Evidence map›Paper›PMID 27913673›Full record

ReviewBiochemical Society transactions2016

Structural insights into functional amyloid inhibition in Gram -ve bacteria.

William Hawthorne, Sarah Rouse, Lee Sewell, Stephen J Matthews

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

Review in Biochemical Society transactions, 2016. 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
0.8field-weighted citation impact, top 24% 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, 14 citations in OpenAlex.

  1. 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

4 authors at 1 institution in 1 country.

William HawthorneDepartment of Life Sciences, Imperial College London, South Kensington, London SW7 2AZ, U.K.
Sarah RouseDepartment of Life Sciences, Imperial College London, South Kensington, London SW7 2AZ, U.K.
Lee SewellDepartment of Life Sciences, Imperial College London, South Kensington, London SW7 2AZ, U.K.
Stephen J MatthewsDepartment of Life Sciences, Imperial College London, South Kensington, London SW7 2AZ, U.K.
Imperial College London · GB

Funding

Medical Research Council G1001664Wellcome Trust 100280Wellcome Trust 104833Wellcome Trust 104933
6 · The paper itself

Abstract

Amyloids are proteinaceous aggregates known for their role in debilitating degenerative diseases involving protein dysfunction. Many forms of functional amyloid are also produced in nature and often these systems require careful control of their assembly to avoid the potentially toxic effects. The best-characterised functional amyloid system is the bacterial curli system. Three natural inhibitors of bacterial curli amyloid have been identified and recently characterised structurally. Here, we compare common structural features of CsgC, CsgE and CsgH and discuss the potential implications for general inhibition of amyloid.

Indexed as

AmyloidBacterial ProteinsEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsModels, MolecularProtein ConformationStatic ElectricityAmyloidBacterial ProteinsCrl protein, BacteriaCsgC protein, E coliCsgE protein, E coliEscherichia coli ProteinsMembrane Transport Proteinsamyloid inhibitorscurliFapfunctional amyloid

Identifiers

PMID27913673
PMCPMC5135000
OpenAlexW2559466007

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.