Results 71 to 80 of about 85,510 (321)
The Beta Amyloid Dysfunction (BAD) Hypothesis for Alzheimer’s Disease
Frontiers in Neuroscience, 2019 Beta amyloid, Aβ 1–42, originally named as Amyloid A4 protein, is one of the most investigated peptides in neuroscience and has attracted substantial interest since its discovery as the main insoluble fibril-type protein in cerebrovascular amyloid ...
Heinz Hillen
doaj +1 more source
Manipulating the Assembly and Architecture of Fibrillar Silk
Advanced Materials, EarlyView.In this study, advanced in situ AFM, PiFM, and Cryo‐EM are leveraged to realize in situ observations of nucleation, growth, and degradation of silk nanofibrils. A clear picture of the assembly and structural evolution of regenerated silk nanofibrils is defined and demonstrates a novel strategy for manipulating their structure and properties, which ...
Chenyang Shi +3 more
wiley +1 more source
Insights into the variability of nucleated amyloid polymerization by a minimalistic model of stochastic protein assembly [PDF]
, 2015 Self-assembly of proteins into amyloid aggregates is an important biological phenomenon associated with human diseases such as Alzheimer's disease. Amyloid fibrils also have potential applications in nano-engineering of biomaterials. The kinetics of amyloid assembly show an exponential growth phase preceded by a lag phase, variable in duration as seen ...
arxiv +1 more source
Cerebrospinal fluid Aβ42/40 corresponds better than Aβ42 to amyloid PET in Alzheimer’s disease [PDF]
, 2016 Background: Decreased concentrations of amyloid-β 1-42 (Aβ(42)) in cerebrospinal fluid (CSF) and increased retention of Aβ tracers in the brain on positron emission tomography (PET) are considered the earliest biomarkers of Alzheimer’s disease (AD ...
Blennow, Kaj +8 more
core +3 more sources
Harnessing Photo‐Energy Conversion in Nanomaterials for Precision Theranostics
Advanced Materials, EarlyView.Harnessing photo‐energy conversion in nanomaterials enables precision theranostics through light‐driven mechanisms such as photoluminescence, photothermal, photoelectric, photoacoustic, photo‐triggered surface‐enhanced Raman scattering (SERS), and photodynamic processes. This review explores six fundamental principles of photo‐energy conversion, recent
Jingyu Shi +4 more
wiley +1 more source
What drives amyloid molecules to assemble into oligomers and fibrils? [PDF]
, 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
A single dose of the γ-secretase inhibitor semagacestat alters the cerebrospinal fluid peptidome in humans [PDF]
, 2016 Background In Alzheimer’s disease, beta-amyloid peptides in the brain aggregate into toxic oligomers and plaques, a process which is associated with neuronal degeneration, memory loss, and cognitive decline. One therapeutic strategy is to
Bateman, Randall J +11 more
core +3 more sources
Mechanochemistry: Fundamental Principles and Applications
Advanced Science, EarlyView.In this review, the physicochemical principles of mechanochemistry are first clarified. Based on this foundation, the research basis and cutting‐edge scientific achievements in four areas are introduced: solid‐state organic chemistry, polymers, interface science, and biomechanochemistry.
Liang Dong +4 more
wiley +1 more source
A novel canonical dual computational approach for prion AGAAAAGA amyloid fibril molecular modeling [PDF]
J Theor Biol 284 (1) 149-157 (2011); selected by Protein
Crystallography Newsletter Volume 3, No. 9, September 2011, Crystallography
Times; Prions Research Today Volume 7 Issue 7, July 2011, p.14; the 18th of
the Top 25 Hottest Articles (picked up from papers of Jul 2011 to Sept 2011
of J Theor Biol), 2011 Many experimental studies have shown that the prion AGAAAAGA palindrome hydrophobic region (113-120) has amyloid fibril forming properties and plays an important role in prion diseases. However, due to the unstable, noncrystalline and insoluble nature of the amyloid fibril, to date structural information on AGAAAAGA region (113-120) has been very ...
arxiv +1 more source
Advanced Science, EarlyView.The globular shape and hydrophobicity of zein made it unsuitable to be processed in pure aqueous environment. Pepsin‐mediated hydrolysis converts zein into water‐soluble and fibril‐forming peptides with a bioconversion rate exceeding 70%, enabling the self‐assembly of amyloid‐like nanofibrils.
Mingqin Li +8 more
wiley +1 more source