Evidence map›Paper›PMID 33532577›Full record

ArticleACS central science2021

Residue-Selective Protein C-Formylation via Sequential Difluoroalkylation-Hydrolysis.

Mateusz Imiołek, Patrick G Isenegger, Wai-Lung Ng, Aziz Khan, Véronique Gouverneur, Benjamin G Davis

Open access · diamondAbstract read
In one paragraph

Article in ACS central science, 2021. 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
2.3field-weighted citation impact, top 12% 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, 35 citations in OpenAlex.

  1. Article
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  4. Site-selectiveChemical science · 2024
    Article
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  7. Review
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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

6 authors at 1 institution in 1 country.

Mateusz ImiołekDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, United Kingdom of Great Britain and Northern Ireland.
Patrick G IseneggerDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, United Kingdom of Great Britain and Northern Ireland.
Wai-Lung NgDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, United Kingdom of Great Britain and Northern Ireland.
Aziz KhanDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, United Kingdom of Great Britain and Northern Ireland.
Véronique GouverneurDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, United Kingdom of Great Britain and Northern Ireland.
Benjamin G DavisDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, United Kingdom of Great Britain and Northern Ireland.
University of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The carbonyl group is now a widely useful, nonproteinogenic functional group in chemical biology, yet methods for its generation in proteins have relied upon either cotranslational incorporation of unnatural amino acids bearing carbonyls or oxidative conversion (chemical or enzymatic) of existing natural amino acids. If available, alternative strategies for directly adding the C=O group through C-C bond-forming C-carbonylation, particularly at currently inaccessible amino acid sites, would provide a powerful method for adding valuable reactivity and expanding possible function in proteins. Here, following a survey of methods for HCF

Identifiers

PMID33532577
PMCPMC7845020
OpenAlexW3118641445

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.