Evidence map›Paper›PMID 34832078›Full record

ArticleMembranes2021

Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities.

Claudio Catalano, Danya Ben-Hail, Weihua Qiu, Paul Blount, Amedee des Georges, Youzhong Guo

Open access · goldAbstract read
In one paragraph

Article in Membranes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Advances in native cell membrane nanoparticles system.Current opinion in structural biology · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
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  10. Characterization of CaBiochimica et biophysica acta. Biomembranes · 2023
    Article
  11. Review
  12. Review
  13. Article
  14. 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

6 authors at 3 institutions in 1 country.

Claudio CatalanoDepartment of Medicinal Chemistry, Virginia Commonwealth University, Richmond, VA 23298-0540, USA.ORCID 0000-0002-2437-6235
Danya Ben-HailStructural Biology Initiative, CUNY Advanced Science Research Center, New York, NY 10017, USA.ORCID 0000-0002-8210-3446
Weihua QiuDepartment of Medicinal Chemistry, Virginia Commonwealth University, Richmond, VA 23298-0540, USA.
Paul BlountDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9040, USA.
Amedee des GeorgesStructural Biology Initiative, CUNY Advanced Science Research Center, New York, NY 10017, USA.ORCID 0000-0002-9704-3781
Youzhong GuoDepartment of Medicinal Chemistry, Virginia Commonwealth University, Richmond, VA 23298-0540, USA.ORCID 0000-0001-7177-9603
Virginia Commonwealth University · USThe Graduate Center, CUNY · USThe University of Texas Southwestern Medical Center · US

Funding

Understanding membrane proteins’ allosteric modulation with cryo-EMR35GM133598 · NIGMS · NEW YORK UNIVERSITY · PI Amedee des Georges · 2019 to 2026
$3.4M
Proposal for an Administrative Supplement for Equipment Purchases for NIGMS Awardees NOT-GM-22-017R01GM132329 · NIGMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI GUO, YOUZHONG · 2019 to 2022
$1.9M
Using Small Compounds as Probes for Studying Mechanosensitive Channel GatingR01GM121780 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI BLOUNT, PAUL · 2017 to 2020
$1.1M
NIGMS NIH HHS R01-GM121780NIGMS NIH HHS R01 GM132329NIGMS NIH HHS R01-GM132329NIGMS NIH HHS R35 GM133598NIGMS NIH HHS R35GM133598Welch Foundation I-1420
6 · The paper itself

Abstract

Mechanosensitive channels respond to mechanical forces exerted on the cell membrane and play vital roles in regulating the chemical equilibrium within cells and their environment. High-resolution structural information is required to understand the gating mechanisms of mechanosensitive channels. Protein-lipid interactions are essential for the structural and functional integrity of mechanosensitive channels, but detergents cannot maintain the crucial native lipid environment for purified mechanosensitive channels. Recently, detergent-free systems have emerged as alternatives for membrane protein structural biology. This report shows that while membrane-active polymer, SMA2000, could retain some native cell membrane lipids on the transmembrane domain of the mechanosensitive-like YnaI channel, the complete structure of the transmembrane domain of YnaI was not resolved. This reveals a significant limitation of SMA2000 or similar membrane-active copolymers. This limitation may come from the heterogeneity of the polymers and nonspecific interactions between the polymers and the relatively large hydrophobic pockets within the transmembrane domain of YnaI. However, this limitation offers development opportunities for detergent-free technology for challenging membrane proteins.

Indexed as

cryo-EMMechanosensitive ChannelNCMNSMA2000YnaI

Identifiers

PMID34832078
PMCPMC8621939
OpenAlexW3209354752

What OpenQuestion holds

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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 OpenQuestion graph.