Molecular crowding: the history and development of a scientific paradigm
It is now generally accepted that macromolecules do not act in isolation but “live” in a
crowded environment, that is, an environment populated by numerous different molecules …
crowded environment, that is, an environment populated by numerous different molecules …
Supersaturation, a critical factor underlying proteostasis of amyloid fibril formation
From a physicochemical viewpoint, amyloid fibril formation is a phase transition from soluble
to crystal-like sates limited by supersaturation. It occurs only above solubility (ie, the …
to crystal-like sates limited by supersaturation. It occurs only above solubility (ie, the …
Substitution of Met-38 to Ile in γ-synuclein found in two patients with amyotrophic lateral sclerosis induces aggregation into amyloid
LD Aubrey, N Ninkina, SM Ulamec… - Proceedings of the …, 2024 - National Acad Sciences
α-, β-, and γ-Synuclein are intrinsically disordered proteins implicated in physiological
processes in the nervous system of vertebrates. α-synuclein (αSyn) is the amyloidogenic …
processes in the nervous system of vertebrates. α-synuclein (αSyn) is the amyloidogenic …
Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation
Amyloid fibrils of proteins such as α-synuclein are a hallmark of neurodegenerative diseases
and much research has focused on their kinetics and mechanisms of formation. The …
and much research has focused on their kinetics and mechanisms of formation. The …
Atomic resolution structure of full-length human insulin fibrils
Patients with type 1 diabetes mellitus who are dependent on an external supply of insulin
develop insulin-derived amyloidosis at the sites of insulin injection. A major component of …
develop insulin-derived amyloidosis at the sites of insulin injection. A major component of …
PatchProt: Hydrophobic patch prediction using protein foundation models
D Gogishvili, E Minois-Genin, J van Eck… - arXiv preprint arXiv …, 2024 - arxiv.org
Hydrophobic patches on protein surfaces play important functional roles in protein-protein
and protein-ligand interactions. Large hydrophobic surfaces are also involved in the …
and protein-ligand interactions. Large hydrophobic surfaces are also involved in the …
Exploring the Molecular Pathology of Iatrogenic Amyloidosis
B Bonilauri - Journal of Molecular Pathology, 2024 - mdpi.com
Iatrogenic amyloidosis results from medical therapeutic interventions, leading to the
misfolding and aggregation of proteins into amyloid fibrils or to their direct deposition in …
misfolding and aggregation of proteins into amyloid fibrils or to their direct deposition in …
Unraveling the Complex Pathology of Neurodegenerative Diseases: Multiple Prions, Cross-β Networks and Baicalein's ReproFold
HY Chang, IF Wang - 2024 - preprints.org
The origin of neurodegenerative diseases is linked to the abnormal folding of disease-
associated proteins. The traditional amyloid hypothesis has been a focal point of research …
associated proteins. The traditional amyloid hypothesis has been a focal point of research …
[引用][C] Substitution of Met-38 to Ile in γ-synuclein found in two patients with amyotrophic lateral sclerosis induces aggregation into amyloid
W show that Ile38-containing - 2024 - europepmc.org
Results The NAC Region of γSyn Does Not Form Amyloid at Neutral pH. αSyn and γSyn
have 77, 51, and 13% sequence identity in their N-terminal, NAC, and C-terminal regions …
have 77, 51, and 13% sequence identity in their N-terminal, NAC, and C-terminal regions …