Amyloid-type protein aggregation and prion-like properties of amyloids
This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …
an important hallmark of protein misfolding diseases and therefore have been investigated …
Physical and structural basis for polymorphism in amyloid fibrils
R Tycko - Protein Science, 2014 - Wiley Online Library
As our understanding of the molecular structures of amyloid fibrils has matured over the past
15 years, it has become clear that, while amyloid fibrils do have well‐defined molecular …
15 years, it has become clear that, while amyloid fibrils do have well‐defined molecular …
Atomic structure and hierarchical assembly of a cross-β amyloid fibril
The cross-β amyloid form of peptides and proteins represents an archetypal and widely
accessible structure consisting of ordered arrays of β-sheet filaments. These complex …
accessible structure consisting of ordered arrays of β-sheet filaments. These complex …
Pathologic polyglutamine aggregation begins with a self-poisoning polymer crystal
A long-standing goal of amyloid research has been to characterize the structural basis of the
rate-determining nucleating event. However, the ephemeral nature of nucleation has made …
rate-determining nucleating event. However, the ephemeral nature of nucleation has made …
Huntingtin exon 1 fibrils feature an interdigitated β-hairpin–based polyglutamine core
CL Hoop, HK Lin, K Kar… - Proceedings of the …, 2016 - National Acad Sciences
Polyglutamine expansion within the exon1 of huntingtin leads to protein misfolding,
aggregation, and cytotoxicity in Huntington's disease. This incurable neurodegenerative …
aggregation, and cytotoxicity in Huntington's disease. This incurable neurodegenerative …
Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence
R Wetzel - Journal of molecular biology, 2012 - Elsevier
Polyglutamine (polyQ) sequences of unknown normal function are present in a significant
number of proteins, and their repeat expansion is associated with a number of genetic …
number of proteins, and their repeat expansion is associated with a number of genetic …
[HTML][HTML] Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR
Solid-state nuclear magnetic resonance (ssNMR) spectroscopy enables the structural
characterization of a diverse array of biological assemblies that include amyloid fibrils, non …
characterization of a diverse array of biological assemblies that include amyloid fibrils, non …
Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity
We structurally compare, using solid-state NMR, two different polymorphs of α-synuclein
which, as established recently, display contrasting biochemical properties, toxicity, and …
which, as established recently, display contrasting biochemical properties, toxicity, and …
Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core
HK Lin, JC Boatz, IE Krabbendam, R Kodali… - Nature …, 2017 - nature.com
Polyglutamine expansion in the huntingtin protein is the primary genetic cause of
Huntington's disease (HD). Fragments coinciding with mutant huntingtin exon1 aggregate in …
Huntington's disease (HD). Fragments coinciding with mutant huntingtin exon1 aggregate in …
[HTML][HTML] Protofilament structure and supramolecular polymorphism of aggregated mutant huntingtin exon 1
Huntington's disease is a progressive neurodegenerative disease caused by expansion of
the polyglutamine domain in the first exon of huntingtin (HttEx1). The extent of expansion …
the polyglutamine domain in the first exon of huntingtin (HttEx1). The extent of expansion …