Results 111 to 120 of about 69,622 (226)

Overproduction of 42 Amino Acids Long Amyloid Beta Leads to Activation of Secretory Autophagy and Development of Drusen‐Like Structures Originating From Retinal Pigment Epithelium

The FASEB Journal, Volume 40, Issue 5, 15 March 2026.
The role of 42 amino acids long amyloid beta (Aβ) in the retinal pigment epithelium (RPE) was investigated using 5xFAD mice model overproducing Aβ. The RPE cells of 5xFAD mice showed increased oxidative stress, accumulation of autophagy‐destined proteins, increased expression of secretory autophagy markers, and increase in epithelial‐to‐mesenchymal ...
Johanna Ruuth, Toni Tamminen, Elisa Toropainen, Heikki Tanila, Juha M. T. Hyttinen, Tarja Malm, Kai Kaarniranta, Ali Koskela   +7 more
wiley   +1 more source

Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity. [PDF]

, 2012
The amyloid protein aggregation associated with diseases such as Alzheimer's, Parkinson's and type II diabetes (among many others) features a bewildering variety of β-sheet-rich structures in transition from native proteins to ordered oligomers and ...
Cheng, Pin-Nan, Eisenberg, David, Liu, Cong, Nowick, James S, Zhao, Minglei   +4 more
core  

Influence of Nanoparticle Size and Shape on Oligomer Formation of an Amyloidogenic Peptide [PDF]

, 2011
Understanding the influence of macromolecular crowding and nanoparticles on the formation of in-register $\beta$-sheets, the primary structural component of amyloid fibrils, is a first step towards describing \emph{in vivo} protein aggregation and ...
Allen M. P., Asakura S., Auer S., Batra J., Behe M., Bernard R. Brooks, Brooks B. R., Chan J. C. C., Cheung M. S., Chiti F., Colvin V. L., Colvin V. L., Cotter M. A., Cunha S., D. Thirumalai, del Álamao M., Dhar A., Dima R. I., Edward P. O’Brien, Elcock A. H., Fleer G. J., Flory P. J., Hall D., Hofrichter J., Jaroniec C. P., Jaroniec C. P., John. E. Straub, Lazaridis T., Lindner R. A., Linse S., Magno A., McGuffee S. R., Nelson R., Nelson R., Nguyen P. H., Petty S. A., Pierotti R. A., Rohrig U. F., Ross P. D., Sacchettini J. C., Schreiber G., Shaw M. R., Stagg L., Straub J. E., Tarus B., Tellam R. L., Tycko R., Walter H., Wu C., Zhou H. X., Zimmerman S. B.   +50 more
core   +1 more source

Amyloid Alpha: The Neglected Cousin of Amyloid Beta

ChemBioChem, Volume 27, Issue 5, 13 March 2026.
Amyloid α (Aα), also known as P3, is an alternative processing product of amyloid precursor protein that may be formed instead of Amyloid β (Aβ). Unlike Aβ, Aα/P3 has received little attention and is commonly dismissed as nonamyloidogenic. This perspective article refutes the notion that Aα/P3 is nonamyloidogenic and nontoxic.
Jevgenij A. Raskatov
wiley   +1 more source

Tyr(682) in the intracellular domain of APP regulates amyloidogenic APP processing in vivo.

PLoS ONE, 2010
BackgroundThe pathogenesis of Alzheimer's disease is attributed to misfolding of Amyloid-β (Aβ) peptides. Aβ is generated during amyloidogenic processing of Aβ-precursor protein (APP).
Alessia P M Barbagallo, Richard Weldon, Robert Tamayev, Dawang Zhou, Luca Giliberto, Oded Foreman, Luciano D'Adamio, Luciano D'Adamio   +7 more
doaj   +1 more source

Modulation of Tau Protein Neurotoxic Hallmarks by Novel σ1R Agonists/HDAC Inhibitor Dual‐Acting Compounds

