Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Marko Ušaj"'
Improved longevity of actomyosin in vitro motility assays for sustainable lab-on-a-chip applications
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-15 (2024)
Abstract In the in vitro motility assay (IVMA), actin filaments are observed while propelled by surface-adsorbed myosin motor fragments such as heavy meromyosin (HMM). In addition to fundamental studies, the IVMA is the basis for a range of lab-on-a-
Externí odkaz:
https://doaj.org/article/fe341cff723b492aac0481db0bd3cf01
Publikováno v:
International Journal of Molecular Sciences, Vol 25, Iss 12, p 6747 (2024)
Production of functional myosin heavy chain (MHC) of striated muscle myosin II for studies of isolated proteins requires mature muscle (e.g., C2C12) cells for expression. This is important both for fundamental studies of molecular mechanisms and for
Externí odkaz:
https://doaj.org/article/1c1a2a587d014a96bdf9ad96584e59e9
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-15 (2023)
Abstract Myosin expression and purification is important for mechanistic insights into normal function and mutation induced changes. The latter is particularly important for striated muscle myosin II where mutations cause several debilitating disease
Externí odkaz:
https://doaj.org/article/9f5ce61eb1af461d9eabd7e7ef8513bf
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-18 (2022)
Release of the ATP hydrolysis product orthophosphate (Pi) from the myosin active site is central in force generation but is poorly understood. Here, Moretto et al. present evidence for multistep Pi-release reconciling apparently contradictory results
Externí odkaz:
https://doaj.org/article/7192ea2e91f44302a27283b4a6501efa
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
With fluorescence based-TIRF microspectroscopy, Ušaj et al. unveil mechanistic details about the ATP turnover rates by myosin and actomyosin with enzymatic reaction pathways that were not possible to obtain from ensemble studies. This study could be
Externí odkaz:
https://doaj.org/article/a252da2be4d243cda3d351bfda7a4cbb
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 4, p 2195 (2022)
Hereditary hypertrophic cardiomyopathy (HCM), due to mutations in sarcomere proteins, occurs in more than 1/500 individuals and is the leading cause of sudden cardiac death in young people. The clinical course exhibits appreciable variability. Howeve
Externí odkaz:
https://doaj.org/article/fd6ecf1cad4c4463a7a3b1fa1ddb7afa
Prolonged function and optimization of actomyosin motility for upscaled network-based biocomputation
Autor:
Aseem Salhotra, Jingyuan Zhu, Pradheebha Surendiran, Christoph Robert Meinecke, Roman Lyttleton, Marko Ušaj, Frida W Lindberg, Marlene Norrby, Heiner Linke, Alf Månsson
Publikováno v:
New Journal of Physics, Vol 23, Iss 8, p 085005 (2021)
Significant advancements have been made towards exploitation of naturally available molecular motors and their associated cytoskeletal filaments in nanotechnological applications. For instance, myosin motors and actin filaments from muscle have been
Externí odkaz:
https://doaj.org/article/e47f906aab4f4a7e81f38ae017d6479f
Publikováno v:
International Journal of Molecular Sciences, Vol 19, Iss 7, p 1863 (2018)
In muscle, but not in single-molecule mechanics studies, actin, myosin and accessory proteins are incorporated into a highly ordered myofilament lattice. In view of this difference we compare results from single-molecule studies and muscle mechanics
Externí odkaz:
https://doaj.org/article/4a14a9c8325a48359492307ea6db8e9b
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
Communications Biology
Communications Biology
Benefits of single molecule studies of biomolecules include the need for minimal amounts of material and the potential to reveal phenomena hidden in ensembles. However, results from recent single molecule studies of fluorescent ATP turnover by myosin
Publikováno v:
Nature communications. 13(1)
Muscle contraction and a range of critical cellular functions rely on force-producing interactions between myosin motors and actin filaments, powered by turnover of adenosine triphosphate (ATP). The relationship between release of the ATP hydrolysis