Year |
Citation |
Score |
2014 |
Morales MA, Gergely JR, McMinis J, McMahon JM, Kim J, Ceperley DM. Quantum Monte Carlo Benchmark of Exchange-Correlation Functionals for Bulk Water. Journal of Chemical Theory and Computation. 10: 2355-62. PMID 26580755 DOI: 10.1021/Ct500129P |
0.196 |
|
2011 |
Gergely J, Seidel JC. Conformational Changes and Molecular Dynamics of Myosin Comprehensive Physiology. 257-274. DOI: 10.1002/Cphy.Cp100109 |
0.438 |
|
2010 |
Gergely J. Obituary S.V. Perry. Journal of Muscle Research and Cell Motility. 31: 7-8. PMID 20512525 DOI: 10.1007/S10974-010-9210-0 |
0.312 |
|
2010 |
Gergely J. Muscle structure. Science (New York, N.Y.). 216: 1310-1. PMID 17750612 DOI: 10.1126/science.216.4552.1310-a |
0.332 |
|
2008 |
ISSEKUTZ B, GERGELY J, HETENYI G. Central and peripheral mechanism in the increase of metabolic rate; mode of action of thyroxine. Nature. 163: 363. PMID 18208192 DOI: 10.1038/163363b0 |
0.167 |
|
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 |
0.416 |
|
2008 |
GERGELY J. Factors influencing the renal threshold. Nature. 163: 449. PMID 18124929 DOI: 10.1038/163449a0 |
0.173 |
|
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 |
0.421 |
|
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 |
0.417 |
|
2004 |
CSAPO A, GERGELY J. Energetics of uterine muscle contraction. Nature. 166: 1078-9. PMID 14796702 DOI: 10.1038/1661078a0 |
0.344 |
|
2002 |
VARGA L, GERGELY J. Double refraction of flow studies on hyaluronic acid prepared from the vitreous body. Biochimica Et Biophysica Acta. 23: 1-6. PMID 13412669 DOI: 10.1016/0006-3002(57)90276-7 |
0.329 |
|
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 |
0.491 |
|
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 |
0.521 |
|
2001 |
Koncz G, Tóth GK, Bökönyi G, Kéri G, Pecht I, Medgyesi D, Gergely J, Sármay G. Co-clustering of Fcgamma and B cell receptors induces dephosphorylation of the Grb2-associated binder 1 docking protein. European Journal of Biochemistry. 268: 3898-906. PMID 11453982 DOI: 10.1046/J.1432-1327.2001.02295.X |
0.291 |
|
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 |
0.499 |
|
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 |
0.413 |
|
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 |
0.458 |
|
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 |
0.496 |
|
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 |
0.507 |
|
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 |
0.51 |
|
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 |
0.408 |
|
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 |
0.422 |
|
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 |
0.5 |
|
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 |
0.406 |
|
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 |
0.48 |
|
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 |
0.509 |
|
1996 |
SAMAHA FJ, GERGELY J. CA++ UPTAKE AND ATPASE OF HUMAN SARCOPLASMIC RETICULUM. The Journal of Clinical Investigation. 44: 1425-31. PMID 14322047 DOI: 10.1172/JCI105248 |
0.318 |
|
1996 |
SAMAHA FJ, GERGELY J. NA - AND K-STIMULATED ATPASE IN HUMAN STRIATED MUSCLE. Archives of Biochemistry and Biophysics. 109: 76-9. PMID 14281957 DOI: 10.1016/0003-9861(65)90289-4 |
0.387 |
|
1996 |
Rozsnyay Z, Sarmay G, Zoller M, Gergely J. Membrane-bound ezrin is involved in B-cell receptor-mediated signaling: potential role of an ITAM-like ezrin motif. Immunology Letters. 54: 163-9. PMID 9052872 |
0.237 |
|
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 |
0.436 |
|
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 |
0.483 |
|
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 |
0.439 |
|
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 |
0.506 |
|
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 |
0.434 |
|
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 |
0.48 |
|
1991 |
