Evidence map›Paper›PMID 27276264›Full record

ArticleBiophysical journal2016

Oligomerization of the Tetraspanin CD81 via the Flexibility of Its δ-Loop.

Thomas H Schmidt, Yahya Homsi, Thorsten Lang

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. The SMARCA4-TMEM47 axis plays an essential role in chikungunya virus RNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. The molecular mechanism of CD81 antibody inhibition of metastasis.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Assembly and Analysis of Cell-Scale Membrane Envelopes.Journal of chemical information and modeling · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Tetraspanin Assemblies in Virus Infection.Frontiers in immunology · 2018
    Review
  16. Article
  17. Article
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

3 authors at 1 institution in 1 country.

Thomas H SchmidtMembrane Biochemistry, Life and Medical Sciences Institute, Bonn, Germany. Electronic address: thomas.schmidt@uni-bonn.de.
Yahya HomsiMembrane Biochemistry, Life and Medical Sciences Institute, Bonn, Germany.
Thorsten LangMembrane Biochemistry, Life and Medical Sciences Institute, Bonn, Germany. Electronic address: thorsten.lang@uni-bonn.de.
Life & Brain (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tetraspanins are master organizers in the plasma membrane, forming tetraspanin-enriched microdomains with one another and other surface molecules. Their rod-shaped structure includes a large extracellular loop (LEL) that plays a pivotal role in tetraspanin network formation. We performed comparative atomistic and coarse-grain molecular-dynamics simulations of the LEL in isolation and full-length CD81, and reproduced LEL flexibility patterns known from wet-lab experiments in which the LEL δ-loop region showed a pronounced flexibility. In a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine lipid bilayer and a plasma membrane environment, the conformational flexibility of the δ-loop initiates CD81-CD81 contacts for oligomerization. Furthermore, in the plasma membrane, CD81-ganglioside bridges arising from preformed glycolipid patches cross-link the complexes. The data suggest that exposing a flexible domain enables binding to interaction partners by circumventing the restriction of orientation and conformational freedom of membrane proteins.

Indexed as

Cell MembraneElasticityGangliosidesHumansJurkat CellsLipid BilayersMolecular Dynamics SimulationPhosphatidylcholinesProtein MultimerizationProtein Structure, SecondarySolventsTetraspanin 281-palmitoyl-2-oleoylphosphatidylcholineCD81 protein, humanGangliosidesLipid BilayersPhosphatidylcholinesSolventsTetraspanin 28

Identifiers

PMID27276264
PMCPMC4906359
OpenAlexW2418598518

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.