Results 31 to 40 of about 53,939 (158)

Protein misfolding and cellular stress in disease and ageing - Concepts and protocols

European Journal of Histochemistry, 2011
To those readers that already got the Protein misfolding and disease volume, this new title can sound as an update or a second edition of the previous volume: well, this is not the case.
Carlo Alberto Redi
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RETRACTED ARTICLE: Neurotropic influenza A virus infection causes prion protein misfolding into infectious prions in neuroblastoma cells

Scientific Reports, 2021
Misfolding of the cellular prion protein, PrPC, into the amyloidogenic isoform, PrPSc, which forms infectious protein aggregates, the so-called prions, is a key pathogenic event in prion diseases.
Hideyuki Hara, Junji Chida, Keiji Uchiyama, Agriani Dini Pasiana, Etsuhisa Takahashi, Hiroshi Kido, Suehiro Sakaguchi   +6 more
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Molecular mechanisms of proteinopathies across neurodegenerative disease: a review

Neurological Research and Practice, 2019
Background Although there is a range of different symptoms across neurodegenerative diseases, they have been noted to have common pathogenic features.
Alexander P. Marsh
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Nanomedicine and protein misfolding diseases [PDF]

Nanomedicine: Nanotechnology, Biology and Medicine, 2005
Misfolding and self assembly of proteins in nano-aggregates of different sizes and morphologies (nano-ensembles, primarily nanofilaments and nano-rings) is a complex phenomenon that can be facilitated, impeded, or prevented, by interactions with various intracellular metabolites, intracellular nanomachines controlling protein folding and interactions ...
Alexey V, Kransnoslobodtsev, Luda S, Shlyakhtenko, Egor, Ukraintsev, Tatiana O, Zaikova, John F W, Keana, Yuri L, Lyubchenko   +5 more
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Prion protein misfolding and disease [PDF]

Current Opinion in Structural Biology, 2009
Transmissible spongiform encephalopathies (TSEs or prion diseases) are a rare group of invariably fatal neurodegenerative disorders that affect humans and other mammals. TSEs are protein misfolding diseases that involve the accumulation of an abnormally aggregated form of the normal host prion protein (PrP).
Roger A, Moore, Lara M, Taubner, Suzette A, Priola   +2 more
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Abnormal degradation of the neuronal stress-protective transcription factor HSF1 in Huntington’s disease

Nature Communications, 2017
Huntington’s disease (HD) is caused by misfolding of mutant Htt protein. The authors find that in HD models, the decreased expression of heat shock transcription factor 1 that usually protects against protein misfolding, is in part caused by elevated ...
Rocio Gomez-Pastor, Eileen T. Burchfiel, Daniel W. Neef, Alex M. Jaeger, Elisa Cabiscol, Spencer U. McKinstry, Argenia Doss, Alejandro Aballay, Donald C. Lo, Sergey S. Akimov, Christopher A. Ross, Cagla Eroglu, Dennis J. Thiele   +12 more
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Protein aggregation in progressive myoclonus epilepsies and related syndromes [PDF]

Exploration of Neuroscience
For this review paper, data on protein misfolding and aggregation in progressive myoclonus epilepsies and some developmental encephalopathies are gathered.
Eva Žerovnik
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Effect of primary structural variation on cervid prion protein in flexibility, stability, and spontaneous misfolding propensity

Neurobiology of Disease
Protein misfolding is central to numerous neurodegenerative disorders, collectively known as proteinopathies, which include Alzheimer's disease, Parkinson's disease, and prion diseases, among others.
Carlos M. Díaz-Domínguez, Hasier Eraña, Francesca Peccati, Enric Vidal, Jorge M. Charco, Cristina Sampedro-Torres-Quevedo, Miguel A. Pérez-Castro, Nuria L. Lorenzo, Samanta Giler, Glenn C. Telling, Mariví Geijo, Jesús R. Requena, Gonzalo Jiménez-Osés, Joaquín Castilla   +13 more
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Misfolded Proteins and Retinal Dystrophies [PDF]

, 2009
Many mutations associated with retinal degeneration lead to the production of misfolded proteins by cells of the retina. Emerging evidence suggests that these abnormal proteins cause cell death by activating the Unfolded Protein Response, a set of conserved intracellular signaling pathways that detect protein misfolding within the endoplasmic reticulum
Jonathan H, Lin, Matthew M, Lavail
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Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae

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