Online publications (restricted access)

Online publications (open access)

Selected Publications

  • Chavan, A. G., Swan, J., Heisler, J., Sancar, C., Erns, D. C., Fang, M., Palacios, J. G., Spangler, R. K., Bagshaw, C. R., Tripathi, S., Crosby, P., Golden, S. S., Partch, C. L. and LiWang, A. (2021) Reconstitution of an intact clock reveals mechanisms of circadian timekeeping. Science in press.
  • Labbe, A. B., Bagshaw, C. R. and Uttal, L. (2020) Inexpensive adaptations of basic microscopes for the identification of microplastic contamination using polarization and Nile Red fluorescence detection. J. Chem. Educ. 97, 4026-4032.
  • Bagshaw, C. R. (2020) A beginner's guide to flow kinetics. The Biochemist, 42, 40-44.
  • Jansson, L. I., Hentschel, J., Parks, J. W., Chang, T. R., Cheng, L., Baral, R., Bagshaw, C. R. and Stone, M. D. (2019) Telomere DNA G-quadruplex folding within actively extending human telomerase. Proc. Nat. Acad. Sci. USA, 116, 9350-9359.
  • McShan AC, Natarajan K, Kumirov VK, Flores-Solis D, Jiang J, Badstübner M, Toor JS, Bagshaw CR, Kovrigin EL, Margulies DH and Sgourakis NG (2018) Peptide exchange on MHC-I by TAPBPR is driven by a negative allostery release cycle. Nature Chem. Biol. 14, 811-820.
  • Bagshaw CR (2018) Kinetics (section editor) in Encyclopedia of Biophysics (G. C. K. Roberts and A. Watts, ed). Springer-Verlag, Berlin Heidelberg.
  • Bagshaw CR (2017) Biomolecular kinetics: a step-by-step guide. CRC Press, Taylor & Francis. ISBN 9781498727235
  • Su W, Bagshaw CR, and Burley GA (2013) Addressable and unidirectional energy transfer along a DNA three-way junction programmed by pyrrole-imidazole polyamides. Sci. Rep. 3, 1883.
  • Seward HE, Basran J, Denton R, Pfuhl M, Muskett FW and Bagshaw CR (2013) Halide and proton binding kinetics of Yellow Fluorescent Protein variants. Biochemistry, 52, 2482-2491.

  • Long X, Parks JW, Bagshaw CR and Sone MD (2013) Mechanical unfolding of human telomere G-quadruplex DNA probed by Intergrated Fluorescence and Magnetic Tweezers Spectrosopy. Nucleic Acids Research, 41, 2746-2755.
  • Bagshaw, CR (2013) Kinetics (section editor)  in Encyclopedia of Biophysics (G. C. K. Roberts, ed). Springer-Verlag, Berlin Heidelberg. pp2797.
  • 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 and Barsukov IL (2012) Asymmetric mode of Ca2+-S100A4 interaction with non-muscle myosin IIA generates nanomolar affinity required for filament remodelling. Structure, 20, 654-666.
  • Friel CT, Bagshaw CR and Howard, J. (2011) Analysing the ATP hydrolysis cycle of microtubule motors. in Microtubule Dynamics: Methods and Protocols (ed. A. Struabe), Methods in Molecular Biology 777, 177-192.
  • Su W, Schuster M, Bagshaw CR, Rant U and Burley GA (2011) Site-specific assembly of DNA-based photonic wires using programmable polyamides. Angew. Chemie - Int. Ed. 50, 2712-2715.
  • Badyal SK, Basran J, Bhanji N, Kim JW, Chavda  AP, Jung HS, Craig R, Elliott PR, Irvine AF, Barsukov IL, Kriajevska M  and Bagshaw CR (2011) The mechanism of the Ca2+-dependent interaction between S100A4 and tail fragments of non-muscle myosin heavy chain IIA  J.Mol. Biol. 450, 1004-1026.
