Evidence map›Paper›PMID 34652139›Full record

ArticleBiochemistry2021

Epoxyqueuosine Reductase QueH in the Biosynthetic Pathway to tRNA Queuosine Is a Unique Metalloenzyme.

Qiang Li, Rémi Zallot, Brian S MacTavish, Alvaro Montoya, Daniel J Payan, You Hu, John A Gerlt, Alexander Angerhofer, Valérie de Crécy-Lagard, Steven D Bruner

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

9 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  7. Article
  8. Review
  9. Metal retention and replacement in QueD2 protect queuosine-tRNA biosynthesis in metal-starvedProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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

10 authors at 2 institutions in 1 country.

Qiang LiDepartment of Chemistry, University of Florida, Gainesville, Florida 32611, United States.
Rémi ZallotInstitute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Brian S MacTavishDepartment of Chemistry, University of Florida, Gainesville, Florida 32611, United States.
Alvaro MontoyaDepartment of Chemistry, University of Florida, Gainesville, Florida 32611, United States.
Daniel J PayanInstitute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
You HuDepartment of Chemistry, University of Florida, Gainesville, Florida 32611, United States.
John A GerltInstitute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID 0000-0002-5625-1218
Alexander AngerhoferDepartment of Chemistry, University of Florida, Gainesville, Florida 32611, United States.ORCID 0000-0002-8580-6024
Valérie de Crécy-LagardDepartment of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611, United States.ORCID 0000-0002-9955-3785
Steven D BrunerDepartment of Chemistry, University of Florida, Gainesville, Florida 32611, United States.ORCID 0000-0002-0522-480X
University of Florida · USUniversity of Illinois Urbana-Champaign · US

Funding

Protein/Structure CoreP01GM118303 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI GERLT, JOHN A · 2016 to 2020
$11.4M
TRANSITION STATE ANALYSIS OF ENZYMATIC REACTIONSR01GM041916 · NIGMS · YESHIVA UNIVERSITY · PI SCHRAMM, VERN L. · 1989 to 2023
$10.0M
Synthesis and function of Queuosine in BacteriaR01GM070641 · NIGMS · UNIVERSITY OF FLORIDA · PI DE CRECY-LAGARD, VALERIE A · 2006 to 2023
$5.3M
NIGMS NIH HHS P01 GM118303NIGMS NIH HHS R01 GM041916NIGMS NIH HHS R01 GM070641
6 · The paper itself

Abstract

Queuosine is a structurally unique and functionally important tRNA modification, widely distributed in eukaryotes and bacteria. The final step of queuosine biosynthesis is the reduction/deoxygenation of epoxyqueuosine to form the cyclopentene motif of the nucleobase. The chemistry is performed by the structurally and functionally characterized cobalamin-dependent QueG. However, the

Indexed as

Bacterial ProteinsCatalytic DomainIronIron-Sulfur ProteinsOxidoreductases Acting on CH-CH Group DonorsThermotoga maritimaBacterial ProteinsIronIron-Sulfur ProteinsOxidoreductases Acting on CH-CH Group Donors

Identifiers

PMID34652139
PMCPMC8884141
OpenAlexW3204984038

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.