Evidence map›Paper›PMID 29386631›Full record

ArticleScientific reports2018

The intrinsically disordered Tarp protein from chlamydia binds actin with a partially preformed helix.

James Tolchard, Samuel J Walpole, Andrew J Miles, Robin Maytum, Lawrence A Eaglen, Ted Hackstadt, B A Wallace, Tharin M A Blumenschein

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
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  5. Review
  6. A context-dependent and disordered ubiquitin-binding motif.Cellular and molecular life sciences : CMLS · 2022
    Article
  7. The Impact of Lateral Gene Transfer inFrontiers in cellular and infection microbiology · 2022
    Review
  8. Idiosyncratic Biogenesis of Intracellular Pathogens-Containing Vacuoles.Frontiers in cellular and infection microbiology · 2021
    Review
  9. Non-covalent Encapsulation of siRNA with Cell-Penetrating Peptides.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  10. Article
  11. Article
  12. Review
  13. 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

8 authors at 3 institutions in 1 country.

James TolchardCenter for Molecular and Structural Biology, School of Chemistry, University of East Anglia, Norwich Research Park, Norwich, NR4 7TJ, UK.ORCID http://orcid.org/0000-0002-5779-4935
Samuel J WalpoleCenter for Molecular and Structural Biology, School of Chemistry, University of East Anglia, Norwich Research Park, Norwich, NR4 7TJ, UK.
Andrew J MilesInstitute of Structural and Molecular Biology, Birkbeck College, University of London, London, WC1E 7HX, UK.
Robin MaytumSchool of Life Sciences, University of Bedfordshire, Park Square, Luton, LU1 3JU, UK.
Lawrence A EaglenCenter for Molecular and Structural Biology, School of Chemistry, University of East Anglia, Norwich Research Park, Norwich, NR4 7TJ, UK.
Ted HackstadtHost-parasite Interactions Section, Laboratory of Intracellular Parasites, NIAID, NIH, Rocky Mountain Laboratories, Hamilton, MT, 59840, USA.
B A WallaceInstitute of Structural and Molecular Biology, Birkbeck College, University of London, London, WC1E 7HX, UK.
Tharin M A BlumenscheinCenter for Molecular and Structural Biology, School of Chemistry, University of East Anglia, Norwich Research Park, Norwich, NR4 7TJ, UK. t.blumenschein@uea.ac.uk.ORCID http://orcid.org/0000-0002-4932-5178
University of East Anglia · GBInstitute of Structural and Molecular Biology · GBUniversity of Bedfordshire · GB

Funding

Cellular Biology Of Host/parasite InteractionsZIAAI000567 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI HACKSTADT, TED · 2009 to 2025
$16.3M
Biotechnology and Biological Sciences Research Council BB/D526196/1Biotechnology and Biological Sciences Research Council BB/D526202/1Biotechnology and Biological Sciences Research Council J019135
6 · The paper itself

Abstract

Tarp (translocated actin recruiting phosphoprotein) is an effector protein common to all chlamydial species that functions to remodel the host-actin cytoskeleton during the initial stage of infection. In C. trachomatis, direct binding to actin monomers has been broadly mapped to a 100-residue region (726-825) which is predicted to be predominantly disordered, with the exception of a ~10-residue α-helical patch homologous to other WH2 actin-binding motifs. Biophysical investigations demonstrate that a Tarp

Indexed as

ActinsAmino Acid SequenceBacterial ProteinsChlamydia trachomatisCircular DichroismIntrinsically Disordered ProteinsModels, MolecularProtein BindingProtein DomainsProtein Structure, SecondaryProton Magnetic Resonance SpectroscopySynchrotronsActinsBacterial ProteinsIntrinsically Disordered Proteins

Identifiers

PMID29386631
PMCPMC5792643
OpenAlexW2806412809

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.