Evidence map›Paper›PMID 31566354›Full record

ArticleBiochemistry2019

The Crystal Structure of Dph2 in Complex with Elongation Factor 2 Reveals the Structural Basis for the First Step of Diphthamide Biosynthesis.

Michael K Fenwick, Min Dong, Hening Lin, Steven E Ealick

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.4field-weighted citation impact, top 47% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Biomolecules · 2023
    Article
  8. Article
  9. Article
  10. Structural basis of elongation factor 2 switching.Current research in structural biology · 2020
    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

4 authors at 2 institutions in 1 country.

Cornell University · USHoward Hughes Medical Institute · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
Diphthamide biosynthesisR01GM088276 · NIGMS · CORNELL UNIVERSITY · PI LIN, HENING · 2009 to 2017
$2.5M
Howard Hughes Medical InstituteNIGMS NIH HHS P30 GM124165NIGMS NIH HHS R01 GM088276
6 · The paper itself

Abstract

Elongation factor 2 (EF-2), a five-domain, GTP-dependent ribosomal translocase of archaebacteria and eukaryotes, undergoes post-translational modification to form diphthamide on a specific histidine residue in domain IV prior to binding the ribosome. The first step of diphthamide biosynthesis in archaebacteria is catalyzed by Dph2, a homodimeric radical

Indexed as

Amino Acid SequenceArchaeal ProteinsArginineCatalytic DomainCrystallography, X-RayDeoxyadenosinesHistidineMethanobrevibacterMutagenesis, Site-DirectedOxidoreductasesPeptide Elongation Factor 2Protein BindingProtein ConformationProtein DomainsThionucleosides5'-methylthioadenosineArchaeal ProteinsArginineDeoxyadenosinesdiphthamideHistidineOxidoreductasesPeptide Elongation Factor 2Thionucleosides

Identifiers

PMID31566354
PMCPMC7857147
OpenAlexW2978164973

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.