Evidence map›Paper›PMID 29686075›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Molecular mechanism to recruit galectin-3 into multivesicular bodies for polarized exosomal secretion.

Sebastian Bänfer, Dominik Schneider, Jenny Dewes, Maximilian T Strauss, Sven-A Freibert, Thomas Heimerl, Uwe G Maier, Hans-Peter Elsässer, Ralf Jungmann, Ralf Jacob

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

90 citing papers in PubMed, 126 citations in OpenAlex.

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  11. The Role of Galectin-3 in Liver Inflammation and Fibrosis.Journal of inflammation research · 2026
    Review
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30 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

10 authors at 3 institutions in 1 country.

Sebastian BänferDepartment of Cell Biology and Cell Pathology, Philipps University Marburg, 35032 Marburg, Germany.
Dominik SchneiderDepartment of Cell Biology and Cell Pathology, Philipps University Marburg, 35032 Marburg, Germany.
Jenny DewesDepartment of Cell Biology and Cell Pathology, Philipps University Marburg, 35032 Marburg, Germany.
Maximilian T StraussDepartment of Physics and Center for Nanoscience, Ludwig Maximilian University, 80539 Munich, Germany.
Sven-A FreibertDepartment of Cell Biology and Cell Pathology, Philipps University Marburg, 35032 Marburg, Germany.ORCID 0000-0002-8521-2963
Thomas HeimerlLOEWE Centre for Synthetic Microbiology, Philipps University Marburg, 35032 Marburg, Germany.
Uwe G MaierLOEWE Centre for Synthetic Microbiology, Philipps University Marburg, 35032 Marburg, Germany.
Hans-Peter ElsässerDepartment of Cell Biology and Cell Pathology, Philipps University Marburg, 35032 Marburg, Germany.
Ralf JungmannDepartment of Physics and Center for Nanoscience, Ludwig Maximilian University, 80539 Munich, Germany.
Ralf JacobDepartment of Cell Biology and Cell Pathology, Philipps University Marburg, 35032 Marburg, Germany; jacob@staff.uni-marburg.de.
Philipps University of Marburg · DECenter for NanoScience · DELoewe Center for Synthetic Microbiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The beta-galactoside binding lectin galectin-3 (Gal3) is found intracellularly and in the extracellular space. Secretion of this lectin is mediated independently of the secretory pathway by a not yet defined nonclassical mechanism. Here, we found Gal3 in the lumen of exosomes. Superresolution and electron microscopy studies visualized Gal3 recruitment and sorting into intraluminal vesicles. Exosomal Gal3 release depends on the endosomal sorting complex required for transport I (ESCRT-I) component Tsg101 and functional Vps4a. Either Tsg101 knockdown or expression of dominant-negative Vps4a

Indexed as

AnimalsDNA-Binding ProteinsDogsEndosomal Sorting Complexes Required for TransportEndosomesExosomesGalectin 3Madin Darby Canine Kidney CellsMicroscopy, ElectronMultivesicular BodiesTranscription FactorsTsg101 ProteinVacuolar Proton-Translocating ATPasesDNA-Binding ProteinsEndosomal Sorting Complexes Required for TransportGalectin 3Transcription FactorsTsg101 ProteinVacuolar Proton-Translocating ATPasesESCRTexosomesgalectinsP(S/T)AP motifunconventional secretion

Identifiers

PMID29686075
PMCPMC5948969
OpenAlexW2801966687

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.