Currently there are no copies of publication texts here, but the PubMed link leads to the abstract and often leads to a link to obtain the full text.

  1. Webb, M. R., and Knowles, J. R. (1974): The existence of an electrophilic component in the reaction catalysed by triosephosphate isomerase. Biochem. J. 141, 589-592. (PubMed abstract)

  2. Webb, M. R., and Knowles, J. R. (1975): The orientation and accessibility of substrates on the active site of triosephosphate isomerase. Biochemistry 14, 4692-4698. (PubMed abstract)

  3. Webb, M. R. (1976): Stereochemical aspects of the interaction between isomerases and their substrates. D. Phil. Thesis. Oxford: Oxford University.

  4. Webb, M. R., Standring, D. R., and Knowles, J. R. (1977): Phosphorus-31 nuclear magnetic resonance of dihydroxyacetone phosphate in the presence of triosephosphate isomerase The question of non-productive binding of the substrate hydrate. Biochemistry 16, 2738-2741. (PubMed abstract)

  5. Webb, M. R., McDonald, G. G., and Trentham, D. R. (1978): Kinetics of oxygen-18 exchange between inorganic phosphate and water catalyzed by myosin subfragment 1, using the 18O shift in 31P NMR. J. Biol. Chem. 253, 2908-2911. (PubMed abstract)

  6. Webb, M. R., and Trentham, D. R. (1980): Analysis of chiral inorganic [16O,17O,18O]thiophosphate and the stereochemistry of the 3-phosphoglycerate kinase reaction. J. Biol. Chem. 255, 1775-1779. (PubMed abstract)

  7. Webb, M. R. (1980): A method for determining positional isotope exchange in a nucleoside triphosphate: cyclization of nucleoside triphosphate by dicyclohexylcarbodiimide. Biochemistry 19, 4744-4748. (PubMed abstract)

  8. Webb, M. R., and Trentham, D. R. (1980): The stereochemical course of phosphoric residue transfer during the myosin ATPase reaction. J. Biol. Chem. 255, 8629-8632. (PubMed abstract)

  9. Geeves, M. A., Webb, M. R., Midelfort, C. F., and Trentham, D. R. (1980): Mechanism of adenosine 5'-triphosphate cleavage by myosin: studies with oxygen-18-labeled adenosine 5'-triphosphate.. Biochemistry 19, 4748-4754. (PubMed abstract)

  10. Webb, M. R., Grubmeyer, C., Penefsky, H. S., and Trentham, D. R. (1980): The stereochemical course of phosphoric residue transfer catalyzed by beef heart mitochondrial ATPase. J. Biol. Chem. 255, 11637-11639. (PubMed abstract)

  11. Webb, M. R., and Trentham, D. R. (1981): The stereochemical course of phosphoric residue transfer catalyzed by sarcoplasmic reticulum ATPase. J. Biol. Chem. 256, 4884-4887. (PubMed abstract)

  12. Webb, M. R., and Trentham, D. R. (1981): The mechanism of ATP hydrolysis catalyzed by myosin and actomyosin, using rapid reaction techniques to study oxygen exchange. J. Biol. Chem. 256, 10910-10916. (PubMed abstract)

  13. Eccleston, J. F., Webb, M. R., Ash, D. E., and Reed, G. H. (1981): EPR studies of the Mn(II) complex with elongation factor Tu and GDP; identification of oxygen ligands to Mn(II) by observation of 17O superhyperfine coupling. J. Biol. Chem. 256, 10774-10777. (PubMed abstract)

  14. Webb, M. R., and Eccleston, J. F. (1981): The stereochemical course of the ribosome-dependent GTPase reaction of elongation factor G from Escherichia coli. J. Biol. Chem. 256, 7734-7737. (PubMed abstract)

  15. Webb, M. R. (1982): The stereochemistry of nucleoside triphosphatase reactions. Methods Enzymol. 87, 301-316. (PubMed abstract)

  16. Eccleston, J. F., and Webb, M. R. (1982): Characterization of the GTPase reaction of elongation factor Tu: determination of the stereochemical course in the presence of antibiotic X5108. J. Biol. Chem. 257, 5046-5049. (PubMed abstract)

  17. Webb, M. R., Ash, D. E., Leyh, T. S., Trentham, D. R., and Reed, G. H. (1982): Electron paramagnetic resonance studies of Mn(II) complexes with myosin subfragment 1 and oxygen-17 labeled ligands. J. Biol. Chem. 257, 3068-3072. (PubMed abstract)

  18. Webb, M. R., and Trentham, D. R. (1983): The chemical mechanism of myosin-catalyzed ATP hydrolysis. In: Peachey, L. D., Adrian, R. D., and Geiger, S. R., editors. Handbook of Physiology: Skeletal Muscle. Washington: American Physiological Soc. P. 237-255.

