Evidence map›Paper›PMID 33871147›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Directed Evolution of an Improved Aminoacyl-tRNA Synthetase for Incorporation of L-3,4-Dihydroxyphenylalanine (L-DOPA).

Ross Thyer, Simon d'Oelsnitz, Molly S Blevins, Dustin R Klein, Jennifer S Brodbelt, Andrew D Ellington

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. In Vivo Biosynthesis and Direct Incorporation of Noncanonical Amino Acids into Proteins.Chembiochem : a European journal of chemical biology · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Impact of queuosine modification of endogenousFrontiers in molecular biosciences · 2022
    Article
  18. 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

6 authors.

Ross ThyerDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-0356-5790
Simon d'OelsnitzDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
Molly S BlevinsDepartment of Chemistry, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0001-7423-2099
Dustin R KleinDepartment of Chemistry, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0001-7327-6479
Jennifer S BrodbeltDepartment of Chemistry, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0003-3207-0217
Andrew D EllingtonDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0001-6246-5338

Funding

Ultraviolet Photodissociation Mass Spectrometry for Characterization of Biological MoleculesR35GM139658 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2021 to 2025
$2.9M
UVPD Mass Spectrometry of Protein ComplexesR01GM121714 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2017 to 2020
$1.4M
Recombinant antibodies containing L-DOPA for stability, functionalization and selectionK99CA207870 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI THYER, ROSS T · 2016 to 2017
$186k
NCI NIH HHS K99 CA207870NIGMS NIH HHS R01 GM121714NIGMS NIH HHS R35 GM139658
6 · The paper itself

Abstract

The catechol group of 3,4-dihydroxyphenylalanine (L-DOPA) derived from L-tyrosine oxidation is a key post-translational modification (PTM) in many protein biomaterials and has potential as a bioorthogonal handle for precision protein conjugation applications such as antibody-drug conjugates. Despite this potential, indiscriminate enzymatic modification of exposed tyrosine residues or complete replacement of tyrosine using auxotrophic hosts remains the preferred method of introducing the catechol moiety into proteins, which precludes many protein engineering applications. We have developed new orthogonal translation machinery to site-specifically incorporate L-DOPA into recombinant proteins and a new fluorescent biosensor to selectively monitor L-DOPA incorporation in vivo. We show simultaneous biosynthesis and incorporation of L-DOPA and apply this translation machinery to engineer a novel metalloprotein containing a DOPA-Fe chromophore.

Indexed as

Amino Acyl-tRNA SynthetasesDihydroxyphenylalanineModels, MolecularMolecular StructureAmino Acyl-tRNA SynthetasesDihydroxyphenylalanineenzymesmetalloproteinsprotein designprotein engineeringsynthetic biology

Identifiers

PMID33871147
PMCPMC8217333

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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.