| Year |
Citation |
Score |
| 2023 |
Hentschel J, Badstübner M, Choi J, Bagshaw CR, Lapointe CP, Wang J, Jansson LI, Puglisi JD, Stone MD. Real-time detection of human telomerase DNA synthesis by multiplexed single-molecule FRET. Biophysical Journal. PMID 37515327 DOI: 10.1016/j.bpj.2023.07.019 |
0.531 |
|
| 2021 |
Bagshaw CR, Hentschel J, Stone MD. The Processivity of Telomerase: Insights from Kinetic Simulations and Analyses. Molecules (Basel, Switzerland). 26. PMID 34946615 DOI: 10.3390/molecules26247532 |
0.497 |
|
| 2019 |
Jansson LI, Hentschel J, Parks JW, Chang TR, Lu C, Baral R, Bagshaw CR, Stone MD. Telomere DNA G-quadruplex folding within actively extending human telomerase. Proceedings of the National Academy of Sciences of the United States of America. PMID 31019071 DOI: 10.1073/Pnas.1814777116 |
0.532 |
|
| 2013 |
Seward HE, Basran J, Denton R, Pfuhl M, Muskett FW, Bagshaw CR. Halide and proton binding kinetics of yellow fluorescent protein variants Biochemistry. 52: 2482-2491. PMID 23514090 DOI: 10.1021/Bi3016839 |
0.441 |
|
| 2013 |
Long X, Parks JW, Bagshaw CR, Stone MD. Mechanical unfolding of human telomere G-quadruplex DNA probed by integrated fluorescence and magnetic tweezers spectroscopy. Nucleic Acids Research. 41: 2746-55. PMID 23303789 DOI: 10.1093/Nar/Gks1341 |
0.563 |
|
| 2012 |
Elliott PR, Irvine AF, Jung HS, Tozawa K, Pastok MW, Picone R, Badyal SK, Basran J, Rudland PS, Barraclough R, Lian LY, Bagshaw CR, Kriajevska M, Barsukov IL. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993). 20: 654-66. PMID 22483112 DOI: 10.1016/J.Str.2012.02.002 |
0.458 |
|
| 2011 |
Friel CT, Bagshaw CR, Howard J. Analysing the ATP turnover cycle of microtubule motors. Methods in Molecular Biology (Clifton, N.J.). 777: 177-92. PMID 21773929 DOI: 10.1007/978-1-61779-252-6_13 |
0.463 |
|
| 2011 |
Badyal SK, Basran J, Bhanji N, Kim JH, Chavda AP, Jung HS, Craig R, Elliott PR, Irvine AF, Barsukov IL, Kriajevska M, Bagshaw CR. Mechanism of the Ca²+-dependent interaction between S100A4 and tail fragments of nonmuscle myosin heavy chain IIA. Journal of Molecular Biology. 405: 1004-26. PMID 21110983 DOI: 10.1016/J.Jmb.2010.11.036 |
0.491 |
|
| 2010 |
Cherny D, Gooding C, Eperon GE, Coelho MB, Bagshaw CR, Smith CW, Eperon IC. Stoichiometry of a regulatory splicing complex revealed by single-molecule analyses. The Embo Journal. 29: 2161-72. PMID 20502437 DOI: 10.1038/Emboj.2010.103 |
0.384 |
|
| 2010 |
Frye JJ, Klenchin VA, Bagshaw CR, Rayment I. Insights into the importance of hydrogen bonding in the gamma-phosphate binding pocket of myosin: structural and functional studies of serine 236. Biochemistry. 49: 4897-907. PMID 20459085 DOI: 10.1021/Bi1001344 |
0.455 |
|
| 2009 |
Seward HE, Bagshaw CR. The photochemistry of fluorescent proteins: implications for their biological applications. Chemical Society Reviews. 38: 2842-51. PMID 19771331 DOI: 10.1039/B901355P |
0.337 |
|
| 2009 |
Cherny DI, Eperon IC, Bagshaw CR. Probing complexes with single fluorophores: factors contributing to dispersion of FRET in DNA/RNA duplexes. European Biophysics Journal : Ebj. 38: 395-405. PMID 19015840 DOI: 10.1007/S00249-008-0383-Z |
0.325 |
|
| 2008 |
Wegener KL, Basran J, Bagshaw CR, Campbell ID, Roberts GC, Critchley DR, Barsukov IL. Structural basis for the interaction between the cytoplasmic domain of the hyaluronate receptor layilin and the talin F3 subdomain. Journal of Molecular Biology. 382: 112-26. PMID 18638481 DOI: 10.1016/J.Jmb.2008.06.087 |
