Evidence map›Paper›PMID 35972526›Full record

ReviewThe Journal of membrane biology2022

Emerging Insights into the Molecular Architecture of Caveolin-1.

Melanie D Ohi, Anne K Kenworthy

Open access · greenAbstract readReview
In one paragraph

Review in The Journal of membrane biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. 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
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Lipid Organization by the Caveolin-1 Complex.bioRxiv : the preprint server for biology · 2024
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Renal Organic Anion Transporters 1 and 3 In Vitro: Gone but Not Forgotten.International journal of molecular sciences · 2023
    Review
  20. Cytomembrane Trafficking Pathways of Connexin 26, 30, and 43.International journal of molecular sciences · 2023
    Review
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

2 authors at 2 institutions in 1 country.

Melanie D OhiLife Sciences Institute, University of Michigan, Ann Arbor, MI, USA. mohi@umich.edu.ORCID 0000-0003-1750-4793
Anne K KenworthyCenter for Membrane and Cell Physiology, University of Virginia, Charlottesville, VA, USA. akk7hp@virginia.edu.ORCID 0000-0001-6567-9059
University of Michigan · USUniversity of Virginia · US

Funding

Structural basis for caveolae assembly and functionR01HL144131 · NHLBI · VANDERBILT UNIVERSITY · PI KENWORTHY, ANNE K, OHI, MELANIE DIANE · 2018 to 2021
$2.2M
NHLBI NIH HHS R01 HL144131
6 · The paper itself

Abstract

Caveolins are an unusual family of membrane proteins whose primary biological function is to build small invaginated membrane structures at the surface of cells known as caveolae. Caveolins and caveolae regulate numerous signaling pathways, lipid homeostasis, intracellular transport, cell adhesion, and cell migration. They also serve as sensors and protect the plasma membrane from mechanical stress. Despite their many important functions, the molecular basis for how these 50-100 nm "little caves" are assembled and regulate cell physiology has perplexed researchers for 70 years. One major impediment to progress has been the lack of information about the structure of caveolin complexes that serve as building blocks for the assembly of caveolae. Excitingly, recent advances have finally begun to shed light on this long-standing question. In this review, we highlight new developments in our understanding of the structure of caveolin oligomers, including the landmark discovery of the molecular architecture of caveolin-1 complexes using cryo-electron microscopy.

Indexed as

CaveolaeCaveolin 1Cell MembraneCryoelectron MicroscopyLipidsMembrane ProteinsCaveolin 1LipidsMembrane ProteinsCaveolaeCaveolinCryo-electron microscopyMembrane nanodomainsMembrane protein structure

Identifiers

PMID35972526
PMCPMC9588732
OpenAlexW4291954669

What OpenQuestion holds

Textmetadata
LicenceTDM
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.