IndraLab

Statements


3 | 1 7

sparser
"The type II receptor ActRIIA and the type I receptor Alk4, which form heteromeric complexes in NMuMG cells ( xref ), were detected in cell lysates with higher levels of the type II receptor observed in E1KD cells."

No evidence text available

sparser
"Compound NUCC-555 blocked activin/ ActRIIA complex binding with ALK4 in the Blitz label-free binding assay, further supporting our view that the functional effects measured in our cellular assays are caused by NUCC-555 preventing the activin/ActRIIA complex from binding ALK4."

sparser
"Our results show that ACVR2A can form stable heteromeric complexes with ALK4 (an activin type I receptor), as well as with several BMP type I receptors (ALK2/3/6)."

reach
"70 NUCC-555 strongly inhibited activin and ActRIIA complex binding to ALK4 at 25 microM, whereas there was no inhibition of myostatin / ActRIIA complex binding to ALK4 at the same drug concentration in the Blitz binding system equipped with the " dip and read " probe sensor."

No evidence text available

No evidence text available

sparser
"Two subunits of Inhba form the homodimer Activin A, which signals through canonical ALK4-ACVR2 receptor complexes activating the transcription factors SMAD2 and SMAD3."
| PMC

sparser
"The precise mechanism of this antagonism is not yet clear, but preliminary data suggest that in the presence of InhBP and inhibin B, there is an abrogation of actRII's association with ALK4 in respons[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"These data expand our understanding of how endocrine inhibin achieves potent antagonism of local, constitutive activin action in the pituitary, through a combined mechanism of competitive binding of both ActRII and ALK4 by each subunit of the inhibin heterodimer, in conjunction with the co-receptor betaglycan, to block activin receptor-ligand binding, complex assembly, and downstream signaling."

sparser
"ACVR2A forms stable complexes with ALK4 and with BMP type I receptors."