski W, Leavis PC, Rosenfeld SS, Gergely J. Proteolytic fragments of troponin C. Interactions with the other troponin subunits and biological activity. The Journal of Biological Chemistry. 256: 13121-7. PMID 6458609 |
0.344 |
|
| 1980 |
Evans JS, Levine BA, Leavis PC, Gergely J, Grabarek Z, Drabikowski W. Proton magnetic resonance studies on proteolytic fragments of troponin-C. Structural homology with the native molecule. Biochimica Et Biophysica Acta. 623: 10-20. PMID 7378465 DOI: 10.1016/0005-2795(80)90003-3 |
0.39 |
|
| 1980 |
Leavis PC, Nagy B, Lehrer SS, Bialkowska H, Gergely J. Terbium binding to troponin C: binding stoichiometry and structural changes induced in the protein. Archives of Biochemistry and Biophysics. 200: 17-21. PMID 7362251 DOI: 10.1016/0003-9861(80)90324-0 |
0.417 |
|
| 1980 |
Carew EB, Leavis PC, Stanley HE, Gergely J. A laser Raman spectroscopic study of Ca2+ binding to troponin C. Biophysical Journal. 30: 351-8. PMID 7260280 DOI: 10.1016/S0006-3495(80)85099-5 |
0.39 |
|
| 1980 |
Gergely J. Ca2+ control of actin-myosin interaction. Basic Research in Cardiology. 75: 18-25. PMID 6992765 |
0.314 |
|
| 1980 |
Thomas DD, Ishiwata S, Seidel JC, Gergely J. Submillisecond rotational dynamics of spin-labeled myosin heads in myofibrils Biophysical Journal. 32: 873-889. PMID 6266538 DOI: 10.1016/S0006-3495(80)85023-5 |
0.497 |
|
| 1979 |
Thomas DD, Seidel JC, Gergely J. Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range Journal of Molecular Biology. 132: 257-273. PMID 230351 DOI: 10.1016/0022-2836(79)90259-6 |
0.47 |
|
| 1978 |
Nagy B, Potter JD, Gergely J. Calcium-induced conformational changes in a cyanogen bromide fragment of troponin C that contains one of the binding sites Journal of Biological Chemistry. 253: 5971-5974. PMID 681332 |
0.467 |
|
| 1978 |
Bálint M, Wolf I, Tarcsafalvi A, Gergely J, Sréter FA. Location of SH-1 and SH-2 in the heavy chain segment of heavy meromyosin. Archives of Biochemistry and Biophysics. 190: 793-9. PMID 152606 DOI: 10.1016/0003-9861(78)90339-9 |
0.341 |
|
| 1978 |
Rubinstein N, Mabuchi K, Pepe F, Salmons S, Gergely J, Sreter F. Use of type-specific antimyosins to demonstrate the transformation of individual fibers in chronically stimulated rabbit fast muscles. The Journal of Cell Biology. 79: 252-61. PMID 151690 DOI: 10.1083/Jcb.79.1.252 |
0.342 |
|
| 1977 |
Gergely J. Molecular aspects of muscle contraction and regulation. Basic Research in Cardiology. 72: 109-17. PMID 860989 |
0.335 |
|
| 1976 |
Gergely J. Excitation-contraction coupling--cardiac muscle events in the myofilament. Federation Proceedings. 35: 1283-7. PMID 770201 |
0.397 |
|
| 1975 |
Potter JD, Gergely J. The regulatory system of the actin-myosin interaction Recent Advances in Studies On Cardiac Structure and Metabolism. 5: 235-244. PMID 1103243 |
0.535 |
|
| 1975 |
Sréter FA, Bálint M, Gergely J. Structural and functional changes of myosin during development: comparison with adult fast, slow and cardiac myosin. Developmental Biology. 46: 317-25. PMID 241672 DOI: 10.1016/0012-1606(75)90108-6 |
0.381 |
|
| 1975 |
Thomas DD, Seidel JC, Gergely J, Hyde JS. The quantitative measurement of rotational motion of the subfragment-1 region of myosin by saturation transfer epr spectroscopy. Journal of Supramolecular Structure. 3: 376-90. PMID 172739 DOI: 10.1002/Jss.400030410 |
0.498 |
|
| 1975 |
Thomas DD, Seidel JC, Hyde JS, Gergely J. Motion of subfragment-1 in myosin and its supramolecular complexes: saturation transfer electron paramagnetic resonance. Proceedings of the National Academy of Sciences of the United States of America. 72: 1729-33. PMID 168572 DOI: 10.1073/Pnas.72.5.1729 |
0.511 |
|
| 1975 |
Potter JD, Gergely J. The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase Journal of Biological Chemistry. 250: 4628-4633. PMID 124731 |
0.503 |
|
| 1974 |
Potter JD, Gergely J. Troponin, tropomyosin, and actin interactions in the Ca2+ regulation of muscle contraction Biochemistry. 13: 2697-2703. PMID 4847540 DOI: 10.1021/Bi00710A007 |
0.562 |
|
| 1974 |
