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Wang J, Barnett JT, Pollard MR, Kad NM. Integrating Optical Tweezers, DNA Tightropes, and Single-Molecule Fluorescence Imaging: Pitfalls and Traps. Methods Enzymol. 2017;582:171-192. doi: 10.1016/bs.mie.2016.08.003.

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Kad NM, Van Houten B. DNA repair: Clamping down on copy errors. Nature. 2016 Nov 24;539(7630):498-499. doi: 10.1038/nature20475.

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Kong M, Liu L, Chen X, Driscoll KI, Mao P, Böhm S, Kad NM, Watkins SC, Bernstein KA, Wyrick JJ, Min JH, Van Houten B. Single-Molecule Imaging Reveals that Rad4 Employs a Dynamic DNA Damage Recognition Process. Molecular Cell. 2016 Oct 20;64(2):376-387.

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Lin J., Countryman P., Chen H., Pan H., Fan Y., Jiang Y., Kaur P., Miao W., Gurgel G., You C., Piehler J., Kad N.M., Riehn R., Opresko P.L., Smith S., Tao Y.J., Wang H. Functional interplay between SA1 and TRF1 in telomeric DNA binding and DNA-DNA pairing. Nucleic Acids Res. 2016 Jun 13. pii: gkw518.

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Springall L., Inchingolo A.V., Kad N.M. DNA-Protein Interactions Studied Directly Using Single Molecule Fluorescence Imaging of Quantum Dot Tagged Proteins Moving on DNA Tightropes. Methods Mol Biol. 2016;1431:141-50. doi: 10.1007/978-1-4939-3631-1_11.

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Simons M, Pollard M.R., Hughes C.D., Ward A.D., Van Houten B., Towrie M., Botchway S.W., Parker A.W., Kad N.M. Directly interrogating single quantum dot labelled UvrA2 molecules on DNA tightropes using an optically trapped nanoprobe. Sci Rep. 2015 Dec 22;5:18486. doi: 10.1038/srep18486.

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Walcott S., Kad N.M. Direct Measurements of Local Coupling between Myosin Molecules Are Consistent with a Model of Muscle Activation. 2015.PLoS Comput Biol. Vol 4, No. 11:e1004599.

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Cheruvara H., Allen-Baume V.L., Kad N.M., Mason J.M. Intracellular screening of a peptide library to derive a potent peptide inhibitor of α-synuclein aggregation. Journal of Biological Chemistry. 2015 Vol 290, No. 12, 7426-35.

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Desai R., Geeves M.A., Kad N.M. Using fluorescent Myosin to directly visualize cooperative activation of thin filaments. Journal of Biological Chemistry. 2015. Vol 290, No. 4, 1915-25

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Kad NM, Van Houten B.Single molecule approaches: watching DNA repair one molecule at a time. Preface.DNA Repair (Amst), 2014, Vol 20, 1

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Acerra N, Kad N.M., Cheruvara H., Mason J.M. Intracellular selection of peptide inhibitors that target disulphide-bridged Aβ42 oligomers. Protein Science, 2014, Vol 23, No. 9, 1262-74.

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Hughes CD, Simons M, Mackenzie CE, Van Houten B, Kad NM.Single molecule techniques in DNA repair: a primer.DNA Repair (Amst), 2014, Vol 20, 2-13

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Acerra N., Kad N.M., Griffith D.A., Ott S., Crowther D.C., Mason J.M. Retro-inversal of Intracellular Selected Aβ Interacting Peptides: Implications for a Novel Alzheimer's Disease Treatment. Biochemistry, 2014, Vol. 53, No. 13, 2101-11.

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Lin J., Countryman P., Buncher N., Kaur P.E.L., Zhang Y., Gibson G., You C., Watkins S.C., Piehler J., Opresko P.L., Kad N.M., Wang H.  TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres. Nucleic Acids Research, 2013, 2014, Vol 42, No. 4, 2493-504.

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Acerra N., Kad N.M., Mason J.M. Combining Intracellular Selection with Protein-fragment Complementation to Derive Peptide Inhibitors of β-amyloid. Protein Engineering, Design and Selection, 2013, Vol. 26, No. 7, 463-470.

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Hughes C.D., Wang H., Ghodke H., Simons M., Towheed M.A., Peng Y., Van Houten B., Kad N.M. Real time single molecule imaging reveals a direct interaction between UvrC and UvrB on DNA tightropes. Nucleic Acids Research 2013 Vol. 41 No. 9 4901-12.

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Zhang C., Ali M.Y.,Warshaw D.M., Kad N.M. A Branched Kinetic Scheme Describes the Mechanochemical Coupling of Myosin Va Processivity in Response to Substrate. Biophysical Journal 2012 Vol. 103 No. 4 728-737.

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Kad N.M. and Van Houten B. Dynamics of lesion processing by bacterial nucleotide excision repair proteins. Prog Mol Biol Transl Sci. 2012;110:1-24

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Dunn A.R., Kad N.M., Nelson S.R., Warshaw D.M., Wallace S.S. Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA. Nucleic Acids Research 2011 Jun 11.

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Kad N. M., Wang H., Kennedy G. G., Warshaw D. M., Van Houten B. Collaborative Dynamic DNA Scanning by Nucleotide Excision Repair Proteins Investigated by Single- Molecule Imaging of Quantum-Dot-Labeled Proteins. Molecular Cell. 2010. Vol 37 No. 5, 702-13.

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Walcott S., Kad N.M. Theoretical prediction of run speed distribution for a molecular motor. Proceedings of the 2008 ASME international mechanical engineering congress and exposition. 2009. Vol 2, 437-446.

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Kad N. M., Trybus K. M., Warshaw D. M., Load and Pi Control Flux through the Branched Kinetic Cycle of Myosin V. Journal of Biological Chemistry. 2008. Vol 283 No. 25, 17477-84.

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Kad N. M., Patlak J. B., Fagnant P. M., Trybus K. M., Warshaw D. M., Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin. Biophysical journal. 2007. Biophysical journal, Vol 92, pp. 1623-31.

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Kad N. M., Kim S., Warshaw D. M., VanBuren P., Baker J.E. Single myosin crossbridge interactions with actin filaments regulated by troponin-tropomyosin. Proceedings of the National Academy of Sciences (USA). 2005. Vol. 102 No. 47, 16990-5.

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Kad N. M., Rovner A. S., Fagnant P. M., Joel P. B., Kennedy G. G., Patlak J. B., Warshaw D. M., Trybus K. M. A mutant heterodimeric myosin with one inactive head generates maximal displacement. Journal of Cell Biology. 2003. Vol. 162. No. 3, 481-8.

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Kad N. M., Myers S. L., Smith D. P., Smith D.A.M., Radford S. E., Thomson N. H. Hierarchical assembly of β2-microglobulin amyloid in vitro revealed by atomic force microscopy. Journal of Molecular Biology, 2003, Vol. 330, No. 4, 785-97.

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Jones S., Manning J., Kad N. M., Radford S.E. Amyloid-forming Peptides from β2-Microglobulin - Insights into the Mechanism of Fibril Formation in vitro. Journal of Molecular Biology, 2003, Vol. 325, No. 2, p. 249-257.

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Kad N.M., Thomson, N., Smith, D.P., Smith, D.A.M., Radford, S.E. β2-Microglobulin and its Deamidated Variant, N17D Form Amyloid Fibrils with a Range of Morphologies in vitro. Journal of Molecular Biology, 2001, Vol. 313, No. 3, p. 559-571.

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McParland V. J., Kad N. M., Kalverda A. P., Brown A., Kirwin-Jones P., Hunter M. G., Sunde M., Radford S. E. Partially unfolded states of β2-microglobulin and amyloid formation in vitro. Biochemistry, 2000, Vol.39, No.30, p.8735 –8746.

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Cliff M. J., Kad N. M., Hay N., Lund P. A., Webb M. R., Burston S. G., Clarke A. R. A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL. Journal of Molecular Biology, 1999, Vol.293, No.3, p.667-684.

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Kad N. M., Ranson N. A., Cliff M. J., Clarke A. R. Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings. Journal of Molecular Biology, 1998, Vol.278, No.1, p.267-278.

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Kong M, Liu L, Chen X, Driscoll KI, Mao P, Böhm S, Kad NM, Watkins SC, Bernstein KA, Wyrick JJ, Min JH, Van Houten B.