Evidence map›Paper›PMID 32229583›Full record

ArticleThe Journal of biological chemistry2020

The streptococcal multidomain fibrillar adhesin CshA has an elongated polymeric architecture.

Catherine R Back, Victoria A Higman, Kristian Le Vay, Viren V Patel, Alice E Parnell, Daniel Frankel, Howard F Jenkinson, Steven G Burston, Matthew P Crump, Angela H Nobbs and 1 more

Open access · hybridAbstract read
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 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. The long and the short of Periscope Proteins.Biochemical Society transactions · 2022
    Review
  4. Article
  5. Article
  6. Periscope Proteins are variable-length regulators of bacterial cell surface interactions.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

11 authors at 3 institutions in 1 country.

Catherine R BackBristol Dental School, University of Bristol, Bristol BS1 2LY, United Kingdom.
Victoria A HigmanSchool of Chemistry, University of Bristol, Bristol BS8 1TS, United Kingdom.ORCID 0000-0002-3204-2665
Kristian Le VaySchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.
Viren V PatelSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.
Alice E ParnellSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.
Daniel FrankelSchool of Engineering, Newcastle University, Newcastle-upon-Tyne NE1 7RU, United Kingdom.
Howard F JenkinsonBristol Dental School, University of Bristol, Bristol BS1 2LY, United Kingdom.ORCID 0000-0002-9195-7945
Steven G BurstonSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.ORCID 0000-0003-1848-1853
Matthew P CrumpBrisSynBio Synthetic Biology Research Centre, University of Bristol, Bristol BS8 1TQ, United Kingdom.ORCID 0000-0002-7868-5818
Angela H NobbsBristol Dental School, University of Bristol, Bristol BS1 2LY, United Kingdom Angela.Nobbs@bristol.ac.uk.ORCID 0000-0003-3813-4410
Paul R RaceSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom Paul.Race@bristol.ac.uk.ORCID 0000-0003-0184-5630
University of Bristol · GBUniversity Of Bristol Dental Hospital · GBNewcastle University · GB

Funding

Streptococcus-Candida Communication in Oral BiofilmsR01DE016690 · NIDCR · UNIVERSITY OF BRISTOL · PI JENKINSON, HOWARD F, LAMONT, RICHARD J · 2006 to 2016
$3.8M
Biotechnology and Biological Sciences Research Council BB/L01386X/1Biotechnology and Biological Sciences Research Council BB/M025624/1British Heart Foundation PG/17/10/32829NIDCR NIH HHS R01 DE016690
6 · The paper itself

Abstract

The cell surfaces of many bacteria carry filamentous polypeptides termed adhesins that enable binding to both biotic and abiotic surfaces. Surface adherence is facilitated by the exquisite selectivity of the adhesins for their cognate ligands or receptors and is a key step in niche or host colonization and pathogenicity.

Indexed as

Protein MultimerizationAmino Acid SequenceBacterial ProteinsMembrane ProteinsModels, MolecularProtein DomainsProtein Structure, QuaternaryRepetitive Sequences, Amino AcidBacterial ProteinsCshA protein, Streptococcus gordoniiMembrane Proteinsadhesinbacterial pathogenicitybiofilmCshAfibrilmicrobiologynuclear magnetic resonance (NMR)protein foldingsmall-angle X-ray scattering (SAXS)virulence factor

Identifiers

PMID32229583
PMCPMC7212634
OpenAlexW3013976339

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.