Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
M Stefani, CM Dobson - Journal of molecular medicine, 2003 - Springer
The deposition of proteins in the form of amyloid fibrils and plaques is the characteristic feature
of more than 20 degenerative conditions affecting either the central nervous system or a …
of more than 20 degenerative conditions affecting either the central nervous system or a …
[HTML][HTML] Plant selective autophagy—still an uncharted territory with a lot of hidden gems
M Stephani, Y Dagdas - Journal of Molecular Biology, 2020 - Elsevier
Selective autophagy has emerged as a major quality control pathway that surgically removes
damaged or unwanted macromolecules to maintain cellular health. Defects in selective …
damaged or unwanted macromolecules to maintain cellular health. Defects in selective …
[HTML][HTML] Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world
M Stefani - Biochimica et biophysica acta (BBA)-Molecular basis of …, 2004 - Elsevier
The data reported in the past 5 years have highlighted new aspects of protein misfolding
and aggregation. Firstly, it appears that protein aggregation may be a generic property of …
and aggregation. Firstly, it appears that protein aggregation may be a generic property of …
A cross-kingdom conserved ER-phagy receptor maintains endoplasmic reticulum homeostasis during stress
M Stephani, L Picchianti, A Gajic, R Beveridge… - elife, 2020 - elifesciences.org
Eukaryotes have evolved various quality control mechanisms to promote proteostasis in the
endoplasmic reticulum (ER). Selective removal of certain ER domains via autophagy (…
endoplasmic reticulum (ER). Selective removal of certain ER domains via autophagy (…
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
A range of human degenerative conditions, including Alzheimer's disease, light-chain
amyloidosis and the spongiform encephalopathies, is associated with the deposition in tissue of …
amyloidosis and the spongiform encephalopathies, is associated with the deposition in tissue of …
Designing conditions for in vitro formation of amyloid protofilaments and fibrils
…, N Taddei, A Clark, M Stefani… - Proceedings of the …, 1999 - National Acad Sciences
We have been able to convert a small α/β protein, acylphosphatase, from its soluble and
native form into insoluble amyloid fibrils of the type observed in a range of pathological …
native form into insoluble amyloid fibrils of the type observed in a range of pathological …
Rationalization of the effects of mutations on peptide andprotein aggregation rates
In order for any biological system to function effectively, it is essential to avoid the inherent
tendency of proteins to aggregate and form potentially harmful deposits 1 , 2 , 3 , 4 . In each of …
tendency of proteins to aggregate and form potentially harmful deposits 1 , 2 , 3 , 4 . In each of …
Medical management with or without interventional therapy for unruptured brain arteriovenous malformations (ARUBA): a multicentre, non-blinded, randomised trial
…, WL Young, E Houdart, C Cordonnier, MA Stefani… - The Lancet, 2014 - thelancet.com
Background The clinical benefit of preventive eradication of unruptured brain arteriovenous
malformations remains uncertain. A Randomised trial of Unruptured Brain Arteriovenous …
malformations remains uncertain. A Randomised trial of Unruptured Brain Arteriovenous …
Shuffled ATG8 interacting motifs form an ancestral bridge between UFMylation and autophagy
…, N Zhan, NAT Irwin, R Groh, M Stephani… - The EMBO …, 2023 - embopress.org
UFMylation involves the covalent modification of substrate proteins with UFM1 (Ubiquitin‐fold
modifier 1) and is important for maintaining ER homeostasis. Stalled translation triggers …
modifier 1) and is important for maintaining ER homeostasis. Stalled translation triggers …
A causative link between the structure of aberrant protein oligomers and their toxicity
…, C Parrini, E Evangelisti, A Relini, M Stefani… - Nature chemical …, 2010 - nature.com
The aberrant assembly of peptides and proteins into fibrillar aggregates proceeds through
oligomeric intermediates that are thought to be the primary pathogenic species in many …
oligomeric intermediates that are thought to be the primary pathogenic species in many …