Evidence map›Paper›PMID 27038819›Full record

ArticleEuropean biophysics journal : EBJ2016

Probing the structure and dynamics of caveolin-1 in a caveolae-mimicking asymmetric lipid bilayer model.

Hanqi Liu, Linlin Yang, Qiansen Zhang, Lingxue Mao, Hualiang Jiang, Huaiyu Yang

Abstract read
PubMed Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Caveolin assemblies displace one bilayer leaflet to organize and bend membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. Rafting on the Plasma Membrane: Lipid Rafts in Signaling and Disease.Advances in experimental medicine and biology · 2023
    Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. 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

6 authors at 2 institutions in 1 country.

Hanqi LiuSchool of Pharmacy, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China.
Linlin YangDrug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Science, 555 Zuchongzhi Road, Shanghai, 201203, China.
Qiansen ZhangDrug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Science, 555 Zuchongzhi Road, Shanghai, 201203, China.
Lingxue MaoSchool of Pharmacy, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China.
Hualiang JiangSchool of Pharmacy, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China. hljiang@simm.ac.cn.
Huaiyu YangDrug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Science, 555 Zuchongzhi Road, Shanghai, 201203, China. hyyang@simm.ac.cn.
Shanghai Institute of Materia Medica · CNEast China University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Caveolin-1 is the principle membrane protein of caveolae and plays an important role in various cellular processes. The protein contains two helices (H1 and H2) connected by a three-residue break. Although caveolin-1 is assumed to adopt a U-shaped conformation in the transmembrane domain, with both the N-terminus and C-terminus exposed to the cytoplasm, the structure and dynamics of caveolin-1 in membranes are still unclear. Here, we performed six molecular dynamics simulations to characterize the structure and dynamics of caveolin-1 (residues D82-S136; Cav182-136) in a caveolae-mimicking asymmetric lipid bilayer. The simulations reveal that the structure of the caveolin scaffolding domain of caveolin-1 is dynamic, as it could be either fully helical or partly unstructured. Cav182-136 inserts into the inner leaflet of the asymmetric lipid bilayer with a stable U-shaped conformation and orients almost vertical to the bilayer surface. The simulations also provide new insights into the effects of caveolin-1 on the morphology of caveolae and the possible interacting site of cholesterol on caveolin-1.

Indexed as

Molecular Dynamics SimulationCaveolin 1Lipid BilayersPeptide FragmentsProtein Structure, SecondaryCaveolin 1Lipid BilayersPeptide FragmentsCaveolaeCaveolinLipid raftMolecular dynamics simulation

Identifiers

PMID27038819
OpenAlexW2324780584

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.