0.611 |
|
| 2008 |
Gingras AR, Basran J, Prescott A, Kriajevska M, Bagshaw CR, Barsukov IL. Crystal structure of the Ca2+-form and Ca2+-binding kinetics of metastasis-associated protein, S100A4 Febs Letters. 582: 1651-1656. PMID 18435928 DOI: 10.1016/J.Febslet.2008.04.017 |
0.359 |
|
| 2008 |
Gyimesi M, Kintses B, Bodor A, Perczel A, Fischer S, Bagshaw CR, Málnási-Csizmadia A. The mechanism of the reverse recovery step, phosphate release, and actin activation of Dictyostelium myosin II. The Journal of Biological Chemistry. 283: 8153-63. PMID 18211892 DOI: 10.1074/Jbc.M708863200 |
0.801 |
|
| 2007 |
Shi X, Basran J, Seward HE, Childs W, Bagshaw CR, Boxer SG. Anomalous negative fluorescence anisotropy in yellow fluorescent protein (YFP 10C): quantitative analysis of FRET in YFP dimers. Biochemistry. 46: 14403-17. PMID 18027983 DOI: 10.1021/Bi701575N |
0.362 |
|
| 2007 |
Lamb HK, Thompson P, Elliott C, Charles IG, Richards J, Lockyer M, Watkins N, Nichols C, Stammers DK, Bagshaw CR, Cooper A, Hawkins AR. Functional analysis of the GTPases EngA and YhbZ encoded by Salmonella typhimurium. Protein Science : a Publication of the Protein Society. 16: 2391-402. PMID 17905831 DOI: 10.1110/Ps.072900907 |
0.397 |
|
| 2007 |
Bagshaw CR. Myosin mechanochemistry. Structure (London, England : 1993). 15: 511-2. PMID 17502095 DOI: 10.1016/j.str.2007.04.005 |
0.321 |
|
| 2007 |
Málnási-Csizmadia A, Tóth J, Pearson DS, Hetényi C, Nyitray L, Geeves MA, Bagshaw CR, Kovács M. Selective perturbation of the myosin recovery stroke by point mutations at the base of the lever arm affects ATP hydrolysis and phosphate release. The Journal of Biological Chemistry. 282: 17658-64. PMID 17449872 DOI: 10.1074/Jbc.M701447200 |
0.787 |
|
| 2007 |
Kintses B, Gyimesi M, Pearson DS, Geeves MA, Zeng W, Bagshaw CR, Málnási-Csizmadia A. Reversible movement of switch 1 loop of myosin determines actin interaction. The Embo Journal. 26: 265-74. PMID 17213877 DOI: 10.1038/Sj.Emboj.7601482 |
0.796 |
|
| 2007 |
Bagshaw CR, Cherny D. Blinking fluorophores: what do they tell us about protein dynamics? Biochemical Society Transactions. 34: 979-82. PMID 17052241 DOI: 10.1042/Bst0340979 |
0.326 |
|
| 2007 |
Fajer PG, Gyimesi M, Málnási-Csizmadia A, Bagshaw CR, Ilker Sen K, Song L. Myosin cleft closure by double electron-electron resonance and dipolar EPR Journal of Physics Condensed Matter. 19. DOI: 10.1088/0953-8984/19/28/285208 |
0.809 |
|
| 2006 |
Zeng W, Seward HE, Málnási-Csizmadia A, Wakelin S, Woolley RJ, Cheema GS, Basran J, Patel TR, Rowe AJ, Bagshaw CR. Resonance energy transfer between green fluorescent protein variants: complexities revealed with myosin fusion proteins. Biochemistry. 45: 10482-91. PMID 16939200 DOI: 10.1021/Bi060943U |
0.664 |
|
| 2005 |
Málnási-Csizmadia A, Dickens JL, Zeng W, Bagshaw CR. Switch movements and the myosin crossbridge stroke. Journal of Muscle Research and Cell Motility. 26: 31-7. PMID 16075160 DOI: 10.1007/S10974-005-9004-Y |
0.672 |
|
| 2005 |
McAnaney TB, Zeng W, Doe CF, Bhanji N, Wakelin S, Pearson DS, Abbyad P, Shi X, Boxer SG, Bagshaw CR. Protonation, photobleaching, and photoactivation of yellow fluorescent protein (YFP 10C): a unifying mechanism. Biochemistry. 44: 5510-24. PMID 15807545 DOI: 10.1021/Bi047581F |
0.343 |
|
