Evidence map›Paper›PMID 19897724›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Activation of the abundant nuclear factor poly(ADP-ribose) polymerase-1 by Helicobacter pylori.

Carlos W Nossa, Prashant Jain, Batcha Tamilselvam, Vijay R Gupta, Lin-Feng Chen, Valérie Schreiber, Serge Desnoyers, Steven R Blanke

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Protective effects of 18β-glycyrrhetinic acid onFrontiers in veterinary science · 2024
    Article
  4. The role of the inflammasome and its related pathways in ovarian cancer.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2022
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Electroporation of functional bacterial effectors into mammalian cells.Journal of visualized experiments : JoVE · 2015
    Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

8 authors at 4 institutions in 4 countries.

Carlos W NossaDepartment of Microbiology and the Institute for Genomic Biology and Department of Biochemistry, University of Illinois, Urbana, IL 61801, USA.
Prashant Jain
Batcha Tamilselvam
Vijay R Gupta
Lin-Feng Chen
Valérie Schreiber
Serge Desnoyers
Steven R Blanke
University of Illinois Urbana-Champaign · USCentre hospitalier de l'Université Laval · CAÉcole Supérieure de Biotechnologie de Strasbourg · FRUniversity of Houston · US

Funding

MOLECULAR MECHANISMS OF THE H. PYLORI VACUOLATING TOXINR01AI045928 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI BLANKE, STEVEN R. · 2000 to 2010
$1.9M
NF-kB Signaling and H. Pylori-induced Gastric DiseaseR01DK085158 · NIDDK · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI CHEN, LIN-FENG · 2010 to 2014
$1.6M
NIAID NIH HHS R01 AI045928NIDDK NIH HHS R01 DK085158
6 · The paper itself

Abstract

Modification of eukaryotic proteins is a powerful strategy used by pathogenic bacteria to modulate host cells during infection. Previously, we demonstrated that Helicobacter pylori modify an unidentified protein within mammalian cell lysates in a manner consistent with the action of a bacterial ADP-ribosylating toxin. Here, we identified the modified eukaryotic factor as the abundant nuclear factor poly(ADP-ribose) polymerase-1 (PARP-1), which is important in the pathologies of several disease states typically associated with chronic H. pylori infection. However, rather than being ADP-ribosylated by an H. pylori toxin, the intrinsic poly(ADP-ribosyl) polymerase activity of PARP-1 is activated by a heat- and protease-sensitive H. pylori factor, resulting in automodification of PARP-1 with polymers of poly(ADP-ribose) (PAR). Moreover, during infection of gastric epithelial cells, H. pylori induce intracellular PAR-production by a PARP-1-dependent mechanism. Activation of PARP-1 by a pathogenic bacterium represents a previously unrecognized strategy for modulating host cell signaling during infection.

Indexed as

Adenosine Diphosphate RiboseAnimalsCatalytic DomainEnzyme ActivationEpithelial CellsGastric MucosaHeLa CellsHelicobacter InfectionsHelicobacter pyloriHumansMiceMice, KnockoutPhosphorus RadioisotopesPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesAdenosine Diphosphate RibosePARP1 protein, humanPhosphorus RadioisotopesPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerases

Identifiers

PMID19897724
PMCPMC2785281
OpenAlexW2042211010

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.