Results 91 to 100 of about 514,761 (295)

Study of cosolvent-induced α-chymotrypsin fibrillogenesis: Does protein surface hydrophobicity trigger early stages of aggregation reaction? [PDF]

open access: yes
The misfolding of specific proteins is often associated with their assembly into fibrillar aggregates, commonly termed amyloid fibrils. Despite the many efforts expended to characterize amyloid formation in vitro, there is no deep knowledge about the ...
A Ahmad   +66 more
core   +1 more source

Astrocytic LRP1 mediates brain Aβ clearance and impacts amyloid deposition [PDF]

open access: yes, 2017
Accumulation and deposition of amyloid-β (Aβ) in the brain represent an early and perhaps necessary step in the pathogenesis of Alzheimer's disease (AD).
Bu, Guojun   +8 more
core   +2 more sources

A Novel Brain Penetrable Nanocarrier Delivers Brain‐Derived Neurotrophic Factor to Treat Alzheimer's Disease

open access: yesAdvanced Healthcare Materials, EarlyView.
A novel blood‐brain barrier‐penetrating terpolymer nanoparticle to deliver brain‐derived neurotrophic factor (BDNF) for the treatment of Alzheimer's disease (AD) is designed. The BDNF‐TPN significantly enhances BDNF accumulation in the brain following intravenous injection, reduces apoptosis and neuroinflammation, thus promoting neuronal survival and ...
Lily Yi Li   +8 more
wiley   +1 more source

APP Expression in Primary Neuronal Cell Cultures fromP6 Mice during in vitro Differentiation [PDF]

open access: yes, 1993
Primary neuronal cell cultures from P6 mice were investigated in order to study amyloid protein precursor (APP) gene expression in differentiating neurons.
Beyreuther, K.   +5 more
core   +1 more source

High-precision plasma β-amyloid 42/40 predicts current and future brain amyloidosis

open access: yesNeurology, 2019
Objective We examined whether plasma β-amyloid (Aβ)42/Aβ40, as measured by a high-precision assay, accurately diagnosed brain amyloidosis using amyloid PET or CSF p-tau181/Aβ42 as reference standards.
S. Schindler   +11 more
semanticscholar   +1 more source

Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials

open access: yesAdvanced Healthcare Materials, EarlyView.
The production of recombinant proteins represents a fundamental step in the characterisation of marine invertebrate adhesives and in the development of bio‐inspired glues. The association of these proteins with other components such as ions, proteins, polysaccharides, or polymers enables the fabrication of biomaterials for various healthcare ...
Alessandra Whaite   +4 more
wiley   +1 more source

Naturally occurring autoantibodies against beta-amyloid: investigating their role in transgenic animal and in vitro models of Alzheimer's disease [PDF]

open access: yes, 2011
Alzheimer's disease (AD) is a neurodegenerative disorder primarily affecting regions of the brain responsible for higher cognitive functions. Immunization against β-amyloid (Aβ) in animal models of AD has been shown to be effective on the molecular level
Al-Abed, Yousef   +13 more
core   +1 more source

A gut bacterial amyloid promotes α-synuclein aggregation and motor impairment in mice

open access: yeseLife, 2020
Amyloids are a class of protein with unique self-aggregation properties, and their aberrant accumulation can lead to cellular dysfunctions associated with neurodegenerative diseases. While genetic and environmental factors can influence amyloid formation,
T. Sampson   +15 more
semanticscholar   +1 more source

Biomimetic Mineralization of Keratin Scaffolds for Enamel Regeneration

open access: yesAdvanced Healthcare Materials, EarlyView.
Keratin‐based films guide biomimetic enamel remineralization by promoting organized hydroxyapatite growth under physiological conditions. Advanced biophysical characterization confirms keratin's structural adaptability and mineral ions‐binding affinity, supporting mineral nucleation and hierarchical crystal assembly. This study establishes keratin as a
Sara Gamea   +19 more
wiley   +1 more source

Crystal structure of monomeric human β-2- microglobulin reveals clues to its amyloidogenic properties [PDF]

open access: yes, 2002
Dissociation of human β-2-microglobulin (β(2)m) from the heavy chain of the class I HLA complex is a critical first step in the formation of amyloid fibrils from this protein.
A. P. Kalverda   +31 more
core   +2 more sources

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