  19. Webb, M. R., Reed, G. H., Cooper, B. F., and Rudolph, F. B. (1984): The stereochemical course of phospho transfer catalyzed by adenylosuccinate synthetase; a reaction pathway via a phosphorylated intermediate with net inversion, J. Biol. Chem. 259, 3044-3046. (PubMed abstract)

  20. Gonzalez, M. A., Webb, M. R., Welsh, K. M., and Cooperman, B. S. (1984): Evidence that catalysis by yeast inorganic pyrophosphatase proceeds by direct phosphoryl transfer to water and not via a phosphoryl enzyme intermediate. Biochemistry 23, 797-801. (PubMed abstract)

  21. Hibberd, M. G., Webb, M. R., Goldman, Y. E., and Trentham, D. R. (1985): Oxygen exchange between phosphate and water accompanies calcium-regulated ATPase activity of skinned fibers from rabbit skeletal muscle. J. Biol. Chem. 260, 3496-3501. (PubMed abstract)

  22. Lund, J., Webb, M. R., and White, D. C. S. (1985): Oxygen exchange studies of insect fibrillar flight muscle. J. Muscle Res. Cell Motil. 6, 665-666.

  23. Goldman, Y. E., Hibberd, M. G., Webb, M. R., Dantzig, J. A., and Trentham, D. R. (1985): Pi release and the power stroke of the skeletal muscle crossbridge cycle. J. Muscle Res. Cell Motil. 6, 664-665.

  24. Kaplan, J. H., Kenney, L. J., and Webb, M. R. (1985): Phosphorylation and oxygen exchange of the red cell Na,K pump. In: Glynn, I. E. C., editor. The Sodium Pump. U.K.: The Company of Biologists Ltd. p 415-421.

  25. Mortensen, L. E., Webb, M. R., Bare, R., Cramer, S. P., and Morgan, T. V. (1985). Studies on the structure and function of the iron molybdenum protein of nitrogenase. In: Evans, H. J., Bottomley, P. Y., and Newton, W. E., editors. Nitrogen Fixation Res. Prog., Proc. 6th Int. Symp. Dordrecht, Netherlands: Nijhoff. p 577-583.

  26. Stitt, B. L., and Webb, M. R. (1986): Absence of a phosphorylated intermediate during ATP hydrolysis by E.coli transcription termination protein rho. J. Biol. Chem. 261, 15906-15909. (PubMed abstract)

  27. Webb, M. R., Hibberd, M. G., Goldman, Y. E., and Trentham, D. R. (1986): Oxygen exchange between water and medium Pi during ATP hydrolysis mediated by skinned fibers from rabbit skeletal muscle: evidence for Pi binding to a force-generating state. J. Biol. Chem. 261, 15557-15564. (PubMed abstract)

  28. Lund, J., Webb, M. R., and White, D. C. S. (1987): Changes in the ATPase mechanism of insect fibrillar flight muscle during Ca2+ and strain activation probed by phosphate-water oxygen exchange. J. Biol. Chem. 262, 8584-8590. (PubMed abstract)

  29. White, D. C. S., Ricigliano, J. W., and Webb, M. R. (1987): Analysis of the ATPase mechanism of myosin subfragment 1 from insect fibrillar flight muscle in the presence and absence of actin, using phosphate-water oxygen exchange measurements. J. Muscle Res. Cell Motil. 8, 537-540. (PubMed abstract)

  30. Lund, J., Webb, M. R., and White, D. C. S. (1988): Changes in the ATPase activity of insect fibrillar flight muscle during sinusoidal length oscillation probed by phosphate-water oxygen exchange. J. Biol. Chem. 263, 5505-5511. (PubMed abstract)

  31. Carlier, M. F., Pantaloni, D., Evans, J. A., Lambooy, P. K., Korn, E. D., and Webb, M. R. (1988): The hydrolysis of ATP that accompanies actin polymerization is essentially irreversible. FEBS Lett. 235, 211-214. (PubMed abstract)

  32. Neal, S. E., Eccleston, J. F., Hall, A., and Webb, M. R. (1988): Kinetic analysis of the hydrolysis of GTP by p21N-ras: the basal GTPase mechanism. J. Biol. Chem. 263, 19718-19722. (PubMed abstract)

  33. White, D. C. S., Lund, J., and Webb, M. R. (1988): Cross-bridge kinetics in asynchronous insect flight muscle, Adv. Exp. Med. Biol. 226, 169-179. (PubMed abstract)

