| Year |
Citation |
Score |
| 2004 |
Lawson JD, Pate E, Rayment I, Yount RG. Molecular dynamics analysis of structural factors influencing back door pi release in myosin. Biophysical Journal. 86: 3794-803. PMID 15189875 DOI: 10.1529/Biophysj.103.037390 |
0.313 |
|
| 2003 |
Naber N, Minehardt TJ, Rice S, Chen X, Grammer J, Matuska M, Vale RD, Kollman PA, Car R, Yount RG, Cooke R, Pate E. Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules. Science (New York, N.Y.). 300: 798-801. PMID 12730601 DOI: 10.1126/Science.1082374 |
0.33 |
|
| 2002 |
Chen X, Grammer J, Lawson JD, Cooke R, Pate E, Yount RG. A novel restricted photoaffinity spin-labeled non-nucleoside ATP analogue as a covalently attached reporter group of the active site of Myosin subfragment 1. Biochemistry. 41: 2609-20. PMID 11851408 DOI: 10.1021/Bi0118411 |
0.469 |
|
| 2000 |
Chen X, Grammer J, Cooke R, Pate E, Yount RG. Synthesis and characterization of novel spin-labeled photoaffinity nonnucleoside analogues of ATP as structural and EPR probes for myosin. Bioconjugate Chemistry. 11: 725-33. PMID 10995217 DOI: 10.1021/Bc000032B |
0.403 |
|
| 2000 |
Gulick AM, Bauer CB, Thoden JB, Pate E, Yount RG, Rayment I. X-ray structures of the Dictyostelium discoideum myosin motor domain with six non-nucleotide analogs. The Journal of Biological Chemistry. 275: 398-408. PMID 10617631 DOI: 10.1074/Jbc.275.1.398 |
0.405 |
|
| 1999 |
Wang D, Luo Y, Cooke R, Grammer J, Pate E, Yount RG. Synthesis of a spin-labeled photoaffinity ATP analogue, and its use to specifically photolabel myosin cross-bridges in skeletal muscle fibers. Journal of Muscle Research and Cell Motility. 20: 743-53. PMID 10730577 DOI: 10.1023/A:1005554924153 |
0.373 |
|
| 1998 |
Xiao M, Li H, Snyder GE, Cooke R, Yount RG, Selvin PR. Conformational changes between the active-site and regulatory light chain of myosin as determined by luminescence resonance energy transfer: the effect of nucleotides and actin. Proceedings of the National Academy of Sciences of the United States of America. 95: 15309-14. PMID 9860965 DOI: 10.1073/Pnas.95.26.15309 |
0.455 |
|
| 1998 |
Deng H, Wang J, Callender RH, Grammer JC, Yount RG. Raman difference spectroscopic studies of the myosin S1.MgADP.vanadate complex. Biochemistry. 37: 10972-9. PMID 9692990 DOI: 10.1021/Bi980556N |
0.351 |
|
| 1996 |
Grammer JC, Loo JA, Edmonds CG, Cremo CR, Yount RG. Chemistry and mechanism of vanadate-promoted photooxidative cleavage of myosin. Biochemistry. 35: 15582-92. PMID 8952512 DOI: 10.1021/Bi961901G |
0.394 |
|
| 1996 |
Rayment I, Smith C, Yount RG. The active site of myosin. Annual Review of Physiology. 58: 671-702. PMID 8815815 DOI: 10.1146/Annurev.Ph.58.030196.003323 |
0.39 |
|
| 1995 |
Luo Y, Wang D, Cremo CR, Pate E, Cooke R, Yount RG. Photoaffinity ADP analogs as covalently attached reporter groups of the active site of myosin subfragment 1. Biochemistry. 34: 1978-87. PMID 7849056 DOI: 10.1021/Bi00006A019 |
0.488 |
|
| 1995 |
Yount RG, Lawson D, Rayment I. Is myosin a "back door" enzyme? Biophysical Journal. 68: 44S-47S; discussion . PMID 7787099 |
0.383 |
|
| 1993 |
Grammer JC, Kuwayama H, Yount RG. Photoaffinity labeling of skeletal myosin with 2-azidoadenosine triphosphate. Biochemistry. 32: 5725-32. PMID 8504091 DOI: 10.1021/Bi00073A001 |
