α-Synuclein misfolding and aggregation: Implications in Parkinson's disease pathogenesis
Abstract α-Synuclein (α-Syn) has been extensively studied for its structural and biophysical
properties owing to its pathophysiological role in Parkinson's disease (PD). Lewy bodies …
properties owing to its pathophysiological role in Parkinson's disease (PD). Lewy bodies …
Introducing protein intrinsic disorder
Proteins are the major component of the living cell. They play crucial roles in the
maintenance of life, and their dysfunctions are known to cause different pathologies. One of …
maintenance of life, and their dysfunctions are known to cause different pathologies. One of …
Protein ensembles: how does nature harness thermodynamic fluctuations for life? The diverse functional roles of conformational ensembles in the cell
All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …
Global structure of the intrinsically disordered protein tau emerges from its local structure
The paradigmatic disordered protein tau plays an important role in neuronal function and
neurodegenerative diseases. To disentangle the factors controlling the balance between …
neurodegenerative diseases. To disentangle the factors controlling the balance between …
Exploring free-energy landscapes of intrinsically disordered proteins at atomic resolution using NMR spectroscopy
The last 15 years have seen a paradigm shift in our understanding of protein biochemistry,
with the realization that an unexpectedly high fraction of the human genome codes for …
with the realization that an unexpectedly high fraction of the human genome codes for …
Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables
Abstract Motivation: Intrinsically disordered proteins (IDPs) represent a significant fraction of
the human proteome. The classical structure function paradigm that has successfully …
the human proteome. The classical structure function paradigm that has successfully …
Sensitivity of secondary structure propensities to sequence differences between α‐and γ‐synuclein: implications for fibrillation
The synucleins are a family of intrinsically disordered proteins involved in various human
diseases. α‐Synuclein has been extensively characterized due to its role in Parkinson's …
diseases. α‐Synuclein has been extensively characterized due to its role in Parkinson's …
The fold of α-synuclein fibrils
The aggregation of proteins into amyloid fibrils is associated with several neurodegenerative
diseases. In Parkinson's disease it is believed that the aggregation of α-synuclein (α-syn) …
diseases. In Parkinson's disease it is believed that the aggregation of α-synuclein (α-syn) …
How random are intrinsically disordered proteins? A small angle scattering perspective
V Receveur-Bréchot, D Durand - Current Protein and Peptide …, 2012 - ingentaconnect.com
While the crucial role of intrinsically disordered proteins (IDPs) in the cell cycle is now
recognized, deciphering their molecular mode of action at the structural level still remains …
recognized, deciphering their molecular mode of action at the structural level still remains …
The C-terminal tail of α-synuclein protects against aggregate replication but is critical for oligomerization
A Farzadfard, JN Pedersen, G Meisl… - Communications …, 2022 - nature.com
Aggregation of the 140-residue protein α-synuclein (αSN) is a key factor in the etiology of
Parkinson's disease. Although the intensely anionic C-terminal domain (CTD) of αSN does …
Parkinson's disease. Although the intensely anionic C-terminal domain (CTD) of αSN does …