Results 101 to 110 of about 288,605 (343)
Structural Variation in Amyloid-β Fibrils from Alzheimer’s Disease Clinical Subtypes
Nature, 2017 Aggregation of amyloid-β peptides into fibrils or other self-assembled states is central to the pathogenesis of Alzheimer’s disease. Fibrils formed in vitro by 40- and 42-residue amyloid-β peptides (Aβ40 and Aβ42) are polymorphic, with variations in ...
W. Qiang +4 more
semanticscholar +1 more source
Disintegration of Amyloid fibrils using chaperones, inorganic chemicals
, 2023 Protein aggregation in the form of amyloid has been implicated in more than 50 human diseases. These diseases range from neuropathic, like Alzheimer's and Parkinson's, to common diseases like cataracts. The number of people getting affected by amyloid is
Bedsole, Sidney Ethan +1 more
core
Smart Nanotechnologies for Multimodal Neuromodulation and Brain Interfacing
Advanced Science, EarlyView.Recent advances in smart nanotechnologies are expanding the toolbox for brain interfacing, from wireless neuromodulation and high‐resolution sensing to targeted delivery within the central nervous system. By combining responsive nanomaterials with bioinspired design, these platforms enable multimodal interactions with neurons and glia, while also ...
Tommaso Curiale +6 more
wiley +1 more source
Angewandte Chemie, EarlyView.A coumarin‐based dual‐emission fluorophore was designed to visualize the maturation of protein liquid droplets. Upon covalent conjugation to droplet‐forming proteins, ratiometric fluorescence imaging allowed real time monitoring of droplet maturation. This probe is applicable to the analysis of droplet formation and maturation mechanisms, as well as to
Tomoya Yamamoto +6 more
wiley +2 more sources
Elevated temperatures accelerate the formation of toxic amyloid fibrils of hen egg‐white lysozyme
Veterinary Medicine and Science, 2021 The formation of amyloid fibrils is critical for neurodegenerative diseases. Some physiochemical conditions can promote the conversion of proteins from soluble globular shapes into insoluble well‐organized amyloid fibrils.
Zili Feng, Ying Li, Yu Bai
doaj +1 more source
Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils
Biochimica et Biophysica Acta, 2010 Intense efforts to detect, diagnose, and analyze the kinetic and structural properties of amyloid fibrils have generated a powerful toolkit of amyloid-specific molecular probes.
M. Biancalana, S. Koide
semanticscholar +1 more source
Enhancedin vitroproduction of amyloid-like fibrils from mutant (S20G) islet amyloid polypeptide
, 2001 Islet amyloid polypeptide (IAPP, “amylin”) is the amyloid-fibril-forming polypeptide in the islets of Langerhans associated with type 2 diabetes mellitus.
Ma, Zhi, +17 more
core +1 more source
Binding of serum-derived amyloid-associated proteins to amyloid fibrils
, 2022 Amyloid signature proteins such as serum amyloid P component, apolipoprotein E (ApoE), and ApoA-IV generally co-localise with amyloid, regardless of the types of amyloid precursor protein or the organs.
Yohei Misumi (3190254) +6 more
core +1 more source
Advanced Science, EarlyView.Tightly focused laser irradiation can accumulate tubulin proteins at/around the laser focus, which leads to the formation of highly ordered microtubule assemblies. The assemblies can exhibit various dynamic behaviors such as radial motion, bundling, and flagella‐like rotation with motor protein and chemical energy, highlighting as a unique tool for ...
Hiroshi Y. Yoshikawa +16 more
wiley +1 more source
Cell Death and DiseaseThe tumor microenvironment is a complex ecosystem that plays a critical role in cancer progression and treatment response. Recently, extracellular amyloid fibrils have emerged as novel components of the tumor microenvironment; however, their function ...
Francesco Farris +12 more
doaj +1 more source