Evidence map›Paper›PMID 26712033›Full record

ReviewScience China. Life sciences2016

Insights into bacterial protein glycosylation in human microbiota.

Fan Zhu, Hui Wu

Erratum issuedOpen access · hybridAbstract readReview
In one paragraph

Review in Science China. Life sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Fan ZhuDepartments of Microbiology and Pediatric Dentistry, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, AL, 35294, USA.
Hui WuDepartments of Microbiology and Pediatric Dentistry, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, AL, 35294, USA. hwu@uab.edu.
University of Alabama at Birmingham · US

Funding

Glycosylation & Function of an Oral Streptococcal AdhesinR01DE017954 · NIDCR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI WU, HUI · 2007 to 2022
$5.8M
SMALL MOLECULE INHIBITORS OF CARIOGENIC BIOFILMSR01DE022350 · NIDCR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Christian Corey Melander, Hui Wu · 2012 to 2026
$4.3M
A novel glycosylation-associated protein is required for fimbriae biogenesisF31DE022995 · NIDCR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI ECHLIN, HALEY L · 2012 to 2013
$86k
NIDCR NIH HHS F31 DE022995NIDCR NIH HHS R01 DE017954NIDCR NIH HHS R01DE017954NIDCR NIH HHS R01 DE022350NIDCR NIH HHS R01DE022350
6 · The paper itself

Abstract

The study of human microbiota is an emerging research topic. The past efforts have mainly centered on studying the composition and genomic landscape of bacterial species within the targeted communities. The interaction between bacteria and hosts is the pivotal event in the initiation and progression of infectious diseases. There is a great need to identify and characterize the molecules that mediate the bacteria-host interaction. Bacterial surface exposed proteins play an important role in the bacteria- host interaction. Numerous surface proteins are glycosylated, and the glycosylation is crucial for their function in mediating the bacterial interaction with hosts. Here we present an overview of surface glycoproteins from bacteria that inhabit three major mucosal environments across human body: oral, gut and skin. We describe the important enzymes involved in the process of protein glycosylation, and discuss how the process impacts the bacteria-host interaction. Emerging molecular details underlying glycosylation of bacterial surface proteins may lead to new opportunities for designing anti-infective small molecules, and developing novel vaccines in order to treat or prevent bacterial infection.

Indexed as

MicrobiotaBacterial ProteinsGastrointestinal MicrobiomeGlycosylationHost-Pathogen InteractionsHumansMouth MucosaProtein Processing, Post-TranslationalSkinBacterial Proteinsbacteria-host interactionglycosylationglycosyltransferasemicrobiotasurface glycoprotein

Identifiers

PMID26712033
PMCPMC5298937
OpenAlexW2214753655

What OpenQuestion holds

Textmetadata
LicenceTDM
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.