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Structural and functional characterization of the myosin VI tail /Yu, Cong. January 2009 (has links)
Includes bibliographical references (p. 123-136).
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Regulation of Myo5p function by phosphorylationGrosshans, Bianka Lucretia. January 1900 (has links) (PDF)
Heidelberg, University, Diss., 2003.
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New model systems for the study of myosin-V mediated transport on biofunctionalized surfacesZhang, Junshan. January 2004 (has links) (PDF)
München, Techn. University, Diss., 2004.
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Funktionsanalyse einzelner Motormoleküle mittels der kombinierten Mikronadel-Laserfallen-TechnikRuff, Christine. January 2000 (has links) (PDF)
Hannover, Universiẗat, Diss., 2000.
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Myosin II alters the viscoelasticity and self-assembly properties of actin networksHumphrey, David Harold. January 2002 (has links)
Thesis (Ph. D.)--University of Texas at Austin, 2002. / Vita. Includes bibliographical references. Available also from UMI Company.
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Myosin II alters the viscoelasticity and self-assembly properties of actin networksHumphrey, David Harold 25 April 2011 (has links)
Not available / text
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Myosin and electrophysiological heterogeneity in cardiac muscleO'Neill, Stephen Charles. January 1987 (has links)
Thesis (Ph.D.) - University of Glasgow, 1987. / Includes bibliographical references. Print version also available.
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The Development of Potential Therapeutic Anti-Myosin S2 Peptides that Modulate Contraction and Append to the Heart Homing Adduct Tannic Acid without Noticeable Effect on Their FunctionsQadan, Motamed 05 1900 (has links)
This dissertation aimed to explore the S2 region with an attempt to modulate its elasticity in order to tune the contraction output. Two peptides, the stabilizer and destabilizer, showed high potential in modifying the S2 region at the cellular level, thus they were prepared for animal model testing. In this research, (i) S2 elasticity was studied, and the stabilizer and destabilizer peptides were built to tune contraction output through modulating S2 flexibility; (ii) the peptides were attached to heart homing adducts and the bond between them was confirmed; and (iii) it was shown that minor changes were imposed on the modulating peptides' functionality upon attaching to the heart homing adducts. S2 flexibility was confirmed through comparing it to other parts of myosin using simulated force spectroscopy. Modulatory peptides were built and computationally tested for their efficacy through interaction energy measurement, simulated force spectroscopy and molecular dynamics; these were attached to heart homing adducts for heart delivery. Interaction energy tests determined that tannic acid (TA) served well for this purpose. The stoichiometry of the bond between the TA and the modulating peptides was confirmed using mass spectroscopy. The functionality of the modulating peptides was shown to be unaltered through expansion microscopy where they located to the same position on the sarcomere with and without TA. They were also shown to cause the sarcomeres to contract similarly with and without the TA in contractility assay. Taken together, this work prepared the modulating peptides for animal model tests by attaching them to tannic acid.
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Identification of CALML4 as a Novel Component of the Intermicrovillar Adhesion Complex that Regulates Intestinal Brush Border AssemblyChoi, Myoung Soo January 2018 (has links)
No description available.
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Endogenous proteinase and myosin gelation of arrowtooth flounder (Atheresthes stomias)Visessanguan, Wonnop 02 June 1999 (has links)
Proteolytic degradation of fish flesh occurring at elevated temperatures is the
primary limitation for the commercial utilization of arrowtooth flounder (ATF).
Characterization of the autolytic activity of ATF muscle incubated at various pHs
and temperatures indicated the involvement of heat-activated proteinases active at
acidic and alkaline pHs. Further characterization of the proteinase extract from fish
muscle indicated the proteinase was more active at acidic pH than at alkaline pH in
hydrolysis of Z-Phe-Arg-NMec and all types of protein substrates tested. Based on
molecular weight and hydrolytic properties, activity peak separated on size exclusion
chromatography, or activity bands observed on activity-stained substrate gels were
presumed to be cathepsin L or like. A muscle proteinase showing similar hydrolytic
properties to a proteinase extract was purified to electrophoretic homogeneity and
subsequently confirmed by kinetic studies to be cathepsin L. Therefore, the results
clearly indicated that cathepsin L is primarily responsible for autolytic activity of
ATF muscle and surimi at the elevated temperatures.
Gelation of fish myofibrillar proteins, mainly myosin, is an important process
for surimi production. Elucidation of the gelation mechanism and the effect of
proteolysis on myosin provide information regarding protein interactions that
improve ATF product quality. Heat-induced changes in physicochemical properties
of myosin, free of endogenous proteinases, indicated myosin gelation consisted of
two processes, denaturation and aggregation. ATF myosin was shown to be
extremely sensitive to heat, resulting in denaturation at a lower temperature than
other fish myosins. Denaturation began at 25°C and was initiated by the unfolding of
the α-helical region. Following denaturation was the exposure of the hydrophobic
and sulfhydryl residues, which were subsequently involved in aggregation and the
gelation process. Changes in dynamic properties indicated ATF myosin formed a gel
in three different stages, as shown by the first increase in gel rigidity at 28°C,
followed by a decrease at 35°C and a second increase at 42°C.
A model system using ATF myosin and papain was developed to investigate
how proteolysis affects the heat-induced gelation of fish myosin. The addition of
papain decreased the onset temperature and the rate at which G' developed during
heating. DSC thermograms indicated papain significantly decreased the enthalpy
required to induce myosin denaturation with no significant changes in the onset or
the maximum temperature. Thermal denaturation kinetics indicated a decrease in
both the activation energy of the denaturation process and the denaturation rate of
myosin. Although myosin gels could be formed, structural disruption caused by
proteolysis, i.e., reduction in molecular size and loss in structural domain, resulted in
lowering of the gelling ability of myosin and rigidity of the formed gels. / Graduation date: 2000
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