|1.||Masuda, Tadashi: 1 article (06/2015)|
|2.||Clobes, Amy M: 1 article (04/2014)|
|3.||Guilford, William H: 1 article (04/2014)|
|4.||Sellers, James R: 1 article (01/2013)|
|5.||Nagy, Attila: 1 article (01/2013)|
|6.||Homsher, Earl: 1 article (01/2013)|
|7.||Billington, Neil: 1 article (01/2013)|
|8.||Wang, Aibing: 1 article (01/2013)|
|9.||Sun, Sara A: 1 article (01/2013)|
|10.||Takagi, Yasuharu: 1 article (01/2013)|
|1.||Dehydration (Water Stress)
|2.||Muscular Diseases (Myopathy)
05/25/2012 - "The in vivo investigation of these mutant phenotypes in IFM development and function provides a useful platform for studying myosin rod and thick filament formation generically, with application to the aetiology of human myosin rod myopathies."
01/01/2013 - "In vitro studies on the effects of different mutations associated with myosin storage myopathy and Laing distal myopathy indicate altered biochemical and biophysical properties of the light meromyosin, which is essential for thick filament assembly. "
12/09/2011 - "While mutations in the myosin subfragment 1 motor domain can directly disrupt the generation and transmission of force along myofibrils and lead to myopathy, the mechanism whereby mutations in the myosin rod influences mechanical function is less clear. "
|3.||Distal Myopathies (Distal Muscular Dystrophy)
|4.||Osteosarcoma (Osteogenic Sarcoma)
06/01/2015 - "Molecular dynamics simulation for the reversed power stroke motion of a myosin subfragment-1."
01/04/2013 - "Using optical tweezers we found that the power stroke sizes of single- and double-headed heavy meromyosin (HMM) were each ~6 nm. No signs of processive stepping at the single molecule level were observed in the case of NMIIB-HMM in optical tweezers or TIRF/in vitro motility experiments. "
01/19/1999 - "Observation of transient disorder during myosin subfragment-1 binding to actin by stopped-flow fluorescence and millisecond time resolution electron cryomicroscopy: evidence that the start of the crossbridge power stroke in muscle has variable geometry."
09/01/1998 - "We found that rabbit heavy meromyosin produced a working stroke of 5.5 nm, and cross-bridge stiffness (kappa xb) was 0.69 +/- 0.47 pN nm-1."
04/01/1995 - "A persistent problem with the rotating cross-bridge model for muscle contraction has been the inability to detect any large conformational changes within the myosin molecule to account for a working stroke of 5-10 nm. The recent crystal structure of myosin subfragment-1 suggests a solution to this problem by showing the presence of two distinct domains: a catalytic or motor domain, from which extends a long, 8.5-nm alpha-helix that is stabilized by the regulatory and essential light chains. "
|1.||Polyethylene Glycols (Polyethylene Glycol)
|2.||Adenosine Triphosphatases (ATPase)
|10.||Actins (F Actin)