Results 41 to 50 of about 3,647,798 (263)
Molecular mechanisms of proteinopathies across neurodegenerative disease: a review
Background Although there is a range of different symptoms across neurodegenerative diseases, they have been noted to have common pathogenic features.
Alexander P. Marsh
doaj +1 more source
Nanomedicine and protein misfolding diseases [PDF]
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 +5 more
openaire +2 more sources
The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer
Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad +2 more
wiley +1 more source
Prion protein self-peptides modulate prion interactions and conversion [PDF]
Background: Molecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (PrPC) into the scrapie associated isoform (PrPSc), are poorly understood.
Bossers, A. +11 more
core +1 more source
Prion protein misfolding and disease [PDF]
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 +2 more
openaire +2 more sources
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 +12 more
doaj +1 more source
Loss of eIF5A rewires thapsigargin‐mediated endoplasmic reticulum stress responses in multiple myeloma cells by selective translation of mRNA transcripts, consequently dampening thapsigargin‐induced unfolded protein response (UPR) activation and shifting the balance from induction of apoptosis toward cell survival and proliferation.
Demi Both +7 more
wiley +1 more source
Neurodegenerative diseases present an enormous challenge to medicine and the need for biomarker discovery and novel drug-directed strategies are thus of high priority.
Lange, S. +4 more
core +1 more source
Protein aggregation in progressive myoclonus epilepsies and related syndromes [PDF]
For this review paper, data on protein misfolding and aggregation in progressive myoclonus epilepsies and some developmental encephalopathies are gathered.
Eva Žerovnik
doaj +1 more source
Adenosine triphosphate as a modulator of protein interactions and stability
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley +1 more source

