Evidence map›Paper›PMID 36897290›Full record

ReviewProtein engineering, design & selection : PEDS2023

Non-canonical amino acids as a tool for the thermal stabilization of enzymes.

Tim Lugtenburg, Alejandro Gran-Scheuch, Ivana Drienovská

Abstract readReview
In one paragraph

Review in Protein engineering, design & selection : PEDS, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Synthetic Biology Approaches to Enzymology in Food and Agriculture Systems.Journal of agricultural and food chemistry · 2026
    Review
  2. Review
  3. Review
  4. Stabilization of a protein by a single halogen-based aromatic amplifier.Protein science : a publication of the Protein Society · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. 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

3 authors.

Tim LugtenburgDepartment of Chemistry & Pharmaceutical Sciences, Vrije Universiteit Amsterdam, 1081 HZ Amsterdam, The Netherlands.
Alejandro Gran-ScheuchDepartment of Chemistry & Pharmaceutical Sciences, Vrije Universiteit Amsterdam, 1081 HZ Amsterdam, The Netherlands.
Ivana DrienovskáDepartment of Chemistry & Pharmaceutical Sciences, Vrije Universiteit Amsterdam, 1081 HZ Amsterdam, The Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biocatalysis has become a powerful alternative for green chemistry. Expanding the range of amino acids used in protein biosynthesis can improve industrially appealing properties such as enantioselectivity, activity and stability. This review will specifically delve into the thermal stability improvements that non-canonical amino acids (ncAAs) can confer to enzymes. Methods to achieve this end, such as the use of halogenated ncAAs, selective immobilization and rational design, will be discussed. Additionally, specific enzyme design considerations using ncAAs are discussed along with the benefits and limitations of the various approaches available to enhance the thermal stability of enzymes.

Indexed as

Amino AcidsBiocatalysisAmino Acidsbiocatalysisenzyme stabilityhalogenated ncAAsncAAsselective pressure incorporationstop codon suppressionunnatural amino acid

Identifiers

PMID36897290
PMCPMC10064326

What OpenQuestion holds

Textmetadata
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.