Results 21 to 30 of about 75,180 (286)

A common beta-sheet architecture underlies in vitro and in vivo beta(2)-microglobulin amyloid fibrils [PDF]

, 2008
Misfolding and aggregation of normally soluble proteins into amyloid fibrils and their deposition and accumulation underlies a variety of clinically significant diseases.
Jahn, T.R., Radford, S.E., Tennent, G.A.
core   +2 more sources

Immunoprecipitation of amyloid fibrils by the use of an antibody that recognizes a generic epitope common to amyloid fibrils.

PLoS ONE, 2014
Amyloid fibrils are associated with many maladies, including Alzheimer's disease (AD). The isolation of amyloids from natural materials is very challenging because the extreme structural stability of amyloid fibrils makes it difficult to apply ...
Erin R Greiner, Jeffery W Kelly, Fernando L Palhano   +2 more
doaj   +1 more source

Cryo-EM structure of a catalytic amyloid fibril

Scientific Reports, 2023
Catalytic amyloid fibrils are novel types of bioinspired, functional materials that combine the chemical and mechanical robustness of amyloids with the ability to catalyze a certain chemical reaction.
Thomas Heerde, Akanksha Bansal, Matthias Schmidt, Marcus Fändrich   +3 more
doaj   +1 more source

Surface-catalyzed Amyloid Fibril Formation [PDF]

Journal of Biological Chemistry, 2002
Light chain (or AL) amyloidosis is characterized by the pathological deposition of insoluble fibrils of immunoglobulin light chain fragments in various tissues, walls of blood vessels, and basement membranes. In the present investigation, the in vitro assembly of a recombinant amyloidogenic light chain variable domain, SMA, on various surfaces was ...
Min, Zhu, Pierre O, Souillac, Cristian, Ionescu-Zanetti, Sue A, Carter, Anthony L, Fink   +4 more
openaire   +2 more sources

?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   +7 more sources

Inflammasome assembly is required for intracellular formation of β2-microglobulin amyloid fibrils, leading to IL-1β secretion

International Journal of Immunopathology and Pharmacology, 2022
Introduction Dialysis-related amyloidosis (DRA) caused by β2-microgloblin (B2M) fibrils is a serious complication for patients with kidney failure on long-term dialysis.
Naoe Kaneko, Wakako Mori, Mie Kurata, Toshihiro Yamamoto, Tamotsu Zako, Junya Masumoto   +5 more
doaj   +1 more source

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

Fibril Fragmentation Enhances Amyloid Cytotoxicity [PDF]

Journal of Biological Chemistry, 2009
Fibrils associated with amyloid disease are molecular assemblies of key biological importance, yet how cells respond to the presence of amyloid remains unclear. Cellular responses may not only depend on the chemical composition or molecular properties of the amyloid fibrils, but their physical attributes such as length, width, or surface area may also ...
Xue WF, Hellewell AL, Gosal WS, Homans SW, Hewitt EW, Radford SE   +5 more
openaire   +3 more sources

Mouse senile amyloid fibrils deposited in skeletal muscle exhibit amyloidosis-enhancing activity. [PDF]

PLoS Pathogens, 2010
Amyloidosis describes a group of protein folding diseases in which amyloid proteins are abnormally deposited in organs and/or tissues as fine fibrils.
Jinze Qian, Jingmin Yan, Fengxia Ge, Beiru Zhang, Xiaoying Fu, Hiroshi Tomozawa, Jinko Sawashita, Masayuki Mori, Keiichi Higuchi   +8 more
doaj   +1 more source

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