  34. Feuerstein, J., Goody, R. S., and Webb, M. R. (1989): The mechanism of guanosine nucleotide hydrolysis by p21c-Ha-ras: the stereochemical course of the GTPase reaction. J. Biol. Chem. 264, 6188-6190. (PubMed abstract)

  35. Bowater, R., Webb, M. R., and Ferenczi, M. A. (1989): Measurement of the reversibility of ATP binding to myosin in calcium-activated, skinned fibers from rabbit skeletal muscle: oxygen exchange between water and ATP released to the solution. J. Biol. Chem. 264, 7193-7201. (PubMed abstract)

  36. Eccleston, J. F., Kanagasabai, T. F., Molloy, D. P., Neal, S. E., and Webb, M. R. (1989): The application of fluorescence and photosensitive analogues of guanine nucleotides to the function and structure of G-binding proteins. In: Bosch, L., Kraal, B., and Parmeggiani, A., editors. Guanine nucleotide binding proteins: common structural and functional approaches. New York: Plenum. p 87-97.

  37. Bowater, R., Zimmerman, R. W., and Webb, M. R. (1990): Kinetics of ATP and inorganic phosphate release during hydrolysis of ATP by skeletal actomyosin subfragment 1: oxygen exchange between water and ATP or phosphate. J. Biol. Chem. 265, 171-176. (PubMed abstract)

  38. Neal, S. E., Eccleston, J. F., and Webb, M. R. (1990): Hydrolysis of GTP by p21N-ras, 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. Proc. Natl. Acad. Sci. U.S.A. 87, 3562-3565. (PubMed abstract)

  39. Eccleston, J. F., Moore, K. J. M., Brownbridge, G. G., Webb, M. R., and Lowe, P. N. (1991): Fluorescence approaches to the study of the p21ras GTPase mechanism. Biochem Soc. Trans. 19, 432-437. (PubMed abstract)

  40. Webb, M. R., Lund, J., Hunter, J. L., and White, D. C. S. (1991): Kinetics of ATP release and Pi binding during the ATPase cycle of Lethocerus flight muscle fibres, using phosphate-water oxygen exchange. J. Muscle Res. Cell Motil. 12, 254-261. (PubMed abstract)

  41. Thorneley, R. N. F., Ashby, G. A., Julius, C., Hunter, J. L., and Webb, M. R. (1991): Nitrogenase of Klebsiella pneumoniae. Reversibility of the reductant-independent MgATP-cleavage reaction is shown by MgADP-catalysed phosphate/water oxygen exchange. Biochem. J. 277, 735-741. (PubMed abstract)

  42. Webb, M. R. (1992): A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc. Natl. Acad. Sci. U.S.A. 89, 4884-4887. (PubMed abstract)

  43. Webb, M. R. (1992): The role of nucleoside triphosphate hydrolysis in transducing systems: p21ras and muscle. Philosophical Transactions of the Royal Society, London B 336, 19-24. (PubMed abstract)

  44. Webb, M. R., and Hunter, J. L. (1992): Interaction of GAP with p21ras, measured using a continuous assay for inorganic phosphate release. Biochem. J. 287, 555-559. (PubMed abstract)

  45. Brownbridge, G. G., Lowe, P. N., Moore, K. J. M., Skinner, R. H., and Webb, M. R. (1993): Interaction of GTPase activating proteins (GAPs) with p21ras measured by a novel fluorescence anisotropy method. Essential role of Arg-903 of GAP in activation of GTP hydrolysis on p21ras. J. Biol. Chem. 268, 10914-10919. (PubMed abstract)

  46. Moore, K. J. M., Webb, M. R., and Eccleston, J. F. (1993): Mechanism of GTP hydrolysis by p21N-ras catalyzed by GAP: studies with a fluorescent GTP analogue. Biochemistry 32, 7451-7459. (PubMed abstract)

  47. Abo, A., Webb, M.R., Grogan, A., and Segal, A.W. (1994): Activation of NADPH oxidase involves the dissociation of p21rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to the plasma membrane. Biochem. J. 298, 585-591. (PubMed abstract)

  48. Brune, M., Hunter, J.L., Corrie, J.E.T., and Webb, M.R. (1994): Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase. Biochemistry 33, 8262-8271. (PubMed abstract)

  49. Gilbert, S.P., Webb, M.R., Brune, M., and Johnson, K.A. (1995): Pathway of processive ATP hydrolysis by kinesin. Nature 373, 671-676. (PubMed abstract)