  • Cherny D, Gooding C, Eperon GE, Coelho MB, Bagshaw CR, Smith CWJ and Eperon, IC (2010) Stoichiometry of a regulatory splicing complex revealed by single molecule analysis. EMBO J. 29, 2161-2172.
  • Frye JL, Klenchin VA, Bagshaw CR and Rayment I (2010) Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236. Biochemistry, 49, 4897-4907.
  • Seward HE. and Bagshaw CR (2009) The Photochemistry of Fluorescent Proteins; Implications for their Biological Applications. Chem. Soc. Rev. 38, 2842-2851.

  • Cherny DI, Eperon IC, Bagshaw CR. (2009) Probing complexes with single fluorophores: factors contributing to dispersion of FRET in DNA/RNA duplexes. Eur. Biophys. J. 38, 395-405.
  • Wegener KL, Basran J, Bagshaw CR, Campbell ID, Roberts GCK, Critchley DR, Barsukov I. (2008) Structural basis for the interaction between the cytoplasmic domain of  the hyaluronate receptor layilin and the talin F3 sub-domain. J. Mol. Biol. 382, 112-126.
  • Gingras AR, Basran J, Prescott A, Kriajevska M, Bagshaw CR, Barsukov IL. (2008) Crystal structure of the Ca2+-form and Ca2+-binding kinetics of metastasis-associated protein, S100A4. FEBS Lett. 582, 1651-1656.
  • Gyimesi M, Kintses B, Bodor A, Perczel A, Fischer S, Bagshaw CR, Málnási-Csizmadia A. (2008) The mechanism of the reverse recovery-step, phosphate release and actin activation of Dictyostelium myosin II. J. Biol. Chem. 283, 8153-8163.
  • El-Mezgueldi M, Bagshaw CR. (2008) The myosin family: biochemical and kinetic properties. in Myosin (ed. Coluccio, LM) Springer .pp 59-93.
  • Bagshaw CR. (2007) Journal Club: a universal glue for molecular biology. Nature. 450, 323.
  • Shi X, Basran J, Seward HE, Childs W, Bagshaw CR, Boxer SG. (2007) Anomalous Negative Fluorescence Anisotropy in Yellow Fluorescent Protein (YFP 10C): Quantitative Analysis of FRET in YFP Dimers. Biochemistry, 46, 14403-14417.
  • Lamb HK, Thompson P, Elliott C, Charles IG, Richards J, Lockyer M, Watkins N, Nichols C, Stammers DK, Bagshaw CR, Cooper A, Hawkins AR. (2007) Functional analysis of the GTPases EngA and YHBZ encoded by Salmonella typhimurium. Protein Science.16, 2391-2402.
  • Bagshaw CR. (2007) Myosin mechanochemistry. Structure, 15, 511-512.
  • Málnási-Csizmadia A, Tóth J, Pearson DS, Hetenyi C, Nyitray L, Geeves MA, Bagshaw CR, Kovács, M. (2007) Selective perturbation of the myosin recovery stroke by point mutations at the base of the lever arm affects ATP hydrolysis and phosphate release J. Biol. Chem. 282, 17658-17664.
  • Fajer PG, Gyimesi M, Málnási-Csizmadia A, Bagshaw CR, Sen KI, Song L. (2007) Myosin cleft closure by double electron electron resonance and dipolar EPR. J. Phys. Condens. Matter. 19, 285208 (10pp).
  • Kintses B, Gyimesi M, Pearson DS, Geeves MA, Zeng W, Bagshaw CR, Malnasi-Csizmadia A. (2007) Reversible movement of switch 1 loop of myosin determines actin interaction. EMBO J. 26, 265-274.
  • Bagshaw CR, Cherny D. (2006) Blinking fluorophores; what do they tell us about protein dynamics? Biochem. Soc. Trans. 34, 979-982. (pdf online with permission from Portland Press 2006)
  • Zeng W, Seward HE, Malnasi-Csizmadia A, Wakelin S, Woolley RJ, Cheema GS, Basran J, Patel TR, Rowe AJ, Bagshaw CR. (2006) Resonance Energy Transfer between Green Fluorescent Protein Variants: complexities revealed with Myosin Fusion Proteins. Biochemistry, 45, 10482-10491.
