Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Si-Kao Guo"'
Publikováno v:
PLoS Computational Biology, Vol 18, Iss 3, p e1009969 (2022)
Clathrin-coated structures must assemble on cell membranes to internalize receptors, with the clathrin protein only linked to the membrane via adaptor proteins. These structures can grow surprisingly large, containing over 20 clathrin, yet they often
Externí odkaz:
https://doaj.org/article/eca754f7ade44519805ba3b06765e7d4
Publikováno v:
FEBS Open Bio, Vol 8, Iss 8, Pp 1332-1351 (2018)
Kinesin‐1 is a homodimeric motor protein that can move along microtubule filaments by hydrolyzing ATP with a high processivity. How the two motor domains are coordinated to achieve such high processivity is not clear. To address this issue, we comp
Externí odkaz:
https://doaj.org/article/bc1edc7c63b9441e9b178f5b7260b713
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 19, p 4911 (2019)
A general kinetic model is presented for the chemomechanical coupling of dimeric kinesin molecular motors with and without extension of their neck linkers (NLs). A peculiar feature of the model is that the rate constants of ATPase activity of a kines
Externí odkaz:
https://doaj.org/article/1646b871286947e2b352dca396e2e03f
Publikováno v:
Molecules, Vol 24, Iss 2, p 287 (2019)
Kinesin-1, kinesin-2 and kinesin-5 are three families of a superfamily of motor proteins; which can walk processively on microtubule filaments by hydrolyzing ATP. It was experimentally shown that while the three kinesin dimers show similar feature on
Externí odkaz:
https://doaj.org/article/ef1ded57191142c8ab0afc2991a60f96
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-14 (2019)
Scientific Reports
Scientific Reports
Kinesin-3 and kinesin-1 molecular motors are two families of the kinesin superfamily. It has been experimentally revealed that in monomeric state kinesin-3 is inactive in motility and cargo-mediated dimerization results in superprocessive motion, wit
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 88:545-557
Kinesin dimer walks processively along a microtubule (MT) protofilament in a hand-over-hand manner, transiting alternately between one-head-bound (1HB) and two-heads-bound (2HB) states. In 1HB state, one head bound by adenosine diphosphate (ADP) is d
Clathrin-coated structures must assemble on cell membranes to perform their primary function of receptor internalization. These structures show marked plasticity and instability, but what conditions are necessary to stabilize against disassembly have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cfecc3ef79e6b51e98107db6c7c0d8c9
https://doi.org/10.1101/2021.04.19.440502
https://doi.org/10.1101/2021.04.19.440502
Publikováno v:
FEBS Open Bio
Kinesin-1 is a homodimeric motor protein that can move along microtubule filaments by hydrolyzing ATP with a high processivity. How the two motor domains are coordinated to achieve such high processivity is not clear. To address this issue, we comput
Publikováno v:
International Journal of Biological Macromolecules. 105:1126-1137
Conventional kinesin (kinesin-1) can walk on microtubule filaments in an asymmetric hand-over-hand manner, exhibiting a marked alternation in the mean dwell time in successive steps. Here, we study computationally the asymmetric stepping dynamics of
Publikováno v:
Journal of chemical information and modeling. 59(1)
A model is presented for the chemomechanical coupling of kinesin motors, which proposes that the rate constants of the chemical reaction are independent of the external force. On the basis of the model, we study theoretically the movement dynamics of