Evidence map›Paper›PMID 37010764›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Reconstitution of the Arginyltransferase (ATE1) Iron-Sulfur Cluster.

Verna Van, Aaron T Smith

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. 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
1.1field-weighted citation impact, top 26% 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.

  1. Review
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

2 authors at 1 institution in 1 country.

Verna VanDepartment of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, MD, USA.
Aaron T SmithDepartment of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, MD, USA. smitha@umbc.edu.
University of Maryland, Baltimore County · US

Funding

Deciphering the Mechanisms of Pathogenic Ferrous Iron Acquisition and Eukaryotic Post-Translational ArginylationR35GM133497 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI Aaron T Smith · 2019 to 2026
$2.9M
NIGMS NIH HHS R35 GM133497
6 · The paper itself

Abstract

As global regulators of eukaryotic homeostasis, arginyltransferases (ATE1s) have essential functions within the cell. Thus, the regulation of ATE1 is paramount. It was previously postulated that ATE1 was a hemoprotein and that heme was an operative cofactor responsible for enzymatic regulation and inactivation. However, we have recently shown that ATE1 instead binds an iron-sulfur ([Fe-S]) cluster that appears to function as an oxygen sensor to regulate ATE1 activity. As this cofactor is oxygen-sensitive, purification of ATE1 in the presence of O

Indexed as

AminoacyltransferasesIron-Sulfur ProteinsAnimalsMiceProtein IsoformsProteolysisSaccharomyces cerevisiaeAminoacyltransferasesarginyltransferaseIron-Sulfur ProteinsProtein IsoformsAnoxic reconstitutionArginylationArginyltransferasesChemical reconstitutionFerrozine assayIron-sulfur clusters

Identifiers

PMID37010764
OpenAlexW4362500114

What OpenQuestion holds

Textmetadata
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.