ArticleNature communications2019
General structural features that regulate integrin affinity revealed by atypical αVβ8.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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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.
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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.
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Who cites it
29 citing papers in PubMed, 39 citations in OpenAlex.
- Outside-In Signaling as a Detonator-like Stimulus of Integrin Activation by Promoting Both Affinity and Avidity.Biomolecules · 2026Review
- Graphene Oxide-Hydroxyapatite Nanocomposite Coatings and Extracellular Matrix Protein Interactions for Enhanced Osseointegration in Dental Implants.Journal of cellular and molecular medicine · 2026Article
- Targeting α v β 8 Integrin with mAb MEDI8367 Prevents Fibrosis in Preclinical Models of CKD.Kidney360 · 2026Article
- Antifibrotic Efficacy of a Nintedanib-Peptide Conjugate and Diagnostic Potential of a Fluorescent Companion Probe Targeting αACS pharmacology & translational science · 2025Article
- Therapeutic Prospects of αv Integrins Inhibition in Fibrotic Lung Diseases and Carcinogenesis.International journal of molecular sciences · 2025Review
- A Review of Talin- and Integrin-Dependent Molecular Mechanisms in Cancer Invasion and Metastasis.International journal of molecular sciences · 2025Review
- Innovative Theranostics Strategies in the Fight Against Lung Cancer.Mini reviews in medicinal chemistry · 2025Review
- Synthetic integrin antibodies discovered by yeast display reveal αV subunit pairing preferences with β subunits.bioRxiv : the preprint server for biology · 2024Article
- Molecular View on theJournal of chemical information and modeling · 2023Article
- Family-wide analysis of integrin structures predicted by AlphaFold2.bioRxiv : the preprint server for biology · 2023Article
- De novo design of highly selective miniprotein inhibitors of integrins αvβ6 and αvβ8.Nature communications · 2023Article
- Structural analysis of peptide binding to integrins for cancer detection and treatment.Biophysical reviews · 2023Review
- A specialized integrin-binding motif enables proTGF-β2 activation by integrin αVβ6 but not αVβ8.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Irisin acts through its integrin receptor in a two-step process involving extracellular Hsp90α.Molecular cell · 2023Article
- Family-wide analysis of integrin structures predicted by AlphaFold2.Computational and structural biotechnology journal · 2023Article
- Mini review of first-in-human integrin αvβ6 PET tracers.Frontiers in nuclear medicine · 2023Review
- Article
- Dynamics of integrin α5β1, fibronectin, and their complex reveal sites of interaction and conformational change.The Journal of biological chemistry · 2022Article
- Specificity of TGF-β1 signal designated by LRRC33 and integrin αNature communications · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Integrin αVβ8, which like αVβ6 functions to activate TGF-βs, is atypical. Its β8 subunit binds to a distinctive cytoskeleton adaptor and does not exhibit large changes in conformation upon binding to ligand. Here, crystal structures, hydrogen-deuterium exchange dynamics, and affinity measurements on mutants are used to compare αVβ8 and αVβ6. Lack of a binding site for one of three βI domain divalent cations and a unique β6-α7 loop conformation in β8 facilitate movements of the α1 and α1' helices at the ligand binding pocket toward the high affinity state, without coupling to β6-α7 loop reshaping and α7-helix pistoning that drive large changes in βI domain-hybrid domain orientation seen in other integrins. Reciprocal swaps between β6 and β8 βI domains increase affinity of αVβ6 and decrease affinity of αVβ8 and define features that regulate affinity of the βI domain and its coupling to the hybrid domain.
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Registered trials
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.