Gusev NB, Grabarek Z, Gergely J. Stabilization by a disulfide bond of the N-terminal domain of a mutant troponin C (TnC48/82). The Journal of Biological Chemistry. 266: 16622-6. PMID 1885591 |
0.328 |
|
1991 |
Kobayashi T, Tao T, Grabarek Z, Gergely J, Collins JH. Cross-linking of residue 57 in the regulatory domain of a mutant rabbit skeletal muscle troponin C to the inhibitory region of troponin I. The Journal of Biological Chemistry. 266: 13746-51. PMID 1856208 |
0.379 |
|
1991 |
Füchtbauer EM, Rowlerson AM, Götz K, Friedrich G, Mabuchi K, Gergely J, Jockusch H. Direct correlation of parvalbumin levels with myosin isoforms and succinate dehydrogenase activity on frozen sections of rodent muscle. The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society. 39: 355-61. PMID 1825216 |
0.349 |
|
1990 |
Gergely J. A hard act to follow Biophysical Journal. 58: 1349. PMID 19431780 DOI: 10.1016/S0006-3495(90)82480-2 |
0.308 |
|
1990 |
Grabarek Z, Gergely J. Zero-length crosslinking procedure with the use of active esters. Analytical Biochemistry. 185: 131-5. PMID 2344038 DOI: 10.1016/0003-2697(90)90267-D |
0.368 |
|
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 |
0.395 |
|
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 |
0.515 |
|
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 |
0.451 |
|
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 |
0.491 |
|
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 |
0.478 |
|
1989 |
Grabarek Z, Gergely J. Information transfer in the regulation of striated muscle contraction. Biomedica Biochimica Acta. 48: S297-305. PMID 2547358 |
0.392 |
|
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 |
0.45 |
|
1988 |
Sweeney HL, Kushmerick MJ, Mabuchi K, Sréter FA, Gergely J. Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers. The Journal of Biological Chemistry. 263: 9034-9. PMID 3379059 |
0.281 |
|
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 |
0.395 |
|
1987 |
Wang CL, Zhan Q, Tao T, Gergely J. pH-dependent structural transition in rabbit skeletal troponin C. The Journal of Biological Chemistry. 262: 9636-40. PMID 3597429 |
0.285 |
|
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 |
0.444 |
|
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 |
0.415 |
|
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 |
0.419 |
|
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 |
0.414 |
|
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 |
0.448 |
|
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 |
0.416 |
|
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 |
0.476 |
|
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 |
0.435 |
|
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 |
0.44 |
|
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 |
0.437 |
|
1985 |
Sweeney HL, Kushmerick MJ, Mabuchi K, Gergely J, Sreter F. DIFFERENTIAL MYOSIN ISOZYME DISTRIBUTIONS AND SHORTENING VELOCITIES OF RABBIT SKINED SKELETAL MUSCLE FIBERS Medicine & Science in Sports & Exercise. 17: 244. DOI: 10.1249/00005768-198504000-00279 |
0.326 |
|
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 |
0.468 |
|
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 |
0.421 |
|
1984 |
Leavis PC, Gergely J. Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction. Crc Critical Reviews in Biochemistry. 16: 235-305. PMID 6383715 |
0.366 |
|
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 |
0.404 |
|
1984 |
Takács L, Uher F, Oláh I, Gergely J, Törö I. Characterization of high dose protein induced rat rosette forming cells. Developmental and Comparative Immunology. 7: 575-80. PMID 6139303 DOI: 10.1016/0145-305X(83)90043-5 |
0.214 |
|
1984 |
Correa AC, Gergely J, Blanchard AJ. 4434364 Method and apparatus for underwater detection of hydrocarbons Marine Pollution Bulletin. 15: ii-iii. DOI: 10.1016/0025-326X(84)90213-3 |
0.175 |
|
1983 |
