Výsledky vyhledávání - "Yuri E. Nesmelov"

Akademický článek

The Local Environment of Loop Switch 1 Modulates the Rate of ATP-Induced Dissociation of Human Cardiac Actomyosin

Publikováno v: International Journal of Molecular Sciences, Vol 23, Iss 3, p 1220 (2022)

Two isoforms of human cardiac myosin, alpha and beta, share significant sequence similarities but show different kinetics. The alpha isoform is a faster motor; it spends less time being strongly bound to actin during the actomyosin cycle. With alpha

Externí odkaz: https://doaj.org/article/0a099f7826154ce9a33be8c4be2393df

Zobrazit plný text záznamu

Plný text ve formátu HTML

Loop 1 of human cardiac myosin regulates the rate of ATP induced actomyosin dissociation but not the rate of ADP release

Autor: Akhil Gargey Iragavarapu, Yuri E. Nesmelov

Double mutation D208Q:K450L was introduced in the beta isoform of human cardiac myosin to remove the salt bridge D208:K450 connecting loop 1 and the seven-stranded beta sheet within the myosin head. Beta isoform-specific salt bridge D208:K450 was pre

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fa2cf24d9a4500aa212ab8a8d96d52ae
https://doi.org/10.1101/2021.10.08.463735

Zobrazit plný text záznamu

Electrostatic interaction of loop 1 and backbone of human cardiac myosin regulates the rate of ATP induced actomyosin dissociation

Autor: Yuri E. Nesmelov, Akhil Gargey

Publikováno v: J Muscle Res Cell Motil

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ff0cf253650a2724c6135688284111f
https://pubmed.ncbi.nlm.nih.gov/34825297

Zobrazit plný text záznamu

Electrostatic interactions in the force-generating region of the human cardiac myosin modulate ADP dissociation from actomyosin

Autor: Yuri E. Nesmelov, Jinghua Ge, Akhil Gargey, Yaroslav V. Tkachev

Publikováno v: Biochemical and Biophysical Research Communications. 509:978-982

Human cardiac myosin has two isoforms, alpha and beta, sharing significant sequence similarity, but different in kinetics: ADP release from actomyosin is an order of magnitude faster in the alpha myosin isoform. Apparently, small differences in the s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb219f2bcc4b6625a221179d050f707d
https://doi.org/10.1016/j.bbrc.2019.01.045

Zobrazit plný text záznamu

Electrostatic interactions in the SH1-SH2 helix of human cardiac myosin modulate the time of strong actomyosin binding

Autor: Shiril Bhardwaj Iragavarapu, Alexander V. Grdzelishvili, Akhil Gargey, Yuri E. Nesmelov

Publikováno v: J Muscle Res Cell Motil

Two single mutations, R694N and E45Q, were introduced in the beta isoform of human cardiac myosin to remove permanent salt bridges E45:R694 and E98:R694 in the SH1-SH2 helix of the myosin head. Beta isoform-specific bridges E45:R694 and E98:R694 were

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc9d580c0c27444f6a506dd39dc13f9d
https://europepmc.org/articles/PMC7956043/

Zobrazit plný text záznamu

The time of strong actomyosin binding depends on electrostatic interactions within the force generating region in human cardiac myosin

Autor: Shiril Bhardwaj Iragavarapu, Yuri E. Nesmelov, Alexander V. Grdzelishvili, Akhil Gargey Iragavarapu

Two single mutations, R694N and E45Q, were introduced in the beta isoform of human cardiac myosin to remove permanent salt bridges E45:R694 and E98:R694 in the force-generating region of myosin head. Beta isoform-specific bridges E45:R694 and E98:R69

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::125e0f3754361a0b2932b1017e4b8d15

Zobrazit plný text záznamu

Metal cation controls phosphate release in the myosin ATPase

Autor: Jinghua Ge, Yuri E. Nesmelov, Furong Huang

Publikováno v: Protein Science. 26:2181-2186

Myosin is an enzyme that utilizes ATP to produce a conformational change generating a force. The kinetics of the myosin reverse recovery stroke depends on the metal cation complexed with ATP. The reverse recovery stroke is slow for MgATP and fast for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d5fbf06f4ab006de642f79dc2be7b0b6
https://doi.org/10.1002/pro.3267

Zobrazit plný text záznamu

CaATP prolongs strong actomyosin binding and promotes futile myosin stroke

Autor: Jinghua Ge, Yuri E. Nesmelov, A. G. Iragavarapu, Irina V. Nesmelova

Publikováno v: J Muscle Res Cell Motil

Calcium plays an essential role in muscle contraction, regulating actomyosin interaction by binding troponin of thin filaments. There are several buffers for calcium in muscle, and those buffers play a crucial role in the formation of the transient c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d20f8579f12ac66802b57323f0df2e2
https://doi.org/10.1101/756627

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání