Evidence map›Paper›PMID 35715229›Full record

ReviewChemical reviews2022

Cryo-electron Microscopic Analysis of Single-Pass Transmembrane Receptors.

Kai Cai, Xuewu Zhang, Xiao-Chen Bai

Open access · greenAbstract readReview
In one paragraph

Review in Chemical reviews, 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
2.0field-weighted citation impact, top 13% 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, 29 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Article
  6. Article
  7. Review
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  9. Article
  10. Structure and organization of full-length epidermal growth factor receptor in extracellular vesicles by cryo-electron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. The MET Oncogene Network of Interacting Cell Surface Proteins.International journal of molecular sciences · 2024
    Review
  17. Engineering signalling pathways in mammalian cells.Nature biomedical engineering · 2024
    Review
  18. Article
  19. Review
  20. AberrantCells · 2024
    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

3 authors at 1 institution in 1 country.

Kai CaiDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas 75231, United States.
Xuewu ZhangDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas 75231, United States.
Xiao-Chen BaiDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas 75231, United States.ORCID 0000-0002-4234-5686
The University of Texas Southwestern Medical Center · US

Funding

Transmembrane signaling mechanisms of plexin - SupplementR35GM130289 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI Xuewu Zhang · 2019 to 2026
$3.6M
Structural and Functional Analyses of the Full-length Insulin Receptor (IR) and Type 1 Insulin-like Growth Factor Receptor (IGF1R) in the Liganded Active StateR01GM136976 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI BAI, XIAOCHEN · 2020 to 2024
$1.8M
Structural insights into the unique activation mechanisms of receptor tyrosine kinasesR01GM143158 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI BAI, XIAOCHEN · 2021 to 2024
$1.6M
NIGMS NIH HHS R01 GM136976NIGMS NIH HHS R01 GM143158NIGMS NIH HHS R35 GM130289
6 · The paper itself

Abstract

Single-pass transmembrane receptors (SPTMRs) represent a diverse group of integral membrane proteins that are involved in many essential cellular processes, including signal transduction, cell adhesion, and transmembrane transport of materials. Dysregulation of the SPTMRs is linked with many human diseases. Despite extensive efforts in past decades, the mechanisms of action of the SPTMRs remain incompletely understood. One major hurdle is the lack of structures of the full-length SPTMRs in different functional states. Such structural information is difficult to obtain by traditional structural biology methods such as X-ray crystallography and nuclear magnetic resonance (NMR). The recent rapid development of single-particle cryo-electron microscopy (cryo-EM) has led to an exponential surge in the number of high-resolution structures of integral membrane proteins, including SPTMRs. Cryo-EM structures of SPTMRs solved in the past few years have tremendously improved our understanding of how SPTMRs function. In this review, we will highlight these progresses in the structural studies of SPTMRs by single-particle cryo-EM, analyze important structural details of each protein involved, and discuss their implications on the underlying mechanisms. Finally, we also briefly discuss remaining challenges and exciting opportunities in the field.

Indexed as

ElectronsMembrane ProteinsCryoelectron MicroscopyCrystallography, X-RayHumansMagnetic Resonance SpectroscopyMembrane Proteins

Identifiers

PMID35715229
PMCPMC10026182
OpenAlexW4283071640

What OpenQuestion holds

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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.