Results 41 to 50 of about 3,403,581 (279)

Theoretical model of prion propagation: A misfolded protein induces misfolding [PDF]

open access: yesProceedings of the National Academy of Sciences, 2005
There is a hypothesis that dangerous diseases such as bovine spongiform encephalopathy, Creutzfeldt-Jakob, Alzheimer's, fatal familial insomnia, and several others are induced by propagation of wrong or misfolded conformations of some vital proteins. If for some reason the misfolded conformations were acquired by many such protein molecules it might ...
Edyta, Małolepsza   +3 more
openaire   +2 more sources

Cytoprotective functions of amyloid precursor protein family members in stress signaling and aging [PDF]

open access: yes, 2013
Poster presentation: Molecular Neurodegeneration: Basic biology and disease pathways Cannes, France. 10-12 September 2013. Background: The amyloid precursor protein (APP) is processed via two different metabolic pathways: the amyloidogenic and the non ...
Kundu, Arpita   +9 more
core   +1 more source

Nanomedicine and protein misfolding diseases [PDF]

open access: yesNanomedicine: 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   +5 more
openaire   +2 more sources

Outline and computational approaches of protein misfolding.

open access: yes, 2010
Protein misfolding is a general causation of classical conformational diseases and many pathogenic changes that are the result of structural conversion.
刘鑫
core   +2 more sources

Molecular mechanisms of proteinopathies across neurodegenerative disease: a review

open access: yesNeurological 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
doaj   +1 more source

Prion protein misfolding and disease [PDF]

open access: yesCurrent 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   +2 more
openaire   +2 more sources

Abnormal degradation of the neuronal stress-protective transcription factor HSF1 in Huntington’s disease

open access: yesNature 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   +12 more
doaj   +1 more source

The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer

open access: yesMolecular Oncology, EarlyView.
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

Protein aggregation in progressive myoclonus epilepsies and related syndromes [PDF]

open access: yesExploration of Neuroscience
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

open access: yesFEBS Open Bio, EarlyView.
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

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