Evidence map›Paper›PMID 34163800›Full record

ArticleChemical science2020

Development of an active site titration reagent for α-amylases.

Ryan P Sweeney, Phillip M Danby, Andreas Geissner, Ryan Karimi, Jesper Brask, Stephen G Withers

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

Article in Chemical science, 2020. 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 40% 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, 3 citations in OpenAlex.

  1. Review
  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

6 authors at 2 institutions in 2 countries.

Ryan P SweeneyDepartment of Chemistry, The University of British Columbia 2036 Main Mall Vancouver BC V6T 1Z1 Canada withers@chem.ubc.ca.ORCID https://orcid.org/0000-0003-4022-3041
Phillip M DanbyDepartment of Chemistry, The University of British Columbia 2036 Main Mall Vancouver BC V6T 1Z1 Canada withers@chem.ubc.ca.
Andreas GeissnerDepartment of Chemistry, The University of British Columbia 2036 Main Mall Vancouver BC V6T 1Z1 Canada withers@chem.ubc.ca.
Ryan KarimiDepartment of Chemistry, The University of British Columbia 2036 Main Mall Vancouver BC V6T 1Z1 Canada withers@chem.ubc.ca.ORCID https://orcid.org/0000-0003-2300-4824
Jesper BraskNovozymes Krogshoejvej 36 2880 Bagsvaerd Denmark.ORCID https://orcid.org/0000-0002-0425-9875
Stephen G WithersDepartment of Chemistry, The University of British Columbia 2036 Main Mall Vancouver BC V6T 1Z1 Canada withers@chem.ubc.ca.ORCID https://orcid.org/0000-0002-6722-5701
University of British Columbia · CANovozymes (Denmark) · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Amylases are among the most widely used classes of enzymes in industry and considerable effort has gone into optimising their activities. Efforts to find better amylase mutants, such as through high-throughput screening, would be greatly aided by access to precise and robust active site titrating agents for quantitation of active mutants in crude cell lysates. While active site titration reagents designed for retaining β-glycosidases quantify these enzymes down to nanomolar levels, convenient titrants for α-glycosidases are not available. We designed such a reagent by incorporating a highly reactive fluorogenic leaving group onto unsaturated cyclitol ethers, which have been recently shown to act as slow substrates for retaining glycosidases that operate

Identifiers

PMID34163800
PMCPMC8178983
OpenAlexW3097879725

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.