Results 51 to 60 of about 75,180 (286)

Amyloid fibril proteomics of AD brains reveals modifiers of aggregation and toxicity

Molecular Neurodegeneration, 2023
Background The accumulation of amyloid beta (Aβ) peptides in fibrils is prerequisite for Alzheimer’s disease (AD). Our understanding of the proteins that promote Aβ fibril formation and mediate neurotoxicity has been limited due to technical challenges ...
Arun Upadhyay, Deepak Chhangani, Nalini R. Rao, Julia Kofler, Robert Vassar, Diego E. Rincon-Limas, Jeffrey N. Savas   +6 more
doaj   +1 more source

The LBFGS Quasi-Newtonian Method for Molecular Modeling Prion AGAAAAGA Amyloid Fibrils [PDF]

, 2012
Experimental X-ray crystallography, NMR (Nuclear Magnetic Resonance) spectroscopy, dual polarization interferometry, etc are indeed very powerful tools to determine the 3-Dimensional structure of a protein (including the membrane protein); theoretical ...
Hou, Yating, Wang, Changyu, Wang, Yiju, Zhang, Jiapu, Zhang, Xiangsun   +4 more
core   +3 more sources

Supersaturation-Dependent Formation of Amyloid Fibrils

Molecules, 2022
The supersaturation of a solution refers to a non-equilibrium phase in which the solution is trapped in a soluble state, even though the solute’s concentration is greater than its thermodynamic solubility. Upon breaking supersaturation, crystals form and the concentration of the solute decreases to its thermodynamic solubility. Soon after the discovery
Yuji Goto, Masahiro Noji, Kichitaro Nakajima, Keiichi Yamaguchi   +3 more
openaire   +3 more sources

Staphylococcus aureus delta toxin modulates both extracellular membrane vesicle biogenesis and amyloid formation

mBio, 2023
Staphylococcus aureus secretes phenol-soluble modulins (PSMs), a family of small, amphipathic, secreted peptides with multiple biologic activities. Community-acquired S.
Xiaogang Wang, Divakara SSM Uppu, Seth W. Dickey, Dylan J. Burgin, Michael Otto, Jean C. Lee   +5 more
doaj   +1 more source

The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy [PDF]

, 2015
Structural analysis of protein fibrillation is inherently challenging. Given the crucial role of fibrils in amyloid diseases, method advancement is urgently needed.
Annette E. Langkilde, Balbirnie, Bente Vestergaard, Berryman, Berryman, Blanchet, Cecchi, Collins, Debelouchina, Diaz-Avalos, Dmitri I. Svergun, Dunbrack, Eisenberg, Esposito, Fitzpatrick, Franke, Giehm, Gras, Jiménez, Kantardjieff, Knowles, Konarev, Kyle L. Morris, Langkilde, Langkilde, Lewandowski, Louise C. Serpell, Makin, Marshall, Morris, Narayanan, Nasica-Labouze, Nelson, Oliveira, Periole, Pettersen, Powers, Qi, Reches, Sawaya, Sikorski, Strodel, Stroud, Sunde, Svergun, Svergun, Vestergaard, Wel, Wel, Wickner, Wiltzius   +50 more
core   +1 more source

Large‐scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation

FEBS Open Bio, EarlyView.
Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane, Lea Nikolić, Lorenzo Maraio, Thomas Goiran, Nathan Karpilovsky, Stefano Sellitto, Vangelis Bouris, Jiang‐An Yin, Ronald Melki, Edward A Fon, Adriano Aguzzi, Elena De Cecco   +11 more
wiley   +1 more source

Statistical Mechanics and Kinetics of Amyloid Fibrillation

, 2016
Amyloid fibrillation is a protein self-assembly phenomenon that is intimately related to well-known human neurodegenerative diseases. During the past few decades, striking advances have been achieved in our understanding of the physical origin of this ...
Hong, Liu, Huang, Ya Jing, Lee, Chiu Fan
core   +1 more source

Entropy of water and the temperature-induced stiffening of amyloid networks [PDF]

, 2017
In water, networks of semi-flexible fibrils of the protein $\alpha$-synuclein stiffen significantly with increasing temperature. We make plausible that this reversible stiffening is a result of hydrophobic contacts between the fibrils that become more ...
Claessens, Mireille M. A. E., Lindhoud, Saskia, Semerdzhiev, Slav A., Stefanovic, Anja, Subramaniam, Vinod, van der Schoot, Paul   +5 more
core   +5 more sources

Polyphenolic Biflavonoids Inhibit Amyloid-Beta Fibrillation and Disaggregate Preformed Amyloid-Beta Fibrils [PDF]

Biomolecules & Therapeutics, 2019
Alzheimer's disease (AD) is a devastating neurodegenerative disease and a major cause of dementia in elderly individuals worldwide. Increased deposition of insoluble amyloid β (Aβ) fibrils in the brain is thought be a key neuropathological hallmark of AD.
Choi, Erika Y., Kang, Sam Sik, Lee, Sang Kook, Han, Byung Hee   +3 more
openaire   +2 more sources

Intercompartmental communication in senescence

FEBS Open Bio, EarlyView.
Senescent cells experience structural changes in the plasma membrane, endoplasmic reticulum, mitochondria, lysosomes, nucleus, and cytoskeleton. These alterations disrupt crosstalk among cellular compartments, impairing vesicular trafficking, contact sites, and molecular flow.
Krystyna Mazan‐Mamczarz, Eleanor J. Wind, Jixiang Leng, Myriam Gorospe   +3 more
wiley   +1 more source