Results 81 to 90 of about 75,180 (286)

Comparative Analysis of the Relative Fragmentation Stabilities of Polymorphic Alpha-Synuclein Amyloid Fibrils

Biomolecules, 2022
The division of amyloid fibril particles through fragmentation is implicated in the progression of human neurodegenerative disorders such as Parkinson’s disease.
Sarina Sanami, Tracey J. Purton, David P. Smith, Mick F. Tuite, Wei-Feng Xue   +4 more
doaj   +1 more source

Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs. [PDF]

, 2019
Deposits of amyloid fibrils of α-synuclein are the histological hallmarks of Parkinson's disease, dementia with Lewy bodies and multiple system atrophy, with hereditary mutations in α-synuclein linked to the first two of these conditions.
Boyer, David R, Eisenberg, David S, Fan, Weijia, Jiang, Lin, Li, Binsen, Sawaya, Michael R, Sun, Chuanqi   +6 more
core  

Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta. [PDF]

, 2013
Amyloid protein aggregates are associated with dozens of devastating diseases including Alzheimer's, Parkinson's, ALS, and diabetes type 2. While structure-based discovery of compounds has been effective in combating numerous infectious and metabolic ...
Eisenberg, David S, Hughes, Michael P, Jiang, Lin, Landau, Meytal, Leibly, David, Liu, Cong, Zhao, Minglei   +6 more
core   +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

Structural basis for amyloid fibril assembly by the master cell-signaling regulator receptor-interacting protein kinase 1

Nature Communications
Amyloid fibrils can form biologically relevant functional assemblies. The RIP homotypic interaction motifs (RHIMs) in receptor-interacting protein kinases 1 and 3 (RIPK1 and RIPK3) orchestrate the formation of amyloid-like fibrils essential for ...
Paula Polonio, Jorge Pedro López-Alonso, Hanxing Jiang, Sara Andrés-Campos, Fátima C. Escobedo-González, Gustavo A. Titaux-Delgado, Iban Ubarretxena-Belandia, Miguel Mompeán   +7 more
doaj   +1 more source

UV-light exposed prion protein fails to form amyloid fibrils. [PDF]

PLoS ONE, 2008
Amyloid fibril formation involves three steps; structural perturbation, nucleation and elongation. We have investigated amyloidogenesis using prion protein as a model system and UV-light as a structural perturbant.
Abhay Kumar Thakur, Ch Mohan Rao
doaj   +1 more source

Activated Bone Marrow-Derived Macrophages Eradicate Alzheimer's-Related Aβ42 Oligomers and Protect Synapses. [PDF]

, 2020
Impaired synaptic integrity and function due to accumulation of amyloid β-protein (Aβ42) oligomers is thought to be a major contributor to cognitive decline in Alzheimer's disease (AD). However, the exact role of Aβ42 oligomers in synaptotoxicity and the
Black, Keith L, Daley, David A, Fuchs, Dieu-Trang, Garcia, Veronica J, Hayden, Eric Y, Koronyo, Yosef, Koronyo-Hamaoui, Maya, Li, Songlin, Rentsendorj, Altan, Rutishauser, Ueli, Sheyn, Julia, Teplow, David B, Torbati, Tania   +12 more
core  

Beta2-Microglobulin Amyloid Fibrils Are Nanoparticles That Disrupt Lysosomal Membrane Protein Trafficking and Inhibit Protein Degradation by Lysosomes. [PDF]

, 2014
Fragmentation of amyloid fibrils produces fibrils that are reduced in length but have an otherwise unchanged molecular architecture. The resultant nanoscale fibril particles inhibit the cellular reduction of the tetrazolium dye 3-(4,5-dimethylthi-azol-2 ...
Appelqvist, Argilés, Baglioni, Beattie, Beaufay, Berridge, Berthelot, Boot, Bucciantini, Casey, Chafekar, Chiti, Colvin, Cremades, Dehay, Dell'Angelica, Desplats, Eisenberg, Eskelinen, Follett, Friedrich, García-García, Gharibyan, Goodchild, Grudzielanek, Halle, Harold, Heegaard, Isobe, Jahn, Jiang, Julien, Kanatsu, Kayed, Kepp, Kerokoski, Khurana, Kubo, Kurz, Kågedal, Lee, Lee, Lesné, Liu, Liu, Liu, Lorincz, Macia, MacLeod, Martins, Mazzulli, Milanesi, Monti, Morten, Mossuto, Mossuto, Myers, Münch, Nekooki-Machida, Nesterov, Nixon, Novitskaya, Petkova, Pieri, Pols, Porter, Reixach, Ren, Shankar, Sheynis, Simoneau, Sims, Sipe, Sorkin, Soura, Stefani, Torres, Treusch, Uversky, Villamil Giraldo, Walsh, Winner, Xue, Xue, Xue, Zhang, Zhang, Zhao   +87 more
core   +2 more sources

Crystallin proteins and amyloid fibrils

Cellular and Molecular Life Sciences, 2008
Improper protein folding (misfolding) can lead to the formation of disordered (amorphous) or ordered (amyloid fibril) aggregates. The major lens protein, alpha-crystallin, is a member of the small heat-shock protein (sHsp) family of intracellular molecular chaperone proteins that prevent protein aggregation.
Ecroyd, Heath, Carver, John
openaire   +4 more sources

The Uppsala APP Mutation Promotes Wild‐Type Amyloid‐β Aggregation and Deposition In Vivo

Advanced Science, EarlyView.
We investigated in vivo cross‐seeding of amyloid‐β (Aβ) isoforms in transgenic mice co‐expressing wild‐typeAβ and the Uppsala‐mutant Aβ variant (AβUpp), lacking six central residues. Weleveraged MALDI‐MS imaging and hyperspectral microscopy to follow spatio‐temporalAβ deposition.
Junyue Ge, María Pagnon de la Vega, Silvia Zampar, Enrica Cerilli, Srinivas Koutarapu, Ling Wu, Paul Fraser, Sertan Arkan, Vilmantas Giedraitis, Lars Lannfelt, Greta Hultqvist, Stina Syvänen, Martin Ingelsson, Jörg Hanrieder, Dag Sehlin   +14 more
wiley   +1 more source