Grabarek Z, Gergely J. Appendix. On the applicability of Hill type analysis to fluorescence data. The Journal of Biological Chemistry. 258: 14103-5. PMID 6643470 |
0.195 |
|
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 |
0.416 |
|
1983 |
Wang CL, Leavis PC, Gergely J. Kinetics of Ca2+ release shows interactions between the two classes of sites of troponin-C. The Journal of Biological Chemistry. 258: 9175-7. PMID 6409902 |
0.38 |
|
1983 |
Carew EB, Stanley HE, Seidel JC, Gergely J. Studies of myosin and its proteolytic fragments by laser Raman spectroscopy. Biophysical Journal. 44: 219-24. PMID 6360227 DOI: 10.1016/S0006-3495(83)84294-5 |
0.381 |
|
1983 |
Nyitray L, Mocz G, Szilagyi L, Balint M, Lu RC, Wong A, Gergely J. The proteolytic substructure of light meromyosin. Localization of a region responsible for the low ionic strength insolubility of myosin. The Journal of Biological Chemistry. 258: 13213-20. PMID 6355107 |
0.312 |
|
1983 |
Correa AC, Gergely J, Blanchard AJ. 7394573 Method and apparatus for underwater detection of hydrocarbons Deep Sea Research Part B. Oceanographic Literature Review. 30: 948. DOI: 10.1016/0198-0254(83)96686-4 |
0.175 |
|
1982 |
Gergely J, Erdei A, Sándor M, Sármay G, Uher F. The Fc receptor model of membrane cytoplasmic signalling. Molecular Immunology. 19: 1223-8. PMID 7177113 DOI: 10.1016/0161-5890(82)90287-5 |
0.192 |
|
1982 |
Wang CL, Tao T, Gergely J. The distance between the high affinity sites of troponin-C measured by interlanthanide ion energy transfer. The Journal of Biological Chemistry. 257: 8372-5. PMID 7085671 |
0.318 |
|
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 |
0.446 |
|
1982 |
Gergely J. Structural and contractile proteins: the contractile apparatus and the cytoskeleton. Introduction. Methods in Enzymology. 85: 1-6. PMID 6214688 |
0.272 |
|
1982 |
Gergely J. Cell and Membrane Physiology Annual Review of Physiology. 44: 295-295. DOI: 10.1146/annurev.ph.44.030182.001455 |
0.186 |
|
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 |
0.446 |
|
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 |
0.424 |
|
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 |
0.459 |
|
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 |
0.484 |
|
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 |
0.46 |
|
1980 |
Gergely J. Ca2+ control of actin-myosin interaction. Basic Research in Cardiology. 75: 18-25. PMID 6992765 |
0.403 |
|
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 |
0.541 |
|
1979 |
Nagy B, Gergely J. Extent and localization of conformational changes in troponin C caused by calcium binding. Spectral studies in the presence and absence of 6 M urea Journal of Biological Chemistry. 254: 12732-12737. PMID 500734 |
0.315 |
|
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 |
0.519 |
|
1979 |
Szilagyi L, Balint M, Sreter FA, Gergely J. Photoaffinity labelling with an ATP analog of the N-terminal peptide of myosin. Biochemical and Biophysical Research Communications. 87: 936-45. PMID 156543 |
0.269 |
|
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 |
0.625 |
|
1978 |
Leavis PC, Rosenfeld SS, Gergely J, Grabarek Z, Drabikowski W. Proteolytic fragments of troponin C. Localization of high and low affinity Ca2+ binding sites and interactions with troponin I and troponin T. The Journal of Biological Chemistry. 253: 5452-9. PMID 670208 |
0.372 |
|
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 |
0.42 |
|
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 |
0.428 |
|
1978 |
Gergely J. Immunochemistry of proteins, volumes 1 and 2. Edited by M. Z. Atassi, 439 pp (Vol 1), 416 pp (Vol 2), illus, Plenum Publishing Corp, New York, 1977. $44.50 (per vol) Muscle and Nerve. 1: 255-256. DOI: 10.1002/mus.880010314 |
0.203 |
|
1977 |
