Results 61 to 70 of about 75,180 (286)

ENTAIL: Yet Another Amyloid Fibrils Classifier

open access: yesBMC Bioinformatics, 2022
Abstract Background: This research aims to increase our knowledge of amyloidoses. These disorders cause incorrect protein folding, affecting protein functionality (on structure). Fibrillar deposits are the basis of some wellknown diseases, such as Alzheimer, Creutzfeldt -Jakob diseases and type II diabetes.
Auriemma Citarella A.   +3 more
openaire   +4 more sources

A Systematic Comparison of Alpha‐Synuclein Seed Amplification Assays for Increasing Reproducibility

open access: yesAnnals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Seed amplification assays (SAAs) enable ultrasensitive detection of misfolded α‐synuclein across biofluids and tissues. Yet, heterogeneity in protocols limits cross‐study comparability and clinical translation. Here, we review α‐synuclein SAA methods and their performance across various biological matrices.
Manuela Amaral‐do‐Nascimento   +3 more
wiley   +1 more source

Prediction of peptide and protein propensity for amyloid formation [PDF]

open access: yes, 2014
Understanding which peptides and proteins have the potential to undergo amyloid formation and what driving forces are responsible for amyloid-like fiber formation and stabilization remains limited.
A Quintas   +80 more
core   +5 more sources

Amyloidogenic Peptide Fragments Designed From Bacterial Collagen‐like Proteins Form Hydrogel

open access: yesAdvanced Functional Materials, EarlyView.
This study identified amyloidogenic sequence motifs in bacterial collagen‐like proteins and exploited these to design peptides that self‐assemble into β‐sheet fibers and form hydrogels. One hydrogel supported healthy fibroblast growth, showing promise for biocompatible materials. Our work demonstrates that bacterial sequences can be harnessed to create
Vamika Sagar   +5 more
wiley   +1 more source

A Peptide Derived from the HIV-1 gp120 Coreceptor-Binding Region Promotes Formation of PAP248-286 Amyloid Fibrils to Enhance HIV-1 Infection.

open access: yesPLoS ONE, 2015
BackgroundSemen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) fragments, such as PAP248-286, in human semen can form amyloid fibrils to enhance HIV infection.
Jinquan Chen   +9 more
doaj   +1 more source

Dynamics of the formation of a hydrogel by a pathogenic amyloid peptide: islet amyloid polypeptide [PDF]

open access: yes, 2016
Many chronic degenerative diseases result from aggregation of misfolded polypeptides to form amyloids. Many amyloidogenic polypeptides are surfactants and their assembly can be catalysed by hydrophobic-hydrophilic interfaces (an air-water interface in ...
Hawkins, N   +4 more
core   +1 more source

Cytochrome Display on Amyloid Fibrils

open access: yesJournal of the American Chemical Society, 2006
Protein amyloid fibrils can be functionalized by coating the core protofilament with high concentrations of proteins and enzymes. This can be done elegantly by appending a functional domain to an amyloidogenic protein monomer, then assembling the monomers into a fibril. To display an array of biologically functional porphyrins on the surface of protein
Baldwin, A   +5 more
openaire   +3 more sources

Small Extracellular Vesicles from Neural Cells: Physiological and Pathological Roles, and Potential in Neurodegenerative Therapy

open access: yesAdvanced Healthcare Materials, EarlyView.
Neural cell–derived small extracellular vesicles (sEVs) are emerging as pivotal mediators in neurodegenerative diseases, exerting both pathogenic and therapeutic functions. This review synthesizes current evidence on how sEVs from distinct neural cell types regulate neurodegeneration, neuroprotection, biomarker discovery, and targeted drug delivery ...
Muhammad Waqas Salim   +4 more
wiley   +1 more source

On the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.

open access: yesPLoS ONE, 2014
Formation of amyloid fibrils in vivo has been linked to disorders such as Alzheimer's disease and prion-associated transmissible spongiform encephalopathies.
Weronika Surmacz-Chwedoruk   +4 more
doaj   +1 more source

Structure-based inhibitors of amyloid beta core suggest a common interface with tau. [PDF]

open access: yes, 2019
Alzheimer's disease (AD) pathology is characterized by plaques of amyloid beta (Aβ) and neurofibrillary tangles of tau. Aβ aggregation is thought to occur at early stages of the disease, and ultimately gives way to the formation of tau tangles which ...
Bowler, Jeannette   +13 more
core   +1 more source

Home - About - Disclaimer - Privacy