Evidence map›Paper›PMID 27571175›Full record

ArticleNature structural & molecular biology2016

Methyl transfer by substrate signaling from a knotted protein fold.

Thomas Christian, Reiko Sakaguchi, Agata P Perlinska, Georges Lahoud, Takuhiro Ito, Erika A Taylor, Shigeyuki Yokoyama, Joanna I Sulkowska, Ya-Ming Hou

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

47 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Review
  3. Nicotinamide-Based Covalent Inhibitors of tRNA (mACS medicinal chemistry letters · 2026
    Article
  4. Article
  5. Novel Knotted Solenoid fold with order-shifted coil arrangement leads to nontrivial 3Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Is There a Functional Role for the Knotted Topology in Protein UCH-L1?Journal of chemical information and modeling · 2024
    Article
  15. Theta-curves in proteins.Protein science : a publication of the Protein Society · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. AlphaFold predicts novel human proteins with knots.Protein science : a publication of the Protein Society · 2023
    Article
  20. Are there double knots in proteins? Prediction andFrontiers in molecular biosciences · 2023
    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

9 authors at 4 institutions in 3 countries.

Thomas ChristianDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania, USA.
Reiko SakaguchiDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania, USA.
Agata P PerlinskaCenter of New Technologies, University of Warsaw, Warsaw, Poland.
Georges LahoudDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania, USA.
Takuhiro ItoRIKEN Systems and Structural Biology Center, Yokohama, Japan.
Erika A TaylorDepartment of Chemistry, Wesleyan University, Middletown, Connecticut, USA.
Shigeyuki YokoyamaRIKEN Systems and Structural Biology Center, Yokohama, Japan.
Joanna I SulkowskaCenter of New Technologies, University of Warsaw, Warsaw, Poland.
Ya-Ming HouDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania, USA.
Thomas Jefferson University · USSystems Biology Institute · JPUniversity of Warsaw · PLWesleyan University · US

Funding

AdoMet-dependent tRNA methyl transferasesR01GM114343 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2015 to 2018
$1.3M
FUNCTIONS OF tRNA MODIFICATIONSR01GM081601 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2008 to 2011
$1.3M
Probes for a tRNA modification enzymeU01GM108972 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2015 to 2016
$603k
Probes for a tRNA modification enzymeR01GM108972 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2014 to 2014
$295k
NIGMS NIH HHS R01 GM081601NIGMS NIH HHS R01 GM108972NIGMS NIH HHS R01 GM114343NIGMS NIH HHS U01 GM108972
6 · The paper itself

Abstract

Proteins with knotted configurations, in comparison with unknotted proteins, are restricted in conformational space. Little is known regarding whether knotted proteins have sufficient dynamics to communicate between spatially separated substrate-binding sites. TrmD is a bacterial methyltransferase that uses a knotted protein fold to catalyze methyl transfer from S-adenosyl methionine (AdoMet) to G37-tRNA. The product, m

Indexed as

Escherichia coliEscherichia coli ProteinsMolecular Dynamics SimulationProtein ConformationProtein FoldingRNA, TransferS-AdenosylmethionineSubstrate SpecificitytRNA MethyltransferasesEscherichia coli ProteinsRNA, TransferS-AdenosylmethionineTrmD protein, E colitRNA Methyltransferases

Identifiers

PMID27571175
PMCPMC5429141
OpenAlexW2516486208

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.