Evidence map›Paper›PMID 28645896›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Nucleotide-dependent farnesyl switch orchestrates polymerization and membrane binding of human guanylate-binding protein 1.

Sergii Shydlovskyi, Anke Y Zienert, Semra Ince, Christine Dovengerds, Annika Hohendahl, Julia M Dargazanli, Ailisa Blum, Saskia D Günther, Nikolay Kladt, Michael Stürzl and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Article
  8. Autophagy and Bacterial infections.Autophagy reports · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Integrative modeling of guanylate binding protein dimers.Protein science : a publication of the Protein Society · 2023
    Article
  14. Article
  15. Article
  16. Human GBP1 Is Involved in the Repair of Damaged Phagosomes/Endolysosomes.International journal of molecular sciences · 2023
    Article
  17. LPS-aggregating proteins GBP1 and GBP2 are each sufficient to enhance caspase-4 activation both in cellulo and in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Review
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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

15 authors at 4 institutions in 2 countries.

Sergii ShydlovskyiPhysical Chemistry I, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, D-44780 Bochum, Germany.
Anke Y ZienertInstitute for Genetics, University of Cologne, D-50674 Cologne, Germany.
Semra IncePhysical Chemistry I, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, D-44780 Bochum, Germany.
Christine DovengerdsPhysical Chemistry I, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, D-44780 Bochum, Germany.
Annika HohendahlBiochemistry Department, University of Geneva, CH-1211 Geneva, Switzerland.
Julia M DargazanliInstitute for Genetics, University of Cologne, D-50674 Cologne, Germany.
Ailisa BlumInstitute for Genetics, University of Cologne, D-50674 Cologne, Germany.
Saskia D GüntherInstitute for Genetics, University of Cologne, D-50674 Cologne, Germany.
Nikolay KladtCologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases, Institute for Genetics, University of Cologne, D-50931 Cologne, Germany.
Michael StürzlDivision of Molecular and Experimental Surgery, Department of Surgery, University Medical Center Erlangen, Friedrich-Alexander University Erlangen-Nürnberg, D-91054 Erlangen, Germany.ORCID 0000-0002-9276-2824
Astrid C SchaussCologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases, Institute for Genetics, University of Cologne, D-50931 Cologne, Germany.
Miriam KutschPhysical Chemistry I, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, D-44780 Bochum, Germany.
Aurélien RouxBiochemistry Department, University of Geneva, CH-1211 Geneva, Switzerland.ORCID 0000-0002-6088-0711
Gerrit J K PraefckeInstitute for Genetics, University of Cologne, D-50674 Cologne, Germany; chr.herrmann@rub.de gerrit.praefcke@pei.de.
Christian HerrmannPhysical Chemistry I, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, D-44780 Bochum, Germany; chr.herrmann@rub.de gerrit.praefcke@pei.de.ORCID 0000-0002-1824-3647
University of Cologne · DERuhr University Bochum · DEUniversity of Geneva · CHFriedrich-Alexander-Universität Erlangen-Nürnberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dynamin-like proteins (DLPs) mediate various membrane fusion and fission processes within the cell, which often require the polymerization of DLPs. An IFN-inducible family of DLPs, the guanylate-binding proteins (GBPs), is involved in antimicrobial and antiviral responses within the cell. Human guanylate-binding protein 1 (hGBP1), the founding member of GBPs, is also engaged in the regulation of cell adhesion and migration. Here, we show how the GTPase cycle of farnesylated hGBP1 (hGBP1

Indexed as

Binding SitesCatalysisCell MembraneGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateHeLa CellsHumansHydrolysisImmunity, InnateLiposomesMicroscopy, ElectronPolymerizationPolymersPrenylationGBP1 protein, humanGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateLiposomesPolymersGBPslarge GTPasesmembrane bindingmembrane tetheringpolymerization

Identifiers

PMID28645896
PMCPMC5514708
OpenAlexW2701613709

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.