The nucleotide binding affinities of two critical conformations of Escherichia coli ATP synthase.

Yunxiang Li, Neydy A Valdez, Nelli Mnatsakanyan, Joachim Weber

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In one paragraph

Article in Archives of biochemistry and biophysics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact, top 96% of its field

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 1 citations in OpenAlex.

A minimal chemo-mechanical Markov model for rotary catalysis of FNature communications · 2026
Article

4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Yunxiang LiDepartment of Chemistry and Biochemistry, Texas Woman's University, Denton, TX, 76204, USA; Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX, 79409, USA. Electronic address: yli7@twu.edu.

Neydy A ValdezDepartment of Biology, Texas Woman's University, Denton, TX, 76204, USA.

Nelli MnatsakanyanDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX, 79409, USA; School of Medicine, Yale University, New Haven, CT, 06520, USA.

Joachim WeberDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX, 79409, USA; Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX, 79430, USA. Electronic address: joachim.weber@ttu.edu.

Texas Tech University · USTexas Woman's University · US

Funding

Catalytic mechanism of F1Fo-ATP synthaseR01GM071462 · NIGMS · TEXAS TECH UNIVERSITY · PI WEBER, JOACHIM · 2004 to 2010

$1.2M

NIGMS NIH HHS R01 GM071462

6 · The paper itself

Abstract

ATP synthase is essential in aerobic energy metabolism, and the rotary catalytic mechanism is one of the core concepts to understand the energetic functions of ATP synthase. Disulfide bonds formed by oxidizing a pair of cysteine mutations halted the rotation of the γ subunit in two critical conformations, the ATP-waiting dwell (αE284C/γQ274C) and the catalytic dwell (αE284C/γL276C). Tryptophan fluorescence was used to measure the nucleotide binding affinities for MgATP, MgADP and MgADP-AlF

Indexed as

Adenosine TriphosphateEscherichia coliProtein BindingAdenosine DiphosphateCatalytic DomainEscherichia coli ProteinsModels, MolecularMutationNucleotidesOxidation-ReductionProtein ConformationAdenosine DiphosphateAdenosine TriphosphateEscherichia coli ProteinsNucleotidesATP synthaseCatalytic mechanismDisulfide crosslinkNucleotide bindingRotational catalysisTryptophan fluorescence

Identifiers

PMID33991499

DOI10.1016/j.abb.2021.108899

PMCPMC8278868

OpenAlexW3162169747

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.