Principles of protein folding, misfolding and aggregation
CM Dobson - Seminars in cell & developmental biology, 2004 - Elsevier
This review summarises our current understanding of the underlying and universal
mechanism by which newly synthesised proteins achieve their biologically functional states …
mechanism by which newly synthesised proteins achieve their biologically functional states …
Protein-based inheritance: epigenetics beyond the chromosome
Epigenetics refers to changes in phenotype that are not rooted in DNA sequence. This
phenomenon has largely been studied in the context of chromatin modification. Yet many …
phenomenon has largely been studied in the context of chromatin modification. Yet many …
Cryo-EM structure of a neuronal functional amyloid implicated in memory persistence in Drosophila
R Hervas, MJ Rau, Y Park, W Zhang, AG Murzin… - Science, 2020 - science.org
How long-lived memories withstand molecular turnover is a fundamental question.
Aggregates of a prion-like RNA-binding protein, cytoplasmic polyadenylation element …
Aggregates of a prion-like RNA-binding protein, cytoplasmic polyadenylation element …
Conformational variations in an infectious protein determine prion strain differences
A remarkable feature of prion biology is the strain phenomenon wherein prion particles
apparently composed of the same protein lead to phenotypically distinct transmissible …
apparently composed of the same protein lead to phenotypically distinct transmissible …
[HTML][HTML] Folding versus aggregation: polypeptide conformations on competing pathways
TR Jahn, SE Radford - Archives of biochemistry and biophysics, 2008 - Elsevier
Protein aggregation has now become recognised as an important and generic aspect of
protein energy landscapes. Since the discovery that numerous human diseases are caused …
protein energy landscapes. Since the discovery that numerous human diseases are caused …
Seeding specificity in amyloid growth induced by heterologous fibrils
B O'Nuallain, AD Williams, P Westermark… - Journal of Biological …, 2004 - ASBMB
Over residues 15–36, which comprise the H-bonded core of the amyloid fibrils it forms, the
Alzheimer's disease plaque peptide amyloid β (Aβ) possesses a very similar sequence to …
Alzheimer's disease plaque peptide amyloid β (Aβ) possesses a very similar sequence to …
Resveratrol selectively remodels soluble oligomers and fibrils of amyloid Aβ into off-pathway conformers
Misfolded proteins associated with diverse aggregation disorders assemble not only into a
single toxic conformer but rather into a suite of aggregated conformers with unique …
single toxic conformer but rather into a suite of aggregated conformers with unique …
Structural insights into a yeast prion illuminate nucleation and strain diversity
R Krishnan, SL Lindquist - Nature, 2005 - nature.com
Self-perpetuating changes in the conformations of amyloidogenic proteins play vital roles in
normal biology and disease. Despite intense research, the architecture and conformational …
normal biology and disease. Despite intense research, the architecture and conformational …
Polymorphism in the intermediates and products of amyloid assembly
R Kodali, R Wetzel - Current opinion in structural biology, 2007 - Elsevier
Amyloid formation reactions exhibit two classes of polymorphisms: the metastable
intermediates commonly observed during amyloid formation and the range of …
intermediates commonly observed during amyloid formation and the range of …
The structural basis of yeast prion strain variants
Among the many surprises to arise from studies of prion biology, perhaps the most
unexpected is the strain phenomenon whereby a single protein can misfold into structurally …
unexpected is the strain phenomenon whereby a single protein can misfold into structurally …