Structural determinants of integrin β-subunit specificity for latent TGF-β.
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Structural and Mechanistic Insights into the Tropism of Epstein-Barr Virusβ1 Integrins as Therapeutic Targets to Disrupt Hallmarks of CancerRules of engagement between αvβ6 integrin and foot-and-mouth disease virus.The αvβ1 integrin plays a critical in vivo role in tissue fibrosis.Leukocyte integrin αLβ2 headpiece structures: The αI domain, the pocket for the internal ligand, and concerted movements of its loops.αIIbβ3: structure and functionStructural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins.Matters of context guide future research in TGFβ superfamily signaling.Conformational equilibria and intrinsic affinities define integrin activation.Stable Peptides Instead of Stapled Peptides: Highly Potent αvβ6-Selective Integrin Ligands.Structural Biology and Evolution of the TGF-β FamilyTargeting TGF-β Signaling for Therapeutic Gain.TGF-β Family Signaling in Connective Tissue and Skeletal Diseases.Ammonium trichloro [1,2-ethanediolato-O,O']-tellurate cures experimental visceral leishmaniasis by redox modulation of Leishmania donovani trypanothione reductase and inhibiting host integrin linked PI3K/Akt pathway.Integrin engagement by the helical RGD motif of the Helicobacter pylori CagL protein is regulated by pH-induced displacement of a neighboring helix.Force interacts with macromolecular structure in activation of TGF-βDistinct recognition of complement iC3b by integrins αXβ2 and αMβ2Molecular Basis of the Ligand Binding Specificity of αvβ8 Integrin.Atypical interactions of integrin αVβ8 with pro-TGF-β1.Blocking immunosuppression by human Tregs in vivo with antibodies targeting integrin αVβ8.Investigating the Interaction of Cyclic RGD Peptidomimetics with αVβ₆ Integrin by Biochemical and Molecular Docking Studies.Prodomain-Growth Factor Swapping in the Structure of pro-TGF-β1.Energy landscape differences among integrins establish the framework for understanding activation.High integrin αVβ6 affinity reached by hybrid domain deletion slows ligand-binding on-rate.TGF-β and the Tissue Microenvironment: Relevance in Fibrosis and Cancer.Alpha-v-containing integrins are host receptors for the sporozoite surface protein, TRAP
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P2860
Structural determinants of integrin β-subunit specificity for latent TGF-β.
description
2014 nî lūn-bûn
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2014年の論文
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年學術文章
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2014年學術文章
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name
Structural determinants of integrin β-subunit specificity for latent TGF-β.
@ast
Structural determinants of integrin β-subunit specificity for latent TGF-β.
@en
type
label
Structural determinants of integrin β-subunit specificity for latent TGF-β.
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Structural determinants of integrin β-subunit specificity for latent TGF-β.
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prefLabel
Structural determinants of integrin β-subunit specificity for latent TGF-β.
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Structural determinants of integrin β-subunit specificity for latent TGF-β.
@en
P2093
P2860
P356
P1476
Structural determinants of integrin β-subunit specificity for latent TGF-β
@en
P2093
Timothy A Springer
Xianchi Dong
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P304
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10.1038/NSMB.2905
P577
2014-11-10T00:00:00Z