Results 201 to 210 of about 288,605 (343)

Structural polymorphism of ex-vivo ALECT2 amyloid fibrils revealed by cryo-EM. [PDF]

Nat Commun
Afrin S, Nguyen BA, Singh V, Singh P, Bassett P, Pekala M, Evers B, Lopez C, Ahmed Y, Li L, Kallem RR, Lemoff A, Argyropoulos C, Kluve-Beckerman B, Saelices L.   +14 more
europepmc   +1 more source

Detection of amyloid fibrils in Parkinson’s disease using plasmonic chirality

Proceedings of the National Academy of Sciences of the United States of America, 2018
J. Kumar, Hasier Eraña, Elena López-Martínez, N. Claes, V. Martín, D. M. Solís, S. Bals, A. Cortajarena, J. Castilla, L. Liz‐Marzán   +9 more
semanticscholar   +1 more source

Proteostasis of organelles in aging and disease

The FEBS Journal, EarlyView.
Cells rely on regulated proteostasis mechanisms to keep their internal compartments functioning properly. When these mechanisms fail, damaged proteins accumulate, disrupting organelles, such as the nucleus, mitochondria, endoplasmic reticulum, Golgi, and lysosomes, as well as membraneless organelles, such as stress granules, processing bodies, the ...
Yara Nabawi, Cansu Doğan, Dunja Petrović, Gülce Perçin, Seda Koyuncu, David Vilchez   +5 more
wiley   +1 more source

Amyloid Fibrils: Potential Food Safety Implications

, 2008
The demonstration of oral Amyloid-A (AA) fibril transmissibility has raised food safety questions about the consumption of amyloidotic viscera. In a presumed prion-like mechanism, amyloid fibrils have been shown to trigger and accelerate the development ...
Greger, Michael
core   +1 more source

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation

The FEBS Journal, EarlyView.
Investigated mutations in transthyretin (TTR) disrupt the F87‐centered hydrophobic core that stabilizes its tetrameric structure. The mild I107V mutation weakens inter‐chain packing, while H88R fully abolishes tetramer formation, yielding a monomeric, aggregation‐prone form. Structural, biophysical, and computational analyses reveal that both mutations
István L. Bódy, Zsolt Fazekas, Nóra Wágner, Anna J. Kiss‐Szemán, Veronika Harmat, Zoltán Pozsonyi, Dóra K. Menyhárd, András Perczel   +7 more
wiley   +1 more source

YB-1 AP-CSD Forms Cross-β Amyloid Fibrils Without Secondary-Structure Conversion In Vitro. [PDF]

Int J Mol Sci
Timchenko MA, Galzitskaya OV, Chulkov AV, Likhachev IV, Glyakina AV, Molchanov MV, Molochkov NV, Penkov NV, Bobyleva LG, Balobanov VA, Yegorov AY, Guryanov SG, Nikulin AD, Lyabin DN, Vikhlyantsev IM, Bobylev AG.   +15 more
europepmc   +1 more source

Water, water, every where—the advent of hydrated pili structure

The FEBS Journal, EarlyView.
Protein structure is defined by its surrounding water. Naturally, this is also true for the gigantic protein filaments that pathogenic bacteria use to attach to and colonize their host cells. Structures of these filaments for which water can be identified with high confidence have stayed elusive for the longest time.
Hiroya Oki, Hideki Shigematsu, Kazuki Kawahara, Christoph Gerle   +3 more
wiley   +1 more source

Unraveling in vitro phase separation and aggregation properties of the structured region of FMRP and the impact of Fragile X syndrome‐linked mutations

The FEBS Journal, EarlyView.
Fragile X messenger ribonucleoprotein 1 (FMRP) is a multidomain RNA‐binding protein associated with Fragile X Syndrome (FXS). We found that its N‐terminal structured region has an intrinsic propensity to undergo liquid–liquid phase separation and fibril formation. FXS‐associated mutations perturb protein stability and aggregation propensity, suggesting
Flavia Catalano, Alessandra Bigi, Francesca Troilo, Federica Gabriele, Gianluca Pistoia, Italia A. Asteriti, Francesco Angelucci, Giorgio Giardina, Fabrizio Chiti, Carlo Travaglini‐Allocatelli, Adele Di Matteo   +10 more
wiley   +1 more source

An Optimized Protocol for High-Quality AFM Imaging of Amyloid Fibrils. [PDF]

Bio Protoc
Kumar RR, Das U, Uttamrao PP, Rathinavelan T.   +3 more
europepmc   +1 more source

Stimulating proteasomal degradation in human proteinopathies

The FEBS Journal, EarlyView.
The proteasome mediates the degradation of a wide range of proteins. Boosting proteasomal degradation may be beneficial in several disease contexts and can be achieved either by modulating proteasome activity or by improving substrate delivery. Proteasome activity can be enhanced by increasing proteasome abundance, inducing constitutive gate opening ...
Maria E. Gierisch, Enrica Barchi, Nico P. Dantuma   +2 more
wiley   +1 more source