| 2004 |
Zeng W, Conibear PB, Dickens JL, Cowie RA, Wakelin S, Málnási-Csizmadia A, Bagshaw CR. Dynamics of actomyosin interactions in relation to the cross-bridge cycle. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 359: 1843-55. PMID 15647160 DOI: 10.1098/Rstb.2004.1527 |
0.723 |
|
| 2004 |
Conibear PB, Málnási-Csizmadia A, Bagshaw CR. The effect of F-actin on the relay helix position of myosin II, as revealed by tryptophan fluorescence, and its implications for mechanochemical coupling. Biochemistry. 43: 15404-17. PMID 15581352 DOI: 10.1021/Bi048338J |
0.749 |
|
| 2004 |
Kovács M, Tóth J, Málnási-Csizmadia A, Bagshaw CR, Nyitray L. Engineering lysine reactivity as a conformational sensor in the Dictyostelium myosin II motor domain. Journal of Muscle Research and Cell Motility. 25: 95-102. PMID 15160493 DOI: 10.1023/B:Jure.0000021352.80800.B8 |
0.8 |
|
| 2004 |
Málnási-Csizmadia A, Pearson DS, Kovács M, Woolley RJ, Geeves MA, Bagshaw CR. Kinetic Resolution of a Conformational Transition and the ATP Hydrolysis Step Using Relaxation Methods with aDictyosteliumMyosin II Mutant Containing a Single Tryptophan Residue Biochemistry. 43: 14316-14316. DOI: 10.1021/Bi040043I |
0.785 |
|
| 2003 |
Conibear PB, Bagshaw CR, Fajer PG, Kovács M, Málnási-Csizmadia A. Myosin cleft movement and its coupling to actomyosin dissociation. Nature Structural Biology. 10: 831-5. PMID 14502269 DOI: 10.1038/Nsb986 |
0.792 |
|
| 2003 |
Barsukov IL, Prescot A, Bate N, Patel B, Floyd DN, Bhanji N, Bagshaw CR, Letinic K, Di Paolo G, De Camilli P, Roberts GC, Critchley DR. Phosphatidylinositol phosphate kinase type 1gamma and beta1-integrin cytoplasmic domain bind to the same region in the talin FERM domain. The Journal of Biological Chemistry. 278: 31202-9. PMID 12782621 DOI: 10.1074/Jbc.M303850200 |
0.614 |
|
| 2003 |
Wakelin S, Bagshaw CR. A prism combination for near isotropic fluorescence excitation by total internal reflection. Journal of Microscopy. 209: 143-8. PMID 12588531 DOI: 10.1046/J.1365-2818.2003.01118.X |
0.31 |
|
| 2003 |
Bagshaw CR. Motors in muscle: the function of conventional myosin II. Essays in Biochemistry. 35: 19-31. PMID 12471887 DOI: 10.1042/Bse0350019 |
0.489 |
|
| 2002 |
Wakelin S, Conibear PB, Woolley RJ, Floyd DN, Bagshaw CR, Kovács M, Málnási-Csizmadia A. Engineering Dictyostelium discoideum myosin II for the introduction of site-specific fluorescence probes. Journal of Muscle Research and Cell Motility. 23: 673-83. PMID 12952066 DOI: 10.1023/A:1024411208497 |
0.767 |
|
| 2002 |
Kovacs M, Malnasi-Csizmadia A, Woolley RJ, Bagshaw CR. Analysis of nucleotide binding to Dictyostelium myosin II motor domains containing a single tryptophan near the active site. The Journal of Biological Chemistry. 277: 28459-67. PMID 11971905 DOI: 10.1074/Jbc.M202180200 |
0.803 |
|
| 2002 |
Bass MD, Patel B, Barsukov IG, Fillingham IJ, Mason R, Smith BJ, Bagshaw CR, Critchley DR. Further characterization of the interaction between the cytoskeletal proteins talin and vinculin. The Biochemical Journal. 362: 761-8. PMID 11879206 DOI: 10.1042/Bj3620761 |
0.636 |
|
| 2001 |
Málnási-Csizmadia A, Pearson DS, Kovács M, Woolley RJ, Geeves MA, Bagshaw CR. Kinetic resolution of a conformational transition and the ATP hydrolysis step using relaxation methods with a Dictyostelium myosin II mutant containing a single tryptophan residue. Biochemistry. 40: 12727-37. PMID 11601998 DOI: 10.1021/Bi010963Q |
