Evidence map›Paper›PMID 42775918›Full record

ArticleChembiochem : a European journal of chemical biology2026

Synthesis and In Vivo Incorporation of 4-Difluoromethyl-L-Phenylalanine Into Proteins.

Daniel S Honeycutt, Jason M Mrosla, Sarah A Sexton, Giovanni E Cavalli, Emmerson G Bartels, Brian Pallares, William K McCarthy, Ruojun Wu, Fang Wang, Jacob M Goldberg

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Daniel S HoneycuttDepartment of Chemistry, University of Rhode Island, Kingston, Rhode Island, USA.
Jason M MroslaDepartment of Chemistry, Colgate University, Hamilton, New York, USA.ORCID https://orcid.org/0009-0001-1957-355X
Sarah A SextonDepartment of Chemistry, Colgate University, Hamilton, New York, USA.ORCID https://orcid.org/0009-0008-4008-8664
Giovanni E CavalliDepartment of Chemistry, Colgate University, Hamilton, New York, USA.ORCID https://orcid.org/0009-0003-2259-8330
Emmerson G BartelsDepartment of Chemistry, Colgate University, Hamilton, New York, USA.ORCID https://orcid.org/0009-0000-6014-3802
Brian PallaresDepartment of Chemistry, Colgate University, Hamilton, New York, USA.ORCID https://orcid.org/0009-0003-8651-7392
William K McCarthyDepartment of Chemistry, Colgate University, Hamilton, New York, USA.ORCID https://orcid.org/0009-0001-7778-0821
Ruojun WuDepartment of Chemistry, Colgate University, Hamilton, New York, USA.ORCID https://orcid.org/0000-0003-0097-6698
Fang WangDepartment of Chemistry, University of Rhode Island, Kingston, Rhode Island, USA.ORCID https://orcid.org/0000-0002-9192-6858
Jacob M GoldbergDepartment of Chemistry, Colgate University, Hamilton, New York, USA.ORCID https://orcid.org/0000-0002-8004-3769

Funding

Training CoreP20GM103430 · NIGMS · UNIVERSITY OF RHODE ISLAND · PI Christopher Lee Hemme · 2012 to 2026
$63.6M
NMR User Program at NMRFAMR24GM141526 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Katherine Anne Henzler-Wildman · 2021 to 2026
$6.4M
Integrated state-of-the-art LC-MS/NMR system for the University of WisconsinS10RR025062 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2008 to 2008
$1.7M
American Chemical Society Petroleum Research Fund 70501-ND4National Science Foundation CHE-2117141NCRR NIH HHS S10 RR025062NCRR NIH HHS S10RR025062NIGMS NIH HHS P20 GM103430NIGMS NIH HHS P20GM103430NIGMS NIH HHS R24 GM141526NIGMS NIH HHS R24GM141526
6 · The paper itself

Abstract

The difluoromethyl group exhibits unique chemical and nuclear magnetic resonance (NMR) spectroscopic properties. Here, the synthesis and characterization of 4-difluoromethyl-L-phenylalanine is reported. Methods have been developed to incorporate this versatile unnatural amino acid into full-length green fluorescent protein and carbonic anhydrase, using an orthogonal transfer RNA (tRNA)/synthetase pair with standard genetic code expansion techniques. Taking advantage of the characteristic

Indexed as

Carbonic AnhydrasesGreen Fluorescent ProteinsPhenylalanineAmino Acyl-tRNA SynthetasesNuclear Magnetic Resonance, BiomolecularRNA, TransferAmino Acyl-tRNA SynthetasesCarbonic AnhydrasesGreen Fluorescent ProteinsPhenylalanineRNA, Transferamino acidsbioorganic chemistrydifluoromethyl groupfluorinehydrogen bonds

Identifiers

PMID42775918
PMCPMC13599698

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.