Results 1 to 10 of about 202,201 (346)

TRANSMISSION ELECTRON MICROSCOPY FOR THE DIRECT ANALYSIS OF FIBRIN CLOT STRUCTURE [PDF]

Biotechnologia Acta, 2023
The aim of our study was to compare the structure of clots formed as a result of thrombin-induced fibrin polymerization in the presence or absence of monoclonal fibrin-specific antibodies fragments as factors that change the clot structure.
Y.P. Kucheriavyi,, I.D. Panas
doaj   +1 more source

Food amyloid fibrils are safe nutrition ingredients based on in-vitro and in-vivo assessment

Nature Communications, 2023
Food protein amyloid fibrils have superior technological, nutritional, sensorial, and physical properties compared to native monomers, but there is as yet insufficient understanding of their digestive fate and safety for wide consumption.
Dan Xu, Jiangtao Zhou, W. L. Soon, Ines Kutzli, Adrian Molière, Sabine Diedrich, Milad Radiom, S. Handschin, Bing Li, Lin Li, S. Sturla, Collin Y Ewald, R. Mezzenga   +12 more
semanticscholar   +1 more source

The RHIM of the Immune Adaptor Protein TRIF Forms Hybrid Amyloids with Other Necroptosis-Associated Proteins

Molecules, 2022
TIR-domain-containing adapter-inducing interferon-β (TRIF) is an innate immune protein that serves as an adaptor for multiple cellular signalling outcomes in the context of infection. TRIF is activated via ligation of Toll-like receptors 3 and 4.
Max O. D. G. Baker, Nirukshan Shanmugam, Chi L. L. Pham, Sarah R. Ball, Emma Sierecki, Yann Gambin, Megan Steain, Margaret Sunde   +7 more
doaj   +1 more source

Plant Protein Amyloid Fibrils for Multifunctional Sustainable Materials

Advanced Sustainable Systems, 2023
Artificial functional materials based on amyloid fibrils are proven to be a promising strategy toward functional materials. However, scaling‐up applications present sustainability concerns, as animal proteins are the main sources for fabricating amyloid ...
Ting Li, Jiangtao Zhou, M. Peydayesh, Yang Yao, Massimo Bagnani, Ines Kutzli, Zhengxing Chen, Li Wang, R. Mezzenga   +8 more
semanticscholar   +1 more source

Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation

Biomolecules, 2021
Henipaviruses are BSL-4 zoonotic pathogens responsible in humans for severe encephalitis. Their V protein is a key player in the evasion of the host innate immune response.
Edoardo Salladini, Frank Gondelaud, Juliet F. Nilsson, Giulia Pesce, Christophe Bignon, Maria Grazia Murrali, Roxane Fabre, Roberta Pierattelli, Andrey V. Kajava, Branka Horvat, Denis Gerlier, Cyrille Mathieu, Sonia Longhi   +12 more
doaj   +1 more source

Inhibition of Protein Aggregation and Endoplasmic Reticulum Stress as a Targeted Therapy for α-Synucleinopathy

Pharmaceutics, 2023
α-synuclein (α-syn) is an intrinsically disordered protein abundant in the central nervous system. Physiologically, the protein regulates vesicle trafficking and neurotransmitter release in the presynaptic terminals. Pathologies related to misfolding and
Natalia Siwecka, Kamil Saramowicz, Grzegorz Galita, Wioletta Rozpędek-Kamińska, Ireneusz Majsterek   +4 more
doaj   +1 more source

The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils

bioRxiv, 2022
Understanding of the molecular mechanisms underlying the maturation of protein condensates into amyloid fibrils associated with neurodegenerative diseases has so far remained elusive. Now it has been shown that in condensates formed by the low-complexity
Miriam Linsenmeier, L. Faltova, Chiara Morelli, Umberto Capasso Palmiero, Charlotte Seiffert, A. Küffner, D. Pinotsi, Jiangtao Zhou, R. Mezzenga, P. Arosio   +9 more
semanticscholar   +1 more source

Structure-based discovery of small molecules that disaggregate Alzheimer’s disease tissue derived tau fibrils in vitro

Nature Communications, 2022
Alzheimer’s disease (AD) is the consequence of neuronal death and brain atrophy associated with the aggregation of protein tau into fibrils. Thus disaggregation of tau fibrils could be a therapeutic approach to AD.
P. Seidler, K. Murray, D. Boyer, P. Ge, M. Sawaya, Carolyn Hu, Xinyi Cheng, R. Abskharon, Hope Pan, M. DeTure, C. K. Williams, D. Dickson, H. Vinters, D. Eisenberg   +13 more
semanticscholar   +1 more source

The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells

Nature Communications, 2021
The self-assembly of α-synuclein (αS) into intraneuronal inclusion bodies is a key characteristic of Parkinson’s disease. To define the nature of the species giving rise to neuronal damage, we have investigated the mechanism of action of the main αS ...
R. Cascella, Serene W. Chen, A. Bigi, José D. Camino, Catherine K. Xu, C. Dobson, F. Chiti, Nunilo Cremades, C. Cecchi   +8 more
semanticscholar   +1 more source

Amyloid fibrils in disease FTLD-TDP are composed of TMEM106B not TDP-43

Nature, 2022
Frontotemporal lobar degeneration (FTLD) is the third most common neurodegenerative condition after Alzheimer’s and Parkinson’s diseases1. FTLD typically presents in 45 to 64 year olds with behavioural changes or progressive decline of language skills2 ...
Yi-Xiao Jiang, Qin Cao, M. Sawaya, R. Abskharon, P. Ge, M. DeTure, D. Dickson, Janine Y. Fu, R. Ogorzalek Loo, J. Loo, D. Eisenberg   +10 more
semanticscholar   +1 more source