0.808 |
|
| 2001 |
Malnasi-Csizmadia A, Kovacs M, Woolley RJ, Botchway SW, Bagshaw CR. The dynamics of the relay loop tryptophan residue in the Dictyostelium myosin motor domain and the origin of spectroscopic signals. The Journal of Biological Chemistry. 276: 19483-90. PMID 11278775 DOI: 10.1074/Jbc.M010886200 |
0.775 |
|
| 2001 |
Málnási-Csizmadia A, Woolley RJ, Bagshaw CR. Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan (W501) mutants: implications for the open-closed transition identified by crystallography. Biochemistry. 39: 16135-46. PMID 11123942 DOI: 10.1021/Bi001125J |
0.731 |
|
| 2000 |
Conibear PB, Bagshaw CR. Myosin monomer density and exchange in synthetic thick filaments investigated using fluorescence microscopy with single molecule sensitivity. Proceedings. Biological Sciences. 267: 415-21. PMID 10722224 DOI: 10.1098/Rspb.2000.1016 |
0.407 |
|
| 2000 |
Shirakawa I, Chaen S, Bagshaw CR, Sugi H. Measurement of nucleotide exchange rate constants in single rabbit soleus myofibrils during shortening and lengthening using a fluorescent ATP analog. Biophysical Journal. 78: 918-26. PMID 10653804 DOI: 10.1016/S0006-3495(00)76649-5 |
0.461 |
|
| 2000 |
Bakolitsa C, Pereda JMD, Bagshaw CR, Critchley DR, Liddington RC. Crystal Structure of the Vinculin Tail and a Pathway for Activation Cell. 99: 603. DOI: 10.2210/Pdb1Qkr/Pdb |
0.507 |
|
| 2000 |
Bagshaw CR, Conibear PB. Single-Molecule Enzymology: Critical Aspects Exemplified by Myosin ATPase Activity Single Molecules. 1: 271-277. DOI: 10.1002/1438-5171(200012)1:4<271::Aid-Simo271>3.0.Co;2-N |
0.365 |
|
| 1999 |
Bakolitsa C, de Pereda JM, Bagshaw CR, Critchley DR, Liddington RC. Crystal structure of the vinculin tail suggests a pathway for activation. Cell. 99: 603-13. PMID 10612396 DOI: 10.1016/S0092-8674(00)81549-4 |
0.638 |
|
| 1999 |
Bagshaw CR, Conibear PB. Single molecule enzyme kinetics: application to myosin ATPases. Biochemical Society Transactions. 27: 33-7. PMID 10093702 DOI: 10.1042/Bst0270033 |
0.351 |
|
| 1999 |
Conibear PB, Kuhlman PA, Bagshaw CR. Measurement of ATPase activities of myosin at the level of tracks and single molecules. Advances in Experimental Medicine and Biology. 453: 15-26; discussion 26. PMID 9889810 DOI: 10.1007/978-1-4684-6039-1_3 |
0.816 |
|
| 1998 |
Chaen S, Shirakawa I, Bagshaw CR, Sugi H. Measurement of ATP turnover during shortening and lengthening of rabbit psoas myofibrils using a fluorescent ATP analog. Advances in Experimental Medicine and Biology. 453: 569-76. PMID 9889869 DOI: 10.1007/978-1-4684-6039-1_62 |
0.398 |
|
| 1998 |
Kuhlman PA, Bagshaw CR. ATPase kinetics of the Dictyostelium discoideum myosin II motor domain. Journal of Muscle Research and Cell Motility. 19: 491-504. PMID 9682136 DOI: 10.1023/A:1005304408812 |
0.833 |
|
| 1997 |
Bauer CB, Kuhlman PA, Bagshaw CR, Rayment I. X-ray crystal structure and solution fluorescence characterization of Mg.2'(3')-O-(N-methylanthraniloyl) nucleotides bound to the Dictyostelium discoideum myosin motor domain. Journal of Molecular Biology. 274: 394-407. PMID 9405148 DOI: 10.1006/Jmbi.1997.1325 |
0.811 |
|
| 1997 |
Bagshaw CR. Muscle contraction. Myosin trapped but not tamed. Nature. 390: 345-6. PMID 9389471 DOI: 10.1038/37002 |
0.359 |
|
| 1997 |
