Cargando…
Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism
Proteins in either a native or denatured conformation often aggregate at an isoelectric point (pI), a phenomenon known as pI precipitation. However, only a few studies have addressed the role of pI precipitation in amyloid formation, the crystal-like aggregation of denatured proteins. We found that...
Autores principales: | Furukawa, Koki, Aguirre, Cesar, So, Masatomo, Sasahara, Kenji, Miyanoiri, Yohei, Sakurai, Kazumasa, Yamaguchi, Keiichi, Ikenaka, Kensuke, Mochizuki, Hideki, Kardos, Jozsef, Kawata, Yasushi, Goto, Yuji |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8244297/ https://www.ncbi.nlm.nih.gov/pubmed/34235468 http://dx.doi.org/10.1016/j.crstbi.2020.03.001 |
Ejemplares similares
-
Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners
por: Yamaguchi, Keiichi, et al.
Publicado: (2021) -
Breakdown of supersaturation barrier links protein folding to amyloid formation
por: Noji, Masahiro, et al.
Publicado: (2021) -
The residual structure of acid‐denatured β(2)‐microglobulin is relevant to an ordered fibril morphology
por: Tomiyama, Ryosuke, et al.
Publicado: (2023) -
Macromolecular crowding and supersaturation protect hemodialysis patients from the onset of dialysis-related amyloidosis
por: Nakajima, Kichitaro, et al.
Publicado: (2022) -
Strong acids induce amyloid fibril formation of β(2)-microglobulin via an anion-binding mechanism
por: Yamaguchi, Keiichi, et al.
Publicado: (2021)