Evidence map›Paper›PMID 31139251›Full record

ReviewJournal of biological engineering2019

Non-canonical amino acid labeling in proteomics and biotechnology.

Aya M Saleh, Kristen M Wilding, Sarah Calve, Bradley C Bundy, Tamara L Kinzer-Ursem

Abstract readReview
In one paragraph

Review in Journal of biological engineering, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed, 1 pooled it
–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

57 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Expanding the methionine toolkit:bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Review
  5. Review
  6. Production of Antibody Fragments Suitable for 1:1, Site-Specific Labeling.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Article
  8. Advances in Proximity-Assisted Bioconjugation.Accounts of chemical research · 2025
    Review
  9. Review
  10. Article
  11. Substrate recognition by a peptide-aminoacyl-tRNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. 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

5 authors.

Aya M Saleh1Weldon School of Biomedical Engineering, Purdue University, West Lafayette, IN USA.
Kristen M Wilding2Department of Chemical Engineering, Brigham Young University, Provo, UT USA.
Sarah Calve1Weldon School of Biomedical Engineering, Purdue University, West Lafayette, IN USA.
Bradley C Bundy2Department of Chemical Engineering, Brigham Young University, Provo, UT USA.
Tamara L Kinzer-Ursem1Weldon School of Biomedical Engineering, Purdue University, West Lafayette, IN USA.ORCID 0000-0001-7343-115X

Funding

Defining the mechanical link that unites the musculoskeletal system during limb developmentDP2AT009833 · NCCIH · UNIVERSITY OF COLORADO · PI CALVE, SARAH · 2017 to 2017
$2.2M
Biomechanical Influence of ECM Remodeling on the Developing EnthesisR01AR071359 · NIAMS · UNIVERSITY OF COLORADO · PI CALVE, SARAH · 2017 to 2021
$1.7M
Bioorthogonal labeling of extracellular matrix assemblyR21AR069248 · NIAMS · PURDUE UNIVERSITY · PI CALVE, SARAH · 2016 to 2017
$355k
NCCIH NIH HHS DP2 AT009833NIAMS NIH HHS R01 AR071359NIAMS NIH HHS R21 AR069248
6 · The paper itself

Abstract

Metabolic labeling of proteins with non-canonical amino acids (ncAAs) provides unique bioorthogonal chemical groups during de novo synthesis by taking advantage of both endogenous and heterologous protein synthesis machineries. Labeled proteins can then be selectively conjugated to fluorophores, affinity reagents, peptides, polymers, nanoparticles or surfaces for a wide variety of downstream applications in proteomics and biotechnology. In this review, we focus on techniques in which proteins are residue- and site-specifically labeled with ncAAs containing bioorthogonal handles. These ncAA-labeled proteins are: readily enriched from cells and tissues for identification via mass spectrometry-based proteomic analysis; selectively purified for downstream biotechnology applications; or labeled with fluorophores for in situ analysis. To facilitate the wider use of these techniques, we provide decision trees to help guide the design of future experiments. It is expected that the use of ncAA labeling will continue to expand into new application areas where spatial and temporal analysis of proteome dynamics and engineering new chemistries and new function into proteins are desired.

Indexed as

Bioorthogonal chemistryBiotechnologyMetabolic labelingProteomicsResidue-specific labelingSite-specific labeling

Identifiers

PMID31139251
PMCPMC6529998

What OpenQuestion holds

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LicenceCC BY
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.