Evidence map›Paper›PMID 29106828›Full record

ArticleBiochemistry2018

Expanding the Scope of Single- and Double-Noncanonical Amino Acid Mutagenesis in Mammalian Cells Using Orthogonal Polyspecific Leucyl-tRNA Synthetases.

Yunan Zheng, Raja Mukherjee, Melissa A Chin, Peter Igo, Martin J Gilgenast, Abhishek Chatterjee

Abstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

38 citing papers in PubMed, 65 citations in OpenAlex.

  1. Ribosome engineering enhances genetic code expansion inSynthetic and systems biotechnology · 2027
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  4. An Expanded Toolbox for Versatile Chemical Editing of Adeno-Associated Virus.Angewandte Chemie (International ed. in English) · 2026
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  7. Review
  8. BeyondChemical reviews · 2025
    Review
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  14. Article
  15. Review
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  17. Article
  18. Article
  19. Review
  20. A Facile Platform to EngineerACS central science · 2022
    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

6 authors at 1 institution in 1 country.

Yunan ZhengDepartment of Chemistry, Boston College , 2609 Beacon Street, Chestnut Hill, Massachusetts 02467, United States.
Raja MukherjeeDepartment of Chemistry, Boston College , 2609 Beacon Street, Chestnut Hill, Massachusetts 02467, United States.
Melissa A ChinDepartment of Chemistry, Boston College , 2609 Beacon Street, Chestnut Hill, Massachusetts 02467, United States.
Peter IgoDepartment of Chemistry, Boston College , 2609 Beacon Street, Chestnut Hill, Massachusetts 02467, United States.
Martin J GilgenastDepartment of Chemistry, Boston College , 2609 Beacon Street, Chestnut Hill, Massachusetts 02467, United States.
Abhishek ChatterjeeDepartment of Chemistry, Boston College , 2609 Beacon Street, Chestnut Hill, Massachusetts 02467, United States.ORCID 0000-0002-6231-5302
Boston College · US

Funding

A novel approach to define the roles of oxidative and nitrative post-trasnlational modifications of tryptophan in human biologyR01GM124319 · NIGMS · BOSTON COLLEGE · PI CHATTERJEE, ABHISHEK · 2017 to 2019
$916k
NIGMS NIH HHS R01 GM124319
6 · The paper itself

Abstract

Engineered aminoacyl-tRNA synthetase/tRNA pairs that enable site-specific incorporation of noncanonical amino acids (ncAAs) into proteins in living cells have emerged as powerful tools in chemical biology. The Escherichia coli-derived leucyl-tRNA synthetase (EcLeuRS)/tRNA pair is a promising candidate for ncAA mutagenesis in mammalian cells, but it has been engineered to charge only a limited set of ncAAs so far. Here we show that two highly polyspecific EcLeuRS mutants can efficiently charge a large array of useful ncAAs into proteins expressed in mammalian cells, while discriminating against the 20 canonical amino acids. When combined with an opal-suppressing pyrrolysyl pair, these EcLeuRS variants further enabled site-specific incorporation of different combinations of two distinct ncAAs into proteins expressed in mammalian cells.

Indexed as

Amino AcidsEscherichia coliEscherichia coli ProteinsHEK293 CellsHumansLeucine-tRNA LigaseMolecular StructureMutagenesis, Site-DirectedSubstrate SpecificityAmino AcidsEscherichia coli ProteinsLeucine-tRNA Ligase

Identifiers

PMID29106828
PMCPMC6413323
OpenAlexW2767673635

What OpenQuestion holds

Textmetadata
LicenceTDM
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.