0.482 |
|
| 1993 |
Kerwin BA, Yount RG. Photolabeling evidence for calcium-induced conformational changes at the ATP binding site of scallop myosin. Proceedings of the National Academy of Sciences of the United States of America. 90: 35-9. PMID 8419940 DOI: 10.1073/Pnas.90.1.35 |
0.377 |
|
| 1993 |
Wang D, Pate E, Cooke R, Yount R. Synthesis of non-nucleotide ATP analogues and characterization of their chemomechanical interaction with muscle fibres Journal of Muscle Research and Cell Motility. 14: 484-497. PMID 8300844 DOI: 10.1007/Bf00297211 |
0.4 |
|
| 1992 |
Kerwin BA, Yount RG. Photoaffinity labeling of scallop myosin with 2-[(4-azido-2-nitrophenyl)amino]ethyl diphosphate: identification of an active site arginine analogous to tryptophan-130 in skeletal muscle myosin. Bioconjugate Chemistry. 3: 328-36. PMID 1390988 DOI: 10.1021/Bc00016A012 |
0.459 |
|
| 1992 |
Cole DG, Yount RG. Stability and photochemical properties of vanadate-trapped nucleotide complexes of gizzard myosin in the 6S and 10S conformations: identification of an active-site serine. Biochemistry. 31: 6186-92. PMID 1385724 DOI: 10.1021/Bi00142A003 |
0.629 |
|
| 1992 |
Yount RG, Cremo CR, Grammer JC, Kerwin BA. Photochemical mapping of the active site of myosin. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 336: 55-60; discussion 60. PMID 1351297 DOI: 10.1098/Rstb.1992.0044 |
0.46 |
|
| 1991 |
Pate E, Nakamaye KL, Franks-Skiba K, Yount RG, Cooke R. Mechanics of glycerinated muscle fibers using nonnucleoside triphosphate substrates. Biophysical Journal. 59: 598-605. PMID 2049521 DOI: 10.1016/S0006-3495(91)82275-5 |
0.37 |
|
| 1991 |
Cremo CR, Grammer JC, Yount RG. Vanadate-mediated photocleavage of myosin. Methods in Enzymology. 196: 442-9. PMID 2034134 DOI: 10.1016/0076-6879(91)96038-S |
0.461 |
|
| 1991 |
Garabedian TE, Yount RG. Direct photoaffinity labeling of gizzard myosin with vanadate-trapped adenosine diphosphate. Biochemistry. 30: 10126-32. PMID 1931944 DOI: 10.1021/Bi00106A008 |
0.447 |
|
| 1990 |
Cole DG, Yount RG. Photolabeling of the 6 and 10 S conformations of gizzard myosin with 3'(2')-O-(4-Benzoyl)benzoyl-ATP. Proline 324 is near the active site. The Journal of Biological Chemistry. 265: 22537-46. PMID 2266144 |
0.627 |
|
| 1990 |
Cremo CR, Neuron JM, Yount RG. Interaction of myosin subfragment 1 with fluorescent ribose-modified nucleotides. A comparison of vanadate trapping and SH1-SH2 cross-linking. Biochemistry. 29: 3309-19. PMID 2110475 DOI: 10.1021/Bi00465A023 |
0.446 |
|
| 1990 |
Garabedian TE, Yount RG. Direct photoaffinity labeling of gizzard myosin with [3H]uridine diphosphate places Glu185 of the heavy chain at the active site. The Journal of Biological Chemistry. 265: 22547-53. PMID 1979981 |
0.332 |
|
| 1989 |
Cremo CR, Grammer JC, Yount RG. Direct chemical evidence that serine 180 in the glycine-rich loop of myosin binds to ATP. The Journal of Biological Chemistry. 264: 6608-11. PMID 2523383 |
0.379 |
|
| 1989 |
Mahmood R, Elzinga M, Yount RG. Serine-324 of myosin's heavy chain is photoaffinity-labeled by 3'(2')-O-(4-benzoylbenzoyl)adenosine triphosphate. Biochemistry. 28: 3989-95. PMID 2502175 DOI: 10.1021/Bi00435A054 |
0.431 |
|
| 1988 |
