Evidence map›Paper›PMID 21680813›Full record

ArticleScience (New York, N.Y.)2011

De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila.

M Ramona Neunuebel, Yang Chen, Andrew H Gaspar, Peter S Backlund, Alfred Yergey, Matthias P Machner

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.

0numbers the graph read from it
0cells of the map it votes in
130citing papers in PubMed
15.6field-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

130 citing papers in PubMed, 231 citations in OpenAlex.

  1. PHLPP is neither a Phosphatase nor a Tumor Suppressor.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. AMPylation: key roles in biological regulation across prokaryotes and eukaryotes.Frontiers in cellular and infection microbiology · 2026
    Review
  3. Molecular evolution and adaptations ofFrontiers in cellular and infection microbiology · 2026
    Review
  4. Review
  5. Journal of bacteriology · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. AMPylation and Endoplasmic Reticulum Protein Folding Homeostasis.Cold Spring Harbor perspectives in biology · 2023
    Review
  18. Article
  19. Article
  20. VpdC is a ubiquitin-activated phospholipase effector that regulatesProceedings of the National Academy of Sciences of the United States of America · 2022
    Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

M Ramona NeunuebelCell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
Yang Chen
Andrew H Gaspar
Peter S Backlund
Alfred Yergey
Matthias P Machner
National Institutes of Health · USEunice Kennedy Shriver National Institute of Child Health and Human Development · USPeking University · CN

Funding

Virulence strategies of the respiratory pathogen Legionella pneumophilaZIAHD008893 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI MACHNER, MATTHIAS · 2010 to 2025
$19.6M
Characterization Of Proteins By Mass SpectrometryZICHD001421 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI STRATAKIS, CONSTANTINE A. · 2009 to 2018
$9.6M
Intramural NIH HHS ZIA HD008893
6 · The paper itself

Abstract

The bacterial pathogen Legionella pneumophila exploits host cell vesicle transport by transiently manipulating the activity of the small guanosine triphosphatase (GTPase) Rab1. The effector protein SidM recruits Rab1 to the Legionella-containing vacuole (LCV), where it activates Rab1 and then AMPylates it by covalently adding adenosine monophosphate (AMP). L. pneumophila GTPase-activating protein LepB inactivates Rab1 before its removal from LCVs. Because LepB cannot bind AMPylated Rab1, the molecular events leading to Rab1 inactivation are unknown. We found that the effector protein SidD from L. pneumophila catalyzed AMP release from Rab1, generating de-AMPylated Rab1 accessible for inactivation by LepB. L. pneumophila mutants lacking SidD were defective for Rab1 removal from LCVs, identifying SidD as the missing link connecting the processes of early Rab1 accumulation and subsequent Rab1 removal during infection.

Indexed as

Adenosine MonophosphateAnimalsBacterial ProteinsChlorocebus aethiopsCOS CellsGolgi ApparatusGuanine Nucleotide Exchange FactorsGuanosine MonophosphateGuanosine TriphosphateHumansLegionella pneumophilaLigandsMacrophagesMiceMice, Inbred AModels, BiologicalAdenosine MonophosphateBacterial ProteinsGuanine Nucleotide Exchange FactorsGuanosine MonophosphateGuanosine TriphosphateLepB protein, Legionella pneumophilaLigandsMutant Proteinsrab1 GTP-Binding ProteinsSidD protein, Legionella pneumophilaSidM protein, Legionella pneumophila

Identifiers

PMID21680813
PMCPMC3209958
OpenAlexW1977272060

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.