Evidence map›Paper›PMID 31690664›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Deubiquitination of phosphoribosyl-ubiquitin conjugates by phosphodiesterase-domain-containing

Min Wan, Alan G Sulpizio, Anil Akturk, Wendy H J Beck, Michael Lanz, Vitor M Faça, Marcus B Smolka, Joseph P Vogel, Yuxin Mao

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

72 citing papers in PubMed, 98 citations in OpenAlex.

  1. Life science alliance · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. mBio · 2026
    Article
  7. Article
  8. iScience · 2026
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Journal of bacteriology · 2024
    Review
  16. Review
  17. Article
  18. Covalent Probes To CaptureJournal of the American Chemical Society · 2024
    Article
  19. Article
  20. Article

12 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

9 authors at 2 institutions in 1 country.

Min WanWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853.
Alan G SulpizioWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853.
Anil AkturkWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853.ORCID 0000-0002-5792-4840
Wendy H J BeckWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853.
Michael LanzWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853.
Vitor M FaçaWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853.
Marcus B SmolkaWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853.
Joseph P VogelDepartment of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110.
Yuxin MaoWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853; ym253@cornell.edu.ORCID 0000-0002-5064-1397
Cornell University · USWashington University in St. Louis · US

Funding

Cellular Responses to DNA Replication StressR01GM097272 · NIGMS · CORNELL UNIVERSITY · PI SMOLKA, MARCUS · 2011 to 2020
$2.7M
Non-canonical phosphoribosyl ubiquitination and de-ubiquitination by legionella effectors (McMillan Supplement 2023)R01GM135379 · NIGMS · CORNELL UNIVERSITY · PI MAO, YUXIN · 2020 to 2023
$1.3M
THE MECHANISM OF A NOVEL FAMILY OF BACTERIAL UBIQUITIN E3 LIGASES IMPORTANT FOR PHAGOSOME REMODELINGR01GM116964 · NIGMS · CORNELL UNIVERSITY · PI MAO, YUXIN · 2016 to 2019
$1.3M
NIGMS NIH HHS R01 GM097272NIGMS NIH HHS R01 GM116964NIGMS NIH HHS R01 GM135379
6 · The paper itself

Abstract

Posttranslational protein modification by ubiquitin (Ub) is a central eukaryotic mechanism that regulates a plethora of physiological processes. Recent studies unveiled an unconventional type of ubiquitination mediated by the SidE family of

Indexed as

ADP-RibosylationBacterial ProteinsDeubiquitinating EnzymesGolgi ApparatusHeLa CellsHumansLegionella pneumophilaPhosphoric Diester HydrolasesProtein DomainsProtein Processing, Post-TranslationalUbiquitinUbiquitinationVacuolesBacterial ProteinsDeubiquitinating EnzymesPhosphoric Diester HydrolasesUbiquitindeubiquitinasephosphoribosyl ubiquitinationSdeASidEubiquitin

Identifiers

PMID31690664
PMCPMC6876201
OpenAlexW2984884237

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.