Cargando…
First eight residues of apolipoprotein A-I mediate the C-terminus control of helical bundle unfolding and its lipidation
The crystal structure of a C-terminal deletion of apolipoprotein A-I (apoA1) shows a large helical bundle structure in the amino half of the protein, from residues 8 to 115. Using site directed mutagenesis, guanidine or thermal denaturation, cell free liposome clearance, and cellular ABCA1-mediated...
Autores principales: | Brubaker, Gregory, Lorkowski, Shuhui W., Gulshan, Kailash, Hazen, Stanley L., Gogonea, Valentin, Smith, Jonathan D. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6964839/ https://www.ncbi.nlm.nih.gov/pubmed/31945064 http://dx.doi.org/10.1371/journal.pone.0221915 |
Ejemplares similares
-
The pattern of apolipoprotein A-I lysine carbamylation reflects its lipidation state and the chemical environment within human atherosclerotic aorta
por: Battle, Shawna, et al.
Publicado: (2022) -
Helices and vector bundles
por: Rudakov, A N
Publicado: (1990) -
Pressure and Chemical Unfolding of an α-Helical Bundle Protein: The GH2 Domain of the Protein Adaptor GIPC1
por: Dubois, Cécile, et al.
Publicado: (2021) -
The N-terminus of mature human frataxin is intrinsically unfolded
por: Prischi, Filippo, et al.
Publicado: (2009) -
Mechanism of Unfolding of A Model Helical Peptide
por: Pastrana-Rios, Belinda, et al.
Publicado: (2002)