Results 131 to 140 of about 67,311 (287)

In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances

Protein Science, Volume 35, Issue 4, April 2026.
Abstract Oligomeric assemblies of amyloidogenic proteins, such as Aβ, tau, α‐synuclein, amylin, transthyretin, and TDP‐43, are increasingly recognized as key drivers of cellular dysfunction across a range of neurodegenerative and systemic disorders.
Magdalena I. Ivanova, Carmelo La Rosa, Ayyalusamy Ramamoorthy   +2 more
wiley   +1 more source

Pyroglutamate-modified amyloid -B amplifies cytotoxicity and induces prion-like properties in conventional amyloid-B

, 2011
Justin Michael Nussbaum
openalex   +1 more source

In silico peptide self‐assembly reveals the importance of N‐terminal motifs and the inhibition mechanism of the mutation L38M in α‐synuclein fibrillation

Protein Science, Volume 35, Issue 4, April 2026.
Abstract Alpha‐synuclein (αSyn) is a presynaptic protein associated with several neurodegenerative diseases. While the non‐amyloid component (NAC) region of the αSyn sequence (residues 65–90) forms the core of all αSyn fibrils, recent findings suggest that the flanking regions play a key role in initiating or preventing amyloid formation. Two motifs in
Van T. T. Nguyen, Sabine M. Ulamec, David J. Brockwell, Sheena E. Radford, Carol K. Hall   +4 more
wiley   +1 more source

NMR refinement of under-determined loop regions of the E200K variant of the human prion protein using database-derived distance constraints

, 2005
Kriti Gautam Mukhopadhyay
openalex   +2 more sources

The role of the prion protein in the immune system [PDF]

, 2013
Veronika Kana
openalex   +1 more source

Prion Diseases [PDF]

Microbiology and Immunology, 1995
openaire   +3 more sources

Scalable assay to identify inhibitors of prion‐like propagation of protein misfolding as potential therapeutics for neurodegeneration

Protein Science, Volume 35, Issue 4, April 2026.
Abstract Protein misfolding is linked to many neurodegenerative diseases. In some cases, misfolding can propagate through a prion‐like mechanism whereby natively folded molecules are converted into more copies of the misfolded isoform. Prion‐like propagation of misfolding is an attractive therapeutic target, but difficulties with assaying conversion ...
Abhishek Narayan, Krishna Neupane, Michael T. Woodside   +2 more
wiley   +1 more source

PRION DISEASES [PDF]

Journal of Neurology, Neurosurgery & Psychiatry, 2004
R S G, Knight, R G, Will
openaire   +3 more sources

The extracellular regulated kinase-1 (ERK1) controls regulated α-secretase-mediated processing, promoter transactivation, and mRNA levels of the cellular prion protein. [PDF]

, 2011
Moustapha Cissé, Eric Duplan, Marie‐Victoire Guillot‐Sestier, Joaquim Rumigny, Charlotte Bauer, Gilles Pagès, Hans‐Dieter Orzechowski, Barbara E. Slack, Frédéric Checler, Bruno Vincent   +9 more
openalex   +1 more source

NOTCH3 CADASIL Variant Receptor Aggregation Requires NOTCH3 Wild‐Type Receptors: Identification of Highly Selective Inhibitors That Block the Process

The FASEB Journal, Volume 40, Issue 6, 31 March 2026.
CADASIL is the major cause of early‐onset stroke and cognitive dysfunction, including dementia. It is caused by mutations in the NOTCH3 receptor that result in the formation of protein aggregates in the small vessel walls of the brain. We demonstrated that NOTCH3 CADASIL variant receptor aggregation is strictly dependent on interactions with NOTCH3 ...
Haijiang Wang, Xinxin Liu, Gido Gravesteijn, Alessia Atella, Jin Liu, Julie W. Rutten, Peter ten Dijke, Manuel A. F. V. Gonçalves, Saskia A. J. Lesnik Oberstein, David A. Baker   +9 more
wiley   +1 more source