Evidence map›Paper›PMID 32518157›Full record

ArticleThe Journal of biological chemistry2020

A unique combination of glycoside hydrolases in

Ping Chen, Ran Liu, Mengmeng Huang, Jinlu Zhu, Dong Wei, Francis J Castellino, Guanghui Dang, Fang Xie, Gang Li, Ziyin Cui and 2 more

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

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 29% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Pan-genome analysis ofFrontiers in microbiology · 2024
    Article
  2. Effects of Module Truncation of a New Alginate Lyase VxAly7C from MarineInternational journal of molecular sciences · 2022
    Article
  3. Review
  4. 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

12 authors at 2 institutions in 2 countries.

Ping ChenState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Ran LiuState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Mengmeng HuangState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Jinlu ZhuState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Dong WeiState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Francis J CastellinoDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.ORCID 0000-0003-0317-9539
Guanghui DangState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Fang XieState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Gang LiState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Ziyin CuiState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Siguo LiuState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China zhangyueling@caas.cn zhang.yl@foxmail.com liusiguo@caas.cn.
Yueling ZhangState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China zhangyueling@caas.cn zhang.yl@foxmail.com liusiguo@caas.cn.ORCID 0000-0002-5619-8410
Chinese Academy of Agricultural Sciences · CNUniversity of Notre Dame · US

Funding

STRUCTURE-FUNCTION STUDIES ON PLASMINOGEN AND PLASMINR01HL013423 · NHLBI · UNIVERSITY OF NOTRE DAME · PI CASTELLINO, FRANCIS J, LEE, SHAUN · 1985 to 2021
$7.9M
6 · The paper itself

Abstract

Infections by many bacterial pathogens rely on their ability to degrade host glycans by producing glycoside hydrolases (GHs). Here, we discovered a conserved multifunctional GH, SsGalNagA, containing a unique combination of two family 32 carbohydrate-binding modules (CBM), a GH16 domain and a GH20 domain, in the zoonotic pathogen

Indexed as

AnimalsBacterial ProteinsDisaccharidesEpitopesGlycoside HydrolasesMicePolysaccharides, BacterialProtein DomainsRabbitsStreptococcus suisSwineBacterial ProteinsDisaccharidesEpitopesgalactosyl-(1-3)galactoseGlycoside HydrolasesPolysaccharides, Bacterialcarbohydrate-binding proteincarbohydrate processingendo-(β1,4)-galactosidaseenzyme catalysisenzyme kineticserythrocyteevolutionfamily 32 carbohydrate-binding module (CBM32)GalNagAglycoside hydrolase (GH)host–pathogen interactionmultifunctional enzymeStreptococcusStreptococcus suissubstrate specificityswine tracheal epithelial cells (STEC)αGal epitopeβ-acetylhexosaminidase

Identifiers

PMID32518157
PMCPMC7397095
OpenAlexW3033256233

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.