Search Results - "prion"
Suggested Topics within your search.
Suggested Topics within your search.
- Protein Folding
- Neurodegenerative Diseases 5
- Degeneration 4
- Nervous system 4
- Protein folding 4
- Proteins 4
- Prion Diseases 3
- Protein Conformation 3
- Metabolism 2
- Prion diseases 2
- Aging 1
- Brain 1
- Diseases 1
- Disorders 1
- Endoplasmic Reticulum Stress 1
- Endoplasmic reticulum 1
- Genetic aspects 1
- HSP40 Heat-Shock Proteins 1
- Molecular aspects 1
- Molecular chaperones 1
- Proteasome Endopeptidase Complex 1
- Proteasome Inhibitors 1
- Proteolysis 1
- Proteostasis Deficiencies 1
- Stress, Physiological 1
- Ubiquitin 1
- Unfolded Protein Response 1
- chemistry 1
- etiology 1
- metabolism 1
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Prion diseases
Published 2007Table of Contents: “…Contents: Understanding the biophysical aspects of a disease of protein misfolding -- Structural studies of PrPc and PrPsc -- The development of synthetic mammalian prions and the proof of their infectivity and serial transmissibility -- Heterocyclic pharmacotherapies for prion disease -- Pyridinyl based therapies and structure based design -- Serendipitous discovery of acridines as anti-prion agents -- Bisacridines as potent inhibitors of prion replication in cell culture -- The relationship between the prion diseases and other diseases of protein misfolding.…”
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2
Pathogenic mechanisms in prion disease
Published 2014Table of Contents: “…Contents: Neurodegenerative diseases and protein misfolding disorders -- Prion disease in mice to study mechanisms of neurodegeneration due to misfolded protein accumulation -- Early prion neurodegenerative change is reversible: access to key neurotoxic pathways -- Critical change is loss of synaptic proteins due to activation of PERK branch of the unfolded protein response -- Modifying this pathway genetically is neuroprotective -- Modifying this pathway pharmacologically is neuroprotective -- Relevance of this pathway in other neurodegenerative diseases with misolded proteins e.g. …”
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Electronic Video -
3
Endoplasmic reticulum stress in neurodegenerative diseases
Published 2012Table of Contents: “…Contents: Neurodegenerative disease -- Misfolded aggregates deposited in the brain -- Research strategy -- Prion diseases -- Two conformations of the prion protein -- Experimental scrapie model in mice -- Upregulation of ER chaperones -- ER-stress and UPR in human CJD -- PrP interaction with ER chaperones in brain -- PrPSc induction of ER-stress and neuronal death -- Calcineurin properties -- A novel treatment for prion diseases.…”
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Electronic Video -
4
Roles for Hsp40 molecular chaperones in protein misfolding disease
Published 2012Table of Contents: “…Contents: Protein aggregation in conformational disease -- The Hsp40 system -- The Hsp70 system -- Small oligomers, prion, yeast, Huntington's disease and protein triage -- Mechanisms for proteotoxicity -- Mechanisms for amyloid disease.…”
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Electronic Video -
5
Protein aggregation, metals and oxidative stress in neurodegenerative diseases
Published 2007Table of Contents: “…Contents: Introduction to protein conformational brain diseases -- Alzheimer's disease, A-beta and tau -- A-beta oligomers and toxicity -- A-beta generates hydrogen peroxide -- Results from experiments using electron spin resonance spectroscopy -- Parkinson's disease -- Generation of hydrogen peroxide from alpha synuclein, toxic fragments of the prion protein and the familial British dementia peptide -- Early oligomers appear to generate hydrogen peroxide -- Huntington's disease -- Protein aggregates could be protective -- Potential common toxic pathway for these brain diseases.…”
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Electronic Video -
6
Protein degradation and defense against neurodegenerative disease part 2 of 2 /
Published 2014Table of Contents: “…Contents: The 26S proteasome -- The 20S proteasome -- Proteasome inhibitors -- PS-341 -- Proteasome inhibitors in multiple myeloma -- Structures of the archaeal PAN ATPase-20S complex and the eukaryotic 26S proteasome -- Multiple ATP-dependent steps in proteasome function -- The gating mechanism of the proteasome -- Prions inhibit proteasome function -- Binding of ubiquitin conjugates activate the 26S proteasome by stimulating 20S gate-opening and ATP hydrolysis -- Ubiquitin conjugates activate their own degradation by the 26S Proteasome -- The inhibitor of proteasome-associated deubiquitinating enzyme Usp14, IU1, enhances degradation of tau.…”
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Electronic Video