A comprehensive review of protein misfolding disorders, underlying mechanism, clinical diagnosis, and therapeutic strategies

S Basha, DC Mukunda, J Rodrigues… - Ageing Research …, 2023 - Elsevier
Introduction The most prevalent biological macromolecules in living systems are proteins,
the building block of life, extremely dynamic in structure and functions. Due to several …

Intercommunication between metal ions and amyloidogenic peptides or proteins in protein misfolding disorders

JM Suh, M Kim, J Yoo, J Han, C Paulina… - Coordination Chemistry …, 2023 - Elsevier
The aggregation and accumulation of amyloidogenic peptides and proteins are observed as
pathological features in the brains of patients suffering from neurodegenerative disorders …

Advances in the understanding of protein misfolding and aggregation through molecular dynamics simulation

A Rahman, B Saikia, CR Gogoi, A Baruah - Progress in Biophysics and …, 2022 - Elsevier
Aberrant protein folding known as protein misfolding is counted as one of the striking factors
of neurodegenerative diseases. The extensive range of pathologies caused by protein …

Prion protein biology through the lens of liquid-liquid phase separation

A Agarwal, S Mukhopadhyay - Journal of Molecular Biology, 2022 - Elsevier
Conformational conversion of the α-helix-rich cellular prion protein into the misfolded, β-rich,
aggregated, scrapie form underlies the molecular basis of prion diseases that represent a …

Detecting the insoluble protein aggregates in live cells using an AIE derivative of fluorescent protein chromophore

L Liu, W Jin, Y Huang, J Dai, X Zheng, Y Liu… - Sensors and Actuators B …, 2022 - Elsevier
Many incurable or unmanageable human protein conformational diseases are associated
with the misfolding or aggregation of the aberrantly processed or mutant proteins. In this …

Intrinsic determinants of prion protein neurotoxicity in Drosophila: from sequence to (dys)function

A Cembran, P Fernandez-Funez - Frontiers in Molecular …, 2023 - frontiersin.org
Prion diseases are fatal brain disorders characterized by deposition of insoluble isoforms of
the prion protein (PrP). The normal and pathogenic structures of PrP are relatively well …

Multi-eGO: An in silico lens to look into protein aggregation kinetics at atomic resolution

E Scalone, L Broggini, C Visentin… - Proceedings of the …, 2022 - National Acad Sciences
Protein aggregation into amyloid fibrils is the archetype of aberrant biomolecular self-
assembly processes, with more than 50 associated diseases that are mostly uncurable …

Realization of amyloid-like aggregation as a common cause for pathogenesis in diseases

S Naskar, N Gour - Life, 2023 - mdpi.com
Amyloids were conventionally referred to as extracellular and intracellular accumulation of
Aβ42 peptide, which causes the formation of plaques and neurofibrillary tangles inside the …

Modulating effects of zingiberaceae phenolic compounds on neurotrophic factors and their potential as neuroprotectants in brain disorders and age-associated …

AM Razak, JK Tan, M Mohd Said, S Makpol - Nutrients, 2023 - mdpi.com
The Zingiberaceae family possess various phenolic compounds that have significant
systemic bioactivities in the brain, including in age-related neurodegenerative diseases …

Functional, pathogenic, and pharmacological roles of protein folding intermediates

E Biasini, P Faccioli - Proteins: Structure, Function, and …, 2023 - Wiley Online Library
Protein expression and function in eukaryotic cells are tightly harmonized processes
modulated by the combination of different layers of regulation, including transcription …