Evidence map›Paper›PMID 30061598›Full record

ArticleNature structural & molecular biology2018

Cryo-EM structure of the αvβ8 integrin reveals a mechanism for stabilizing integrin extension.

Anthony Cormier, Melody G Campbell, Saburo Ito, Shenping Wu, Jianlong Lou, James Marks, Jody L Baron, Stephen L Nishimura, Yifan Cheng

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

40 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
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  8. Cryo-EM heterogeneity analysis using regularized covariance estimation and kernel regression.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. The role and regulation of integrins in cell migration and invasion.Nature reviews. Molecular cell biology · 2025
    Review
  10. Integrins as Key Mediators of Metastasis.International journal of molecular sciences · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Family-wide analysis of integrin structures predicted by AlphaFold2.bioRxiv : the preprint server for biology · 2023
    Article
  18. Integrin αBiophysical journal · 2023
    Article
  19. Review
  20. INTEGRINS: A BEDSIDE TO BENCH TO BEDSIDE STORY.Transactions of the American Clinical and Climatological Association · 2023
    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

9 authors at 2 institutions in 1 country.

Anthony CormierDepartment of Pathology, University of California San Francisco, San Francisco, CA, USA.ORCID http://orcid.org/0000-0002-2848-9536
Melody G CampbellDepartment of Biochemistry and Biophysics, University of California San Francisco, San Francisco, CA, USA.ORCID http://orcid.org/0000-0003-1909-5751
Saburo ItoDepartment of Pathology, University of California San Francisco, San Francisco, CA, USA.
Shenping WuDepartment of Biochemistry and Biophysics, University of California San Francisco, San Francisco, CA, USA.
Jianlong LouDepartment of Anesthesia and Perioperative Care, University of California San Francisco, San Francisco, CA, USA.
James MarksDepartment of Anesthesia and Perioperative Care, University of California San Francisco, San Francisco, CA, USA.
Jody L BaronDepartment of Medicine, University of California San Francisco, San Francisco, CA, USA.
Stephen L NishimuraDepartment of Pathology, University of California San Francisco, San Francisco, CA, USA. stephen.nishimura@ucsf.edu.ORCID http://orcid.org/0000-0003-2312-4113
Yifan ChengDepartment of Biochemistry and Biophysics, University of California San Francisco, San Francisco, CA, USA. yifan.cheng@ucsf.edu.
University of California, San Francisco · USHoward Hughes Medical Institute · US

Funding

UC BRAID Center for Accelerated Innovation COVID-19 diagnostic project developmentU54HL119893 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI PALAZZOLO, MICHAEL J · 2013 to 2020
$18.3M
Structural mechanism of integrin-mediated TGF-b activationR01HL134183 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Yifan Cheng, Stephen L Nishimura · 2016 to 2026
$5.9M
Renewable antibodies to secreted proteins and single and multi-pass cell surfaceP41CA196276 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2014 to 2018
$5.8M
Structures and gating mechanisms of TRP ion channelsR01GM098672 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2011 to 2018
$2.6M
Role of genetic variation in TGF-beta overactivation in COPDR01HL113032 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI NISHIMURA, STEPHEN L · 2012 to 2015
$2.1M
Acquisition of an electron microscope for high-resolution single particle cryo-EMS10OD021741 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2016 to 2016
$2.0M
Linux cluster for near atomic resolution single particle cryo-EMS10OD020054 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2015 to 2015
$456k
NCI NIH HHS P41 CA196276NHLBI NIH HHS R01 HL113032NHLBI NIH HHS R01 HL134183NHLBI NIH HHS U54 HL119893NIGMS NIH HHS R01 GM098672NIH HHS S10 OD020054NIH HHS S10 OD021741
6 · The paper itself

Abstract

Integrins are conformationally flexible cell surface receptors that survey the extracellular environment for their cognate ligands. Interactions with ligands are thought to be linked to global structural rearrangements involving transitions between bent, extended-closed and extended-open forms. Thus far, structural details are lacking for integrins in the extended conformations due to extensive flexibility between the headpiece and legs in this conformation. Here we present single-particle electron cryomicroscopy structures of human αvβ8 integrin in the extended-closed conformation, which has been considered to be a low-affinity intermediate. Our structures show the headpiece rotating about a flexible αv knee, suggesting a ligand surveillance mechanism for integrins in their extended-closed form. Our model predicts that the extended conformation is mainly stabilized by an interface formed between flexible loops in the upper and lower domains of the αv leg. Confirming these findings with the αvβ3 integrin suggests that our model of stabilizing the extended-closed conformation is generalizable to other integrins.

Indexed as

Amino Acid SequenceCryoelectron MicroscopyHumansIntegrinsProtein ConformationSequence Homology, Amino Acidintegrin alphavbeta8Integrins

Identifiers

PMID30061598
PMCPMC6214843
OpenAlexW2884564748

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.