Results 41 to 50 of about 69,622 (226)

Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation. [PDF]

, 2018
The normally soluble TAR DNA-binding protein 43 (TDP-43) is found aggregated both in reversible stress granules and in irreversible pathogenic amyloid. In TDP-43, the low-complexity domain (LCD) is believed to be involved in both types of aggregation. To
A Jain, A Molliex, A Patel, A Saini, A Soragni, AE Conicella, AF Harrison, AJ McCoy, AK Chen, AK Walker, AWP Fitzpatrick, C Amador-Ortiz, C Colombrita, C Lagier-Tourenne, C Schwab, C Yang, C-H Chiang, CK Chang, CM Dewey, Collaborative Computational Project, Number 4., D Shi, DA Bosco, David R. Boyer, David S. Eisenberg, DS Eisenberg, DT Murray, Duilio Cascio, E Bentmann, E Buratti, E Kabashi, EB Lee, Elizabeth L. Guenther, EM Marcotte, F Meersman, GM Sheldrick, GN Murshudov, GS Pesiridis, H Nakashima-Yasuda, Hamilton Trinh, HB Schmidt, HJ Dyson, HJ Kim, HY Zoghbi, J Hattne, JA Rodriguez, Jiahui Lu, JJ Wiltzius, Jose A. Rodriguez, JP Ling, JR Wheeler, L Goldschmidt, L Lim, LC Reineke, LL Jiang, LL Jiang, LM Igaz, M Budini, M Cushman, M Hasegawa, M Kato, M Mompeán, M Neumann, M Xu, MA Gitcho, Masato Kato, MC Lawrence, MD Winn, Michael P. Hughes, Michael R. Sawaya, MP Hughes, MR Sawaya, N Gilks, N Kedersha, P Emsley, P Hackman, P-N Cheng, PD Adams, PJ Lukavsky, PM Seidler, PS Estes, Qin Cao, RA Fuentealba, S Higashi, S Xiang, SC Ling, TM Franzmann, TPJ Knowles, W Guo, W Kabsch, W Kabsch, Y Dang, Y Lin, Z Otwinowski, ZM March   +93 more
core   +1 more source

Amyloidogenic and non-amyloidogenic pathways of amyloid precursor protein processing in oligodendrocytes

Brain Research
Excessive accumulation of toxic amyloid-β (Aβ) species in the brain is a major pathological process triggering neurodegeneration in Alzheimer's disease (AD). Recent studies indicate that both neurons and glial cells, including oligodendrocyte lineages (OLs), contribute to brain homeostasis and affect AD pathology; however, the roles of oligodendrocyte ...
Misaki Hida, Ken Yasuda, Masaru Toyokawa, Megumi Asada-Utsugi, Shintaro Toda, Narufumi Yanagida, Ryosuke Takahashi, Ayae Kinoshita, Takakuni Maki   +8 more
openaire   +3 more sources

Amyloidogenic Protein of α-Synuclein

Hanyang Medical Reviews, 2013
Amyloidogenesis is the key pathological phenomenon commonly observed in various neurodegenerative disorders. α-Synuclein is the major constituent of Lewy bodies as a common pathological signature of Lewy body diseases (LBDs) including Parkinson’s disease (PD), PD with dementia (PDD), and Dementia with Lewy bodies (DLB).
Jee Eun Yang, Seung R. Paik
openaire   +1 more source

Prediction of amyloidogenic and disordered regions in protein chains.

PLoS Computational Biology, 2006
The determination of factors that influence protein conformational changes is very important for the identification of potentially amyloidogenic and disordered regions in polypeptide chains. In our work we introduce a new parameter, mean packing density,
Oxana V Galzitskaya, Sergiy O Garbuzynskiy, Michail Yurievich Lobanov   +2 more
doaj   +1 more source

Quantitative flow cytometric selection of tau conformational nanobodies specific for pathological aggregates

Frontiers in Immunology, 2023
Single-domain antibodies, also known as nanobodies, are broadly important for studying the structure and conformational states of several classes of proteins, including membrane proteins, enzymes, and amyloidogenic proteins.
Jennifer M. Zupancic, Jennifer M. Zupancic, Matthew D. Smith, Matthew D. Smith, Hanna Trzeciakiewicz, Mary E. Skinner, Sean P. Ferris, Emily K. Makowski, Emily K. Makowski, Michael J. Lucas, Michael J. Lucas, Michael J. Lucas, Nikki McArthur, Ravi S. Kane, Henry L. Paulson, Henry L. Paulson, Henry L. Paulson, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier   +22 more
doaj   +1 more source

Minocycline 200 mg or 400 mg versus placebo for mild Alzheimer’s disease: the MADE Phase II, three-arm RCT

Efficacy and Mechanism Evaluation, 2020
Background: Minocycline is an anti-inflammatory drug and protects against the toxic effects of β-amyloid in vitro and in animal models of Alzheimer’s disease. To the best of our knowledge, no randomised placebo-controlled clinical trials in patients with
Robert Howard, Olga Zubko, Richard Gray, Rosie Bradley, Emma Harper, Linda Kelly, Lynn Pank, John O’Brien, Chris Fox, Naji Tabet, Gill Livingston, Peter Bentham, Rupert McShane, Alistair Burns, Craig Ritchie, Suzanne Reeves, Simon Lovestone, Clive Ballard, Wendy Noble, Gordon Wilcock, Ramin Nilforooshan   +20 more
doaj   +1 more source

Oat Plant Amyloids for Sustainable Functional Materials

Advanced Science, 2022
Amyloid functional materials from amyloid fibril building blocks, produced in vitro from amyloidogenic natural proteins or synthetic peptides, show diverse functionalities ranging from environmental science and biomedicine, to nanotechnology and ...
Jiangtao Zhou, Ting Li, Mohammad Peydayesh, Mattia Usuelli, Viviane Lutz‐Bueno, Jie Teng, Li Wang, Raffaele Mezzenga   +7 more
doaj   +1 more source

Chain Collapse of an Amyloidogenic Intrinsically Disordered Protein [PDF]

Biophysical Journal, 2011
Natively unfolded or intrinsically disordered proteins (IDPs) are under intense scrutiny due to their involvement in both normal biological functions and abnormal protein misfolding disorders. Polypeptide chain collapse of amyloidogenic IDPs is believed to play a key role in protein misfolding, oligomerization, and aggregation leading to amyloid fibril
Jain, Neha, Bhattacharya, Mily, Mukhopadhyay, Samrat   +2 more
openaire   +2 more sources

Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae [PDF]

, 2017
The early stages of protein misfolding remain incompletely understood, as most mammalian proteinopathies are only detected after irreversible protein aggregates have formed.
Keefer, Kathryn M, Stein, Kevin C, true, Heather L   +2 more
core   +2 more sources

The preaggregated state of an amyloidogenic protein: Hydrostatic pressure converts native transthyretin into the amyloidogenic state [PDF]

Proceedings of the National Academy of Sciences, 2000
Protein misfolding and aggregation cause several diseases, by mechanisms that are poorly understood. The formation of amyloid aggregates is the hallmark of most of these diseases. Here, the properties and formation of amyloidogenic intermediates of transthyretin (TTR) were investigated by the use of hydrostatic pressure and spectroscopic ...
A D, Ferrão-Gonzales, S O, Souto, J L, Silva, D, Foguel   +3 more
openaire   +2 more sources