Zobrazeno 1 - 8
of 8
pro vyhledávání: '"D. T. Zakrjevskaya"'
Publikováno v:
Biophysical Chemistry. 134:20-24
A kinetic model for dynein, a molecular motor, is considered. This model explains the oscillatory behaviour, observed by Chikako Shingyoji et al. [Ch. Shingyoji, H. Higuchi, M. Yoshimura, E. Katayama, T. Yanagida, Dynein arms are oscillatory force ge
Publikováno v:
Molecular Biology. 42:123-126
A kinetic model was proposed for dynein, a motor protein, complexed with microtubule fragments. The model explains the experimental observations of oscillatory movements in surprisingly simple axoneme fragments perfused with an ATP solution. This is
Publikováno v:
Biophysics. 52:593-597
Plasma membrane Ca2+-ATPase is the pump that extrudes calcium ions from cells using ATP hydrolysis to maintain low Ca2+ concentrations in the cell. Calmodulin stimulates Ca2+-ATPase by binding to the autoinhibitory enzyme domain, which allows the acc
Publikováno v:
Biophysics. 52:327-330
A simple kinetic model is proposed for a hysteretic enzyme with an inflow of substrate (or transported ion). There can be two steady states of activity, with an abrupt transition to the lower level. The duration of the first, activated state rather t
Publikováno v:
Biochemistry (Moscow). 70:445-448
A kinetic model for the membrane Ca2+-ATPase is considered. The catalytic cycle in the model is extended by enzyme auto-inhibition and by oscillatory calcium influx. It is shown that the conductive enzyme activity can be registered as damped or susta
Publikováno v:
Bio Systems. 104(1)
Our simple kinetic model, based on the classic “binding change mechanism”, describes the stepping kinetics for the rotary enzyme motors. The model shows that the cooperative interactions between active sites in the motor enzyme F1-ATPase induce t
Publikováno v:
Biophysical chemistry. 145(2-3)
A graphical analysis demonstrates the ability of slow substrate activation and certain types of cooperativity between the two enzyme active sites to generate sustained oscillations. The analysis allows us to estimate kinetic parameter values for whic
Publikováno v:
Biochemistry. Biokhimiia. 70(4)
A kinetic model for membrane P-type adenosine triphosphatases is considered, the main application being to the erythrocyte Ca2+-ATPase. It is shown that a simple modification of the known catalytic mechanism of the ATPase by addition of a self-inhibi