  50. Ferenczi, M.A., He, Z.-H., Chillingworth, R.K., Brune, M., Corrie, J.E.T., Trentham, D.R., and Webb, M.R. (1995): A new method for the time-resolved measurement of phosphate release in permeabilized muscle fibers. Biophys. J. 68, 191s-193s. (PubMed abstract)

  51. Nixon, A.E., Brune, M., Lowe, P.N., and Webb, M.R. (1995): Kinetics of inorganic phosphate release during the interaction of p21ras with the GTPase activating proteins, p120-GAP and neurofibromin. Biochemistry 34, 15592-15598. (PubMed abstract)

  52. Lionne, C., Brune, M., Webb, M. R., Travers, F., and Barman, T. (1995): Time resolved measurements show that phosphate release is the rate limiting step on myofibrillar ATPases. FEBS Lett. 364, 59-62. (PubMed abstract)

  53. Lowe, D. J., Ashby, G. A., Brune, M., Knights, H., Webb, M. R., and Thorneley, R. N. F. (1995): ATP hydrolysis and energy transduction by nitrogenase. In: Tikhonovich, I. A., editor. Nitrogen fixation: fundamentals and applications. Dordrecht, The Netherlands: Kluwer Academic Publishers. p 103-108.

  54. Bershitsky, S., Tsaturyan, A., Bershitskaya, O., Mashanov, G., Brown, P., Webb, M. R., and Ferenczi, M. A. (1996): Mechanical and structural properties underlying contraction of skeletal muscle fibers after partial 1-ethyl-3-[3-dimethylamino)propyl]carbodiimide cross-linking. Biophys. J. 71, 1462-1474. (PubMed abstract)

  55. Hirshberg, M., Stockley, R. W., Dodson, G., and Webb, M. R. (1997): The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue. Nature Struct. Biol. 4, 147-152. (PubMed abstract)

  56. He, Z.-H., Chillingworth, R. K., Brune, M., Corrie, J. E. T., Trentham, D. R., Webb, M. R., and Ferenczi, M. A. (1997): ATPase kinetics on activation of rabbit and frog permeabilized isometric muscle fibres: a real time phosphate assay. J. Physiol. 501, 125-148. (PubMed abstract)

  57. White, H. D., Belknap, B., and Webb, M. R. (1997): Kinetics of nucleoside triphosphate cleavage and phosphate release steps by associated rabbit skeletal actomyosin, measured using a novel fluorescent probe for phosphate. Biochemistry 36, 11828-11836. (PubMed abstract)

  58. Barman, T., Brune, M., Lionne, C., Piroddi, N., Poggesi, C., Stehle, R., Tesi, C., Travers, F., and Webb, M. R. (1998): ATPase and shortening rates in frog fast skeletal myofibrils by time resolved measurements of protein-bound and free Pi. Biophys. J. 74, 3120-3130. (PubMed abstract)

  59. Wang, J. H., Xiao, D. G., Deng, H., Callender, R., and Webb, M. R. (1998): Vibrational study of phosphate modes in GDP and GTP and their interaction with magnesium in aqueous solution. Biospectroscopy 4, 219-227. (PubMed abstract)

  60. Brune, M., Hunter, J. L., Howell, S. A., Martin, S. R., Hazlett, T. L., Corrie, J. E. T., and Webb, M. R. (1998): Mechanism of inorganic phosphate interaction with phosphate binding protein from Escherichia coli. Biochemistry 37, 10370-10380. (PubMed abstract)

  61. Hirshberg, M., Henrick, K., Haire, L. L., Vasisht, N., Brune, M., Corrie, J. E. T., and Webb, M. R. (1998): The crystal structure of phosphate binding protein labeled with a coumarin fluorophore, a probe for inorganic phosphate. Biochemistry 37, 10381-10385. (PubMed abstract)

  62. Wang, J. H., Xiao, D. G., Deng, H., Webb, M. R., and Callender, R. (1998): Raman difference studies of GDP and GTP binding to c-Harvey ras. Biochemistry 37, 11106-11116. (PubMed abstract)

  63. Nixon, A. E., Hunter, J. L., Bonifacio, G., Eccleston, J. F., and Webb, M. R. (1998): Purine nucleoside phosphorylase: its use in a spectroscopic assay for inorganic phosphate and to remove inorganic phosphate with the aid of phosphodeoxyribomutase. Anal. Biochem. 265, 299-307. (PubMed abstract)

  64. He, Z.-H., Ferenczi, M. A., Brune, M., Trentham, D. R., Webb, M. R., Somlyo, A. P., and Somlyo, A. V. (1998) Time-resolved measurements of phosphate release by cycling cross-bridges in portal vein smooth muscle, Biophys. J. 75, 3031-3040. (PubMed abstract)

