Evidence map›Paper›PMID 25073739›Full record

ArticleMolecular & cellular proteomics : MCP2014

Copper-catalyzed azide-alkyne cycloaddition (click chemistry)-based detection of global pathogen-host AMPylation on self-assembled human protein microarrays.

Xiaobo Yu, Andrew R Woolery, Phi Luong, Yi Heng Hao, Markus Grammel, Nathan Westcott, Jin Park, Jie Wang, Xiaofang Bian, Gokhan Demirkan and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Functionalised Cofactor Mimics for Interactome Discovery and Beyond.Angewandte Chemie (International ed. in English) · 2022
    Review
  6. Article
  7. MS-BasedACS infectious diseases · 2020
    Article
  8. Article
  9. Developments and Applications of Functional Protein Microarrays.Molecular & cellular proteomics : MCP · 2020
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Mapping transcription factor interactome networks using HaloTag protein arrays.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Review
  16. Article
  17. Article
  18. Structure and function of Fic proteins.Nature reviews. Microbiology · 2015
    Review
  19. Plasma Autoantibodies Associated with Basal-like Breast Cancers.Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology · 2015
    Article
  20. Article
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

13 authors at 4 institutions in 1 country.

Xiaobo YuFrom the ‡The Virginia G. Piper Center for Personalized Diagnostics, Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA;
Andrew R Woolery§Department of Molecular Biology, UT Southwestern Medical Center, Dallas, Texas 75390-9148, USA;
Phi Luong§Department of Molecular Biology, UT Southwestern Medical Center, Dallas, Texas 75390-9148, USA;
Yi Heng Hao§Department of Molecular Biology, UT Southwestern Medical Center, Dallas, Texas 75390-9148, USA;
Markus Grammel¶The Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York 10065, USA.
Nathan Westcott¶The Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York 10065, USA.
Jin ParkFrom the ‡The Virginia G. Piper Center for Personalized Diagnostics, Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA;
Jie WangFrom the ‡The Virginia G. Piper Center for Personalized Diagnostics, Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA;
Xiaofang BianFrom the ‡The Virginia G. Piper Center for Personalized Diagnostics, Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA;
Gokhan DemirkanFrom the ‡The Virginia G. Piper Center for Personalized Diagnostics, Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA;
Howard C Hang¶The Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York 10065, USA.
Kim Orth§Department of Molecular Biology, UT Southwestern Medical Center, Dallas, Texas 75390-9148, USA;
Joshua LaBaerFrom the ‡The Virginia G. Piper Center for Personalized Diagnostics, Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA; jlabaer@asu.edu.
Arizona State University · USRockefeller University · USThe University of Texas Southwestern Medical Center · USSouthwestern Medical Center

Funding

Biomarker Detection Using NAPPA Tumor Antigen ArraysU01CA117374 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI ANDERSON, KAREN SUE, LABAER, JOSHUA · 2005 to 2015
$6.2M
Biochemical Characterization of Yersinia Effector YopJ.R01AI056404 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI ORTH, KIM · 2003 to 2012
$2.8M
Analysis of an orchestrated cell death mediated by Vibrio parahaemolytics T3SS1R01AI087808 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI ORTH, KIM · 2010 to 2014
$1.9M
NCI NIH HHS 5U01CA117374NCI NIH HHS U01 CA117374NIAID NIH HHS R01 AI056404NIAID NIH HHS R01-AI056404NIAID NIH HHS R01 AI087808NIAID NIH HHS R01-AI087808
6 · The paper itself

Abstract

AMPylation (adenylylation) is a recently discovered mechanism employed by infectious bacteria to regulate host cell signaling. However, despite significant effort, only a few host targets have been identified, limiting our understanding of how these pathogens exploit this mechanism to control host cells. Accordingly, we developed a novel nonradioactive AMPylation screening platform using high-density cell-free protein microarrays displaying human proteins produced by human translational machinery. We screened 10,000 unique human proteins with Vibrio parahaemolyticus VopS and Histophilus somni IbpAFic2, and identified many new AMPylation substrates. Two of these, Rac2, and Rac3, were confirmed in vivo as bona fide substrates during infection with Vibrio parahaemolyticus. We also mapped the site of AMPylation of a non-GTPase substrate, LyGDI, to threonine 51, in a region regulated by Src kinase, and demonstrated that AMPylation prevented its phosphorylation by Src. Our results greatly expanded the repertoire of potential host substrates for bacterial AMPylators, determined their recognition motif, and revealed the first pathogen-host interaction AMPylation network. This approach can be extended to identify novel substrates of AMPylators with different domains or in different species and readily adapted for other post-translational modifications.

Indexed as

Cycloaddition ReactionAdenosine MonophosphateBacterial ProteinsBase SequenceClick ChemistryCopperHost-Pathogen InteractionsHumansPasteurellaceaeProtein Array AnalysisProtein Processing, Post-TranslationalProtein Structure, TertiaryRAC2 GTP-Binding Proteinrac GTP-Binding Proteinsrho Guanine Nucleotide Dissociation Inhibitor betaVibrio InfectionsAdenosine MonophosphateARHGDIB protein, humanBacterial ProteinsCopperRAC2 GTP-Binding ProteinRAC3 protein, humanrac GTP-Binding Proteinsrho Guanine Nucleotide Dissociation Inhibitor beta

Identifiers

PMID25073739
PMCPMC4223499
OpenAlexW2121866927

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.