Zobrazeno 1 - 10
of 54
pro vyhledávání: '"FOF1 ATP synthase"'
Autor:
Ken Yokoyama
Publikováno v:
Frontiers in Molecular Biosciences, Vol 10 (2023)
V/A-ATPase is a rotary molecular motor protein that produces ATP through the rotation of its central rotor. The soluble part of this protein, the V1 domain, rotates upon ATP hydrolysis. However, the mechanism by which ATP hydrolysis in the V1 domain
Externí odkaz:
https://doaj.org/article/1dd0a0dd5cba444caee4e0e93bebdd00
Publikováno v:
Microbiology Spectrum, Vol 10, Iss 3 (2022)
ABSTRACT FoF1 ATP synthases produce ATP, the universal biological energy source. ATP synthase complexes on cyanobacterial thylakoid membranes use proton gradients generated either by photosynthesis or respiration. AtpΘ is an ATP synthase regulator i
Externí odkaz:
https://doaj.org/article/a74b5161524b4472872b942187313f8a
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2018 May . 115(22), 5750-5755.
Externí odkaz:
https://www.jstor.org/stable/26509926
Publikováno v:
Molecules, Vol 24, Iss 3, p 504 (2019)
F-ATP synthases use proton flow through the FO domain to synthesize ATP in the F1 domain. In Escherichia coli, the enzyme consists of rotor subunits γεc10 and stator subunits (αβ)3δab2. Subunits c10 or (αβ)3 alone are rotationally symmetric. H
Externí odkaz:
https://doaj.org/article/ef8643f45cef41e886da790a759eb0f0
Autor:
Javier eSantamaría-Gómez, Jesús A.G. Ochoa De Alda, Elvira eOlmedo-Verd, Roque eBru-Martinez, Ignacio eLuque
Publikováno v:
Frontiers in Microbiology, Vol 7 (2016)
tRNAs are charged with cognate amino acids by aminoacyl-tRNA synthetases (aaRSs) and subsequently delivered to the ribosome to be used as substrates for gene translation. Whether aminoacyl-tRNAs are channeled to the ribosome by transit within transla
Externí odkaz:
https://doaj.org/article/cb020c2d601b431c90418d9d9f131d70
Akademický článek
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Autor:
Paolo eBernardi
Publikováno v:
Frontiers in Physiology, Vol 4 (2013)
The permeability transition denotes an increase of the mitochondrial inner membrane permeability to solutes with molecular masses up to about 1,500 Da. It is presumed to be mediated by opening of a channel, the permeability transition pore (PTP), who
Externí odkaz:
https://doaj.org/article/5508b7f5d3d646e6be34b995beda8009
Publikováno v:
Molecules, Vol 24, Iss 3, p 504 (2019)
Molecules
Molecules
F-ATP synthases use proton flow through the FO domain to synthesize ATP in the F1 domain. In Escherichia coli, the enzyme consists of rotor subunits γεc10 and stator subunits (αβ)3δab2. Subunits c10 or (αβ)3 alone are rotationally symmetric. H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45ab4e07fc852d18c9c2235053e1cfb6
https://www.mdpi.com/1420-3049/24/3/504
https://www.mdpi.com/1420-3049/24/3/504
Autor:
Efimova, Iuliia
Mitochondrial ATP synthase represents the final complex of oxidative phosphorylation (OXPHOS) system located in the inner mitochondrial membrane. Its primary role is to utilize mitochondrial membrane potential (Δψm) generated by respiratory chain c
Externí odkaz:
http://www.nusl.cz/ntk/nusl-388410
Autor:
Efimova, Iuliia
Mitochondrial ATP synthase represents the final complex of oxidative phosphorylation (OXPHOS) system located in the inner mitochondrial membrane. Its primary role is to utilize mitochondrial membrane potential (Δψm) generated by respiratory chain c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______2186::013212092ee1ee3e04958e5908d08521
http://www.nusl.cz/ntk/nusl-388410
http://www.nusl.cz/ntk/nusl-388410