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Structure (London, England : 1993)|December 3, 2014
Structure of the microtubule-binding domain of flagellar dyneinYusuke S Kato, Toshiki Yagi, Sarah A Harris, et al.Journal of Molecular Biology|April 17, 2018
A1603P and K1617del, Mutations in β-Cardiac Myosin Heavy Chain that Cause Laing Early-Onset Distal Myopathy, Affect Secondary Structure and Filament Formation In Vitro and In VivoFrancine Parker, Matthew Batchelor, Marcin Wolny, et al.The Journal of Biological Chemistry|August 15, 2014
Stable single α-helices are constant force springs in proteinsMarcin Wolny, Matthew Batchelor, Peter J Knight, et al.Nature|July 14, 2006
The cargo-binding domain regulates structure and activity of myosin 5Kavitha Thirumurugan, Takeshi Sakamoto, John A Hammer, et al.Methods in Molecular Biology (Clifton, N.J.)|July 5, 2018
Determining Stable Single Alpha Helical (SAH) Domain Properties by Circular Dichroism and Atomic Force MicroscopyMatthew Batchelor, Marcin Wolny, Marta Kurzawa, et al.Biochemical and Biophysical Research Communications|December 7, 2007
Calcium and cargoes as regulators of myosin 5a activityJames R Sellers, Kavitha Thirumurugan, Takeshi Sakamoto, et al.The Journal of Biological Chemistry|September 20, 2013
Cardiomyopathy mutations in the tail of β-cardiac myosin modify the coiled-coil structure and affect integration into thick filaments in muscle sarcomeres in adult cardiomyocytesMarcin Wolny, Melanie Colegrave, Lucy Colman, et al.Biochemical Society Transactions|January 27, 2015
Myosin tails and single α-helical domainsMatthew Batchelor, Marcin Wolny, Lorna Dougan, et al.Proceedings of the National Academy of Sciences of the United States of America|March 31, 2010
Myosin complexed with ADP and blebbistatin reversibly adopts a conformation resembling the start point of the working strokeBalázs Takács, Neil Billington, Máté Gyimesi, et al.The Journal of Biological Chemistry|November 25, 2003
Regulated conformation of myosin VFei Wang, Kavitha Thirumurugan, Walter F Stafford, et al.Pageof 5