  65. Vernon, G. G., Brune, M., Webb, M. R., and Woolley, D. M. (1999): Real time detection of Pi released by flagellar dynein ATPase. Pflugers Arch. 437, 771-775. (PubMed abstract)

  66. Vandecandelaere, A., Brune, M., Webb, M. R., and Bayley, P. M. (1999): Relationship between inorganic phosphate release and microtubule assembly. Biochemistry 38, 8179-8188. (PubMed abstract)

  67. Newcombe, A. R., Stockley, R. W., Hunter, J. L., and Webb, M. R. (1999): The interaction between rac1 and its guanine nucleotide dissociation inhibitor (GDI), monitored by a single fluorescent coumarin attached to GDI. Biochemistry 38, 6879-6886. (PubMed abstract)

  68. He, Z.-H., Chillingworth, R. K., Brune, M., Corrie, J. E. T., Webb, M. R., and Ferenczi, M. A. (1999): The efficiency of contraction in rabbit skeletal muscle fibres, determined from the rate of release of inorganic phosphate. J. Physiol. 517, 839-854. (PubMed abstract)

  69. Cliff, M. J., Kad, N. M., Hay, N., Lund, P. A., Webb, M. R., Burston, S. G., and Clarke, A. R. (1999): A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL. J. Mol. Biol. 293, 667-684. (PubMed abstract)

  70. Dillingham, M. S., Wigley, D. B., and Webb, M. R. (2000): Demonstration of unidirectional single-stranded DNA translocation by pcrA helicase: measurement of step size and translocation speed. Biochemistry 39, 205-212. (PubMed abstract)

  71. Bornemann, S., Theoclitou, M.-E., Brune, M., Webb, M. R., Thorneley, R. N. F., and Abell, C. (2000): A secondary beta deuterium kinetic isotope effect in the chorismate synthase reaction. Bioorg. Chem. 28, 191-204. (PubMed abstract)

  72. Soultanas, P., Dillingham, M., Wiley, P., Webb, M. R., and Wigley, D. B. (2000): Uncoupling DNA translocation and helicase activity in pcrA: direct evidence for an active mechanism. EMBO J. 19, 3799-3810. (PubMed abstract)

  73. Brune, M., Corrie, J. E. T., and Webb, M. R. (2001): A fluorescent sensor of the phosphorylation state of nucleoside diphosphate kinase and its use to monitor nucleoside diphosphate concentrations in real time. Biochemistry 40, 5087-5094. (PubMed abstract)

  74. Dillingham, M. S., Soultanas, P., Wiley, P., Webb, M. R. and Wigley, D. B. (2001): Defining the roles of individual residues in the single stranded DNA binding site of PcrA helicase.  Proc. Natl. Acad. Sci. U.S.A. 98, 8381-8387. (PubMed abstract)

  75. Webb, M. R., and Corrie, J. E. T. (2001): Fluorescent coumarin-labeled nucleotides to measure ADP release from actomyosin. Biophys. J. 81, 1562-1569. (PubMed abstract)

  76. Dillingham, M. S., Wigley, D. B., and Webb, M. R. (2002): Direct measurement of single stranded DNA translocation by PcrA helicase using the fluorescent base analogue 2-aminopurine. Biochemistry 41, 643-651. (PubMed abstract)

  77. Shutes, A., Phillips, R. A., Corrie, J. E. T., and Webb, M. R. (2002): The role of magnesium in nucleotide exchange on the small G protein rac, investigated using novel fluorescent guanine nucleotide analogues. Biochemistry 41, 3828-3835. (PubMed abstract)

  78. Uyeda, T. Q. P., Tokuraku, K., Kaseda, K., Webb, M. R., and Patterson, B. (2002): Evidence for a novel, strongly bound acto-S1 complex carrying ADP and phosphate stabilized in the G680V mutant of Dictyostelium myosin II. Biochemistry 41, 9525-9534. (PubMed abstract)

  79. Lionne, C., Iorga, B., Candau, R., Piroddi, N., Webb, M. R., Belus, A., Travers, F., and Barman, T. (2002): Phosphate release is the rate limiting step on the ATPase of psoas myofibrils, prevented from shortening by chemical cross-linking. Biochemistry 41, 13297-13308. (PubMed abstract)

  80. Phillips, R. A., Hunter, J. L., Eccleston, J. F., and Webb, M. R. (2003): The mechanism of Ras GTPase activation by neurofibromin, Biochemistry 42, 3956-3965. (PubMed abstract)

  81. Clark, R. J., Nyitrai, M., Webb, M. R., and Geeves, M. A. (2003): Probing nucleotide dissociation from myosin in vitro using μg quantities of myosin, J. Muscle Res. Cell Motil. 24, 315-321. (PubMed abstract)

  82. Webb, M. R. (2003): A fluorescent sensor to assay inorganic phosphate. In: Johnson, K. A., editor. Kinetic analysis: a practical approach. Oxford, U.K.: Oxford University Press. p 131-152.