  • Málnási-Csizmadia A, Dickens JL, Zeng W, Bagshaw CR. (2005) Switch movements and the myosin crossbridge stroke. J. Muscle Res. Cell Motil., 26, 31-37.
  • McAnaney TB, Zeng W, Doe CEF, Bhanji N, Wakelin S, Pearson DS, Abbyad P, Shi X, Boxer SG, Bagshaw CR. (2005) Protonation, photobleaching and photoactivation of Yellow Fluorescent Protein (YFP 10C): a unifying mechanism. Biochemistry 44, 5510-5524.
  • Zeng W, Conibear PB, Dickens JL, Cowie RA, Wakelin S, Málnási-Csizmadia A, Bagshaw CR. (2004) Dynamics of actomyosin interactions in relation to the crossbridge cycle. Phil. Trans. R. Soc Lond. B Biol Sci., 359, 1843-1855.
  • Conibear PB, Málnási-Csizmadia A, Bagshaw CR. (2004) 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, 15404-15417.
  • Conibear PB, Bagshaw CR, Fajer PG, Kovács M, Málnási-Csizmadia A. (2003) Myosin cleft movement and its coupling to actomyosin dissociation. Nature Struct. Biol. 10, 831-835.
  • Bagshaw CR. (2003) Single Molecule Enzymology: what can it tell us? The Biochemist 25 (4), 24-27.
  • Barsukov IL, Prescot A, Bate N, Patel B, Floyd DN, Bhanji N, Bagshaw CR, Letinic K, Paolo G, De Camilli P, Roberts GCK, Critchley DR. (2003) PIP kinase type 1g and b1-integrin cytoplasmic domain bind to the same region in the talin FERM domain. J. Biol. Chem. 278, 31202-31209.
  • Wakelin S, Conibear PB, Woolley RJ, Floyd DN, Bagshaw CR, Kovács M, Málnási-Csizmadia A. (2003) Engineering Dictyostelium discoideum myosin II for the introduction of site-specific probes. J. Muscle Res. Cell Motil., 23, 673-683.
  • Wakelin S, Bagshaw CR. (2003) A prism combination for near isotropic fluorescence excitation by total internal reflection. J. Microscopy, 209, 143-148.
  • Kovács M, Málnási-Csizmadia A, Woolley RJ, Bagshaw CR. (2002) Analysis of nucleotide binding to Dictyostelium myosin II motor domains containing a single tryptophan near the active site. J. Biol. Chem., 277, 28459-28467.
  • Málnási-Csizmadia A, Pearson DS, Kovács M, Woolley RJ, Geeves MA, Bagshaw CR. (2001) Kinetic resolution of a conformational change and the ATP hydrolysis step using relaxation methods with a Dictyostelium myosin II mutant containing a single tryptophan residue. Biochemistry, 40, 12727-12737.
  • Málnási-Csizmadia A, Kovács M, Woolley RJ, Botchway SW, Bagshaw CR. (2001) The dynamics of the relay loop tryptophan residue in the Dictyostelium myosin motor domain and the origin of spectroscopic signals. J. Biol. Chem., 276, 19483-19490.
  • Málnási-Csizmadia A, Woolley RJ, Bagshaw CR. (2000) 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, 16135-16146.
  • Bagshaw CR. (2001) ATP analogues at a glance. J. Cell Science, 114, 459-460.
  • Bagshaw CR, Conibear PB. (2000) Single molecule enzymology: critical aspects exemplified by myosin ATPase activity. Single Molecules, 1, 269-275.
  • Conibear PB, Bagshaw CR. (2000) Comparison of optical geometries for combined flash photolysis and total internal reflection fluorescence microscopy. J. Microscopy, 200, 217-228.
