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pH-dependent 11° F 1 F o ATP synthase sub-steps reveal insight into the F o torque generating mechanism

bioRxiv (Cold Spring Harbor Laboratory)(2021)10.1101/2021.05.16.444358Source: DataRank Database

pH-dependent 11° F 1 F o ATP synthase sub-steps reveal insight into the F o torque generating mechanism is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2021). On theSindex it has a DataRank of 0. It has been cited 1 time.

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datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (2 grants)OA: greenTopics (41)IDs (PubMed, OpenAlex)SDGs (1)

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Open Access

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Authors (2)

Wayne D. Frasch ORCID,Seiga Yanagisawa

Live enrichment

PubMed:19022398 OpenAlex:https://openalex.org/W3162495149

National Science Foundation

Grant: 2119963

BII: Mechanisms of Cellular Evolution

National Institutes of Health

Grant: 5R01GM097510-02

Fo Motor Mechanisms that Power FoF1 ATP Synthesis

greenLicense: cc-by

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2021/05/17/2021.05.16.444358.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2021.05.16.444358

repositoryhttps://doi.org/10.1101/2021.05.16.444358

https://doi.org/10.7554/elife.70016

Fields of Study

ATP Synthase and ATPases ResearchMitochondrial Function and PathologyAdvanced Electron Microscopy Techniques and Applications0301 basic medicine0303 health sciences03 medical and health sciences

Keywords

ATP synthaseProtein subunitChemistryATP hydrolysisProtonRing (chemistry)ATPaseStereochemistryF-ATPaseStatorRotation (mathematics)ATP synthase gamma subunitBiophysicsCrystallographyEnzymePhysicsBiologyBiochemistryGeometryF1-ATPaseQH301-705.5ScienceStructural Biology and Molecular BiophysicsEscherichia coli ProteinsQRHydrogen-Ion Concentrationproton translocationmolecular motorProton-Translocating ATPasesEscherichia coliMedicinesingle-moleculeBiology (General)F1Fo ATP synthase

Sustainable Development Goals

SDG 0: Clean water and sanitation