Evidence map›Paper›PMID 37762340›Full record

ReviewInternational journal of molecular sciences2023

Non-Canonical Amino Acids in Analyses of Protease Structure and Function.

Peter Goettig, Nikolaj G Koch, Nediljko Budisa

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

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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 at 2 institutions in 3 countries.

Peter GoettigDepartment of Pharmaceutical and Medicinal Chemistry, Institute of Pharmacy, Paracelsus Medical University, Strubergasse 21, 5020 Salzburg, Austria.ORCID 0000-0002-2430-1970
Nikolaj G KochBiocatalysis Group, Technische Universität Berlin, 10623 Berlin, Germany.ORCID 0000-0003-2745-0020
Nediljko BudisaBioanalytics Group, Institute of Biotechnology, Technische Universität Berlin, 10623 Berlin, Germany.ORCID 0000-0001-8437-7304
Technische Universität Berlin · DEParacelsus Medical University · AT

Funding

Austrian Science Fund FWF I 3877
6 · The paper itself

Abstract

All known organisms encode 20 canonical amino acids by base triplets in the genetic code. The cellular translational machinery produces proteins consisting mainly of these amino acids. Several hundred natural amino acids serve important functions in metabolism, as scaffold molecules, and in signal transduction. New side chains are generated mainly by post-translational modifications, while others have altered backbones, such as the β- or γ-amino acids, or they undergo stereochemical inversion, e.g., in the case of D-amino acids. In addition, the number of non-canonical amino acids has further increased by chemical syntheses. Since many of these non-canonical amino acids confer resistance to proteolytic degradation, they are potential protease inhibitors and tools for specificity profiling studies in substrate optimization and enzyme inhibition. Other applications include in vitro and in vivo studies of enzyme kinetics, molecular interactions and bioimaging, to name a few. Amino acids with bio-orthogonal labels are particularly attractive, enabling various cross-link and click reactions for structure-functional studies. Here, we cover the latest developments in protease research with non-canonical amino acids, which opens up a great potential, e.g., for novel prodrugs activated by proteases or for other pharmaceutical compounds, some of which have already reached the clinical trial stage.

Indexed as

Antifibrinolytic AgentsPeptide HydrolasesAmino AcidsEndopeptidasesProteolysisAmino AcidsAntifibrinolytic AgentsEndopeptidasesPeptide Hydrolasesbioorthogonal tagsclick chemistrycross-linkinggenetic code expansioninhibitory potencynon-canonical amino acidspharmaceutical compoundprotease specificityproteinogenic amino acidunnatural amino acid

Identifiers

PMID37762340
PMCPMC10531186
OpenAlexW4386749535

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.