Evidence map›Paper›PMID 21949363›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Ultrasensitive detection of protein translocated through toxin pores in droplet-interface bilayers.

Audrey Fischer, Matthew A Holden, Brad L Pentelute, R John Collier

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 37 citations in OpenAlex.

  1. Covalently Linked Peptides and Membrane Potential Enable CyaA Segment Translocation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Controlled assembly and sophisticated additive manufacturing of macroscopic droplets.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Probing membrane protein properties using droplet interface bilayers.Experimental biology and medicine (Maywood, N.J.) · 2019
    Article
  8. Article
  9. Studies of RNA Sequence and Structure Using Nanopores.Progress in molecular biology and translational science · 2016
    Review
  10. Article
  11. Article
  12. Article
  13. Bordetella pertussis adenylate cyclase toxin translocation across a tethered lipid bilayer.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. Article
  15. Article
  16. Review
  17. Ratcheting up protein translocation with anthrax toxin.Protein science : a publication of the Protein Society · 2012
    Review
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 2 institutions in 1 country.

Audrey FischerDepartment of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA, USA.
Matthew A Holden
Brad L Pentelute
R John Collier
Harvard University · USUniversity of Massachusetts Amherst · US

Funding

Treatments for Nipah Virus InfectionU54AI057159 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI RIDER, TODD H. · 2003 to 2013
$113.7M
MOLECULAR MECHANISMS OF BACTERIAL PATHOGENESISR37AI022021 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI COLLIER, ROBERT JOHN · 1988 to 2007
$6.1M
MOLECULAR MECHANISMS OF BACTERIAL PATHOGENESISR01AI022021 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI COLLIER, ROBERT JOHN · 1985 to 2012
$3.9M
NIAID NIH HHS AI022021NIAID NIH HHS AI057159NIAID NIH HHS R01 AI022021NIAID NIH HHS R37 AI022021NIAID NIH HHS U54 AI057159
6 · The paper itself

Abstract

Many bacterial toxins form proteinaceous pores that facilitate the translocation of soluble effector proteins across cellular membranes. With anthrax toxin this process may be monitored in real time by electrophysiology, where fluctuations in ionic current through these pores inserted in model membranes are used to infer the translocation of individual protein molecules. However, detecting the minute quantities of translocated proteins has been a challenge. Here, we describe use of the droplet-interface bilayer system to follow the movement of proteins across a model membrane separating two submicroliter aqueous droplets. We report the capture and subsequent direct detection of as few as 100 protein molecules that have translocated through anthrax toxin pores. The droplet-interface bilayer system offers new avenues of approach to the study of protein translocation.

Indexed as

Antigens, BacterialBacterial ToxinsCarrier ProteinsElectrophysiologyLipid BilayersPore Forming Cytotoxic ProteinsProtein Transportanthrax toxinAntigens, BacterialBacterial ToxinsCarrier ProteinsLipid BilayersPore Forming Cytotoxic Proteins

Identifiers

PMID21949363
PMCPMC3189069
OpenAlexW2130947724

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.