Evidence map›Paper›PMID 29255954›Full record

ReviewWorld journal of microbiology & biotechnology2017

Amine transaminases in chiral amines synthesis: recent advances and challenges.

Erica E Ferrandi, Daniela Monti

Abstract readReview
PubMed Publisher
In one paragraph

Review in World journal of microbiology & biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed, 97 citations in OpenAlex.

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  15. Biocatalysis: Enzymatic Synthesis for Industrial Applications.Angewandte Chemie (International ed. in English) · 2021
    Review
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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

2 authors at 1 institution in 1 country.

Erica E FerrandiIstituto di Chimica del Riconoscimento Molecolare, C.N.R., Via Mario Bianco 9, 20131, Milan, Italy.ORCID http://orcid.org/0000-0002-3390-9638
Daniela MontiIstituto di Chimica del Riconoscimento Molecolare, C.N.R., Via Mario Bianco 9, 20131, Milan, Italy. daniela.monti@icrm.cnr.it.ORCID http://orcid.org/0000-0002-3399-7973
Institute of Chemistry of Molecular Recognition · IT

Funding

Fondazione Cariplo 2016-0731
6 · The paper itself

Abstract

Transaminases, which catalyze the stereoselective transfer of an amino group between an amino donor and a prochiral ketone substrate, are interesting biocatalytic tools for the generation of optically pure chiral amines. In particular, amine transaminases (ATAs) are of industrial interest because they are capable of performing reductive amination reactions using a broad range of amine donors and acceptors. The most remarkable example of ATAs industrial application is in the production process of the anti-hyperglycaemic drug sitagliptin (Januvia

Indexed as

AminesBacteriaBiocatalysisBioreactorsFungiMetabolic Networks and PathwaysProtein EngineeringStereoisomerismSubstrate SpecificityTransaminasesAminesTransaminasesAmine transaminasesBiocatalysisChiral aminesProcess developmentProtein engineering

Identifiers

PMID29255954
OpenAlexW2771222607

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.