Evidence map›Paper›PMID 25530835›Full record

ArticleChemical science2015

Structural study of a small molecule receptor bound to dimethyllysine in lysozyme.

Róise E McGovern, Brendan D Snarr, Joseph A Lyons, James McFarlane, Amanda L Whiting, Irina Paci, Fraser Hof, Peter B Crowley

Open access · hybridAbstract read
In one paragraph

Article in Chemical science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.4field-weighted citation impact, top 4% 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

14 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Facile Fabrication of Protein-Macrocycle Frameworks.Journal of the American Chemical Society · 2021
    Article
  7. Review
  8. NMR Spectroscopy of supramolecular chemistry on protein surfaces.Beilstein journal of organic chemistry · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Supramolecular Chemistry Targeting Proteins.Journal of the American Chemical Society · 2017
    Article
  13. Article
  14. 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

8 authors at 3 institutions in 2 countries.

Róise E McGovernSchool of Chemistry, National University of Ireland Galway, University Road, Galway, Ireland.
Brendan D SnarrDepartment of Chemistry, University of Victoria, British Columbia, V8W 3V6, Canada.
Joseph A LyonsSchool of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland.
James McFarlaneDepartment of Chemistry, University of Victoria, British Columbia, V8W 3V6, Canada.
Amanda L WhitingDepartment of Chemistry, University of Victoria, British Columbia, V8W 3V6, Canada.
Irina PaciDepartment of Chemistry, University of Victoria, British Columbia, V8W 3V6, Canada.
Fraser HofDepartment of Chemistry, University of Victoria, British Columbia, V8W 3V6, Canada.
Peter B CrowleySchool of Chemistry, National University of Ireland Galway, University Road, Galway, Ireland.
University of Victoria · CAOllscoil na Gaillimhe – University of Galway · IETrinity College Dublin · IE

Funding

Membrane Proteins. Crystallogenesis/X-ray Structure(RMI)R01GM075915 · NIGMS · UNIVERSITY OF LIMERICK · PI CAFFREY, MARTIN D. · 2005 to 2009
$984k
NIGMS NIH HHS R01 GM075915
6 · The paper itself

Abstract

Lysine is a ubiquitous residue on protein surfaces. Post translational modifications of lysine, including methylation to the mono-, di- or trimethylated amine result in chemical and structural alterations that have major consequences for protein interactions and signalling pathways. Small molecules that bind to methylated lysines are potential tools to modify such pathways. To make progress in this direction, detailed structural data of ligands in complex with methylated lysine is required. Here, we report a crystal structure of

Indexed as

Dimethyl lysineMethylationProtein interactionsSynthetic receptor

Identifiers

PMID25530835
PMCPMC4266562
OpenAlexW2150827040

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.