Drabikowski W, Lehrer S, Nagy B, Gergely J. Loss of Cu2+-binding to actin upon removal of the C-terminal phenylalanine by carboxypeptidase A Archives of Biochemistry and Biophysics. 181: 359-361. PMID 879806 DOI: 10.1016/0003-9861(77)90515-X |
0.299 |
|
1977 |
Gergely J. Molecular aspects of muscle contraction and regulation. Basic Research in Cardiology. 72: 109-17. PMID 860989 |
0.427 |
|
1977 |
GERGELY J. Myofibrillar proteins—Their role in muscle contraction and its regulation Journal of Molecular and Cellular Cardiology. 9: 25-25. DOI: 10.1016/S0022-2828(77)80173-9 |
0.342 |
|
1976 |
Gergely J. Excitation-contraction coupling--cardiac muscle events in the myofilament. Federation Proceedings. 35: 1283-7. PMID 770201 |
0.468 |
|
1976 |
Venyaminov SY, Rajnavölgyi E, Medgyesi GA, Gergely J, Závodszky P. The role of interchain disulphide bridges in the conformational stability of human immunoglobulin G1 subclass. Hydrogen-deuterium exchange studies. European Journal of Biochemistry. 67: 81-6. PMID 9279 DOI: 10.1111/j.1432-1033.1976.tb10635.x |
0.269 |
|
1976 |
Ahmed S, Gergely J, Stirbl R, Barone F. Lidar measurements of air pollution using a simultaneous dual frequency dye laser Optics Communications. 18: 189-190. DOI: 10.1016/0030-4018(76)90677-5 |
0.183 |
|
1975 |
Gergely J. Proceedings: The regulatory role of Ca2-induced conformational changes in troponin and myosin. Hoppe-Seyler's Zeitschrift Fur Physiologische Chemie. 356: 380. PMID 1150148 |
0.365 |
|
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 |
0.668 |
|
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 |
0.458 |
|
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 |
0.542 |
|
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 |
0.555 |
|
1975 |
Bálint M, Sréter FA, Wolf I, Nagy B, Gergely J. The substructure of heavy meromyosin. The effect of Ca2+ and Mg2+ on the tryptic fragmentation of heavy meromyosin. The Journal of Biological Chemistry. 250: 6168-77. PMID 125283 |
0.345 |
|
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 |
0.647 |
|
1975 |
Bálint M, Sréter FA, Gergely J. Fragmentation of myosin by papain--studies on myosin from adult fast and slow skeletal and cardiac, and embryonic muscle. Archives of Biochemistry and Biophysics. 168: 557-66. PMID 124554 |
0.354 |
|
1975 |
Sréter FA, Luff AR, Gergely J. Effect of cross-reinnervation on physiological parameters and on properties of myosin and sarcoplasmic reticulum of fast and slow muscles of the rabbit. The Journal of General Physiology. 66: 811-21. PMID 461 |
0.389 |
|
1975 |
Ahmed SA, Gergely JS, Infante D. 1.4 Energy Transfer Processes in Organic Dye Laser Mixtures Ieee Journal of Quantum Electronics. 11: 824-825. DOI: 10.1109/JQE.1975.1068816 |
0.199 |
|
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 |
0.679 |
|
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 |
0.445 |
|
1974 |
Gergely J, Greaser M, Nagy B, Potter J. Troponin: the regulatofy protein complex or muscle. Recent Advances in Studies On Cardiac Structure and Metabolism. 4: 281-90. PMID 4283212 |
0.339 |
|
1974 |
Gergely J. Some aspects of the role of the sarcoplasmic reticulum and the tropomyosin-troponin system in the control of muscle contraction by calcium ions. Circulation Research. 35: 74-82. PMID 4278275 |
0.328 |
|
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 |
0.431 |
|
1974 |
Strzelecka-Golaszewska H, Nagy B, Gergely J. Changes in conformation and nucleotide binding of Ca, Mn, or MgG-actin upon removal of the bound divalent cation. Studies of ultraviolet difference spectra and optical rotation. Archives of Biochemistry and Biophysics. 161: 559-69. PMID 4209137 |
0.376 |
|
1974 |
Ahmed SA, Gergely JS, Infante D. Energy transfer organic dye mixture lasers The Journal of Chemical Physics. 61: 1584-1585. DOI: 10.1063/1.1682111 |
0.198 |
|
1974 |
Gergely J. Book ReviewThe Structure and Function of Muscle. New England Journal of Medicine. 290: 580-580. DOI: 10.1056/NEJM197403072901035 |
