Evidence map›Paper›PMID 23776219›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Prenylome profiling reveals S-farnesylation is crucial for membrane targeting and antiviral activity of ZAP long-isoform.

Guillaume Charron, Melody M H Li, Margaret R MacDonald, Howard C Hang

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

83 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. The poplar pathogenMicrobial genomics · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Host ZAP activity correlates with the levels of CpG suppression in primate lentiviruses.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Modulation of host gene expression by the zinc finger antiviral protein.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

23 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

4 authors at 1 institution in 1 country.

Guillaume CharronLaboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, USA.
Melody M H Li
Margaret R MacDonald
Howard C Hang
Rockefeller University · US

Funding

Studies on Protein LipidationR01GM087544 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI HANG, HOWARD C · 2010 to 2023
$4.4M
Studies on ZAP, a broad-spectrum alphavirus inhibitorR01AI057905 · NIAID · ROCKEFELLER UNIVERSITY · PI MACDONALD, MARGARET R · 2005 to 2009
$1.8M
NIAID NIH HHS AI057905NIAID NIH HHS R01 AI057905NIGMS NIH HHS 1R01GM087544NIGMS NIH HHS R01 GM087544
6 · The paper itself

Abstract

S-prenylation is an important lipid modification that targets proteins to membranes for cell signaling and vesicle trafficking in eukaryotes. As S-prenylated proteins are often key effectors for oncogenesis, congenital disorders, and microbial pathogenesis, robust proteomic methods are still needed to biochemically characterize these lipidated proteins in specific cell types and disease states. Here, we report that bioorthogonal proteomics of macrophages with an improved alkyne-isoprenoid chemical reporter enables large-scale profiling of prenylated proteins, as well as the discovery of unannotated lipidated proteins such as isoform-specific S-farnesylation of zinc-finger antiviral protein (ZAP). Notably, S-farnesylation was crucial for targeting the long-isoform of ZAP (ZAPL/PARP-13.1/zc3hav1) to endolysosomes and enhancing the antiviral activity of this immune effector. These studies demonstrate the utility of isoprenoid chemical reporters for proteomic analysis of prenylated proteins and reveal a role for protein prenylation in host defense against viral infections.

Indexed as

Protein PrenylationAmino Acid SequenceAnimalsCell LineHEK293 CellsHeLa CellsHost-Pathogen InteractionsHumansIntracellular MembranesLipoproteinsMacrophagesMiceMolecular Sequence DataPrenylationProtein IsoformsRatsLipoproteinsProtein IsoformsRNA-Binding ProteinsZAP antiviral protein, mouseZC3HAV1 protein, humanantiviral effectorbioorthogonal labelingclick chemistrylipid chemical reporterprotein prenylation

Identifiers

PMID23776219
PMCPMC3703996
OpenAlexW1979071042

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.