ArticleThe Journal of biological chemistry2017
A pivotal role for a conserved bulky residue at the α1-helix of the αI integrin domain in ligand binding.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
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.
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Who cites it
6 citing papers in PubMed.
- Heterotropic roles of divalent cations in the establishment of allostery and affinity maturation of integrin αXβ2.Cell reports · 2022Article
- The Promiscuous Profile of Complement Receptor 3 in Ligand Binding, Immune Modulation, and Pathophysiology.Frontiers in immunology · 2021Review
- Mechanically Regulated Outside-In Activation of an I-Domain-Containing Integrin.Biophysical journal · 2020Article
- Inter-α-inhibitor heavy chain-1 has an integrin-like 3D structure mediating immune regulatory activities and matrix stabilization during ovulation.The Journal of biological chemistry · 2020Article
- Autonomous conformational regulation of βProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Magnesium Activates Microsecond Dynamics to Regulate Integrin-Collagen Recognition.Structure (London, England : 1993) · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The ligand-binding βI and αI domains of integrin are the best-studied von Willebrand factor A domains undergoing significant conformational changes for affinity regulation. In both βI and αI domains, the α1- and α7-helixes work in concert to shift the metal-ion-dependent adhesion site between the resting and active states. An absolutely conserved Gly in the middle of the α1-helix of βI helps maintain the resting βI conformation, whereas the homologous position in the αI α1-helix contains a conserved Phe. A functional role of this Phe is structurally unpredictable. Using α
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Registered trials
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