  83. Somlyo, A.V., Khromov, A.S., Webb, M.R., Ferenczi, M.A., Trentham, D.R., He, Z.H., Sheng, S., Shao, Z. and Somlyo, A.P. (2004): Smooth muscle myosin: regulation and properties. Phil. Trans. Royal Soc. B359, 1921-1930. (PubMed abstract)

  84. Khromov, A. S., Webb, M. R., Ferenczi, M. A., Trentham, D. R., Somlyo, A. P., and Somlyo, A. V. (2004): Myosin regulatory light chain phosphorylation and strain modulate ADP-release from smooth muscle myosin, Biophys. J. 86, 2318-2328. (PubMed abstract)

  85. Webb, M. R., Reid, G. P., Munasinghe, V. R. N., and Corrie, J. E. T. (2004): A series of related nucleotide analogues that aids optimization of fluorescence signals to probe the mechanism of P-loop ATPases, such as actomyosin, Biochemistry 43, 14463-14471. (PubMed abstract)

  86. Dillingham, M. S., Webb, M. R. and Kowalczykowski, S. C. (2005): Bipolar DNA translocation contributes to highly processive DNA unwinding by RecBCD enzyme. J. Biol. Chem. 280, 37069-37077. (PubMed abstract)

  87. Martinez-Senac, M.M. and Webb, M.R. (2005): Mechanism of translocation and kinetics of DNA unwinding by the helicase RecG. Biochemistry 44, 16967-76. (PubMed abstract)

  88. Alahyan, M., Webb, M.R., Marston, S.B. and El-Mezgueldi, M. (2006): The mechanism of smooth muscle caldesmon-tropomyosin inhibition of the elementary steps of the actomyosin ATPase. J. Biol. Chem. 281, 19433-19448. (PubMed abstract)

  89. Okoh, M.P., Hunter, J.L., Corrie, J.E.T., and Webb, M.R. (2006): A biosensor for inorganic phosphate using a rhodamine-labeled phosphate binding protein. Biochemistry 45, 14764 -14771. (PubMed abstract)

  90. Forgacs, E., Cartwright, S., Kovacs, M., Sakamoto, T., Sellers, J., Corrie, J.E.T., Webb, M.R., and White, H.D. (2006): Kinetic mechanism of myosinV-S1 using a novel fluorescent ATP analogue. Biochemistry 45, 13035-13045. (PubMed abstract)

  91. García, D.I., Lanigan, P., Webb, M.R., Isidro, J.R., Auksorius, E., Dunsby, C., Neil, M., French, P., and Ferenczi, M.A. (2007): Fluorescence lifetime imaging to detect actomyosin states in mammalian muscle sarcomeres. Biophys. J. 93, 2091-2101. (PubMed abstract)

  92. Webb, M.R. (2007): Development of fluorescent biosensors for probing the function of motor proteins. Molecular BioSystems 3, 249-256. (PubMed abstract)

  93. Forgacs, E., Cartwright, S., Sakamoto, T., Sellers, J.R., Corrie, J.E.T., Webb, M.R., and White, H.D. (2008): Kinetics of ADP dissociation from the trail and lead heads of actomyosinV following the power-stroke, J. Biol. Chem. 283, 766-773. (PubMed abstract)

  94. Sakamoto, T., Webb, M.R., Forgacs, E., White, H.D., and Sellers, J. (2008): Direct observation of the mechanochemical coupling in myosin-V during processive movement. Nature 455, 128-132. (PubMed abstract)

  95. Dillingham, M.S., Tibbles, K.L., Hunter, J.L., Bell, J.C., Kowalczykowski, S.C., and Webb, M.R. (2008): A fluorescent single-stranded DNA binding protein as a probe for sensitive, real time assays of helicase activity, Biophys. J. 95, 3330-3339. (PubMed abstract)

  96. Forgacs, E., Sakamoto, T., Cartwright, S., Belknap, B., Kovács, M., Tóth, J., Webb, M.R., Sellers, J.R., and White, H.D. (2009): The switch-1 mutation Ser217Ala converts myosinV into a low duty ratio motor, J. Biol. Chem. 284, 2138-2149. (PubMed abstract)

