Evidence map›Paper›PMID 28455338›Full record

ArticleApplied and environmental microbiology2017

Enzymes Required for Maltodextrin Catabolism in Enterococcus faecalis Exhibit Novel Activities.

Philippe Joyet, Abdelhamid Mokhtari, Eliette Riboulet-Bisson, Víctor S Blancato, Martin Espariz, Christian Magni, Axel Hartke, Josef Deutscher, Nicolas Sauvageot

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

7 citing papers in PubMed, 15 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

9 authors at 7 institutions in 3 countries.

Philippe JoyetMicalis Institute, INRA, AgroParisTech, Université Paris-Saclay, Jouy-en-Josas, France.
Abdelhamid MokhtariMicalis Institute, INRA, AgroParisTech, Université Paris-Saclay, Jouy-en-Josas, France.
Eliette Riboulet-BissonNormandie University, UNICAEN, U2RM Stress/Virulence, Caen, France.
Víctor S BlancatoInstituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina.
Martin EsparizInstituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina.
Christian MagniInstituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina.
Axel HartkeNormandie University, UNICAEN, U2RM Stress/Virulence, Caen, France axel.hartke@unicaen.fr Josef.Deutscher@grignon.inra.fr.
Josef DeutscherMicalis Institute, INRA, AgroParisTech, Université Paris-Saclay, Jouy-en-Josas, France axel.hartke@unicaen.fr Josef.Deutscher@grignon.inra.fr.
Nicolas SauvageotNormandie University, UNICAEN, U2RM Stress/Virulence, Caen, France.
Instituto de Biología Molecular y Celular de Rosario · ARNormandie Université · FRNational University of Rosario · ARSorbonne Paris Cité · FRUniversité de Caen Normandie · FRUniversité Paris-Saclay · FRUniversity of Guelma · DZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maltose and maltodextrins are formed during the degradation of starch or glycogen. Maltodextrins are composed of a mixture of maltooligosaccharides formed by α-1,4- but also some α-1,6-linked glucosyl residues. The α-1,6-linked glucosyl residues are derived from branching points in the polysaccharides. In

Indexed as

ATP-Binding Cassette TransportersBacterial ProteinsEnterococcus faecalisHydrolasesMaltoseOligosaccharidesOperonPolysaccharidesTrisaccharidesATP-Binding Cassette TransportersBacterial ProteinsHydrolasesmaltodextrinmaltooligosaccharidesMaltosemaltotrioseOligosaccharidesPolysaccharidesTrisaccharidesEnterococcus faecalisglucosyl transferasemaltodextrin catabolismα-1,4-glucosidaseα-1,6-glucosidase

Identifiers

PMID28455338
PMCPMC5478983
OpenAlexW2608120001

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.