Chaen S, Shirakawa I, Bagshaw CR, Sugi H. Measurement of nucleotide release kinetics in single skeletal muscle myofibrils during isometric and isovelocity contractions using fluorescence microscopy. Biophysical Journal. 73: 2033-42. PMID 9336198 DOI: 10.1016/S0006-3495(97)78233-X |
0.361 |
|
| 1996 |
Conibear PB, Jeffreys DS, Seehra CK, Eaton RJ, Bagshaw CR. Kinetic and spectroscopic characterization of fluorescent ribose-modified ATP analogs upon interaction with skeletal muscle myosin subfragment 1. Biochemistry. 35: 2299-308. PMID 8652570 DOI: 10.1021/Bi951824+ |
0.496 |
|
| 1996 |
Conibear PB, Bagshaw CR. Measurement of nucleotide exchange kinetics with isolated synthetic myosin filaments using flash photolysis. Febs Letters. 380: 13-6. PMID 8603721 DOI: 10.1016/0014-5793(95)01538-8 |
0.464 |
|
| 1996 |
Jeffreys DS, Eaton RJ, Bagshaw CR. Caged FEDA-ATP: a new tool in the measurement of ATP turnover during the in vitro motility assay. Biochemical Society Transactions. 23: 401S. PMID 8566289 DOI: 10.1042/Bst023401S |
0.472 |
|
| 1996 |
Ellis J, Bagshaw CR, Shaw WV. Kinetic mechanism of chloramphenicol acetyltransferase: the role of ternary complex interconversion in rate determination. Biochemistry. 34: 16852-9. PMID 8527461 DOI: 10.1021/Bi00051A036 |
0.319 |
|
| 1995 |
Conibear PB, Seehra CK, Bagshaw CR, Gingell D. Observation of ATP turnover during in vitro motility assays. Biochemical Society Transactions. 23: 400S. PMID 8566288 DOI: 10.1042/Bst023400S |
0.378 |
|
| 1995 |
Ellis J, Bagshaw CR, Shaw WV. Tryptophan fluorescence of chloramphenicol acetyltransferase: resolution of individual excited-state lifetimes by site-directed mutagenesis and multifrequency phase fluorometry. Biochemistry. 34: 3513-20. PMID 7893646 DOI: 10.1021/Bi00011A004 |
0.408 |
|
| 1994 |
Kuhlman PA, Ellis J, Critchley DR, Bagshaw CR. The kinetics of the interaction between the actin-binding domain of alpha-actinin and F-actin. Febs Letters. 339: 297-301. PMID 8112470 DOI: 10.1016/0014-5793(94)80434-6 |
0.793 |
|
| 1993 |
Sowerby AJ, Seehra CK, Lee M, Bagshaw CR. Turnover of fluorescent nucleoside triphosphates by isolated immobilized myosin filaments. Transient kinetics on the zeptomole scale. Journal of Molecular Biology. 234: 114-23. PMID 8230191 DOI: 10.1006/Jmbi.1993.1567 |
0.498 |
|
| 1991 |
Ellis J, Bagshaw CR, Shaw WV. Substrate binding to chloramphenicol acetyltransferase: evidence for negative cooperativity from equilibrium and kinetic constants for binary and ternary complexes. Biochemistry. 30: 10806-13. PMID 1932000 DOI: 10.1021/Bi00108A029 |
0.344 |
|
| 1991 |
Ankrett RJ, Walmsley AR, Bagshaw CR. Kinetic analysis of regulated myosin ATPase activity using single and limited turnover assays. Journal of Cell Science. Supplement. 14: 1-5. PMID 1832160 DOI: 10.1242/Jcs.1991.Supplement_14.1 |
0.666 |
|
| 1991 |
Ankrett RJ, Rowe AJ, Cross RA, Kendrick-Jones J, Bagshaw CR. A folded (10 S) conformer of myosin from a striated muscle and its implications for regulation of ATPase activity Journal of Molecular Biology. 217: 323-335. PMID 1825121 DOI: 10.1016/0022-2836(91)90546-I |
0.455 |
|
| 1990 |
Walmsley AR, Evans GE, Bagshaw CR. The calcium ion dependence of scallop myosin ATPase activity Journal of Muscle Research and Cell Motility. 11: 512-521. PMID 2150676 DOI: 10.1007/Bf01745218 |
0.675 |
|
| 1990 |
