Results 31 to 40 of about 187,834 (297)

Cellular internalization of alpha-synuclein aggregates by cell surface heparan sulfate depends on aggregate conformation and cell type. [PDF]

, 2017
Amyloid aggregates found in the brain of patients with neurodegenerative diseases, including Alzheimer's and Parkinson's disease, are thought to spread to increasingly larger areas of the brain through a prion-like seeding mechanism.
Esko, Jeffrey D, Ihse, Elisabet, Lawrence, Roger, Masliah, Eliezer, van Wijk, Xander M, Yamakado, Hodaka   +5 more
core   +2 more sources

The triphenylmethane dye brilliant blue G is only moderately effective at inhibiting amyloid formation by human amylin or at disaggregating amylin amyloid fibrils, but interferes with amyloid assays; Implications for inhibitor design. [PDF]

, 2019
The development of inhibitors of islet amyloid formation is important as pancreatic amyloid deposition contributes to type-2 diabetes and islet transplant failure.
Akter, Rehana, Bhatia, Surita R, Raleigh, Daniel P, Zheng, Bingqian, Zhyvoloup, Alexander   +4 more
core   +3 more sources

Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

Molecules, 2020
The self-assembly of proteins is an essential process for a variety of cellular functions including cell respiration, mobility and division. On the other hand, protein or peptide misfolding and aggregation is related to the development of Parkinson’s ...
María Florencia Pignataro, María Georgina Herrera, Verónica Isabel Dodero   +2 more
doaj   +1 more source

Mimiviruses Interfere With IκBα Degradation

Frontiers in Virology, 2022
Many aspects of giant viruses biology still eludes scientists, with viruses such as Acanthamoeba polyphaga mimivirus (APMV) and Tupanvirus (TPV) possessing large virions covered by fibrils and are cultivated in laboratories using Acanthamoeba cells as ...
Juliana dos Santos Oliveira, Dahienne Ferreira Oliveira, Victor Alejandro Essus, Gabriel Henrique Pereira Nunes, Leandro Honorato, José Mauro Peralta, Leonardo Nimrichter, Allan Jefferson Guimarães, Debora Foguel, Alessandra Almeida Filardy, Juliana R. Cortines   +10 more
doaj   +1 more source

?2-Microglobulin Amyloid Fibril-Induced Membrane Disruption Is Enhanced by Endosomal Lipids and Acidic pH [PDF]

, 2014
Although the molecular mechanisms underlying the pathology of amyloidoses are not well understood, the interaction between amyloid proteins and cell membranes is thought to play a role in several amyloid diseases. Amyloid fibrils of ?2-microglobulin (?2m)
A Halle, A Ivankin, AD Petelska, AM Smith, B Boland, B Reed, C Cecchi, C Luquain, CJ Sarell, CL Bergstrom, CM Franzin, D Eisenberg, D Freeman, DE Lee, DP Smith, EE Ambroggio, Eric W. Hewitt, F Ferrone, F Gejyo, G van Meer, H Ohvo-Rekila, HD Gallala, HE White, I Benilova, IJ Morten, J Brotheru, J Brotherus, J Pan, J Villanueva, J Zimmerberg, JH Lee, JN Chebukati, JR Wherrett, JW Becker, K Berthelot, K Ditaranto, Kevin W. Tipping, L Milanesi, L Pieri, L Pieri, L Rajendran, M Arrasate, M Bostrom, M Bucciantini, M Duan, M Garcia-Garcia, M Stefani, MF Sciacca, MFM Engel, MFM Sciacca, MP Fogarty, MR Eftink, MY Porter, N Cremades, N Demaurex, N Liguori, Neil A. Ranson, NM Kad, NP Reynolds, Patrick van der Wel, Paul A. Beales, Rebecca Thompson, RF Chen, S Huterer, S Valleix, S Yamamoto, Sheena E. Radford, SL Myers, Sophia C. Goodchild, T Eichner, T Hayakawa, T Kobayashi, T Kobayashi, T Kobayashi, T Kobayashi, T Ookoshi, T Sheynis, T Umeda, Tania Sheynis, TE Frederick, TE Frederick, TL Williams, TL Williams, TP Knowles, TPJ Knowles, TR Jahn, TR Jahn, V Soura, VJ McParland, VN Uversky, Wei-Feng Xue, WF Xue, WF Xue, WF Xue, WF Xue, WF Xue, WG Wood, Y Hirakura, ZS Ji   +98 more
core   +4 more sources

The Proteome Content of Blood Clots Observed Under Different Conditions: Successful Role in Predicting Clot Amyloid(ogenicity)

Molecules
A recent analysis compared the proteome of (i) blood clots seen in two diseases—sepsis and long COVID—when blood was known to have clotted into an amyloid microclot form (as judged by staining with the fluorogenic amyloid stain thioflavin T) with (ii ...
Douglas B. Kell, Etheresia Pretorius
doaj   +1 more source

The Ancestral N-Terminal Domain of Big Defensins Drives Bacterially Triggered Assembly into Antimicrobial Nanonets

mBio, 2019
Big defensins, ancestors of β-defensins, are composed of a β-defensin-like C-terminal domain and a globular hydrophobic ancestral N-terminal domain.
Karine Loth, Agnès Vergnes, Cairé Barreto, Sébastien N. Voisin, Hervé Meudal, Jennifer Da Silva, Albert Bressan, Nawal Belmadi, Evelyne Bachère, Vincent Aucagne, Chantal Cazevielle, Hélène Marchandin, Rafael Diego Rosa, Philippe Bulet, Lhousseine Touqui, Agnès F. Delmas, Delphine Destoumieux-Garzón   +16 more
doaj   +1 more source

Impact of Aβ40 and Aβ42 Fibrils on the Transcriptome of Primary Astrocytes and Microglia

Biomedicines, 2022
Fibrillar amyloid β-protein (Aβ) deposits in the brain, which are primarily composed of Aβ40 or Aβ42 peptides, are key pathological features of Alzheimer’s disease (AD) and related disorders. Although the underlying mechanisms are still not clear, the Aβ
Xiaoyue Zhu, Joseph M. Schrader, Brandon A. Irizarry, Steven O. Smith, William E. Van Nostrand   +4 more
doaj   +1 more source

Bright fibrils in Ca II K

, 2009
Context: Except for the Ca II resonance lines, fibrils are ubiquitously present in most high-resolution observations of chromospheric lines. Aims: We show that fibrils are also a prevailing feature in Ca II K, provided the spatial-resolution is ...
A. Pietarila, Ayres, Beckers, Bel, Bianda, Carlsson, Carlsson, Cauzzi, Centeno, Cheung, de Boer, de Pontieu, Fontenla, Hansteen, Holzreuter, J. Hirzberger, Janssen, Jefferies, Jones, Lagg, Marsh, McIntosh, Patsourakos, Puschmann, Rutten, Rybicki, Rybicki, S. K. Solanki, Schrijver, Selwa, Smith, Solanki, Solanki, Solanki, Title, Tritschler, Uchida, Uitenbroek, V. Zakharov, van Noort, Vecchio, Vecchio, Veeder, Weigelt, Withbroe, Wöger, Zirin   +46 more
core   +1 more source

Extracellular Alpha-Synuclein: Mechanisms for Glial Cell Internalization and Activation

Biomolecules, 2022
Alpha-synuclein (α-syn) is a small protein composed of 140 amino acids and belongs to the group of intrinsically disordered proteins. It is a soluble protein that is highly expressed in neurons and expressed at low levels in glial cells.
Cecilia Chavarría, Rodrigo Ivagnes, José M. Souza   +2 more
doaj   +1 more source