Sréter FA, Gergely J. The effect of cross reinnervation on the synthesis of myosin light chains. Biochemical and Biophysical Research Communications. 56: 84-9. PMID 4823445 DOI: 10.1016/S0006-291X(74)80318-9 |
0.364 |
|
| 1974 |
Gergely J. Muscle contraction, conformational changes and energy transduction. Annals of the New York Academy of Sciences. 227: 587-93. PMID 4275126 DOI: 10.1111/J.1749-6632.1974.Tb14421.X |
0.344 |
|
| 1973 |
Streter FA, Gergely J, Salmons S, Romanul F. Synthesis by fast muscle of myosin light chains characteristic of slow muscle in response to long-term stimulation. Nature: New Biology. 241: 17-9. PMID 4266906 DOI: 10.1038/Newbio241017A0 |
0.393 |
|
| 1973 |
Greaser ML, Yamaguchi M, Brekke C, Potter J, Gergely J. Troponin Subunits and Their Interactions Cold Spring Harbor Symposia On Quantitative Biology. 37: 235-244. DOI: 10.1101/SQB.1973.037.01.033 |
0.39 |
|
| 1972 |
Sreter FA, Sarkar S, Gergely J. Myosin light chains of slow twitch (red) muscle. Nature: New Biology. 239: 124-5. PMID 4507520 DOI: 10.1038/Newbio239124A0 |
0.354 |
|
| 1972 |
Greaser ML, Gergely J, Han MH, Benson ES. Lack of identity of tropocalcin with troponin components. Biochemical and Biophysical Research Communications. 48: 358-61. PMID 4261367 DOI: 10.1016/S0006-291X(72)80058-5 |
0.428 |
|
| 1971 |
Seidel JC, Gergely J. The conformation of myosin during the steady state of ATP hydrolysis: studies with myosin spin labeled at the S 1 thiol groups. Biochemical and Biophysical Research Communications. 44: 826-30. PMID 4331039 DOI: 10.1016/0006-291X(71)90785-6 |
0.339 |
|
| 1971 |
Sarkar S, Sreter FA, Gergely J. Light chains of myosins from white, red, and cardiac muscles. Proceedings of the National Academy of Sciences of the United States of America. 68: 946-50. PMID 4252540 DOI: 10.1073/Pnas.68.5.946 |
0.317 |
|
| 1970 |
Sreter F, Ikemoto N, Gergely J. The effect of lyophilization and dithiothreitol on vesicles of skeletal and cardiac muscle sarcoplasmic reticulum. Biochimica Et Biophysica Acta. 203: 354-7. PMID 4245537 DOI: 10.1016/0005-2736(70)90154-9 |
0.342 |
|
| 1968 |
Ikemoto N, Sreter F, Nakamura A, Gergely J. Tryptic digestion and localization of calcium uptake and ATPase activity in fragments of sarcoplasmic reticulum Journal of Ultrastructure Research. 23: 216-232. DOI: 10.1016/S0022-5320(68)80002-4 |
0.385 |
|
| 1967 |
Sréter FA, Gergely J. Comparative studies of the MG activated ATPase activity and Ca uptake of fractions of white and red muscle homogenates. Biochemical and Biophysical Research Communications. 16: 438-43. PMID 4224523 DOI: 10.1016/0006-291X(64)90372-9 |
0.389 |
|
| 1964 |
Seidel J, Sreter F, Thompson M, Gergely J. Comparative studies of myofibrils, myosin, and actomyosin from red and white rabbit skeletal muscle Biochemical and Biophysical Research Communications. 17: 662-667. DOI: 10.1016/0006-291X(64)90411-5 |
0.369 |
|
| 1963 |
Seidel JC, Gergely J. Contraction of glycerinated muscle fibers and the role of calcium Biochemical and Biophysical Research Communications. 13: 343-347. DOI: 10.1016/0006-291X(63)90345-0 |
0.328 |
|
| 1961 |
Drabikowski W, Kuehl W, Gergely J. Inhibition of actin polymerization by mercurials without removal of bound nucleotide Biochemical and Biophysical Research Communications. 5: 389-393. DOI: 10.1016/0006-291X(61)90046-8 |
0.307 |
|
| 1959 |
KALDOR G, GERGELY J, BRIGGS FN. Participation of a dialyzable cofactor in the relaxing factor system of muscle. III. Substitution of pyrophosphate for the cofactor. Biochimica Et Biophysica Acta. 34: 224-7. PMID 14404101 DOI: 10.1016/0006-3002(59)90251-3 |
0.377 |
|
| 1959 |
GERGELY J, KALDOR G, BRIGGS FN. Participation of a dialyzable cofactor in the relaxing factor system of muscle. II. Studies with myofibrillar ATP-ase. Biochimica Et Biophysica Acta. 34: 218-24. PMID 13827473 DOI: 10.1016/0006-3002(59)90250-1 |
0.309 |
|
| 1959 |
BRIGGS FN, KALDOR G, GERGELY J. Participation of a dialyzable cofactor in the relaxing factor system of muscle. I. Studies with single glycerinated fibres. Biochimica Et Biophysica Acta. 34: 211-8. PMID 13804409 DOI: 10.1016/0006-3002(59)90249-5 |
0.36 |
|
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