0.318 |
|
1973 |
Seidel JC, Gergely J. The use of spin labels in the study of muscle proteins. Annals of the New York Academy of Sciences. 222: 574-87. PMID 4361871 DOI: 10.1111/j.1749-6632.1973.tb15288.x |
0.314 |
|
1973 |
Seidel JC, Gergely J. Electron spin resonance of myosin spin labeled at the S1 thiol groups during hydrolysis of adenosine triphosphate. Archives of Biochemistry and Biophysics. 158: 853-63. PMID 4361111 DOI: 10.1016/0003-9861(73)90581-X |
0.241 |
|
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 |
0.468 |
|
1973 |
Greaser ML, Gergely J. Purification and properties of the components from troponin. The Journal of Biological Chemistry. 248: 2125-33. PMID 4266138 |
0.204 |
|
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 |
0.577 |
|
1973 |
Seidel JC, Gergely J. Investigation of Conformational Changes in Spin-Labeled Myosin: Implications for the Molecular Mechanism of Muscle Contraction Cold Spring Harbor Symposia On Quantitative Biology. 37: 187-193. DOI: 10.1101/SQB.1973.037.01.028 |
0.354 |
|
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 |
0.438 |
|
1972 |
Burley RW, Seidel JC, Gergely J. The effect of divalent metal binding on the electron spin resonance spectra of spin-labeled actin. Evidence for spin-spin interactions involving manganese. II. Archives of Biochemistry and Biophysics. 150: 792-6. PMID 4339740 DOI: 10.1016/0003-9861(72)90100-2 |
0.25 |
|
1972 |
Lehrer SS, Nagy B, Gergely J. The binding of Cu 2+ to actin without loss of polymerizability: the involvement of the rapidly reacting -SH group. Archives of Biochemistry and Biophysics. 150: 164-74. PMID 4337535 |
0.274 |
|
1972 |
Sreter FA, Bauman ML, Gergely J, Luca N. Changes in muscle chemistry associated with stiffness and pain Neurology. 22: 1172-1175. PMID 4263830 DOI: 10.1212/Wnl.22.11.1172 |
0.386 |
|
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 |
0.493 |
|
1972 |
Ikemoto N, Sreter FA, Gergely J. Structural features of the surface of the vesicles of FSR--lack of functional role in Ca 2+ uptake and ATPase activity. Archives of Biochemistry and Biophysics. 147: 571-82. PMID 4257599 DOI: 10.1016/0003-9861(71)90415-2 |
0.302 |
|
1972 |
Sreter F, Holtzer S, Gergely J, Holtzer H. Some properties of embryonic myosin. The Journal of Cell Biology. 55: 586-94. PMID 4120861 |
0.361 |
|
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 |
0.42 |
|
1971 |
Burley RW, Seidel JC, Gergely J. The stoichiometry of the reaction of the spin labeling of F-actin and the effect of orientation of spin-labeled F-actin filaments. Archives of Biochemistry and Biophysics. 146: 597-602. PMID 4329854 DOI: 10.1016/0003-9861(71)90167-6 |
0.274 |
|
1971 |
Seidel JC, Chopek M, Gergely J. The tryptic digestion of spin-labelled heavy meromyosin. Archives of Biochemistry and Biophysics. 142: 223-30. PMID 4322805 DOI: 10.1016/0003-9861(71)90278-5 |
0.222 |
|
1971 |
Ikemoto N, Bhatnagar GM, Gergely J. Fractionation of solubilized sarcoplasmic reticulum? Biochemical and Biophysical Research Communications. 44: 1510-1517. PMID 4258590 DOI: 10.1016/S0006-291X(71)80257-7 |
0.388 |
|
1971 |
Greaser ML, Gergely J. Reconstitution of troponin activity from three protein components. The Journal of Biological Chemistry. 246: 4226-33. PMID 4253596 |
0.239 |
|
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 |
0.404 |
|
1971 |
Nakamura A, Sreter F, Gergely J. Comparative studies of light meromyosin paracrystals derived from red, white, and cardiac muscle myosins. The Journal of Cell Biology. 49: 883-98. PMID 4103957 |
0.327 |
|
1970 |
Seidel JC, Chopek M, Gergely J. Effect of nucleotides and pyrophosphate on spin labels bound to S1 thiol groups of myosin. Biochemistry. 9: 3265-72. PMID 4321371 |
0.267 |
|
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 |
0.431 |
|
1969 |