  • Shirakawa I, Chaen S, Bagshaw CR, Sugi H. (2000) Measurement of nucleotide exchange rate constants in single rabbit soleus myofibrils during shortening and lengthening using a fluorescent analog. Biophys. J., 78, 918-926.
  • Conibear PB, Bagshaw CR. (2000) Myosin monomer density and exchange in synthetic thick filaments investigated using fluorescence microscopy with single molecule sensitivity. Proc. Roy. Soc. B (London), 267, 415-421.
  • Bakolitsa C, de Pereda JM, Bagshaw CR, Critchley DR, Liddington RC. (1999) Crystal structure of the vinculin tail suggests a pathway for activation. Cell, 99, 603-613.
  • Conibear PB, Kuhlman PA, Bagshaw CR. (1998) Measurement of ATPase activities of myosin at the level of tracks and single molecules. Advances in Experimental Medicine and Biology, 453, 15-27.
  • Bauer CB, Kuhlman PA, Bagshaw CR, Rayment I. (1997). X-ray crystal structure and solution fluorescence characterization of Mg.2'(3')-O-(N-methylanthraniloyl) nucleotides bound to the Dictyostelium discoideum myosin motor domain. J. Mol. Biol., 274, 394-407.
  • Ellis J, Bagshaw CR, Shaw WV. (1995) Tryptophan fluorescence of chloramphenicol acetyltransferase: resolution of individual excited-state lifetimes by site-directed mutagenesis and multifrequency phase fluorimetry. Biochemistry, 34, 3513.
  • Bagshaw CR. (1993) Muscle Contraction. 2nd edition Chapman & Hall, London & New York, 155 pp.3520.
  • Citi S, Cross RA, Bagshaw CR, Kendrick-Jones J. (1989) Parallel modulation of brush border myosin conformation and enzyme activity induced by monoclonal antibodies. J. Cell Biol. 09, 549-556.
  • Walmsley AR, Bagshaw CR. (1989) A logarithmic timebase for stopped-flow data aquisition and analysis. Anal. Biochem. 176, 313-318.
  • Jackson AP, Bagshaw CR. (1988) Transient kinetic studies of the adenosine triphosphatase activity of scallop heavy meromyosin. Biochem. J. 251, 515-526.
  • Wells C, Bagshaw CR. (1985) Calcium regulation of molluscan myosin ATPase in the absence of actin. Nature 313, 696-697.
  • Bagshaw CR, Kendrick-Jones J. (1979) The characterization of homologous divalent metal-ion binding sites of vertebrate and molluscan myosins using electron paramagnetic resonance spectroscopy. J. Mol. Biol. 130, 317-336.
  • Bagshaw CR. (1977) On the location of the divalent metal ion binding sites and the light chain subunits of vertebrate myosin. Biochemistry, 16, 59-67.
  • Trentham DR, Eccleston JF, Bagshaw CR. (1976) Kinetic analysis of ATPase mechanisms. Quart. Rev. Biophys. 9, 217-281.
  • Bagshaw CR, Trentham DR, Wolcott RG, Boyer PD. (1975) Oxygen exchange in the gamma-phosphoryl group of protein bound ATP during the Mg2+-dependent adenosine triphosphatase activity of myosin. Proc. Nat. Acad. Sci. USA 72, 2592-2596.
  • Bagshaw CR, Eccleston JF, Eckstein F, Goody RS, Gutfreund H, Trentham DR. (1974) The Mg2+-dependent adenosine triphosphatase of myosin; Two step processes of ATP association and ADP dissociation. Biochem. J. 141, 351-364.
  • Bagshaw CR, Eccleston JF, Trentham DR, Yates DW, Goody RS. (1972) Transient kinetic studies of the Mg2+-dependent ATPase of myosin and its proteolytic subfragments. Cold Spring Harbor Symp. Quant. Biol. 37, 127-135.

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