Evidence map›Paper›PMID 38252473›Full record

ArticleeLife2024

Disulfide bridge-dependent dimerization triggers FGF2 membrane translocation into the extracellular space.

Fabio Lolicato, Julia P Steringer, Roberto Saleppico, Daniel Beyer, Jaime Fernandez-Sobaberas, Sebastian Unger, Steffen Klein, Petra Riegerová, Sabine Wegehingel, Hans-Michael Müller and 8 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  5. Article
  6. Review
  7. 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

18 authors at 2 institutions in 4 countries.

Fabio Lolicato *Heidelberg University Biochemistry Center, Heidelberg, Germany.ORCID https://orcid.org/0000-0001-7537-0549
Julia P Steringer *Heidelberg University Biochemistry Center, Heidelberg, Germany.ORCID https://orcid.org/0000-0001-9418-2762
Roberto SaleppicoHeidelberg University Biochemistry Center, Heidelberg, Germany.ORCID https://orcid.org/0000-0003-0502-192X
Daniel BeyerHeidelberg University Biochemistry Center, Heidelberg, Germany.
Jaime Fernandez-SobaberasHeidelberg University Biochemistry Center, Heidelberg, Germany.
Sebastian UngerHeidelberg University Biochemistry Center, Heidelberg, Germany.
Steffen KleinSchaller Research Group, Department of Infectious Diseases-Virology, Heidelberg University Hospital, Heidelberg, Germany.
Petra RiegerováJ. Heyrovský Institute of Physical Chemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Sabine WegehingelHeidelberg University Biochemistry Center, Heidelberg, Germany.
Hans-Michael MüllerHeidelberg University Biochemistry Center, Heidelberg, Germany.ORCID https://orcid.org/0000-0002-2384-7285
Xiao J SchmittInstitute for Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany.
Shreyas KaptanDepartment of Physics, University of Helsinki, Helsinki, Finland.
Christian FreundInstitute for Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany.
Martin HofJ. Heyrovský Institute of Physical Chemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Radek ŠachlJ. Heyrovský Institute of Physical Chemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Petr ChlandaSchaller Research Group, Department of Infectious Diseases-Virology, Heidelberg University Hospital, Heidelberg, Germany.ORCID https://orcid.org/0000-0002-7782-2139
Ilpo VattulainenDepartment of Physics, University of Helsinki, Helsinki, Finland.ORCID https://orcid.org/0000-0001-7408-3214
Walter NickelHeidelberg University Biochemistry Center, Heidelberg, Germany.ORCID https://orcid.org/0000-0002-6496-8286
University of Helsinki · FIFreie Universität Berlin · DE

Funding

Academy of Finland 331349Academy of Finland 336234Academy of Finland 346135Deutsche Forschungsgemeinschaft DFG LO 2821/1-1Deutsche Forschungsgemeinschaft DFG Ni 423/10-1Deutsche Forschungsgemeinschaft DFG Ni 423/12-1Deutsche Forschungsgemeinschaft DFG Ni 423/13-1Deutsche Forschungsgemeinschaft INST 35/1314-1 FUGGDeutsche Forschungsgemeinschaft INST 35/1503-1 FUGGDeutsche Forschungsgemeinschaft SFB/TRR 186 project A1Deutsche Forschungsgemeinschaft SFB/TRR 186 project A5Deutsche Forschungsgemeinschaft SFB/TRR 83Grantová Agentura České Republiky 20-01401HORIZON EUROPE Marie Sklodowska-Curie Actions 101033606Human Frontier Science Program RGP0059/2019
6 · The paper itself

Abstract

Fibroblast growth factor 2 (FGF2) exits cells by direct translocation across the plasma membrane, a type I pathway of unconventional protein secretion. This process is initiated by phosphatidylinositol-4,5-bisphosphate (PI(4,5)P

Indexed as

Extracellular SpaceFibroblast Growth Factor 2DimerizationDisulfidesSodium-Potassium-Exchanging ATPaseDisulfidesFibroblast Growth Factor 2Sodium-Potassium-Exchanging ATPasebiochemistrychemical biologychocho k1E. coliFGF2hela s3Protein-lipid interactionProtein-protein interactionProtein traffickingUnconventional protein secretion

Identifiers

PMID38252473
PMCPMC10945597
OpenAlexW4378806566

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.