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On the other hand, GIPC, a glut1-binding protein, has been found to bind to the type I PDZ domains of both α6A and α6B, the interaction being stronger on α6A (27).
The TGF-β family members bind to the type I and type II serine/threonine kinase receptors on the cell surface.
Type I IFNs comprise IFN-α, IFN-β, IFN-ε, IFN-κ and IFN-ω, which bind to the type I IFN heterodimeric receptor complex of IFN-α receptor 1 (IFNand) and receptor 2 (IFNAR2) (Chen et al., 2004).
Betaglycan presents ligand to the type II TGFβ receptor, an action of particular importance for TGFβ2, which does not bind to the type II TGFβ receptor with high affinity alone [15], [17], [18].
Secreted IFNs bind to the type I IFN receptor (IFNAR) on the surface of neighbouring cells, activating the Janus kinase (Jak)/signal transducer and activator of transcription (Stat) signalling pathway.
TGFβ superfamily ligands bind to the type II receptors, which phosphorylates the type I receptors.
Similar(48)
TGFβ signals through type I and type II receptors when TGFβ ligand binds to the type II receptor.
IFN-β binds to the type I interferon receptor (IFNAR), an event that initiates the activation of the associated Janus kinases.
These results are more generalisable than intervention costs, which are always bound to the type of intervention.
After IFN- γ binds to the type II IFN receptor, JAK1 and JAK2 are activated and subsequently phosphorylate only STAT1.
TGF-beta binds to the type II receptor, recruits and phosphorylates the type I receptor and subsequently activates its receptor Smad, Smad2 or Smad3, by phosphorylation [ 21].
More suggestions(18)
bind to the surface
bind to the peptide
bind to the promoter
bind to the estrogen
bind to the tyrosinase
bind to the active-site
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bind to the dialysis
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bind to the lipophilic
bind to the interspace
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