Search Results - "Sellers, J.R"
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1
In vitro actin filament sliding velocities produced by mixtures of different types of myosin
Published in Biophysical journal (01-04-1997)“…Using in vitro motility assays, we examined the sliding velocity of actin filaments generated by pairwise mixings of six different types of actively cycling…”
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2
Inhibition of the relative movement of actin and myosin by caldesmon and calponin
Published in The Journal of biological chemistry (05-08-1992)“…Contractile activity of myosin II in smooth muscle and non-muscle cells requires phosphorylation of myosin by myosin light chain kinase. In addition, these…”
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3
Characterization of in vitro motility assays using smooth muscle and cytoplasmic myosins
Published in The Journal of biological chemistry (05-09-1990)“…We have used two in vitro motility assays to study the relative movement of actin and myosin from turkey gizzards (smooth muscle) and human platelets. In the…”
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4
A kinase-related protein stabilizes unphosphorylated smooth muscle myosin minifilaments in the presence of ATP
Published in The Journal of biological chemistry (05-08-1993)“…An apparent paradox in smooth muscle biology is the ability of unphosphorylated myosin to maintain a filamentous structure in the presence of ATP in vivo,…”
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5
Interferometric Scattering Microscopy for the Study of Molecular Motors
Published in Methods in enzymology (2016)“…Our understanding of molecular motor function has been greatly improved by the development of imaging modalities, which enable real-time observation of their…”
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6
Caldesmon phosphorylation in intact human platelets by cAMP-dependent protein kinase and protein kinase C
Published in The Journal of biological chemistry (25-06-1991)“…Caldesmon is a calmodulin- and actin-binding protein present in both smooth and non-muscle tissue. The present study demonstrates that platelet caldesmon is a…”
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7
Reversible phosphorylation of smooth muscle myosin, heavy meromyosin, and platelet myosin
Published in The Journal of biological chemistry (25-12-1981)“…Smooth muscle myosin was purified from turkey gizzards with the 20,000-dalton light chains in the unphosphorylated state. The actin-activated MgATPase activity…”
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8
Dimerized Drosophila myosin VIIa: a processive motor
Published in Proceedings of the National Academy of Sciences - PNAS (11-04-2006)“…The molecular mechanism of processive movement of single myosin molecules from classes V and VI along their actin tracks has recently attracted extraordinary…”
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9
Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems
Published in The Journal of biological chemistry (05-07-1991)“…Caldesmon is a major calmodulin- and actin-binding protein found in smooth muscle and nonmuscle cells. Current studies suggest a vital role for this protein in…”
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10
Regulation of actomyosin interactions in Limulus muscle proteins
Published in The Journal of biological chemistry (15-02-1993)“…Contraction of striated muscle from Limulus polyphemus, the horseshoe crab, is regulated by both calcium binding to a troponin-tropomyosin-dependent thin…”
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11
Looped Actin Structures for Testing Processive Molecular Motors
Published in 2006 IEEE/NLM Life Science Systems and Applications Workshop (01-07-2006)“…A method is described for constructing looped actin filaments. Circular islands of nitrocellulose were patterned onto a microscope cover slip by micro-contact…”
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Conference Proceeding -
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Effect of phosphorylation on the binding of smooth muscle heavy meromyosin X ADP to actin
Published in The Journal of biological chemistry (25-03-1987)“…Relaxation of both smooth and skeletal muscles appears to be caused primarily by inhibition of the step associated with Pi release in the actomyosin ATPase…”
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13
Actin-dependent motility of melanosomes from fish retinal pigment epithelial (RPE) cells investigated using in vitro motility assays
Published in Cell motility and the cytoskeleton (01-06-2004)“…Melanosomes (pigment granules) within retinal pigment epithelial (RPE) cells of fish and amphibians undergo massive migrations in response to light conditions…”
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