Huston EE, Grammer JC, Yount RG. Flexibility of the myosin heavy chain: direct evidence that the region containing SH1 and SH2 can move 10 A under the influence of nucleotide binding. Biochemistry. 27: 8945-52. PMID 3233215 DOI: 10.1021/Bi00425A011 |
0.426 |
|
| 1988 |
Cremo CR, Grammer JC, Yount RG. UV-induced vanadate-dependent modification and cleavage of skeletal myosin subfragment 1 heavy chain. 2. Oxidation of serine in the 23-kDa NH2-terminal tryptic peptide. Biochemistry. 27: 8415-20. PMID 3149505 DOI: 10.1021/Bi00422A018 |
0.417 |
|
| 1988 |
Grammer JC, Cremo CR, Yount RG. UV-induced vanadate-dependent modification and cleavage of skeletal myosin subfragment 1 heavy chain. 1. Evidence for active site modification. Biochemistry. 27: 8408-15. PMID 2977286 DOI: 10.1021/Bi00422A017 |
0.444 |
|
| 1987 |
Cremo CR, Yount RG. 2'-Deoxy-3'-O-(4-benzoylbenzoyl)- and 3'(2')-O-(4-benzoylbenzoyl)-1,N6-ethenoadenosine 5'-diphosphate, fluorescent photoaffinity analogues of adenosine 5'-diphosphate. Synthesis, characterization, and interaction with myosin subfragment 1. Biochemistry. 26: 7524-34. PMID 3427092 DOI: 10.1021/Bi00397A048 |
0.439 |
|
| 1986 |
Okamoto Y, Sekine T, Grammer J, Yount RG. The essential light chains constitute part of the active site of smooth muscle myosin. Nature. 324: 78-80. PMID 3641060 DOI: 10.1038/324078A0 |
0.434 |
|
| 1986 |
Munson KB, Smerdon MJ, Yount RG. Cross-linking of myosin subfragment 1 and heavy meromyosin by use of vanadate and a bis(adenosine 5'-triphosphate) analogue. Biochemistry. 25: 7640-50. PMID 3542031 DOI: 10.1021/Bi00371A055 |
0.44 |
|
| 1985 |
Nakamaye KL, Wells JA, Bridenbaugh RL, Okamoto Y, Yount RG. 2-[(4-Azido-2-nitrophenyl)amino]ethyl triphosphate, a novel chromophoric and photoaffinity analogue of ATP. Synthesis, characterization, and interaction with myosin subfragment 1. Biochemistry. 24: 5226-35. PMID 4074691 DOI: 10.1021/Bi00340A041 |
0.621 |
|
| 1985 |
Okamoto Y, Yount RG. Identification of an active site peptide of skeletal myosin after photoaffinity labeling with N-(4-azido-2-nitrophenyl)-2-aminoethyl diphosphate. Proceedings of the National Academy of Sciences of the United States of America. 82: 1575-9. PMID 3157189 DOI: 10.1073/Pnas.82.6.1575 |
0.425 |
|
| 1984 |
Mahoney CW, Yount RG. Purification of micromolar quantities of nucleotide analogs by reverse-phase high-performance liquid chromatography using a volatile buffer at neutral pH. Analytical Biochemistry. 138: 246-51. PMID 6731846 DOI: 10.1016/0003-2697(84)90797-8 |
0.305 |
|
| 1984 |
Dalbey RE, Weiel J, Perkins WJ, Yount RG. Resolution of multiple fluorescence lifetimes in heterogeneous systems by phase-modulation fluorometry. Journal of Biochemical and Biophysical Methods. 9: 251-66. PMID 6547966 DOI: 10.1016/0165-022X(84)90030-7 |
0.539 |
|
| 1984 |
Mahmood R, Yount RG. Photochemical probes of the active site of myosin. Irradiation of trapped 3'-O-(4-benzoyl)benzoyladenosine 5'-triphosphate labels the 50-kilodalton heavy chain tryptic peptide. The Journal of Biological Chemistry. 259: 12956-9. PMID 6238030 |
0.401 |
|
| 1984 |
Perkins WJ, Wells JA, Yount RG. Characterization of the properties of ethenoadenosine nucleotides bound or trapped at the active site of myosin subfragment 1. Biochemistry. 23: 3994-4002. PMID 6237680 DOI: 10.1021/Bi00312A029 |
0.583 |
|
| 1984 |
