Orientation of actin monomers in moving actin filaments.
Adv Exp Med Biol. 1993.
PMID: 8109346
Review.
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Orientation of actin monomers in moving actin filaments.
Kinosita K Jr, Suzuki N, Ishiwata S, Nishizaka T, Itoh H, Hakozaki H, Marriott G, Miyata H.
Kinosita K Jr, et al.
Adv Exp Med Biol. 1993;332:321-8; discussion 329. doi: 10.1007/978-1-4615-2872-2_31.
Adv Exp Med Biol. 1993.
PMID: 8109346
Review.
We have visualized, under an optical microscope, the orientations of actin monomers in individual actin filaments undergoing Brownian motion in solution, actively sliding past myosin molecules, or immobile on a surface. ...Within our temporal re …
We have visualized, under an optical microscope, the orientations of actin monomers in individual actin filam …
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Molecular dynamics simulation of a myosin subfragment-1 docking with an actin filament.
Masuda T.
Masuda T.
Biosystems. 2013 Sep;113(3):144-8. doi: 10.1016/j.biosystems.2013.06.001. Epub 2013 Jun 19.
Biosystems. 2013.
PMID: 23791790
Clinical Trial.
After 30 ns of MD simulations, in three cases out of ten trials on average, the myosin made a close contact with two actin monomers by changing the positions and the orientation of both the myosin and the actin as predicted in previous studies. ...If t …
After 30 ns of MD simulations, in three cases out of ten trials on average, the myosin made a close contact with two actin monomer …
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Adsorption of actin at the air-water interface: a monolayer study.
Gicquaud C, Chauvet JP, Grenier G, Tancrède P, Coulombe G.
Gicquaud C, et al.
Biopolymers. 2003 Oct;70(3):289-96. doi: 10.1002/bip.10475.
Biopolymers. 2003.
PMID: 14579302
No collapse occurs. Actin monomers in the presence of magnesium become activated; at concentrations greater than some critical value, actin polymerizes to form filaments of F-actin. The actin filaments have a higher surface activit …
No collapse occurs. Actin monomers in the presence of magnesium become activated; at concentrations greater than some critical …
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Intrastrand cross-linked actin between Gln-41 and Cys-374. III. Inhibition of motion and force generation with myosin.
Kim E, Bobkova E, Miller CJ, Orlova A, Hegyi G, Egelman EH, Muhlrad A, Reisler E.
Kim E, et al.
Biochemistry. 1998 Dec 22;37(51):17801-9. doi: 10.1021/bi981286b.
Biochemistry. 1998.
PMID: 9922146
Structural and functional properties of intrastrand, ANP (N-(4-azido-2-nitrophenyl)-putrescine) cross-linked actin filaments, between Gln-41 and Cys-374 on adjacent monomers, were examined for several preparations of such actin. ...Filaments mad …
Structural and functional properties of intrastrand, ANP (N-(4-azido-2-nitrophenyl)-putrescine) cross-linked actin filaments, …
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