Evidence map›Paper›PMID 23213215›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

In vivo localization and identification of SUMOylated proteins in the brain of His6-HA-SUMO1 knock-in mice.

Marilyn Tirard, He-Hsuan Hsiao, Miroslav Nikolov, Henning Urlaub, Frauke Melchior, Nils Brose

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

54 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
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  7. Review
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  9. Signalling mechanisms and cellular functions of SUMO.Nature reviews. Molecular cell biology · 2022
    Review
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  12. Article
  13. Review
  14. Review
  15. Review
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  18. Small ubiquitin-like modifier 2 (SUMO2) is critical for memory processes in mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  19. Article
  20. Review
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

6 authors at 4 institutions in 1 country.

Marilyn TirardDepartment of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, 37075 Göttingen, Germany.
He-Hsuan Hsiao
Miroslav Nikolov
Henning Urlaub
Frauke Melchior
Nils Brose
Max Planck Institute for Biophysical Chemistry · DEMax Planck Institute of Experimental Medicine · DEHeidelberg University · DEUniversitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMOylation, an essential posttranslational protein modification, is involved in many eukaryotic cellular signaling pathways. The identification of SUMOylated proteins is difficult, because SUMOylation sites in proteins are hard to predict, SUMOylated protein states are transient in vivo and labile in vitro, only a small substrate fraction is SUMOylated in vivo, and identification tools for natively SUMOylated proteins are rare. To solve these problems, we generated knock-in mice expressing His(6)-HA-SUMO1. By anti-HA immunostaining, we show that SUMO1 conjugates in neurons are only detectable in nuclei and annulate lamellae. By anti-HA affinity purification, we identified several hundred candidate SUMO1 substrates, of which we validated Smchd1, Ctip2, TIF1γ, and Zbtb20 as novel substrates. The knock-in mouse represents an excellent mammalian model for studies on SUMO1 localization and screens for SUMO1 conjugates in vivo.

Indexed as

AnimalsBrainCell NucleusCells, CulturedHippocampusImmunohistochemistryMass SpectrometryMiceMice, TransgenicModels, BiologicalNeuronsProtein BindingSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO2 protein, mouse

Identifiers

PMID23213215
PMCPMC3529052
OpenAlexW2025209619

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.