Results 111 to 120 of about 11,568 (285)

Distinct amino acid compositional requirements for formation and maintenance of the [PSI+] prion in yeast [PDF]

, 2015
Multiple yeast prions have been identified that result from the structural conversion of proteins into a self-propagating amyloid form. Amyloid-based prion activity in yeast requires a series of discrete steps.
Ben-Musa, Zobaida, Gruca, Margaret, MacLea, Kyle S., Paul, Kacy R., Ross, Eric D., Shattuck, Jenifer E., Waechter, Aubrey   +6 more
core   +2 more sources

Functional Amyloid Formation within Mammalian Tissue

PLoS Biology, 2005
Amyloid is a generally insoluble, fibrous cross-beta sheet protein aggregate. The process of amyloidogenesis is associated with a variety of neurodegenerative diseases including Alzheimer, Parkinson, and Huntington disease. We report the discovery of an unprecedented functional mammalian amyloid structure generated by the protein Pmel17. This discovery
Douglas M Fowler, Atanas V Koulov, Christelle Alory-Jost, Michael S Marks, William E Balch, Jeffery W Kelly   +5 more
openaire   +3 more sources

Postoperative Stress Accelerates Atherosclerosis Through Inflammatory Remodeling of the HDL Proteome and Impaired Reverse Cholesterol Transport

Advanced Science, EarlyView.
The study shows that noncardiac surgical inflammation rapidly disrupts HDL function and cholesterol efflux in mice and human patients. Impaired reverse cholesterol transport after surgery drives rapid lipid accumulation, NETosis, and apoptosis within atherosclerotic plaques.
Dominique M. Boucher, Victoria Lorant, Valerie Rochon, Abigail Carter, Cameron Stotts, My‐Anh Nguyen, Thomas Laval, Christina Emerton, Nathan Joyce, Nysa Vinayak, Marlena Scaffidi, David Cook, Katey J. Rayner, Rebecca C. Auer, Scott M. Gordon, Mireille I. Ouimet   +15 more
wiley   +1 more source

Immunoprecipitation of amyloid fibrils by the use of an antibody that recognizes a generic epitope common to amyloid fibrils.

PLoS ONE, 2014
Amyloid fibrils are associated with many maladies, including Alzheimer's disease (AD). The isolation of amyloids from natural materials is very challenging because the extreme structural stability of amyloid fibrils makes it difficult to apply ...
Erin R Greiner, Jeffery W Kelly, Fernando L Palhano   +2 more
doaj   +1 more source

The emerging concept of functional amyloid [PDF]

Journal of Internal Medicine, 2009
Abstract.Although amyloid has usually been considered a pathological structure, growing evidence indicates that amyloid may also be a productive part of cell biology contributing to normal physiology. In fact, amyloid formation seems to be an intrinsic propensity of polypeptides in general and the amyloid β‐fold an evolutionary highly conserved ...
openaire   +2 more sources

Amyloid β Instigates Cardiac Neurotrophic Signaling Impairment, Driving Alzheimer's Associated Heart Disease

Advanced Science, EarlyView.
This research identified cardiac amyloid pathology, neurotrophic factor depletion, and reduced myocardial nerve function in a transgenic model of cerebral amyloidosis (Tg2576), Aβ‐challenged cardiomyocytes, and in human AD heart tissue. These findings carry significant diagnostic and therapeutic implications, emphasizing the role of neuro‐signaling ...
Andrea Elia, Rebecca Parodi‐Rullan, Rafael Vazquez‐Torres, Ashley Carey, Huaqing Zhao, Sabzali Javadov, Silvia Fossati   +6 more
wiley   +1 more source

Identification of key amino acid residues modulating intracellular and in vitro microcin E492 amyloid formation

Frontiers in Microbiology, 2016
Microcin E492 (MccE492) is a pore-forming bacteriocin produced and exported by Klebsiella pneumoniae RYC492. Besides its antibacterial activity, excreted MccE492 can form amyloid fibrils in vivo as well as in vitro.
Paulina eAguilera, Andrés eMarcoleta, Pablo eLobos-Ruiz, Rocío eArranz, José María eValpuesta, Octavio eMonasterio, Rosalba eLagos   +6 more
doaj   +1 more source

What makes functional amyloids work? [PDF]

Crit Rev Biochem Mol Biol, 2022
Siemer AB.
europepmc   +1 more source

Time‐Resolved SAXS Reveals Distinct Millisecond Metal‐Induced Conformational Dynamics of Monomeric α‐Synuclein

Advanced Science, EarlyView.
Time‐resolved SAXS reveals how physiologically relevant metal ions shape the earliest conformational responses of monomeric α‐synuclein. Fe3+ induces rapid compaction, Cu2+ generates heterogeneous and partially folded ensembles, while Mn2+ and Zn2+ cause only modest changes.
Rebecca Sternke‐Hoffmann, Miriam Dos Santos Pinto, Xue Wang, Jinghui Luo   +3 more
wiley   +1 more source

The Mitochondrial Guardian α‐Amyrin Mitigates Alzheimer's Disease Pathology via Modulation of the DLK‐SARM1‐ULK1 Axis

Advanced Science, EarlyView.
Dietary habits play a key role in chronic diseases, and higher annual consumption of fruit and vegetable may lower risk of dementia. Artificial intelligence predicts the lipid‐like compound α‐Amyrin (αA) from plants with edible peels as a drug candidate against Alzheimer's disease.
Shu‐Qin Cao, Juan Ignacio Jiménez‐Loygorri, Yunguang Qiu, You Jung Kang, Khanh Van Do, Annabel E. Smith, Junjie Huang, Jun‐ping Pan, Lipeng Mao, Ang Li, Hangge Yang, Yahyah Aman, Maria Jose Donate Lagartos, Sofie Hindkjær Lautrup, Anbin Chen, Kristina Xiao Liang, Hailong Zhang, Juan Yi, Xurui Jin, Tin Cho Cheung, Olympia Apokotou, Florentia Papastefanaki, Rebecca Matsas, William A. McEwan, Feixiong Cheng, Hansang Cho, Guobing Chen, Huanxing Su, Konstantinos Palikaras, Oscar Junhong Luo, Qian Hua Zhao, Ding Ding, Cornelia van Duijn, Nektarios Tavernarakis, Patricia Boya, Tewin Tencomnao, Evandro F. Fang   +36 more
wiley   +1 more source