| Year |
Citation |
Score |
| 2011 |
Xiao B, Sanders MJ, Underwood E, Heath R, Mayer FV, Carmena D, Jing C, Walker PA, Eccleston JF, Haire LF, Saiu P, Howell SA, Aasland R, Martin SR, Carling D, et al. Structure of mammalian AMPK and its regulation by ADP. Nature. 472: 230-3. PMID 21399626 DOI: 10.1038/Nature09932 |
0.301 |
|
| 2010 |
Kunzelmann S, Morris C, Chavda AP, Eccleston JF, Webb MR. Mechanism of interaction between single-stranded DNA binding protein and DNA. Biochemistry. 49: 843-52. PMID 20028139 DOI: 10.1021/Bi901743K |
0.422 |
|
| 2008 |
Petrovic A, Davis CT, Rangachari K, Clough B, Wilson RJ, Eccleston JF. Hydrodynamic characterization of the SufBC and SufCD complexes and their interaction with fluorescent adenosine nucleotides. Protein Science : a Publication of the Protein Society. 17: 1264-74. PMID 18413861 DOI: 10.1110/ps.034652.108 |
0.301 |
|
| 2008 |
Corrie JET, Eccleston JF, Ferenczi MA, Moore MH, Turkenburg JP, Trentham DR. Ring-chain interconversion of sulforhodamine-amine conjugates involves an unusually labile C-N bond and allows measurement of sulfonamide ionization kinetics Journal of Physical Organic Chemistry. 21: 286-298. DOI: 10.1002/Poc.1318 |
0.517 |
|
| 2007 |
Xiao B, Heath R, Saiu P, Leiper FC, Leone P, Jing C, Walker PA, Haire L, Eccleston JF, Davis CT, Martin SR, Carling D, Gamblin SJ. Structural basis for AMP binding to mammalian AMP-activated protein kinase. Nature. 449: 496-500. PMID 17851531 DOI: 10.1038/Nature06161 |
0.37 |
|
| 2006 |
Eccleston JF, Petrovic A, Davis CT, Rangachari K, Wilson RJ. The kinetic mechanism of the SufC ATPase: the cleavage step is accelerated by SufB. The Journal of Biological Chemistry. 281: 8371-8. PMID 16431905 DOI: 10.1074/jbc.M513455200 |
0.425 |
|
| 2003 |
Phillips RA, Hunter JL, Eccleston JF, Webb MR. The mechanism of Ras GTPase activation by neurofibromin Biochemistry. 42: 3956-3965. PMID 12667087 DOI: 10.1021/bi027316z |
0.351 |
|
| 2001 |
Corrie JET, Davis CT, Eccleston JF. Chemistry of sulforhodamine--amine conjugates. Bioconjugate Chemistry. 12: 186-194. PMID 11312679 DOI: 10.1021/Bc0000785 |
0.37 |
|
| 2000 |
Hutchinson JP, Eccleston JF. Mechanism of nucleotide release from Rho by the GDP dissociation stimulator protein Biochemistry. 39: 11348-11359. PMID 10985780 DOI: 10.1021/Bi0007573 |
0.437 |
|
| 2000 |
Binns DD, Helms MK, Barylko B, Davis CT, Jameson DM, Albanesi JP, Eccleston JF. The mechanism of GTP hydrolysis by dynamin II: a transient kinetic study. Biochemistry. 39: 7188-96. PMID 10852717 DOI: 10.1021/Bi000033R |
0.388 |
|
| 2000 |
Oiwa K, Eccleston JF, Anson M, Kikumoto M, Davis CT, Reid GP, Ferenczi MA, Corrie JE, Yamada A, Nakayama H, Trentham DR. Comparative single-molecule and ensemble myosin enzymology: sulfoindocyanine ATP and ADP derivatives. Biophysical Journal. 78: 3048-71. PMID 10827983 DOI: 10.1016/S0006-3495(00)76843-3 |
0.599 |
|
| 2000 |
Sawyer WH, Chan RYS, Eccleston JF, Davidson BE, Samat SA, Yan Y. Distances between DNA and ATP binding sites in the TyrR-DNA complex. Biochemistry. 39: 5653-5661. PMID 10801315 DOI: 10.1021/Bi0000723 |
0.352 |
|
| 1999 |
Graham DL, Eccleston JF, Chung CW, Lowe PN. Magnesium fluoride-dependent binding of small G proteins to their GTPase-activating proteins. Biochemistry. 38: 14981-7. PMID 10555980 DOI: 10.1021/Bi991358E |
0.383 |
|
| 1999 |
Graham DL, Eccleston JF, Lowe PN. The conserved arginine in rho-GTPase-activating protein is essential for efficient catalysis but not for complex formation with Rho.GDP and aluminum fluoride. Biochemistry. 38: 985-91. PMID 9893994 DOI: 10.1021/Bi9821770 |
0.41 |
|
| 1998 |
Nixon AE, Hunter JL, Bonifacio G, Eccleston JF, Webb MR. Purine nucleoside phosphorylase: Its use in a spectroscopic assay for inorganic phosphate and for removing inorganic phosphate with the aid of phosphodeoxyribomutase Analytical Biochemistry. 265: 299-307. PMID 9882406 DOI: 10.1006/abio.1998.2916 |
0.302 |
|
| 1995 |
