Evidence map›Paper›PMID 27694803›Full record

ArticleNature chemical biology2016

Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification.

Zhewang Lin, Min Dong, Yugang Zhang, Eunyoung Alisa Lee, Hening Lin

Abstract read
In one paragraph

Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Biomolecules · 2023
    Article
  5. Yeast geneMicrobial cell (Graz, Austria) · 2023
    Article
  6. Review
  7. Article
  8. Review
  9. The asymmetric function of Dph1-Dph2 heterodimer in diphthamide biosynthesis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Article
  10. Review
  11. Article
  12. Article
  13. 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

5 authors at 1 institution in 1 country.

Zhewang LinHoward Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.ORCID http://orcid.org/0000-0003-1301-6661
Min DongHoward Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Yugang ZhangHoward Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Eunyoung Alisa LeeHoward Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Hening LinHoward Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.ORCID http://orcid.org/0000-0002-0255-2701
Howard Hughes Medical Institute · US

Funding

Diphthamide biosynthesisR01GM088276 · NIGMS · CORNELL UNIVERSITY · PI LIN, HENING · 2009 to 2017
$2.5M
NIGMS NIH HHS R01 GM088276
6 · The paper itself

Abstract

Diphthamide and the tRNA wobble uridine modifications both require diphthamide biosynthesis 3 (Dph3) protein as an electron donor for the iron-sulfur clusters in their biosynthetic enzymes. Here, using a proteomic approach, we identified Saccharomyces cerevisiae cytochrome b

Indexed as

Cytochrome-B(5) ReductaseRepressor ProteinsRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUridineCytochrome-B(5) ReductaseKTI11 protein, S cerevisiaeRepressor ProteinsRNA, TransferSaccharomyces cerevisiae ProteinsUridine

Identifiers

PMID27694803
PMCPMC5110365
OpenAlexW2529761738

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.