ArticleScientific reports2018
On the contributing role of the transmembrane domain for subunit-specific sensitivity of integrin activation.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 18 citations in OpenAlex.
- Molecular Mechanisms Underlying Medium-Chain Free Fatty Acid-Regulated Activity of the Phospholipase PlaF fromJACS Au · 2024Article
- Molecular basis for the recognition of 24-(S)-hydroxycholesterol by integrin αvβ3.Scientific reports · 2023Article
- Structure, signal transduction, activation, and inhibition of integrin αIIbβ3.Thrombosis journal · 2023Review
- Article
- Hydroxyapatite Use in Spine Surgery-Molecular and Clinical Aspect.Materials (Basel, Switzerland) · 2022Review
- Recent Advances and Prospects in the Research of Nascent Adhesions.Frontiers in physiology · 2020Review
- Unique transmembrane domain interactions differentially modulate integrin αvβ3 and αIIbβ3 function.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Multiscale model of integrin adhesion assembly.PLoS computational biology · 2019Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- SHARPIN at the nexus of integrin, immune, and inflammatory signaling in human platelets.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integrins are α/β heterodimeric transmembrane adhesion receptors. Evidence exists that their transmembrane domain (TMD) separates upon activation. Subunit-specific differences in activation sensitivity of integrins were reported. However, whether sequence variations in the TMD lead to differential TMD association has remained elusive. Here, we show by molecular dynamics simulations and association free energy calculations on TMDs of integrin α
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Registered trials
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