Perkins WJ, Weiel J, Grammer J, Yount RG. Introduction of a donor-acceptor pair by a single protein modification. Förster energy transfer distance measurements from trapped 1,N6-ethenoadenosine diphosphate to chromophoric cross-linking reagents on the critical thiols of myosin subfragment. The Journal of Biological Chemistry. 259: 8786-93. PMID 6235217 |
0.362 |
|
| 1983 |
Dalbey RE, Wells JA, Yount RG. Trapping of transition metal-nucleotide complexes in myosin subfragment 1 by cross-linking thiols; divalent transition metal probes of the active site. Biochemistry. 22: 490-6. PMID 6824640 DOI: 10.1021/Bi00271A036 |
0.677 |
|
| 1983 |
Dalbey RE, Weiel J, Yount RG. Förster energy transfer measurements of thiol 1 to thiol 2 distances in myosin subfragment 1. Biochemistry. 22: 4696-706. PMID 6626524 DOI: 10.1021/Bi00289A014 |
0.625 |
|
| 1982 |
Wells JA, Yount RG. Chemical modification of myosin by active-site trapping of metal-nucleotides with thiol crosslinking reagents. Methods in Enzymology. 85: 93-116. PMID 7121292 DOI: 10.1016/0076-6879(82)85013-1 |
0.587 |
|
| 1980 |
Wells JA, Knoeber C, Sheldon MC, Werber MM, Yount RG. Cross-linking of myosin subfragment 1. Nucleotide-enhanced modification by a variety of bifunctional reagents. The Journal of Biological Chemistry. 255: 11135-40. PMID 7440533 |
0.442 |
|
| 1980 |
Wells JA, Werber MM, Yount RG. Mechanism of inactivation of myosin subfragment 1 by Co(III)phenATP. A reinvestigation. The Journal of Biological Chemistry. 255: 7552-5. PMID 6447149 |
0.415 |
|
| 1980 |
Wells JA, Yount RG. Reaction of 5,5'-dithiobis(2-nitrobenzoic acid) with myosin subfragment one: evidence for formation of a single protein disulfide with trapping of metal nucleotide at the active site. Biochemistry. 19: 1711-7. PMID 6445748 DOI: 10.1021/Bi00549A030 |
0.541 |
|
| 1980 |
Wells JA, Sheldon M, Yount RG. Magnesium nucleotide is stoichiometrically trapped at the active site of myosin and its active proteolytic fragments by thiol cross-linking reagents. The Journal of Biological Chemistry. 255: 1598-602. PMID 6444414 |
0.515 |
|
| 1979 |
Wells JA, Werber MM, Yount RG. Inactivation of myosin subfragment one by cobalt(II)/cobalt(III) phenanthroline complexes. 2. Cobalt chelation of two critical SH groups. Biochemistry. 18: 4800-5. PMID 159719 DOI: 10.1021/Bi00589A006 |
0.468 |
|
| 1979 |
Wells JA, Yount RG. Active site trapping of nucleotides by crosslinking two sulfhydryls in myosin subfragment 1. Proceedings of the National Academy of Sciences of the United States of America. 76: 4966-70. PMID 159451 DOI: 10.1073/Pnas.76.10.4966 |
0.6 |
|
| 1979 |
Wells JA, Werber MM, Legg JI, Yount RG. Inactivation of myosin subfragment one by cobalt(II)/cobalt(III) phenanthroline complexes. I. Incorporation of Co(III) by in situ oxidation of Co(II). Biochemistry. 18: 4793-9. PMID 41570 |
0.387 |
|
| 1977 |
Greene LE, Yount RG. Reaction of cardiac myosin with a purine disulfide analog of adenosine triphosphate. II. Stoichiometry and subunit location of labeling. The Journal of Biological Chemistry. 252: 1681-8. PMID 138684 |
0.332 |
|
| 1977 |
Greene LE, Yount RG. Reaction of cardiac myosin with a purine disulfide analog of adenosine triphosphate. I. Kinetics of inactivation and binding of adenylyl imidodiphosphate. The Journal of Biological Chemistry. 252: 1673-80. PMID 138683 |