Watson BS, Hazlett TL, Eccleston JF, Davis C, Jameson DM, Johnson AE. Macromolecular arrangement in the aminoacyl-tRNA.elongation factor Tu.GTP ternary complex. A fluorescence energy transfer study. Biochemistry. 34: 7904-12. PMID 7794902 DOI: 10.1021/Bi00024A015 |
0.348 |
|
| 1994 |
Hazlett TL, Moore KJ, Lowe PN, Jameson DM, Eccleston JF. Solution dynamics of p21ras proteins bound with fluorescent nucleotides: a time-resolved fluorescence study. Biochemistry. 32: 13575-83. PMID 8257693 DOI: 10.1021/Bi00212A025 |
0.367 |
|
| 1993 |
Moore KJM, Webb MR, Eccleston JF. Mechanism of GTP hydrolysis by p21N-ras catalyzed by GAP: studies with a fluorescent GTP analogue. Biochemistry. 32: 7451-7459. PMID 8338843 DOI: 10.1021/Bi00080A016 |
0.406 |
|
| 1992 |
Moore KJ, Lowe PN, Eccleston JF. The kinetic mechanism of the GAP-activated GTPase of p21 ras Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 336: 49-53; discussion 53. PMID 1351296 DOI: 10.1098/rstb.1992.0043 |
0.331 |
|
| 1991 |
Eccleston JF, Moore KJ, Brownbridge GG, Webb MR, Lowe PN. Fluorescence approaches to the study of the p21ras GTPase mechanism. Biochemical Society Transactions. 19: 432-7. PMID 1889625 DOI: 10.1042/bst0190432 |
0.304 |
|
| 1990 |
Neal SE, Eccleston JF, Webb MR. Hydrolysis of GTP by p21NRAS, the NRAS protooncogene product, is accompanied by a conformational change in the wild-type protein: use of a single fluorescent probe at the catalytic site. Proceedings of the National Academy of Sciences of the United States of America. 87: 3562-5. PMID 2185475 DOI: 10.1073/PNAS.87.9.3562 |
0.334 |
|
| 1987 |
Eccleston JF, Gratton E, Jameson DM. Interaction of a fluorescent analogue of GDP with elongation factor Tu: steady-state and time-resolved fluorescence studies. Biochemistry. 26: 3902-7. PMID 3651422 DOI: 10.1021/Bi00387A024 |
0.302 |
|
| 1981 |
Eccleston JF. Spectroscopic studies of the nucleotide binding site of elongation factor Tu from Escherichia coli. An approach to characterizing the elementary steps of the elongation cycle of protein biosynthesis. Biochemistry. 20: 6265-6272. PMID 7030387 DOI: 10.1021/Bi00524A055 |
0.367 |
|
| 1981 |
Rossomando EF, Jahngen JH, Eccleston JF. Formycin 5'-triphosphate, a fluorescent analog of ATP, as a substrate for adenylate cyclase. Proceedings of the National Academy of Sciences of the United States of America. 78: 2278-82. PMID 6941284 DOI: 10.1073/PNAS.78.4.2278 |
0.368 |
|
| 1980 |
Eccleston JF, Bayley PM. Circular dichroic spectra of 6-thioguanosine nucleotides and their complexes with myosin subfragment 1. Biochemistry. 19: 5050-6. PMID 7459323 DOI: 10.1021/Bi00563A018 |
0.405 |
|
| 1979 |
Eccleston JF, Trentham DR. Magnesium ion dependent rabbit skeletal muscle myosin guanosine and thioguanosine triphosphatase mechanism and a novel guanosine diphosphatase reaction. Biochemistry. 18: 2896-904. PMID 224906 DOI: 10.1021/Bi00580A034 |
0.646 |
|
| 1977 |
Eccleston JF, Trentham DR. The interaction of chromophoric nucleotides with subfragment 1 of myosin. The Biochemical Journal. 163: 15-29. PMID 869914 |
0.593 |
|
| 1976 |
Trentham DR, Eccleston JF, Bagshaw CR. Kinetic analysis of ATPase mechanisms. Quarterly Reviews of Biophysics. 9: 217-81. PMID 183232 DOI: 10.1017/S0033583500002419 |
0.62 |
|
| 1974 |
Bagshaw CR, Eccleston JF, Eckstein F, Goody RS, Gutfreund H, Trentham DR. The magnesium ion-dependent adenosine triphosphatase of myosin. Two-step processes of adenosine triphosphate association and adenosine diphosphate dissociation. The Biochemical Journal. 141: 351-64. PMID 4281654 DOI: 10.1042/Bj1410351 |
0.624 |
|
| 1972 |
Trentham DR, Bardsley RG, Eccleston JF, Weeds AG. Elementary processes of the magnesium ion-dependent adenosine triphosphatase activity of heavy meromyosin. A transient kinetic approach to the study of kinases and adenosine triphosphatases and a colorimetric inorganic phosphate assay in situ. The Biochemical Journal. 126: 635-44. PMID 4263038 DOI: 10.1042/Bj1260635 |
0.621 |
|
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