Nauss KM, Kitagawa S, Gergely J. Pyrophosphate binding to and adenosine triphosphatase activity of myosin and its proteolytic fragments. Implications for the substructure of myosin. The Journal of Biological Chemistry. 244: 755-65. PMID 4305882 |
0.361 |
|
1969 |
Kuehl WM, Gergely J. The kinetics of exchange of adenosine triphosphate and calcium with G-actin. The Journal of Biological Chemistry. 244: 4720-9. PMID 4241280 |
0.28 |
|
1969 |
Samaha FJ, Gergely J. Biochemistry of normal and myotonic dystrophic human myosin. Archives of Neurology. 21: 200-7. PMID 4240043 |
0.244 |
|
1969 |
Chimoskey JE, Gergely J. Effect of ions on sarcoplasmic reticulum fragments. Archives of Biochemistry and Biophysics. 128: 601-5. PMID 4236455 DOI: 10.1016/0003-9861(68)90069-6 |
0.221 |
|
1969 |
Samaha FJ, Gergely J. Biochemical abnormalities of the sarcoplasmic reticulum in muscular dystrophy. The New England Journal of Medicine. 280: 184-8. PMID 4235816 DOI: 10.1056/NEJM196901232800403 |
0.274 |
|
1968 |
Pragay DA, Gergely J. Effect of tropomyosin on the polymerization of ATP--G-actin and ADP--G-actin. Archives of Biochemistry and Biophysics. 125: 727-33. PMID 5671039 |
0.281 |
|
1968 |
Kitagawa S, Drabikowski W, Gergely J. Exchange and release of the bound nucleotide of F-actin. Archives of Biochemistry and Biophysics. 125: 706-14. PMID 4968583 |
0.278 |
|
1968 |
Samaha FJ, Gergely J. Properties of human myosin from normal and myotonic dystrophic muscle. Transactions of the American Neurological Association. 93: 177-80. PMID 4237224 |
0.338 |
|
1968 |
Ikemoto N, Kitagawa S, Nakamura A, Gergely J. Electron microscopic investigations of actomyosin as a function of ionic strength. The Journal of Cell Biology. 39: 620-9. PMID 4177379 DOI: 10.1083/Jcb.39.3.620 |
0.383 |
|
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 |
0.456 |
|
1967 |
West JJ, Nagy B, Gergely J. The effect of EDTA on spectral properties of ATP-, ADP-, and ITP-G-actin. Biochemical and Biophysical Research Communications. 29: 611-6. PMID 16496544 DOI: 10.1016/0006-291X(67)90530-X |
0.374 |
|
1967 |
Regoeczi E, Gergely J, McFarlane AS. In vivo effects of Agkistrodon rhodostoma venom: studies with fibrinogen-131I. The Journal of Clinical Investigation. 45: 1202-12. PMID 5967698 DOI: 10.1172/JCI105426 |
0.22 |
|
1967 |
West JJ, Nagy B, Gergely J. Free adenosine diphosphate as an intermediary in the phosphorylation by creatine phosphate of adenosine diphosphate bound to actin. The Journal of Biological Chemistry. 242: 1140-5. PMID 4290314 |
0.296 |
|
1967 |
Samaha FJ, Gergely J. Studies on the Na+- and K+ -activated adenosine triphosphatase in human striated muscle. Archives of Biochemistry and Biophysics. 114: 481-7. PMID 4224949 DOI: 10.1016/0003-9861(66)90371-7 |
0.298 |
|
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 |
0.463 |
|
1967 |
Gergely J, Stanworth D, Jefferis R, Normansell D, Henney C, Pardoe G. Structural studies of immunoglobulins—I. The role of cysteine in papain hydrolysis Immunochemistry. 4: 101-111. DOI: 10.1016/0019-2791(67)90161-9 |
0.224 |
|
1966 |
Siekevitz P, Doermann AH, Gallant JA, McCarthy BJ, Morris DR, Nester E, Rutter WJ, Jukes TH, Green DE, Gergely J, Dameshek W, Baron S. IEG's: Some Evaluations. Science (New York, N.Y.). 154: 332-6. PMID 17751689 DOI: 10.1126/Science.154.3747.332 |
0.389 |
|
1966 |
Gergely J. Contractile proteins. Annual Review of Biochemistry. 35: 691-722. PMID 5329472 DOI: 10.1146/annurev.bi.35.070166.003355 |
0.237 |
|
1966 |
Sreter FA, Seidel JC, Gergely J. Studies on myosin from red and white skeletal muscles of the rabbit. I. Adenosine triphosphatase activity. The Journal of Biological Chemistry. 241: 5772-6. PMID 4224728 |
0.366 |
|
1964 |
MARTONOSII A, MOLINO CM, GERGELY J. THE BINDING OF DIVALENT CATIONS TO ACTIN. The Journal of Biological Chemistry. 239: 1057-64. PMID 14165908 |
0.341 |
|
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 |
