Evidence map›Paper›PMID 37186457›Full record

ArticleJournal of extracellular vesicles2023

Quantitative imaging of vesicle-protein interactions reveals close cooperation among proteins.

Minkwon Cha, Sang Hyeok Jeong, Jaehun Jung, Yoonjin Baeg, Sung-Soo Park, Seoyoon Bae, Chan Seok Lim, Jun Hyuk Park, Jie-Oh Lee, Yong Song Gho and 2 more

Open access · goldAbstract read
In one paragraph

Article in Journal of extracellular vesicles, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. Rethinking Extracellular Vesicle Signaling.Advanced materials (Deerfield Beach, Fla.) · 2026
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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

12 authors at 2 institutions in 1 country.

Minkwon ChaDepartment of Physics, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Sang Hyeok JeongDepartment of Physics, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Jaehun JungDepartment of Physics, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Yoonjin BaegBiodrone Research Institute, MDimune Inc., Seoul, Republic of Korea.
Sung-Soo ParkBiodrone Research Institute, MDimune Inc., Seoul, Republic of Korea.
Seoyoon BaeDepartment of Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Chan Seok LimDepartment of Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Jun Hyuk ParkDepartment of Physics, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Jie-Oh LeeDepartment of Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Yong Song GhoDepartment of Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.ORCID 0000-0003-3366-2345
Seung Wook OhBiodrone Research Institute, MDimune Inc., Seoul, Republic of Korea.
Min Ju ShonDepartment of Physics, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.ORCID 0000-0002-0333-1150
Pohang University of Science and Technology · KRMarine Biodiversity Institute of Korea · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane-bound vesicles such as extracellular vesicles (EVs) can function as biochemical effectors on target cells. Docking of the vesicles onto recipient plasma membranes depends on their interaction with cell-surface proteins, but a generalizable technique that can quantitatively observe these vesicle-protein interactions (VPIs) is lacking. Here, we describe a fluorescence microscopy that measures VPIs between single vesicles and cell-surface proteins, either in a surface-tethered or in a membrane-embedded state. By employing cell-derived vesicles (CDVs) and intercellular adhesion molecule-1 (ICAM-1) as a model system, we found that integrin-driven VPIs exhibit distinct modes of affinity depending on vesicle origin. Controlling the surface density of proteins also revealed a strong support from a tetraspanin protein CD9, with a critical dependence on molecular proximity. An adsorption model accounting for multiple protein molecules was developed and captured the features of density-dependent cooperativity. We expect that VPI imaging will be a useful tool to dissect the molecular mechanisms of vesicle adhesion and uptake, and to guide the development of therapeutic vesicles.

Indexed as

Extracellular VesiclesCell CommunicationCell MembraneMembrane ProteinsMembrane ProteinsCD9cell-derived vesiclesICAM-1integrintotal internal reflection fluorescence microscopyvesicle-protein interactions

Identifiers

PMID37186457
PMCPMC10130417
OpenAlexW4367054194

What Socratic 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 Socratic graph.