Nesterov VP, Peiper U, Hiller J, Krienke B, Schüttler K, Szymanski C, Bottinelli R, Cappelli V, Minelli R, Reggiani C, Schiaffino S, Carlhoff D, D'Haese J, Dabrowska R, Nowak E, ... ... Bagshaw CR, et al. Abstracts of the XVIII European Conference on Muscle and Motility Journal of Muscle Research & Cell Motility. 11: 56-78. DOI: 10.1007/Bf01833326 |
0.606 |
|
| 1989 |
Walmsley AR, Bagshaw CR. Logarithmic timebase for stopped-flow data acquisition and analysis. Analytical Biochemistry. 176: 313-8. PMID 2500867 DOI: 10.1016/0003-2697(89)90315-1 |
0.609 |
|
| 1989 |
Citi S, Cross RA, Bagshaw CR, Kendrick-Jones J. Parallel modulation of brush border myosin conformation and enzyme activity induced by monoclonal antibodies Journal of Cell Biology. 109: 549-556. PMID 2474552 DOI: 10.1083/Jcb.109.2.549 |
0.475 |
|
| 1988 |
Cross RA, Jackson AP, Citi S, Kendrick-Jones J, Bagshaw CR. Active site trapping of nucleotide by smooth and non-muscle myosins Journal of Molecular Biology. 203: 173-181. PMID 3054120 DOI: 10.1016/0022-2836(88)90100-3 |
0.594 |
|
| 1988 |
Jackson AP, Bagshaw CR. Kinetic trapping of intermediates of the scallop heavy meromysin adenosine triphosphatase reaction revealed by formycin nucleotides Biochemical Journal. 251: 527-540. PMID 2969726 DOI: 10.1042/Bj2510527 |
0.595 |
|
| 1988 |
Jackson AP, Bagshaw CR. Transient-kinetic studies of the adenosine triphosphatase activity of scallop heavy meromysin Biochemical Journal. 251: 515-526. PMID 2969725 DOI: 10.1042/Bj2510515 |
0.59 |
|
| 1987 |
Jackson AP, Timmerman MP, Bagshaw CR, Ashley CC. The kinetics of calcium binding to fura-2 and indo-1. Febs Letters. 216: 35-9. PMID 3108033 DOI: 10.1016/0014-5793(87)80752-4 |
0.519 |
|
| 1987 |
STANNERS PJ, BAGSHAW CR. Interaction of scallop heavy meromyosin with pyrene-labelled actin Biochemical Society Transactions. 15: 901-903. DOI: 10.1042/Bst0150901 |
0.337 |
|
| 1987 |
JACKSON AP, WARRINER KE, BAGSHAW CR. Measurement of single turnovers of scallop myosin ATPase in the filamentous state Biochemical Society Transactions. 15: 900-901. DOI: 10.1042/Bst0150900 |
0.48 |
|
| 1986 |
Jackson AP, Warriner KE, Wells C, Bagshaw CR. The actin-activated ATPase of regulated and unregulated scallop heavy meromyosin Febs Letters. 197: 154-158. DOI: 10.1016/0014-5793(86)80317-9 |
0.702 |
|
| 1985 |
Wells C, Warriner KE, Bagshaw CR. Fluorescence studies on the nucleotide- and Ca2+-binding domains of molluscan myosin. The Biochemical Journal. 231: 31-8. PMID 3904736 DOI: 10.1042/Bj2310031 |
0.425 |
|
| 1985 |
Wells C, Bagshaw CR. Calcium regulation of molluscan myosin ATPase in the absence of actin. Nature. 313: 696-7. PMID 3156278 DOI: 10.1038/313696A0 |
0.688 |
|
| 1985 |
WELLS C, WARRINER K, BENNET AJ, BAGSHAW CR. The kinetic mechanism of scallop myosin ATPase activity Biochemical Society Transactions. 13: 925-926. DOI: 10.1042/Bst0130925 |
0.633 |
|
| 1984 |
Bennett AJ, Patel N, Wells C, Bagshaw CR. 8-Anilino-1-naphthalenesulphonate, a fluorescent probe for the regulatory light chain binding site of scallop myosin. Journal of Muscle Research and Cell Motility. 5: 165-82. PMID 6725549 DOI: 10.1007/Bf00712154 |
0.664 |
|
| 1984 |
Wells C, Bagshaw CR. The characterization of vanadate-trapped nucleotide complexes with spin-labelled myosins. Journal of Muscle Research and Cell Motility. 5: 97-112. PMID 6325500 DOI: 10.1007/Bf00713154 |
0.612 |
|
| 1984 |
Wells C, Bagshaw CR. The Ca2+
sensitivity of the actin-activated ATPase of scallop heavy meromyosin Febs Letters. 168: 260-264. DOI: 10.1016/0014-5793(84)80258-6 |
