Evidence map›Paper›PMID 34541099›Full record

ArticleBio-protocol2017

Thermostability Measurement of an α-Glucosidase Using a Classical Activity-based Assay and a Novel Thermofluor Method.

Karin Ernits, Katrin Viigand, Triinu Visnapuu, Kristina Põšnograjeva, Tiina Alamäe

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bio-protocol, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Characterization of a Maltase from an Early-Diverged Non-Conventional YeastInternational journal of molecular sciences · 2019
    Article
  2. 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

5 authors at 1 institution in 1 country.

Karin ErnitsInstitute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
Katrin ViigandInstitute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
Triinu VisnapuuInstitute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
Kristina PõšnograjevaInstitute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
Tiina AlamäeInstitute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
University of Tartu · EE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-glucosidases (including maltases and isomaltases) are enzymes which release glucose from a set of α-glucosidic substrates. Their catalytic activity, substrate specificity and thermostability can be assayed using this trait. Thermostability of proteins can also be determined using a high-throughput differential scanning fluorometry method, also named Thermofluor. We have shown that Thermofluor can also be applied to predict binding of substrates and inhibitors to a yeast α-glucosidase. The methods described here in detail were used in Viigand

Indexed as

Differential scanning fluorometryGlucose liquicolorIsomaltaseMaltaseMaltase assayMethylotrophic yeastOgataea polymorpha

Identifiers

PMID34541099
PMCPMC8410288
OpenAlexW2654355584

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.