Evidence map›Paper›PMID 36413010›Full record

ArticleeLife2022

Molecular basis for the role of disulfide-linked αCTs in the activation of insulin-like growth factor 1 receptor and insulin receptor.

Jie Li, Jiayi Wu, Catherine Hall, Xiao-Chen Bai, Eunhee Choi

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Ligand regulation and function of preformed EGFR dimers.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. A λ-Dynamics Investigation of InsulinJournal of chemical information and modeling · 2024
    Article
  10. Article
  11. A λ-dynamics investigation of insulinbioRxiv : the preprint server for biology · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. 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

5 authors at 2 institutions in 3 countries.

Jie LiDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0002-1059-280X
Jiayi WuDepartment of Pathology and Cell Biology, Vagelos College of Physicians and Surgeons, Columbia University, New York, United States.ORCID 0000-0002-9692-2864
Catherine HallDepartment of Pathology and Cell Biology, Vagelos College of Physicians and Surgeons, Columbia University, New York, United States.
Xiao-Chen BaiDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0002-4234-5686
Eunhee ChoiDepartment of Pathology and Cell Biology, Vagelos College of Physicians and Surgeons, Columbia University, New York, United States.ORCID 0000-0003-3286-6477
Columbia College · CAThe University of Texas Southwestern Medical Center · US

Funding

The Organoid and Cell Culture CoreP30DK132710 · NIDDK · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Robert F. Schwabe · 2022 to 2026
$7.2M
Understanding Selective Signaling and Functional Specificity in Insulin and IGF ReceptorsR35GM142937 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Eunhee Choi · 2021 to 2026
$2.5M
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
NIDDK NIH HHS P30 DK132710NIGMS NIH HHS R01 GM136976NIGMS NIH HHS R35 GM142937
6 · The paper itself

Abstract

The insulin receptor (IR) and insulin-like growth factor 1 receptor (IGF1R) control metabolic homeostasis and cell growth and proliferation. The IR and IGF1R form similar disulfide bonds linked homodimers in the apo-state; however, their ligand binding properties and the structures in the active state differ substantially. It has been proposed that the disulfide-linked C-terminal segment of α-chain (αCTs) of the IR and IGF1R control the cooperativity of ligand binding and regulate the receptor activation. Nevertheless, the molecular basis for the roles of disulfide-linked αCTs in IR and IGF1R activation are still unclear. Here, we report the cryo-EM structures of full-length mouse IGF1R/IGF1 and IR/insulin complexes with modified αCTs that have increased flexibility. Unlike the

Indexed as

Receptor, IGF Type 1Receptor, InsulinAnimalsCryoelectron MicroscopyDisulfidesLigandsMiceProtein MultimerizationDisulfidesLigandsReceptor, IGF Type 1Receptor, Insulincell biologycryo-EMhumaninsulin-like growth factor 1 receptorinsulin receptormolecular biophysicsmousereceptor tyrosine kinasesignalingstructural biologytrafficking

Identifiers

PMID36413010
PMCPMC9731570
OpenAlexW4309575799

What OpenQuestion holds

Textmetadata
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.