Results 101 to 110 of about 94,035 (378)

Generation of App knock-in mice reveals deletion mutations protective against Alzheimer’s disease-like pathology

open access: yesNature Communications, 2018
To date, only one mutation in the gene for amyloid-beta precursor protein APP has been suggested to be protective against Alzheimer’s disease. Here, authors found using gene editing of a mutant App knock-in mouse line that deletion of the 3’UTR region is
Kenichi Nagata   +7 more
doaj   +1 more source

Protein Regge Trajectories, Phase Coexistence and Physics of Alzheimer's Disease [PDF]

open access: yesarXiv, 2011
Alzheimer's disease causes severe neurodegeneration in the brain that leads to a certain death. The defining factor is the formation of extracellular senile amyloid plaques in the brain. However, therapeutic approaches to remove them have not been effective in humans, and so our understanding of the cause of Alzheimer's disease remains incomplete. Here
arxiv  

What drives amyloid molecules to assemble into oligomers and fibrils? [PDF]

open access: yes, 2010
We develop a general theory for three states of equilibrium of amyloid peptides: the monomer, oligomer, and fibril. We assume that the oligomeric state is a disordered micelle-like collection of a few peptide chains held together loosely by hydrophobic interactions into a spherical hydrophobic core.
arxiv   +1 more source

Herpes simplex virus interferes with amyloid precursor protein processing [PDF]

open access: yes, 2005
Background The early events underlying Alzheimer's disease (AD) remain uncertain, although environmental factors may be involved. Work in this laboratory has shown that the combination of herpes simplex virus type 1 (HSV1) in brain and carriage of the
Dobson, C.B.   +3 more
core   +4 more sources

Designed Biomaterial‐Enhanced Cell Transplantation for Neural Tissue Engineering

open access: yesAggregate, EarlyView.
Biomaterials offer a promising solution for cell transplantation in the central nervous system by creating a protective environment that enhances cell survival, integration, and functional recovery in preclinical models of neurological disorders. ABSTRACT Cell transplantation therapy in the central nervous system is hindered by limited survival and ...
Yun Tang   +3 more
wiley   +1 more source

Axonal amyloid precursor protein and its fragments undergo somatodendritic endocytosis and processing. [PDF]

open access: yes, 2015
Deposition of potentially neurotoxic Aβ fragments derived from amyloid precursor protein (APP) at synapses may be a key contributor to Alzheimer's disease.
Goldstein, Lawrence SB   +2 more
core   +1 more source

Hydrogel‐Based Smart Materials for Wound Healing and Sensing

open access: yesAggregate, EarlyView.
The graphical abstract illustrates the role of hydrogel‐based flexible materials in advancing biomedical applications, including wound healing, point‐of‐care diagnostics, smart patches, and wearable devices. Hydrogels are particularly promising in modern wound care due to their high‐water content, flexibility, and biocompatibility.
Thi Kim Ngan Duong   +11 more
wiley   +1 more source

Microglia and amyloid precursor protein coordinate control of transient Candida cerebritis with memory deficits

open access: yesNature Communications, 2019
The potential links between infections and neurodegenerative disorders are unclear. Here, Wu et al. present a mouse model of low-grade candidemia characterized by highly localized cerebritis, accumulation of amyloid precursor protein and beta peptides ...
Yifan Wu   +11 more
doaj   +1 more source

Use of Peptides for the Management of Alzheimer’s Disease: Diagnosis and Inhibition

open access: yesFrontiers in Aging Neuroscience, 2018
Alzheimer’s disease (AD) is a form of dementia and the most common progressive neurodegenerative disease (ND). The targeting of amyloid-beta (Aβ) aggregation is one of the most widely used strategies to manage AD, and efforts are being made globally to ...
Mohammad H. Baig   +3 more
doaj   +1 more source

A common beta-sheet architecture underlies in vitro and in vivo beta(2)-microglobulin amyloid fibrils [PDF]

open access: yes, 2008
Misfolding and aggregation of normally soluble proteins into amyloid fibrils and their deposition and accumulation underlies a variety of clinically significant diseases.
Jahn, T.R., Radford, S.E., Tennent, G.A.
core   +2 more sources

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