0.372 |
|
| 1977 |
Greene LE, Yount RG. Observations on the kinetics, subunit composition, and sulfhydryl reactivity of myosin from Physarum polycephalum. Biochimica Et Biophysica Acta. 480: 326-32. PMID 137751 DOI: 10.1016/0005-2744(77)90345-X |
0.387 |
|
| 1976 |
Wagner PD, Yount RG. Modification of the alkali light chains of skeletal myosin inhibits actin binding and adenosine triphosphate cleavage Journal of Biological Chemistry. 251: 5424-5426. PMID 134039 |
0.309 |
|
| 1975 |
Wagner PD, Yount RG. The covalent modification of myosin's proteolytic fragments by a purine disulfide analog of adenosine triphosphate. Reaction at a binding site other than the active site. Biochemistry. 14: 5156-62. PMID 127613 DOI: 10.1021/Bi00694A021 |
0.487 |
|
| 1975 |
Wagner PD, Yount RG. Subunit location of sulfhydryl groups of myosin labeled with a purine disulfide analog of adenosine triphosphate. Biochemistry. 14: 1908-14. PMID 123761 DOI: 10.1021/Bi00680A016 |
0.43 |
|
| 1975 |
Wagner PD, Yount RG. Stoichiometry of labeling of myosin's proteolytic fragments by a purine disulfide analog of adenosine triphosphate. Biochemistry. 14: 1900-7. PMID 123760 DOI: 10.1021/Bi00680A015 |
0.494 |
|
| 1974 |
Yount RG. Adenylylimidodiphosphate and guanylylimidodiphosphate. Methods in Enzymology. 38: 420-7. PMID 4453194 DOI: 10.1016/0076-6879(74)38059-7 |
0.309 |
|
| 1973 |
Yount RG, Frye JS, O'Keefe KR. Inhibition of Heavy Meromyosin by Purine Disulfide Analogs of Adenosine Triphosphate Cold Spring Harbor Symposia On Quantitative Biology. 37: 113-119. DOI: 10.1101/Sqb.1973.037.01.017 |
0.304 |
|
| 1971 |
Yount RG, Babcock D, Ballantyne W, Ojala D. Adenylyl imidodiphosphate, an adenosine triphosphate analog containing a P--N--P linkage. Biochemistry. 10: 2484-9. PMID 4326768 DOI: 10.1021/Bi00789A009 |
0.382 |
|
| 1966 |
Yount RG, Simchuck S, Yu I, Kottke M. Adenosine-5'-sulfatopyrophosphate, an analogue of adenosine triphosphate. I. Preparation, properties, and mode of cleavage by snake venoms. Archives of Biochemistry and Biophysics. 113: 288-95. PMID 5328736 DOI: 10.1016/0003-9861(66)90189-5 |
0.366 |
|
| 1966 |
Yount RG, Yu I, Simchuk S. Adenosine-5'-sulfatopyrophosphate, an analogue of adenosine triphosphate. II. Interaction with myosin, actomyosin, and muscle fibers. Archives of Biochemistry and Biophysics. 113: 296-303. PMID 4223155 DOI: 10.1016/0003-9861(66)90190-1 |
0.404 |
|
| 1965 |
Swanson JR, Yount RG. A manganese stimulated, nucleotide dependent 18-O-inorganic phosphate exchange reaction catalyzed by heavy meromyosin. Biochemical and Biophysical Research Communications. 19: 765-9. PMID 5840699 DOI: 10.1016/0006-291X(65)90325-6 |
0.303 |
|
| 1963 |
YOUNT RG, KOSHLAND DE. Properties of the O18 exchange reaction catalyzed by heavy meromyosin. The Journal of Biological Chemistry. 238: 1708-13. PMID 14002855 |
0.352 |
|
| 1959 |
YOUNT RG, METZLER DE. Decarboxylation of pyruvate by thiamine analogues. The Journal of Biological Chemistry. 234: 738-41. PMID 13654253 |
0.542 |
|
| 1959 |
YATCO-MANZO E, RODDY F, YOUNT RG, METZLER DE. The catalytic decarboxylation of pyruvate by thiamine. The Journal of Biological Chemistry. 234: 733-7. PMID 13654252 |
0.531 |
|
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