0.452 |
|
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 |
0.419 |
|
1962 |
NODA H, MARUYAMA K, GERGELY J. End-to-end aggregation of myosin. Biochimica Et Biophysica Acta. 58: 598-601. PMID 14480167 DOI: 10.1016/0006-3002(62)90075-6 |
0.36 |
|
1962 |
MARUYAMA K, GERGELY J. Interaction of actomyosin with adenosine triphosphate at low ionic strength. I. Dis-sociation of actomyosin during the clear phase. The Journal of Biological Chemistry. 237: 1095-9. PMID 14470653 |
0.232 |
|
1962 |
MARUYAMA K, GERGELY J. Interaction of actomyosin with adenosine triphosphate at low ionic strength. II. Factors influencing clearing and superprecipitation: adenosine triphosphatase and birefringence of flow studies. The Journal of Biological Chemistry. 237: 1100-6. PMID 14470652 |
0.23 |
|
1962 |
Drabikowski W, Gergely J. The effect of deoxycholate on actin Biochimica Et Biophysica Acta. 63: 225-228. DOI: 10.1016/0006-3002(62)90363-3 |
0.298 |
|
1961 |
MARUYAMA K, GERGELY J. Removal of the bound calcium of G-actin by ethylenediaminetetraacetate (EDTA). Biochemical and Biophysical Research Communications. 6: 245-9. PMID 14470654 DOI: 10.1016/0006-291X(61)90371-0 |
0.376 |
|
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 |
0.398 |
|
1960 |
MARTONOSI A, GOUVEA MA, GERGELY J. Studies on actin. III. G-F transformation of actin and muscular contraction (experiments in vivo). The Journal of Biological Chemistry. 235: 1707-10. PMID 14421877 |
0.296 |
|
1960 |
GERGELY J, GOUVEA MA, MARTONOSI A. Studies on actin. II. Partially polymerized actin solutions. The Journal of Biological Chemistry. 235: 1704-6. PMID 13827472 |
0.273 |
|
1960 |
MARTONOSI A, GOUVEA MA, GERGELY J. Studies on actin. IV. Actin as a component of myosin-B. The Journal of Biological Chemistry. 235: 3169-73. PMID 13767576 |
0.303 |
|
1960 |
GERGELY J, MARUYAMA K. The binding of inorganic phosphate to myosin in the presence of adenosine triphosphate. The Journal of Biological Chemistry. 235: 3174-6. PMID 13704589 |
0.334 |
|
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 |
0.456 |
|
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 |
0.399 |
|
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 |
0.441 |
|
1959 |
Balazs EA, Bothner-By AA, Gergely J. Proton magnetic resonance studies on water in the presence of various macromolecular substances Journal of Molecular Biology. 1: 147-154. DOI: 10.1016/S0022-2836(59)80043-7 |
0.322 |
|
1959 |
Kaldor G, Gergely J. The effect of pyridoxal phosphate and its inhibition by carnosine on the ATPase activity and syneresis of myofibrils Archives of Biochemistry and Biophysics. 80: 393-399. DOI: 10.1016/0003-9861(59)90268-1 |
0.386 |
|
1956 |
GERGELY J. The interaction between actomyosin and adenosine triphosphate, light scattering studies. The Journal of Biological Chemistry. 220: 917-26. PMID 13331949 |
0.224 |
|
1955 |
GERGELY J, GOUVEA MA, KARIBIAN D. Fragmentation of myosin by chymotrypsin. The Journal of Biological Chemistry. 212: 165-77. PMID 13233219 |
0.326 |
|
1953 |
GERGELY J. Studies on myosin-adenosinetriphosphatase. The Journal of Biological Chemistry. 200: 543-50. PMID 13034812 |
0.348 |
|
1951 |
MORALES MF, LAKI K, GERGELY J, CECCHINI LP. Some further infrared absorption studies on the proteins of muscle. Journal of Cellular Physiology. 37: 477-85. PMID 14861269 DOI: 10.1002/jcp.1030370308 |
0.325 |
|
1951 |
GERGELY J, SPICER SS. On factors affecting the reversible superprecipitation of actomyosin. Biochimica Et Biophysica Acta. 6: 456-60. PMID 14820896 |
0.19 |
|
1951 |
SPICER S, GERGELY J. Studies on the combination of myosin with actin. The Journal of Biological Chemistry. 188: 179-84. PMID 14814127 |
0.33 |
|
1948 |
EVANS MG, GERGELY J. [Letters to Editor] Nature. 162: 770-771. DOI: 10.1038/162770b0 |
0.175 |
|
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