Results 11 to 20 of about 2,706 (221)

Unc45b forms a cytosolic complex with Hsp90 and targets the unfolded myosin motor domain. [PDF]

open access: yesPLoS ONE, 2008
Myosin folding and assembly in striated muscle is mediated by the general chaperones Hsc70 and Hsp90 and a myosin specific co-chaperone, UNC45. Two UNC45 genes are found in vertebrates, including a striated muscle specific form, Unc45b.
Rajani Srikakulam   +2 more
doaj   +5 more sources

Internal Motility in Stiffening Actin-Myosin Networks [PDF]

open access: yesPhys. Rev. Lett. 93, 268101 (2004), 2003
We present a study on filamentous actin solutions containing heavy meromyosin subfragments of myosin II motor molecules. We focus on the viscoelastic phase behavior and internal dynamics of such networks during ATP depletion. Upon simultaneously using micro-rheology and fluorescence microscopy as complementary experimental tools, we find a sol-gel ...
A. G. Weeds   +10 more
arxiv   +3 more sources

Protease-sensitive regions in myosin subfragment 1. [PDF]

open access: greenProceedings of the National Academy of Sciences, 1983
Proteolytic digestions of myosin subfragment 1 (S-1) with elastase, subtilisin, papain, thermolysin, and Staphylococcus aureus protease reveal that the two trypsin-sensitive regions in S-1 have broad protease susceptibility. The cleavage of S-1 by these enzymes yields products that correspond within 1-2 kilodaltons (kDa) to the 25-, 50-, and 20-kDa ...
Emil Reisler, Dianne Applegate
openaire   +4 more sources

Flexibility of myosin rod, light meromyosin, and myosin subfragment-2 in solution. [PDF]

open access: greenProceedings of the National Academy of Sciences, 1977
Myosin rod was prepared by papain proteolysis of myosin. The components of rod, light meromyosin (LMM) and subfragment-2 (S-2), were prepared by proteolysis of myosin and rod, respectively, using trypsin treated with tosylphenylalanine chloromethyl ketone.
Manuel F. Morales   +3 more
openaire   +4 more sources

Polymerization of G-actin by myosin subfragment 1.

open access: hybridJournal of Biological Chemistry, 1988
The polymerization of actin from rabbit skeletal muscle by myosin subfragment 1 (S-1) from the same source was studied in the depolymerizing G-actin buffer. The polymerization reactions were monitored in light-scattering experiments over a wide range of actin/S-1 molar rations.
Emil Reisler   +2 more
openaire   +4 more sources

Model for processive movement of myosin V and myosin VI [PDF]

open access: yesChinese Physics, Vol.14, No.4 (2005) 744-752, 2003
Myosin V and myosin VI are two classes of two-headed molecular motors of the myosin superfamily that move processively along helical actin filaments in opposite directions. Here we present a hand-over-hand model for their processive movements. In the model, the moving direction of a dimeric molecular motor is automatically determined by the relative ...
arxiv   +1 more source

Characterization of a caldesmon fragment that competes with myosin-ATP binding to actin. [PDF]

open access: yes, 1993
The protein caldesmon inhibits actin-activated ATP hydrolysis of myosin and inhibits the binding of myosin*ATP to actin. Afragment isolated from a chymotryptic digest of caldesmon contains features of the intact molecule that make it useful as a ...
Chalovich, Joseph M.   +2 more
core   +2 more sources

Cytotoxic mAb from Rheumatic Carditis Recognizes Heart Valves and Laminin [PDF]

open access: yes, 2000
Anti-streptococcal antibodies cross-reactive with N-acetyl-bD-glucosamine (GlcNAc) and myosin are present in the sera of patients with rheumatic fever (RF). However, their role in tissue injury is not clear.
Adderson   +46 more
core   +2 more sources

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