Evidence map›Paper›PMID 32172335›Full record

ReviewWorld journal of microbiology & biotechnology2020

A recent update on the use of microbial transglutaminase for the generation of biotherapeutics.

N Doti, A Caporale, Alessandra Monti, A Sandomenico, Fabio Selis, M Ruvo

Abstract readReview
PubMed Publisher
In one paragraph

Review in World journal of microbiology & biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Rewiring Amino Acid Flux for Efficient Transglutaminase Production inJournal of agricultural and food chemistry · 2026
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  15. Improved Productivity ofFrontiers in bioengineering and biotechnology · 2022
    Article
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  17. 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 at 3 institutions in 1 country.

N DotiInstitute of Biostructure and Bioimaging, CNR (IBB-CNR), Via Mezzocannone, 16, 80134, Naples, Italy. nunzianna.doti@cnr.it.
A CaporaleInstitute of Crystallography, CNR (IC-CNR), c/o Area Science Park s.s. 14 Km 163.5, Basovizza, 34149, Trieste, Italy.
Alessandra MontiInstitute of Biostructure and Bioimaging, CNR (IBB-CNR), Via Mezzocannone, 16, 80134, Naples, Italy.
A SandomenicoInstitute of Biostructure and Bioimaging, CNR (IBB-CNR), Via Mezzocannone, 16, 80134, Naples, Italy.
Fabio SelisBioVIIIx R&D, Via B. Brin, 59C, 80142, Naples, Italy.
M RuvoInstitute of Biostructure and Bioimaging, CNR (IBB-CNR), Via Mezzocannone, 16, 80134, Naples, Italy. menotti.ruvo@unina.it.
Institute of Biostructure and Bioimaging · ITAREA Science Park · ITUniversity of Campania "Luigi Vanvitelli" · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The recent scientific progresses on the use of enzyme-mediated reactions in organic, non-aqueous and aqueous media have significantly supported the growing demand of new biotechnological and/or pharmacological products. Today, a plethora of microbial enzymes, used as biocatalysts, are available. Among these, microbial transglutaminases (MTGs) are broadly used for their ability to catalyse the formation of an isopeptide bond between the γ-amide group of glutamines and the ε-amino group of lysine. Due to their promiscuity towards primary amine-containing substrates and the more stringent specificity for glutamine-containing peptide sequences, several combined approaches can be tailored for different settings, making MTGs very attractive catalysts for generating protein-protein and protein small molecule's conjugates. The present review offers a recent update on the modifications attainable by MTG-catalysed bioreactions as reported between 2014 and 2019. In particular, we present a detailed and comparative overview on the MTG-based methods for proteins and antibodies engineering, with a particular outlook on the synthesis of homogeneous antibody-drug conjugates.

Indexed as

BacteriaBacterial ProteinsBiocatalysisBiotechnologyFungal ProteinsFungiImmunoconjugatesProtein EngineeringSubstrate SpecificityTransglutaminasesBacterial ProteinsFungal ProteinsImmunoconjugatesTransglutaminasesAntibody–drug conjugateChemoenzymatic reactionsMicrobial transglutaminaseProtein bioconjugation

Identifiers

PMID32172335
OpenAlexW3011304206

What OpenQuestion holds

Textmetadata
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.