Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.
The [Het-s] prion of the fungus Podospora anserina represents a good model system for studying the structure-function relationship in amyloid proteins because a high resolution solid-state NMR structure of the amyloid prion form of the HET-s prion forming domain (PFD) is available. The HET-s PFD ado...
Saved in:
Main Authors: | Asen Daskalov, Matthias Gantner, Marielle Aulikki Wälti, Thierry Schmidlin, Celestine N Chi, Christian Wasmer, Anne Schütz, Johanna Ceschin, Corinne Clavé, Sandra Cescau, Beat Meier, Roland Riek, Sven J Saupe |
---|---|
Format: | article |
Language: | EN |
Published: |
Public Library of Science (PLoS)
2014
|
Subjects: | |
Online Access: | https://doaj.org/article/809e9ec61a7d4cdf9fff4e06d3ad7584 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
The mechanism of toxicity in HET-S/HET-s prion incompatibility.
by: Carolin Seuring, et al.
Published: (2012) -
Partial Prion Cross-Seeding between Fungal and Mammalian Amyloid Signaling Motifs
by: Thierry Bardin, et al.
Published: (2021) -
Het veranderende financieringslandschap van het MKB
by: Peter Roosenboom
Published: (2021) -
Functional and genomic analyses of alpha-solenoid proteins.
by: David Fournier, et al.
Published: (2013) -
The development of microfabricated solenoids with magnetic cores for micromagnetic neural stimulation
by: Adam Khalifa, et al.
Published: (2021)