ChemMedChem, Volume 21, Issue 5, 13 March 2026.
This study explores the development of dual‐acting compounds combining σ1R agonists and histone deacetylase inhibitors (HDACi). Key findings include compound 2d and 3a's high affinity for σ1R and favorable pharmacokinetic profile and an in vivo determined σ1R agonist profile by reversing the effect of the σ1R antagonist BD‐1063.
Antonino N. Fallica, Carla Barbaraci, M. Carmen Ruiz‐Cantero, Arianna Scarlatti, Alessandro Coco, Giorgia Giordano, Alfonsina La Mantia, Orazio Prezzavento, Antonio Di Stefano, Ivana Cacciatore, Giacomo Siano, Antonino Cattaneo, Lorella Pasquinucci, Enrique J. Cobos, Cristina Di Primio, Emanuele Amata, Agostino Marrazzo   +16 more
wiley   +1 more source

Catalytic Amyloids: Turning Fibrils Into Biocatalysts

Chemistry – A European Journal, Volume 32, Issue 10, 9 March 2026.
Amyloids, traditionally associated with diseases, have emerged as versatile catalytic scaffolds. From natural amyloid sequences to bioinspired and de novo designs, we highlight strategies to construct catalytic active sites and anchor enzymes onto fibrils, creating versatile nanomaterials with tunable activities. ABSTRACT Amyloids have been regarded as
Alessandra Esposito, Linda Leone, Flavia Nastri, Angela Lombardi   +3 more
wiley   +1 more source

Substituent‐Based Modulation of Self‐Assembly and Immunogenicity of Amphipathic Peptides

Advanced Science, Volume 13, Issue 18, 27 March 2026.
This study systematically investigates how positional and subtle changes, such as substituents on the phenyl ring attached to short amphipathic peptides, influence their self‐assembly, fibril morphology, and immunogenic responses. ABSTRACT Self‐assembled peptide‐based biomaterials provide versatile platforms for biomedical uses, featuring customizable ...
Anirban Das, Ushasi Pramanik, Elise M. Brown, Chih‐Yun Liu, Huan Gong, Jonathan Fascetti, Mark Gibson, Samuel Stealey, Silviya P. Zustiak, Cory Berkland, Piyoosh Sharma, Meredith E. Jackrel, Mark A. White, Jai S. Rudra   +13 more
wiley   +1 more source

Dual‐Target ROS‐Driven Spatiotemporal Senolysis for Vascular Repair and Immune Microenvironment Reprogramming in the Treatment of Ocular Fundus Neovascularization

Advanced Science, Volume 13, Issue 16, 18 March 2026.
We developed a senolytic approach using procyanidin C1 (PCC1)‐loaded platform, a clinically established and safe hyaluronic acid‐based scaffold, to selectively eliminate senescent endothelial and microglial cells. This dual‐targeting strategy significantly suppresses pathological neovascularization and promotes vascular repair, presenting a safe and ...
Yali Zhou, Tianxing Chen, Peiyu Liu, Kangjia Lv, Yifan Wang, Xiaoqian Wang, Junwei Fang, Chong Chen, Zhaoyang Wang, Fang Wei, Xun Xu   +10 more
wiley   +1 more source

Photo‐Catalyzed Labeling of Amyloid Deposits in Human Tissue to Proteotype Amyloidosis Diseases

Aggregate, Volume 7, Issue 3, March 2026.
Amyloid‐ID, a ThT‐like photocatalytic probe, enables proteotyping of amyloid deposits by ROS‐mediated protein labeling. Applied to patient biopsies, amyloid‐ID identifies potential fibrinogen‐derived amyloid in laryngeal amyloidosis, revealing a mechanically sensitive fibrillation mechanism linked to vocal cord friction.
Huan Feng, Fangliang Guo, Yan Wang, Meng You, Qiuxuan Xia, Wang Wan, Di Shen, Kaini Shen, Xin Zhang, Wei Li, Yu Liu   +10 more
wiley   +1 more source