Evidence map›Paper›PMID 28232575›Full record

ArticleScience (New York, N.Y.)2017

The cytotoxic

Einav Tayeb-Fligelman, Orly Tabachnikov, Asher Moshe, Orit Goldshmidt-Tran, Michael R Sawaya, Nicolas Coquelle, Jacques-Philippe Colletier, Meytal Landau

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers.

0numbers the graph read from it
0cells of the map it votes in
145citing papers in PubMed
13.4field-weighted citation impact, top 1% 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

145 citing papers in PubMed, 306 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  5. Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  14. Article
  15. Structural basis ofScience advances · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Structure of biofilm-forming functional amyloid PSMα1 fromProceedings of the National Academy of Sciences of the United States of America · 2024
    Article

85 more citing papers are in PubMed but not listed here.

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 3 countries.

Einav Tayeb-FligelmanDepartment of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel.ORCID 0000-0001-9318-5400
Orly TabachnikovDepartment of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel.ORCID 0000-0001-8372-7392
Asher MosheDepartment of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel.
Orit Goldshmidt-TranDepartment of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel.ORCID 0000-0002-5117-134X
Michael R SawayaDepartment of Biological Chemistry, Department of Chemistry and Biochemistry, and Howard Hughes Medical Institute, University of California at Los Angeles, Los Angeles, CA 90095, USA.ORCID 0000-0003-0874-9043
Nicolas CoquelleInstitut de Biologie Structurale (IBS), Université Grenoble Alpes-CEA-CNRS UMR 5075, Grenoble 38044, France.
Jacques-Philippe ColletierInstitut de Biologie Structurale (IBS), Université Grenoble Alpes-CEA-CNRS UMR 5075, Grenoble 38044, France.
Meytal LandauDepartment of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel. mlandau@technion.ac.il.ORCID 0000-0002-1743-3430
Technion – Israel Institute of Technology · ILCentre National de la Recherche Scientifique · FRHoward Hughes Medical Institute · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

Amyloids are ordered protein aggregates, found in all kingdoms of life, and are involved in aggregation diseases as well as in physiological activities. In microbes, functional amyloids are often key virulence determinants, yet the structural basis for their activity remains elusive. We determined the fibril structure and function of the highly toxic, 22-residue phenol-soluble modulin α3 (PSMα3) peptide secreted by

Indexed as

AmyloidBacterial ToxinsCells, CulturedCrystallography, X-RayHumansProtein ConformationStaphylococcus aureusT-LymphocytesAmyloidBacterial Toxinsstaphylococcal delta toxin

Identifiers

PMID28232575
PMCPMC6372758
OpenAlexW2915521488

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.