Evidence map›Paper›PMID 27638883›Full record

ArticleNucleic acids research2016

Molecular basis of cobalamin-dependent RNA modification.

Daniel P Dowling, Zachary D Miles, Caroline Köhrer, Stephanie J Maiocco, Sean J Elliott, Vahe Bandarian, Catherine L Drennan

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  5. Article
  6. Article
  7. Review
  8. Cobalamin-Dependent RadicalACS bio & med chem Au · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. A New Facet of Vitamin BAnnual review of biochemistry · 2017
    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

7 authors at 4 institutions in 1 country.

Daniel P DowlingHoward Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Zachary D MilesDepartment of Chemistry, University of Utah, Salt Lake City, UT 84112, USA.
Caroline KöhrerDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Stephanie J MaioccoDepartment of Chemistry, Boston University, Boston, MA 02215, USA.
Sean J ElliottDepartment of Chemistry, Boston University, Boston, MA 02215, USA.ORCID http://orcid.org/0000-0003-0096-9551
Vahe BandarianDepartment of Chemistry, University of Utah, Salt Lake City, UT 84112, USA.
Catherine L DrennanHoward Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA cdrennan@mit.edu.
Boston University · USHoward Hughes Medical Institute · USUniversity of Utah · USMassachusetts Institute of Technology · US

Funding

CHEMISTRY-BIOLOGY INTERFACE TRAINING PROGRAMT32GM008804 · NIGMS · UNIVERSITY OF ARIZONA · PI MONTFORT, WILLIAM R. · 2003 to 2023
$3.9M
Biosynthesis of Deazapurine-Containing MetabolitesR01GM072623 · NIGMS · UNIVERSITY OF UTAH · PI BANDARIAN, VAHE · 2005 to 2017
$3.9M
Redox Reactions of the AdoMet Radical Enzyme SuperfamilyR01GM120283 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI ELLIOTT, SEAN J · 2016 to 2019
$1.3M
Mechanistic studies of thioether crosslink formation in peptidesR01GM120638 · NIGMS · UNIVERSITY OF UTAH · PI BANDARIAN, VAHE · 2016 to 2017
$695k
NIGMS NIH HHS R01 GM072623NIGMS NIH HHS R01 GM120283NIGMS NIH HHS R01 GM120638NIGMS NIH HHS T32 GM008804
6 · The paper itself

Abstract

Queuosine (Q) was discovered in the wobble position of a transfer RNA (tRNA) 47 years ago, yet the final biosynthetic enzyme responsible for Q-maturation, epoxyqueuosine (oQ) reductase (QueG), was only recently identified. QueG is a cobalamin (Cbl)-dependent, [4Fe-4S] cluster-containing protein that produces the hypermodified nucleoside Q in situ on four tRNAs. To understand how QueG is able to perform epoxide reduction, an unprecedented reaction for a Cbl-dependent enzyme, we have determined a series of high resolution structures of QueG from Bacillus subtilis Our structure of QueG bound to a tRNA

Indexed as

RNA Processing, Post-TranscriptionalAnticodonBacillus subtilisHydrogen BondingIronModels, MolecularMolecular ConformationNucleic Acid ConformationNucleoside QProtein BindingRibonucleasesRNA, BacterialRNA StabilityRNA, TransferSulfurVitamin B 12AnticodonIronnucleoside oQNucleoside QRibonucleasesRNA, BacterialRNA, TransferSulfurVitamin B 12

Identifiers

PMID27638883
PMCPMC5175355
OpenAlexW2519743213

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.