Cargando…
The fibrillogenic L178H variant of apolipoprotein A-I forms helical fibrils
A number of amyloidogenic variants of apoA-I have been discovered but most have not been analyzed. Previously, we showed that the G26R mutation of apoA-I leads to increased β-strand structure, increased N-terminal protease susceptibility, and increased fibril formation after several days of incubati...
Autores principales: | Petrlova, Jitka, Duong, Trang, Cochran, Megan C., Axelsson, Annika, Mörgelin, Matthias, Roberts, Linda M., Lagerstedt, Jens O. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Biochemistry and Molecular
Biology
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3276462/ https://www.ncbi.nlm.nih.gov/pubmed/22184756 http://dx.doi.org/10.1194/jlr.M020883 |
Ejemplares similares
-
Structural and Functional Analysis of the ApolipoproteinA-I A164S Variant
por: Dalla-Riva, Jonathan, et al.
Publicado: (2015) -
The secondary structure of apolipoprotein A-I on 9.6-nm reconstituted high-density lipoprotein determined by EPR spectroscopy
por: Oda, Michael N, et al.
Publicado: (2013) -
Impact of a Single Point Mutation on the Antimicrobial and Fibrillogenic Properties of Cryptides from Human Apolipoprotein B
por: Gaglione, Rosa, et al.
Publicado: (2021) -
Identification of fibrillogenic regions in human triosephosphate isomerase
por: Carcamo-Noriega, Edson N., et al.
Publicado: (2016) -
Secondary Structure Changes in ApoA-I Milano (R173C) Are Not Accompanied by a Decrease in Protein Stability or Solubility
por: Petrlova, Jitka, et al.
Publicado: (2014)