Acanthamoeba myosin-II minifilaments assemble on a millisecond time scale with rate constants greater than those expected for a diffusion limited reaction.-Reference-Cited by-同舟云学术

Acanthamoeba myosin-II minifilaments assemble on a millisecond time scale with rate constants greater than those expected for a diffusion limited reaction.

Published:1990-03 Issue:7 Volume:265 Page:3654-3660
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Sinard J H,Pollard T D

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference26 articles.

1. Salt dependence of the kinetics of the lac repressor-operator interaction: role of nonoperator deoxyribonucleic acid (DNA) in the association reaction

2. Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM—A flexible, portable system

3. Diffusion-Controlled Macromolecular Interactions

4. Pressure-jump studies on the length-regulation kinetics of the self-assembly of myosin from vertebrate skeletal muscle into thick filament

5. Kinetics and thermodynamics of the assembly of the parallel- and antiparallel-packed sections of synthetic thick filaments of skeletal myosin: a pressure-jump study

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2. Assembly of Acanthamoeba Myosin-II Minifilaments. Definition of C-terminal Residues Required to Form Coiled-coils, Dimers, and Octamers;Journal of Molecular Biology;2005-01

3. Mts1 Regulates the Assembly of Nonmuscle Myosin-IIA;Biochemistry;2003-11-13

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