Evidence map›Paper›PMID 29604180›Full record

ArticleMicrobiologyOpen2018

Glycosylated amyloid-like proteins in the structural extracellular polymers of aerobic granular sludge enriched with ammonium-oxidizing bacteria.

Yuemei Lin, Clara Reino, Julián Carrera, Julio Pérez, Mark C M van Loosdrecht

Open access · goldAbstract read
In one paragraph

Article in MicrobiologyOpen, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

10 citing papers in PubMed, 85 citations in OpenAlex.

  1. Multiple extracellular polymeric substance pathways transcribed byApplied and environmental microbiology · 2025
    Article
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  3. Article
  4. Mechanisms of microbial co-aggregation in mixed anaerobic cultures.Applied microbiology and biotechnology · 2024
    Review
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  6. Article
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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 2 countries.

Yuemei LinDepartment of Biotechnology, Faculty of Applied Sciences, Delft University of Technology, Delft, The Netherlands.ORCID 0000-0002-8952-1253
Clara ReinoGENOCOV Research Group, Department of Chemical, Biological and Environmental Engineering, School of Engineering, Universitat Autònoma de Barcelona, Barcelona, Spain.
Julián CarreraGENOCOV Research Group, Department of Chemical, Biological and Environmental Engineering, School of Engineering, Universitat Autònoma de Barcelona, Barcelona, Spain.
Julio PérezDepartment of Biotechnology, Faculty of Applied Sciences, Delft University of Technology, Delft, The Netherlands.
Mark C M van LoosdrechtDepartment of Biotechnology, Faculty of Applied Sciences, Delft University of Technology, Delft, The Netherlands.
Delft University of Technology · NLUniversitat Autònoma de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A new type of structural extracellular polymers (EPS) was extracted from aerobic granular sludge dominated by ammonium-oxidizing bacteria. It was analyzed by Raman and FTIR spectroscopy to characterize specific amino acids and protein secondary structure, and by SDS-PAGE with different stains to identify different glycoconjugates. Its intrinsic fluorescence was captured to visualize the location of the extracted EPS in the nitrifying granules, and its hydrogel-forming property was studied by rheometry. The extracted EPS is abundant with cross ß-sheet secondary structure, contains glycosylated proteins/polypeptides, and rich in tryptophan. It forms hydrogel with high mechanical strength. The extraction and discovery of glycosylated proteins and/or amyloids further shows that conventionally used extraction and characterization techniques are not adequate for the study of structural extracellular polymers in biofilms and/or granular sludge. Confirming amyloids secondary structure in such a complex sample is challengeable due to the possibility of amyloids glycosylation and self-assembly. A new definition of extracellular polymers components which includes glycosylated proteins and a better approach to studying them is required to stimulate biofilm research.

Indexed as

AerobiosisAmmonium CompoundsAmyloidogenic ProteinsBacteriaGlycosylationOxidation-ReductionPolymersProtein Conformation, beta-StrandSewageSpectroscopy, Fourier Transform InfraredAmmonium CompoundsAmyloidogenic ProteinsPolymersSewageaerobic granular sludgeammonium-oxidizing bacteriaamyloidextracellular polymeric substancesglycoproteins

Identifiers

PMID29604180
PMCPMC6291783
OpenAlexW2794853313

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.