[HTML][HTML] Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)
FX Theillet, A Binolfi, T Frembgen-Kesner… - Chemical …, 2014 - ACS Publications
It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …
α-synuclein aggregation and its modulation
Parkinson's disease (PD) is a neurological disorder marked by the presence of cytoplasmic
inclusions, Lewy bodies (LBs) and Lewy neurites (LNs) as well as the degeneration of …
inclusions, Lewy bodies (LBs) and Lewy neurites (LNs) as well as the degeneration of …
[HTML][HTML] Cellular internalization of alpha-synuclein aggregates by cell surface heparan sulfate depends on aggregate conformation and cell type
Amyloid aggregates found in the brain of patients with neurodegenerative diseases,
including Alzheimer's and Parkinson's disease, are thought to spread to increasingly larger …
including Alzheimer's and Parkinson's disease, are thought to spread to increasingly larger …
[HTML][HTML] The hyaluronidase, TMEM2, promotes ER homeostasis and longevity independent of the UPRER
RT Schinzel, R Higuchi-Sanabria, O Shalem… - Cell, 2019 - cell.com
Cells have evolved complex mechanisms to maintain protein homeostasis, such as the UPR
ER, which are strongly associated with several diseases and the aging process. We …
ER, which are strongly associated with several diseases and the aging process. We …
Protein misfolding and amyloid nucleation through liquid–liquid phase separation
Liquid–liquid phase separation (LLPS) is an emerging phenomenon in cell physiology and
diseases. The weak multivalent interaction prerequisite for LLPS is believed to be facilitated …
diseases. The weak multivalent interaction prerequisite for LLPS is believed to be facilitated …
[HTML][HTML] The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity
Amyloidosis is a protein folding disorder in which normally soluble proteins are deposited
extracellularly as insoluble fibrils, impairing tissue structure and function. Charged …
extracellularly as insoluble fibrils, impairing tissue structure and function. Charged …
The role of heparan sulfates in protein aggregation and their potential impact on neurodegeneration
A Maïza, S Chantepie, C Vera, A Fifre, MB Huynh… - FEBS …, 2018 - Wiley Online Library
Neurodegenerative disorders, such as Alzheimer's, Parkinson's, and prion diseases, are
directly linked to the formation and accumulation of protein aggregates in the brain. These …
directly linked to the formation and accumulation of protein aggregates in the brain. These …
Dual effect of the acidic polysaccharose ulvan on the inhibition of amyloid-β protein fibrillation and disintegration of mature fibrils
F Liu, W Zhao, F Zhao, Q Dong, Y Wang… - … Applied Materials & …, 2020 - ACS Publications
The abnormal folding and aggregation of amyloid-β protein (Aβ) is the main reason for the
occurrence and development of Alzheimer's disease (AD). The discovery of novel inhibitors …
occurrence and development of Alzheimer's disease (AD). The discovery of novel inhibitors …
[HTML][HTML] Proteomics, glycomics, and glycoproteomics of matrisome molecules
The most straightforward applications of proteomics database searching involve intracellular
proteins. Although intracellular gene products number in the thousands, their well-defined …
proteins. Although intracellular gene products number in the thousands, their well-defined …
Mechanistic and therapeutic overview of glycosaminoglycans: the unsung heroes of biomolecular signaling
K Gulati, KM Poluri - Glycoconjugate journal, 2016 - Springer
Immune regulation is a complex biological signaling pathway in which several classes of
biomolecules and small molecules play a complacent role to mediate this process …
biomolecules and small molecules play a complacent role to mediate this process …