Evidence map›Paper›PMID 21734656›Full record

ArticleNature2011

Legionella pneumophila SidD is a deAMPylase that modifies Rab1.

Yunhao Tan, Zhao-Qing Luo

Abstract read
In one paragraph

Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 138 papers.

0numbers the graph read from it
0cells of the map it votes in
138citing papers in PubMed
15.8field-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

138 citing papers in PubMed, 219 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. AMPylation: key roles in biological regulation across prokaryotes and eukaryotes.Frontiers in cellular and infection microbiology · 2026
    Review
  5. Molecular evolution and adaptations ofFrontiers in cellular and infection microbiology · 2026
    Review
  6. Article
  7. Ribonuclease RNase Z is an evolutionarily conserved deAMPylase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Review
  9. Journal of bacteriology · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. TheProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Yunhao TanDepartment of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, Indiana 47907, USA.
Zhao-Qing Luo
State Street (United States) · US

Funding

Modulation of host Apoptotic pathways by Legionella pneumophilaR01AI069344 · NIAID · PURDUE UNIVERSITY · PI LUO, ZHAO-QING · 2007 to 2011
$1.5M
Modulation of Host Vesicle Trafficking by Legionella pneumophilaK02AI085403 · NIAID · PURDUE UNIVERSITY · PI LUO, ZHAO-QING · 2010 to 2014
$556k
The Roles of Host Factors in the AMPylation Activity of a Bacterial EffectorR21AI092043 · NIAID · PURDUE UNIVERSITY · PI LUO, ZHAO-QING · 2011 to 2012
$413k
NIAID NIH HHS K02 AI085403NIAID NIH HHS K02AI085403NIAID NIH HHS R01 AI069344NIAID NIH HHS R01AI069344NIAID NIH HHS R21 AI092043NIAID NIH HHS R21AI092043
6 · The paper itself

Abstract

Legionella pneumophila actively modulates host vesicle trafficking pathways to facilitate its intracellular replication with effectors translocated by the Dot/Icm type IV secretion system (T4SS). The SidM/DrrA protein functions by locking the small GTPase Rab1 into an active form by its guanine nucleotide exchange factor (GEF) and AMPylation activity. Here we demonstrate that the L. pneumophila protein SidD preferably deAMPylates Rab1. We found that the deAMPylation activity of SidD could suppress the toxicity of SidM to yeast and is required to release Rab1 from bacterial phagosomes efficiently. A molecular mechanism for the temporal control of Rab1 activity in different phases of L. pneumophila infection is thus established. These observations indicate that AMPylation-mediated signal transduction is a reversible process regulated by specific enzymes.

Indexed as

AnimalsAspartic AcidBacterial ProteinsCells, CulturedFemaleGuanine Nucleotide Exchange FactorsLegionella pneumophilaLegionnaires' DiseaseMacrophagesMicePhenotypePlasmidsrab1 GTP-Binding ProteinsSaccharomyces cerevisiaeTime FactorsTransformation, GeneticAspartic AcidBacterial ProteinsGuanine Nucleotide Exchange Factorsrab1 GTP-Binding ProteinsSidD protein, Legionella pneumophilaSidM protein, Legionella pneumophila

Identifiers

PMID21734656
PMCPMC3146296
OpenAlexW2080380126

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.