Functional importance of αAsp-350 in the catalytic sites of Escherichia coli ATP synthase.

Samah Raheem, Amanda Steiner, Zulfiqar Ahmad

Open access · greenAbstract read

In one paragraph

Article in Archives of biochemistry and biophysics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

0.5field-weighted citation impact, top 35% 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

0 citing papers in PubMed, 9 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

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

3 authors at 1 institution in 1 country.

Samah RaheemDepartment of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University of Health Sciences, 800 W. Jefferson St., Kirksville, MO, 63501, USA.

Amanda SteinerDepartment of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University of Health Sciences, 800 W. Jefferson St., Kirksville, MO, 63501, USA.

Zulfiqar AhmadDepartment of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University of Health Sciences, 800 W. Jefferson St., Kirksville, MO, 63501, USA. Electronic address: zahmad@atsu.edu.

A.T. Still University · US

Funding

Molecular Modulation of Catalytic Sites of Escherichia coli F1Fo ATP SynthaseR15GM085771 · NIGMS · EAST TENNESSEE STATE UNIVERSITY · PI AHMAD, ZULFIQAR · 2009 to 2009

$209k

NIGMS NIH HHS R15 GM085771

6 · The paper itself

Abstract

Negatively charged residue αAsp-350 of the highly conserved VISIT-DG sequence is required for Pi binding and maintenance of the phosphate-binding subdomain in the catalytic sites of Escherichia coli F

Indexed as

Adenosine DiphosphateAspartic AcidBase SequenceBiocatalysisCatalytic DomainEscherichia coliEscherichia coli ProteinsMutationPhosphatesProtein BindingProtein DomainsProton-Translocating ATPasesAdenosine DiphosphateAspartic AcidEscherichia coli ProteinsPhosphatesProton-Translocating ATPasesATPase inhibitionEscherichia coliF(1)F(o) ATP synthaseOxidative phosphorylationPi binding residues

Identifiers

PMID31330132

DOI10.1016/j.abb.2019.07.015

PMCPMC6718308

OpenAlexW2963586413

What OpenQuestion holds

Textmetadata

LicenceTDM

Read underepoch 390

Registered trials

None linked

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.