Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Inna N. Rybakova"'
Autor:
Brandon T. Larsen, Mariza de Andrade, Sumit Middha, Jeanne L. Theis, Timothy M. Olson, Eric D. Wieben, Inna N. Rybakova, Virginia V. Michels, Richard L. Moss, Michael T. Zimmermann, Jared M. Evans, Pamela A. Long
Publikováno v:
Human Molecular Genetics. 23:5793-5804
Locus mapping has uncovered diverse etiologies for familial atrial fibrillation (AF), dilated cardiomyopathy (DCM), and mixed cardiac phenotype syndromes, yet the molecular basis for these disorders remains idiopathic in most cases. Whole-exome seque
Publikováno v:
Proceedings of the National Academy of Sciences. 109:20437-20442
We have determined the effects of myosin binding protein-C (MyBP-C) and its domains on the microsecond rotational dynamics of actin, detected by time-resolved phosphorescence anisotropy (TPA). MyBP-C is a multidomain modulator of striated muscle cont
Publikováno v:
Journal of Biological Chemistry. 286:2008-2016
Myosin binding protein C (MyBPC) is a multidomain protein associated with the thick filaments of striated muscle. Although both structural and regulatory roles have been proposed for MyBPC, its interactions with other sarcomeric proteins remain obscu
Publikováno v:
Proceedings of the National Academy of Sciences. 106:12658-12663
Cardiac myosin binding protein C (cMyBP-C), bound to the sarcomere's myosin thick filament, plays an important role in the regulation of muscle contraction. cMyBP-C is a large multidomain protein that interacts with myosin, titin, and possibly actin.
Publikováno v:
Journal of Biological Chemistry. 281:9996-10001
This study was designed to define the molecular epitopes of dystrophin-actin interaction and to directly compare the actin binding properties of dystrophin and utrophin. According to our data, dystrophin and utrophin both bound alongside actin filame
Autor:
James M. Ervasti, Inna N. Rybakova
Publikováno v:
Journal of Biological Chemistry. 280:23018-23023
Most studies aimed at characterizing the utrophinactin interaction have focused on the amino-terminal tandem calponin homology domain. However, we recently reported evidence suggesting that spectrin-like repeats of utrophin also participate in bindin
Autor:
Edward H. Egelman, Margaret S. VanLoock, James M. Ervasti, Inna N. Rybakova, Albina Orlova, Vitold E. Galkin
Publikováno v:
The Journal of Cell Biology
Utrophin, like its homologue dystrophin, forms a link between the actin cytoskeleton and the extracellular matrix. We have used a new method of image analysis to reconstruct actin filaments decorated with the actin-binding domain of utrophin, which c
Publikováno v:
Cell Motility and the Cytoskeleton. 41:264-270
We purified actin from bovine brain by DNase I affinity chromatography in order to compare the binding of dystrophin to muscle actin with its binding to nonmuscle actin. While both beta- and gamma-nonmuscle actins are expressed in brain, Western blot
Publikováno v:
The Journal of Cell Biology
The F-actin binding and cross-linking properties of skeletal muscle dystrophin-glycoprotein complex were examined using high and low speed cosedimentation assays, microcapillary falling ball viscometry, and electron microscopy. Dystrophin-glycoprotei
Publikováno v:
Biochemical and Molecular Medicine. 58:113-121
The mechanism by which striated muscle internalizes plasmid DNA is unknown. A survey of nonnuclear membrane-associated DNA binding proteins from both skeletal and cardiac muscle revealed several sarcoplasmic reticulum restricted DNA binding species.