Evidence map›Paper›PMID 29761590›Full record

ArticleProtein science : a publication of the Protein Society2018

Interaction of antidiabetic α-glucosidase inhibitors and gut bacteria α-glucosidase.

Kemin Tan, Christine Tesar, Rosemarie Wilton, Robert P Jedrzejczak, Andrzej Joachimiak

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
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  8. ACS omega · 2023
    Article
  9. Article
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  11. Identification and Isolation of α-Glucosidase Inhibitors fromInternational journal of molecular sciences · 2023
    Article
  12. Review
  13. Article
  14. Article
  15. A review of alpha-glucosidase inhibitors from plants as potential candidates for the treatment of type-2 diabetes.Phytochemistry reviews : proceedings of the Phytochemical Society of Europe · 2022
    Review
  16. 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

5 authors at 2 institutions in 1 country.

Kemin TanMidwest Center for Structural Genomics and Structural Biology Center, Biosciences, Argonne National Laboratory, Argonne, Illinois, 60439.
Christine TesarBiosciences, Argonne National Laboratory, Argonne, Illinois, 60439.
Rosemarie WiltonBiosciences, Argonne National Laboratory, Argonne, Illinois, 60439.
Robert P JedrzejczakBiosciences, Argonne National Laboratory, Argonne, Illinois, 60439.
Andrzej JoachimiakMidwest Center for Structural Genomics and Structural Biology Center, Biosciences, Argonne National Laboratory, Argonne, Illinois, 60439.
Argonne National Laboratory · USUniversity of Chicago · US

Funding

Midwest Center for Structural GenomicsU54GM094585 · NIGMS · UNIVERSITY OF CHICAGO · PI ANDERSON, WAYNE F · 2010 to 2014
$33.7M
The Midwest Center for Structural Genomics - Community ResourceR24GM115586 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ · 2015 to 2017
$2.8M
NIGMS NIH HHS R24 GM115586NIGMS NIH HHS U54 GM094585
6 · The paper itself

Abstract

Carbohydrate hydrolyzing α-glucosidases are commonly found in microorganisms present in the human intestine microbiome. We have previously reported crystal structures of an α-glucosidase from the human gut bacterium Blaubia (Ruminococcus) obeum (Ro-αG1) and its substrate preference/specificity switch. This novel member of the GH31 family is a structural homolog of human intestinal maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) with a highly conserved active site that is predicted to be common in Ro-αG1 homologs among other species that colonize the human gut. In this report, we present structures of Ro-αG1 in complex with the antidiabetic α-glucosidase inhibitors voglibose, miglitol, and acarbose and supporting binding data. The in vitro binding of these antidiabetic drugs to Ro-αG1 suggests the potential for unintended in vivo crossreaction of the α-glucosidase inhibitors to bacterial α-glucosidases that are present in gut microorganism communities. Moreover, analysis of these drug-bound enzyme structures could benefit further antidiabetic drug development.

Indexed as

1-Deoxynojirimycinalpha-GlucosidasesBacterial ProteinsGastrointestinal MicrobiomeGlycoside Hydrolase InhibitorsHumansHypoglycemic AgentsInositolModels, MolecularProtein BindingRuminococcus1-Deoxynojirimycinalpha-GlucosidasesBacterial ProteinsGlycoside Hydrolase InhibitorsHypoglycemic AgentsInositolmiglitolvogliboseacarboseantidiabetic drughuman gut microbiomemiglitolsubstrate/inhibitor selectionvogliboseα-glucosidaseα-glucosidase inhibitor

Identifiers

PMID29761590
PMCPMC6153411
OpenAlexW2804130333

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.