Evidence map›Paper›PMID 42037767›Full record

ArticleBio-protocol2026

Efficient and Site-Specific Incorporation of 3-Nitro-Tyrosine Into Recombinant Proteins in

Sarah B McGee, Stanislau Stanisheuski, Ryan A Mehl, Richard B Cooley

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bio-protocol, 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

4 authors.

Sarah B McGeeDepartment of Biochemistry and Biophysics, Oregon State University, 2011 Agricultural and Life Sciences, Corvallis, OR, USA.
Stanislau StanisheuskiDepartment of Biochemistry and Biophysics, Oregon State University, 2011 Agricultural and Life Sciences, Corvallis, OR, USA.
Ryan A MehlDepartment of Biochemistry and Biophysics, Oregon State University, 2011 Agricultural and Life Sciences, Corvallis, OR, USA.
Richard B CooleyDepartment of Biochemistry and Biophysics, Oregon State University, 2011 Agricultural and Life Sciences, Corvallis, OR, USA.

Funding

The GCE4All Center: Unleashing the Potential of Genetic Code Expansion for Biomedical ResearchRM1GM144227 · NIGMS · OREGON STATE UNIVERSITY · PI RYAN A MEHL · 2022 to 2026
$6.2M
Equipment supplement: Defining Roles Of NitroTyrosine In Disease Via Genetic Code ExpansionR01GM114653 · NIGMS · OREGON STATE UNIVERSITY · PI MEHL, RYAN A · 2015 to 2024
$2.6M
NIGMS NIH HHS R01 GM114653NIGMS NIH HHS RM1 GM144227
6 · The paper itself

Abstract

3-nitro-tyrosine (nitroTyr) is one of numerous oxidative protein modifications implicated in diseases such as cardiovascular disease, cancer, and amyotrophic lateral sclerosis (ALS). Because of this, the ability to site-specifically encode nitroTyr into recombinant proteins is a powerful approach for studying these disease pathways. However, producing proteins with defined nitration sites is technically challenging due to the limitations of traditional chemical nitration via peroxynitrite, which lacks residue and site-specificity. Genetic code expansion (GCE) offers a solution by enabling precise incorporation of nitroTyr at designated TAG codons using engineered aminoacyl-tRNA synthetase/tRNA pairs from

Indexed as

3-nitro-tyrosineAmber suppressionAminoacyl tRNA synthetaseGenetic code expansionMethanocaldococcus jannaschiiMethanomethylophilus alvus

Identifiers

PMID42037767
PMCPMC13103966

What OpenQuestion holds

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Registered trials

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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.