Evidence map›Paper›PMID 18845756›Full record

ArticleScience (New York, N.Y.)2008

Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain.

Patrick J Lupardus, Aimee Shen, Matthew Bogyo, K Christopher Garcia

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
8.7field-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

76 citing papers in PubMed, 127 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Effects of Bile on PathogenicBiomolecules · 2025
    Article
  5. Review
  6. Article
  7. Allosterically switchable network orientsProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. ThemBio · 2022
    Article
  15. Actin Cross-Linking Effector Domain of theInfection and immunity · 2022
    Article
  16. Large Clostridial Toxins: Mechanisms and Roles in Disease.Microbiology and molecular biology reviews : MMBR · 2021
    Review
  17. Article
  18. Review
  19. Article
  20. Virulence Regulation and Innate Host Response in the Pathogenicity ofFrontiers in cellular and infection microbiology · 2020
    Review

16 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

4 authors at 2 institutions in 1 country.

Patrick J LupardusDepartment of Molecular and Cellular Physiology and Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Aimee Shen
Matthew Bogyo
K Christopher Garcia
Howard Hughes Medical Institute · USStanford University · US

Funding

CORE 6 : PROJECT LEADERSHIP AND ADMINISTRATIONU54RR020843 · NCRR · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI SMITH, JEFFREY W · 2004 to 2009
$19.1M
Small Molecule Imaging of Protease ActivityR01EB005011 · NIBIB · STANFORD UNIVERSITY · PI BOGYO, MATTHEW · 2005 to 2013
$3.0M
Chemically Mapping Malarial Rupture ProteasesR01AI078947 · NIAID · STANFORD UNIVERSITY · PI BOGYO, MATTHEW · 2009 to 2013
$2.0M
Howard Hughes Medical InstituteNCRR NIH HHS U54RR020843NIAID NIH HHS R01 AI078947NIBIB NIH HHS R01 EB005011
6 · The paper itself

Abstract

Vibrio cholerae RTX (repeats in toxin) is an actin-disrupting toxin that is autoprocessed by an internal cysteine protease domain (CPD). The RTX CPD is efficiently activated by the eukaryote-specific small molecule inositol hexakisphosphate (InsP6), and we present the 2.1 angstrom structure of the RTX CPD in complex with InsP6. InsP6 binds to a conserved basic cleft that is distant from the protease active site. Biochemical and kinetic analyses of CPD mutants indicate that InsP6 binding induces an allosteric switch that leads to the autoprocessing and intracellular release of toxin-effector domains.

Indexed as

AcyltransferasesAllosteric RegulationBacterial ProteinsBacterial ToxinsBinding SitesCatalytic DomainCrystallography, X-RayCysteine EndopeptidasesEnzyme ActivationGuanosine 5'-O-(3-Thiotriphosphate)Hydrogen BondingModels, MolecularPhytic AcidPoint MutationProtein Structure, SecondarySurface Plasmon ResonanceAcyltransferasesBacterial ProteinsBacterial ToxinsCysteine EndopeptidasesGuanosine 5'-O-(3-Thiotriphosphate)Phytic AcidRtxC protein, Vibrio cholerae

Identifiers

PMID18845756
PMCPMC3272704
OpenAlexW2041664602

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.