Evidence map›Paper›PMID 36806799›Full record

ReviewNature protocols2023

Posttranslational, site-directed photochemical fluorine editing of protein sidechains to probe residue oxidation state via

Patrick G Isenegger, Brian Josephson, Ben Gaunt, Matthew J Davy, Veronique Gouverneur, Andrew J Baldwin, Benjamin G Davis

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature protocols, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Review
  3. 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

7 authors at 2 institutions in 1 country.

Patrick G Isenegger *Department of Chemistry, University of Oxford, Oxford, UK.
Brian Josephson *Department of Chemistry, University of Oxford, Oxford, UK.
Ben GauntThe Rosalind Franklin Institute, Oxfordshire, UK.ORCID http://orcid.org/0000-0002-3071-7227
Matthew J DavyThe Rosalind Franklin Institute, Oxfordshire, UK.
Veronique GouverneurDepartment of Chemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-8638-5308
Andrew J BaldwinDepartment of Chemistry, University of Oxford, Oxford, UK. andrew.baldwin@chem.ox.ac.uk.
Benjamin G DavisDepartment of Chemistry, University of Oxford, Oxford, UK. ben.davis@rfi.ac.uk.ORCID http://orcid.org/0000-0002-5056-407X
University of Oxford · GBRosalind Franklin Institute · GB

Funding

RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/P026311/1RCUK | Engineering and Physical Sciences Research Council (EPSRC) V011359/1 (P)
6 · The paper itself

Abstract

The fluorination of amino acid residues represents a near-isosteric alteration with the potential to report on biological pathways, yet the site-directed editing of carbon-hydrogen (C-H) bonds in complex biomolecules to carbon-fluorine (C-F) bonds is challenging, resulting in its limited exploitation. Here, we describe a protocol for the posttranslational and site-directed alteration of native γCH

Indexed as

CysteineFluorineAmino AcidsCarbonMagnetic Resonance SpectroscopyMethionineProteinsAmino AcidsCarbonCysteineFluorineMethionineProteins

Identifiers

PMID36806799
OpenAlexW4321370025

What OpenQuestion holds

Textmetadata
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.