  97. West, T.G., G. Hild, V.B. Siththanandan, M.R. Webb, J.E.T. Corrie, and M.A. Ferenczi (2009): The time course and strain dependence of ADP release during contraction of permeabilized muscle fibers. Biophys. J. 96, 3281-3294. (PubMed abstract)

  98. Saikrishnan, K., Powell, B., Cook, N.J., Webb, M.R., and Wigley, D.B. (2009): Mechanistic basis of 5’-3’ translocation in SF1B helicases, Cell 137,849-859. (PubMed abstract)

  99. Slatter, A.F., Thomas, C.D., and Webb, M.R. (2009): PcrA helicase tightly couples ATP hydrolysis to unwinding double-stranded DNA, modulated by the replication initiator protein, RepD.  Biochemistry 48,6326–6334. (PubMed abstract)

  100. Toseland, C.P., Martinez-Senac, M.M., Slatter, A.F., and Webb, M.R. (2009): The ATPase cycle of PcrA helicase and its coupling to translocation of DNA. J. Mol. Biol. 392, 1020-1032. (PubMed abstract)

  101. Kunzelmann, S., and Webb, M.R. (2009): A biosensor for fluorescent determination of ADP with high time resolution. J. Biol. Chem. 284, 33130-33138. (PubMed abstract)

  102. Webb MR (2010): Fluorescent biosensors to investigate helicase activity. Methods Mol. Biol.587, 13-27. (PubMed abstract)

  103. Kunzelmann S, Morris C, Chavda A, Eccleston JF, Webb MR (2010): Mechanism of interaction between single-stranded DNA binding protein and DNA. Biochemistry 49, 843-852. (PubMed abstract)

  104. Toseland CP, Webb MR (2010): Fluorescence tools to measure helicase activity in real time. Methods 51, 259-268. (PubMed abstract)

  105. Kunzelmann S, Webb MR (2010): A fluorescent, reagentless biosensor for ADP based on tetramethylrhodamine-labeled ParM. ACS Chem. Biol.  5, 415-425 (PubMed abstract)

  106. Fili N, Mashanov G, Toseland CP, Batters C, Wallace MI, Yeeles JTP, Dillingham MS, Webb MR, Molloy JE (2010): Visualizing DNA unwinding by helicases at the single molecule level. Nucl. Acids Res.38, 4448-4457. (PubMed Abstract)

  107. Ibanez-Garcia D, Requejo-Isidro J, Webb MR, West T, French P, Ferenczi MA (2010): Fluorescence lifetime imaging reveals that the ATP binding site of myosin in muscle senses force. Biophys. J. 99, 2163-2169. (PubMed Abstract)

  108. Yeeles JTP, Gwynn EJ, Webb MR, Dillingham MS (2011): The AddAB helicase-nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain. Nucl. Acids Res. 39, 2271-2285. (PubMed Abstract)

  109. Toseland CP, Webb MR (2011): Fluorescent nucleoside triphosphates for single molecule enzymology. Methods Mol. Biol.778, 161-174. (PubMed Abstract)

  110. Fili N, Toseland CP, Dillingham MS, Webb MR, Molloy JE (2011): A single-molecule approach to visualize DNA unwinding, Methods Mol. Biol. 778, 193-214. (PubMed Abstract)

  111. Kunzelmann S, Webb MR (2011): Fluorescent detection of GDP in real time with the reagentless biosensor, rhodamine-ParM.  Biochem. J. 440, 43-49. (PubMed Abstract)

  112. Bickham D, West T, Webb MR, Woledge RC, Curtin NA, Ferenczi MA (2011): Millisecond-scale biochemical response to change in strain. Biophys. J. 101, 2445-2454. (PubMed Abstract)

  113. Zhou R, Kunzelmann S, Webb MR, Ha T (2011): Detecting intramolecular conformational dynamics of single molecules in short distance range with sub-nanometer sensitivity. Nano Lett.  11, 5482-5488. (PubMed Abstract)

  114. Arbore C, Lewis LM, Webb MR (2012): Kinetic mechanism of initiation by RepD as a part of asymmetric, rolling circle plasmid unwinding. Biochemistry 51, 3684-3693. (PubMed Abstract)

  115. Toseland CP, Powell B, Webb MR (2012): ATPase cycle and DNA unwinding kinetics of RecG helicase. PLOS One, 7, e38270. (PubMed Abstract)

  116. Hedgethorne K, Webb, MR (2012): Fluorescent SSB as a reagentless biosensor for single-stranded DNA. Methods Mol. Biol. 922, 219-233. (PubMed Abstract)

  117. Lallemand P, Leban N, Kunzelmann S, Chaloin L, Serpersu EH, Webb MR, Barman T, Lionne C (2012): Transient kinetics of aminoglycoside phosphotransferase(3')-IIIa reveal a potential drug target in the antibiotic resistance mechanism. FEBS Lett. 586, 4223-4227. (PubMed abstract)

  118. Webb MR, Toseland CP (2013): Helicases in Encyclopedia of Biophysics (ed. Roberts GCK), pub Springer /EBSA, 950-958.