0.599 |
|
| 1983 |
Wells C, Bagshaw CR. Segmental flexibility and head-head interaction in scallop myosin. A study using saturation transfer electron paramagnetic resonance spectroscopy. Journal of Molecular Biology. 164: 137-57. PMID 6302270 DOI: 10.1016/0022-2836(83)90090-6 |
0.668 |
|
| 1983 |
WELLS C, PATEL N, BAGSHAW CR. Saturation-transfer electron-paramagnetic-resonance and fluorescence studies of scallop myosin Biochemical Society Transactions. 11: 177-178. DOI: 10.1042/Bst0110177 |
0.586 |
|
| 1981 |
Bagshaw CR. Divalent metal ion binding and subunit interactions in myosins: a critical review. Journal of Muscle Research and Cell Motility. 1: 255-77. PMID 6453131 DOI: 10.1007/Bf00711931 |
0.326 |
|
| 1980 |
Bagshaw CR, Kendrick-Jones J. Identification of the divalent metal ion binding domain of myosin regulatory light chains using spin-labelling techniques Journal of Molecular Biology. 140: 411-433. PMID 6255164 DOI: 10.1016/0022-2836(80)90392-7 |
0.398 |
|
| 1979 |
Bagshaw CR, Kendrick-Jones J. Characterization of homologous divalent metal ion binding sites of vertebrate and molluscan myosins using electron paramagnetic resonance spectroscopy Journal of Molecular Biology. 130: 317-336. PMID 224193 DOI: 10.1016/0022-2836(79)90544-8 |
0.401 |
|
| 1978 |
Bagshaw CR, Kendrick-Jones J. Homologous metal-binding sites of myosin regulatory light chains revealed by the paramagnetic manganous ion [proceedings] Biochemical Society Transactions. 6: 1262-1264. PMID 217774 DOI: 10.1042/Bst0061262 |
0.395 |
|
| 1978 |
Bagshaw CR. The mechanism of adenosine triphosphate hydrolysis by myosin [proceedings]. Biochemical Society Transactions. 5: 1272-4. PMID 144620 DOI: 10.1042/Bst0051272 |
0.469 |
|
| 1977 |
Bagshaw CR. On the location of the divalent metal binding sites and the light chain subunits of vertebrate myosin. Biochemistry. 16: 59-67. PMID 188447 DOI: 10.1021/Bi00620A010 |
0.373 |
|
| 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 |
0.65 |
|
| 1975 |
Bagshaw CR, Trentham DR. Transient kinetic and isotopic tracer studies of the myosin adenosine triphosphatase reaction. Journal of Supramolecular Structure. 3: 315-22. PMID 172737 DOI: 10.1002/jss.400030402 |
0.623 |
|
| 1975 |
Bagshaw CR, Trentham DR, Wolcott RG, Boyer PD. Oxygen exchange in the gamma-phosphoryl group of protein-bound ATP during Mg2+-dependent adenosine triphosphatase activity of myosin. Proceedings of the National Academy of Sciences of the United States of America. 72: 2592-6. PMID 126449 |
0.615 |
|
| 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 |
0.639 |
|
| 1974 |
Bagshaw CR, Trentham DR. The characterization of myosin-product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reaction. The Biochemical Journal. 141: 331-49. PMID 4281653 |
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| 1973 |
Bagshaw CR, Trentham DR. The reversibility of adenosine triphosphate cleavage by myosin. The Biochemical Journal. 133: 323-8. PMID 4269253 |
0.577 |
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| 1973 |
Bagshaw CR, Eccleston JF, Trentham DR, Yates DW, Goody RS. Transient Kinetic Studies of the Mg++-dependent ATPase of Myosin and Its Proteolytic Subfragments Cold Spring Harbor Symposia On Quantitative Biology. 37: 127-135. DOI: 10.1101/SQB.1973.037.01.020 |
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