Evidence map›Paper›PMID 27722332›Full record

ArticleChemical communications (Cambridge, England)2016

Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins.

Richard C Brewster, Georgina C Gavins, Barbara Günthardt, Sarah Farr, Kimberly M Webb, Philipp Voigt, Alison N Hulme

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemical communications (Cambridge, England), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

7 authors.

Richard C BrewsterEaSTCHEM School of Chemistry, The University of Edinburgh, Joseph Black Building, David Brewster Road, Edinburgh EH9 3FJ, UK. Alison.Hulme@ed.ac.uk.
Georgina C GavinsEaSTCHEM School of Chemistry, The University of Edinburgh, Joseph Black Building, David Brewster Road, Edinburgh EH9 3FJ, UK. Alison.Hulme@ed.ac.uk.
Barbara GünthardtEaSTCHEM School of Chemistry, The University of Edinburgh, Joseph Black Building, David Brewster Road, Edinburgh EH9 3FJ, UK. Alison.Hulme@ed.ac.uk.
Sarah FarrEaSTCHEM School of Chemistry, The University of Edinburgh, Joseph Black Building, David Brewster Road, Edinburgh EH9 3FJ, UK. Alison.Hulme@ed.ac.uk.
Kimberly M WebbThe Wellcome Trust Centre for Cell Biology, The University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh, EH9 3BF, UK.
Philipp VoigtThe Wellcome Trust Centre for Cell Biology, The University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh, EH9 3BF, UK.ORCID http://orcid.org/0000-0003-4366-0490
Alison N HulmeEaSTCHEM School of Chemistry, The University of Edinburgh, Joseph Black Building, David Brewster Road, Edinburgh EH9 3FJ, UK. Alison.Hulme@ed.ac.uk.ORCID http://orcid.org/0000-0002-4619-1506

Funding

Wellcome Trust 092076Wellcome Trust 104175
6 · The paper itself

Abstract

Rapid, site-selective modification of cysteine residues with chloromethyl-triazole derivatives generates pseudo-acyl sLys motifs, mimicking important post-translational modifications. Near-native biotinylation of peptide and protein substrates is shown to be site-selective and modified histone H4 retains functional activity.

Indexed as

Protein Processing, Post-TranslationalAcylationBiotinylationCysteineHistonesHumansPeptide FragmentsProteinsTriazolesCysteineHistonesPeptide FragmentsProteinsTriazoles

Identifiers

PMID27722332
PMCPMC5656099

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.