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A simple method to disrupt and restore subunit interaction of acyl-CoA:cholesterol acyltransferase 1
Publikováno v:
MethodsX, Vol 6, Iss , Pp 2242-2247 (2019)
Acyl-CoA:cholestereol acyltransferase 1 (ACAT1) is a two-fold dimer (homotetramer) and has two distinct dimerization domains. One domain is in an alpha-helical rich region near the cytoplasmic N-terminus. The other is proposed to be near the C-termin
Externí odkaz:
https://doaj.org/article/5390642519fe4efbad6d409ad0eda2fd
A simple method to disrupt and restore subunit interaction of acyl-CoA:cholesterol acyltransferase 1
Publikováno v:
MethodsX, Vol 6, Iss, Pp 2242-2247 (2019)
MethodsX
MethodsX
Graphical abstract
Acyl-CoA:cholestereol acyltransferase 1 (ACAT1) is a two-fold dimer (homotetramer) and has two distinct dimerization domains. One domain is in an alpha-helical rich region near the cytoplasmic N-terminus. The other is proposed
Acyl-CoA:cholestereol acyltransferase 1 (ACAT1) is a two-fold dimer (homotetramer) and has two distinct dimerization domains. One domain is in an alpha-helical rich region near the cytoplasmic N-terminus. The other is proposed
Publikováno v:
Arch Biochem Biophys
To conduct biochemical studies in vitro, membrane proteins (MPs) must be solubilized with detergents. While detergents are great tools, they can also inhibit the biological activity and/or perturb oligomerization of individual MPs. Nanodisc scaffold
Publikováno v:
Arch Biochem Biophys
Cholesterol is an important lipid molecule and is needed for all mammalian cells. In various cell types, excess cholesterol is stored as cholesteryl esters; acyl-CoA:cholesterol acyltransferase 1 (ACAT1) plays an essential role in this storage proces
Publikováno v:
Archives of Biochemistry and Biophysics. 691:108518
To conduct biochemical studies in vitro, membrane proteins (MPs) must be solubilized with detergents. While detergents are great tools, they can also inhibit the biological activity and/or perturb oligomerization of individual MPs. Nanodisc scaffold