Evidence map›Paper›PMID 21262847›Full record

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

Interactions of anthrax lethal factor with protective antigen defined by site-directed spin labeling.

Laura D Jennings-Antipov, Likai Song, R John Collier

Open access · bronzeAbstract 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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.1field-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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Small molecule inhibitors of anthrax lethal factor toxin.Bioorganic & medicinal chemistry · 2014
    Article
  5. Article
  6. Article
  7. Assembly of anthrax toxin pore: lethal-factor complexes into lipid nanodiscs.Protein science : a publication of the Protein Society · 2013
    Article
  8. Ratcheting up protein translocation with anthrax toxin.Protein science : a publication of the Protein Society · 2012
    Review
  9. Ultrasensitive detection of protein translocated through toxin pores in droplet-interface bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  10. Article
  11. 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

3 authors at 1 institution in 1 country.

Laura D Jennings-AntipovDepartment of Microbiology and Molecular Genetics and Medicine, Harvard Medical School, Boston, MA 02115, USA.
Likai Song
R John Collier
Harvard University · 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

The protective antigen (PA) moiety of anthrax toxin forms oligomeric pores that translocate the enzymatic moieties of the toxin--lethal factor (LF) and edema factor (EF)--across the endosomal membrane of mammalian cells. Here we describe site-directed spin-labeling studies that identify interactions of LF with the prepore and pore conformations of PA. Our results reveal a direct interaction between the extreme N terminus of LF (residues 2-5) and the Φ-clamp, a structure within the lumen of the pore that catalyzes translocation. Also, consistent with a recent crystallographic model, we find that, upon binding of the translocation substrate to PA, LF helix α1 separates from helices α2 and α3 and binds in the α-clamp of PA. These interactions, together with the binding of the globular part of the N-terminal domain of LF to domain 1' of PA, indicate that LF interacts with the PA pore at three distinct sites. Our findings elucidate the state from which translocation of LF and EF proceeds through the PA pore.

Indexed as

Spin LabelsAntigens, BacterialBacterial ToxinsCrystallography, X-RayLipid BilayersModels, Molecularanthrax toxinAntigens, BacterialBacterial ToxinsLipid BilayersSpin Labels

Identifiers

PMID21262847
PMCPMC3033316
OpenAlexW1988409540

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.