  119. Goncalves MB,  Dreyer J, Lupieri P, Barrera-Patino C, Ippoliti E,  Webb MR, Corrie JET, Carloni P (2013): Structural prediction of a rhodamine-based biosensor and comparison with biophysical data. Phys. Chem. Chem. Phys. 15, 2177-2183. (PubMed abstract)

  120. Chisty LT, Toseland CP, Fili N, Mashanov G, Dillingham MS, Molloy JE, Webb MR (2013): Monomeric PcrA helicase processively unwinds plasmid lengths of DNA in the presence of the initiator protein RepD. Nucl. Acids Res. 41, 5010–5023. (PubMed abstract)

  121. Toseland CP, Webb MR (2013): ATPase mechanism of the 5'-3' DNA helicase, RecD2: evidence for a pre-hydrolysis conformation change.  J. Biol. Chem. 288, 25183-25193. (PubMed abstract)

  122. Kunzelmann S, Solscheid C, Webb MR (2014): Fluorescent biosensors: design and application to motor proteins. in Fluorescent Methods for Molecular Motors (Toseland CP, Fili N eds.), Springer, 25-47. (PubMed abstract)

  123. Rasheed M, Richter C, Chisty LT, Kirkpatrick J, Blackledge M, Webb MR, Driscoll PC (2014): Ligand-dependent dynamics of the active-site lid in bacterial dimethylarginine dimethylaminohydrolase, Biochemistry 53, 1092-1104. (PubMed abstract)

  124. Arnold LH, Kunzelmann S, Webb MR, Taylor IA (2015): A continuous enzyme-coupled assay for triphosphohydrolase activity of HIV-1 restriction factor SAMHD1. Antimicrob. Agents Chemother. 59, 186-192. (PubMed abstract)

  125. Solscheid C, Kunzelmann S, Davis CT, Hunter JL, Nofer A, Webb MR (2015): Development of a reagentless biosensor for inorganic phosphate, applicable over a wide concentration range. Biochemistry, 54, 5054-5062. (PubMed abstract)

  126. Vancraenenbroeck R, Webb MR (2015): A fluorescent, reagentless biosensor for ATP, based on malonyl-coenzyme A synthetase. ACS Chemical Biology. 10, 2650-2657. (PubMed abstract)

  127. Vancraenenbroeck R, Kunzelmann S, Webb MR (2017): Development of a range of fluorescent reagentless biosensors for ATP, based on malonyl-coenzyme A synthetase. PLOS One 12: e0179547 (PubMed abstract)

  128. Gu X, Yan Y, Novick SJ, Kovach A, Goswami D, Ke J, Tan MHE, Wang L, Li X, de Waal PW, Webb MR, Griffin PR, Xu HE, Melcher K (2017): Deconvoluting AMP-activated protein kinase (AMPK) adenine nucleotide binding and sensing. J Biol Chem. 292, 12653-12666. (PubMed Abstract)

  129. Edgington R, Spillane KM, Papageorgiou G, Wray W, Ishiwata H, Labarca M, Leal-Ortiz S, Reid G, Webb M, Foord J, Melosh N, Schaefer AT (2018): Functionalisation of detonation nanodiamond for monodispersed, soluble DNA-nanodiamond conjugates using mixed silane bead-assisted sonication disintegration. Scientific Reports 8, 728 (PubMed Abstract)

  130. Toleikis A, Webb MR, Molloy JE (2018): oriD structure controls RepD initiation during rolling-circle replication. Scientific Reports 8, 1206 (PubMed Abstract)

  131. Chisty LT, Quaglia D, Webb MR (2018): Fluorescent single-stranded DNA-binding protein from Plasmodium falciparum as a biosensor for single-stranded DNA. PLOS One 13: e0193272 (PubMed Abstract)

  132. Hegedüs É., Kókai E, Nánási P, Imre L, Halász L, Jossé R, Antunovics Z, Webb MR, El Hage A, Pommier Y, Székvölgyi L, Dombrádi V, Szabó G (2018). Endogenous single-strand DNA breaks at RNA polymerase II promoters in Saccharomyces cerevisiae. Nucleic Acids Research 46: 10649-10668. (PubMed Abstract)