Evidence map›Paper›PMID 37446690›Full record

ArticleMolecules (Basel, Switzerland)2023

Novel Design of an α-Amylase with an N-Terminal CBM20 in

Andika Sidar, Gerben P Voshol, Erik Vijgenboom, Peter J Punt

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
4.8field-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

8 citing papers in PubMed, 18 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

4 authors at 1 institution in 2 countries.

Andika SidarInstitute of Biology Leiden, Leiden University, 2333 BE Leiden, The Netherlands.
Gerben P VosholInstitute of Biology Leiden, Leiden University, 2333 BE Leiden, The Netherlands.
Erik VijgenboomInstitute of Biology Leiden, Leiden University, 2333 BE Leiden, The Netherlands.ORCID 0000-0002-5059-069X
Peter J PuntInstitute of Biology Leiden, Leiden University, 2333 BE Leiden, The Netherlands.ORCID 0000-0002-5689-9938
Leiden University · NL

Funding

This study was supported by a scholarship of the Indonesia Endowment Fund for Education (LPDP) from the Ministry of Finance, Indonesia (20160422026103) to AS and by a grant of the Dutch National Organization for Scientific Research NWO, in the framework o (20160422026103) and (053.80.721/EIB.14.021)
6 · The paper itself

Abstract

In the starch processing industry including the food and pharmaceutical industries, α-amylase is an important enzyme that hydrolyses the α-1,4 glycosidic bonds in starch, producing shorter maltooligosaccharides. In plants, starch molecules are organised in granules that are very compact and rigid. The level of starch granule rigidity affects resistance towards enzymatic hydrolysis, resulting in inefficient starch degradation by industrially available α-amylases. In an approach to enhance starch hydrolysis, the domain architecture of a Glycoside Hydrolase (GH) family 13 α-amylase from

Indexed as

alpha-AmylasesAspergillus nigerCarbohydrate MetabolismHydrolysisStarchalpha-AmylasesStarchAspergillus nigercarbohydrate-binding moduleglycoside hydrolase family 13raw starch hydrolysisstarch binding purificationα-amylase

Identifiers

PMID37446690
PMCPMC10343422
OpenAlexW4382402956

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.