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ChemInform Abstract: Molecular and Chemical Basis of Prion‐Related Diseases
ChemInform, 1998AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
S. B. L. NG, A. J. DOIG
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Prion Disorders: Creutzfeldt-Jakob Disease and Related Disorders
2021Abstract Prion disorders, or transmissible spongiform encephalopathies (TSEs), are universally fatal human and animal diseases that cause rapid degeneration of brain neurons by way of a conformational change in the prion protein that autocatalyzes further conformational change and selective neuronal toxicity. TSEs may occur sporadically,
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Prion-protein-related diseases of animals and man
2011Scrapie, bovine spongiform encephalopathy (BSE), Creutzfeldt–Jakob disease (CJD), and related diseases of mink (transmissible mink encephalopathy), mule deer and elk (chronic wasting disease) are the founder members of a group of diseases called the transmissible degenerative (or spongiform) encephalopathies (TSE).
James Hope, Mark P. Dagleish
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Prion's Progress: Patterns and Rates of Molecular Evolution in Relation to Spongiform Disease
Journal of Molecular Evolution, 1998Modification of the cellular prion protein has been correlated with the acquisition of several neurodegenerative diseases, including kuru, scrapie, bovine spongiform encephalopathy (BSE), and Creutzfeldt-Jakob disease (CJD). Sequence conservation and amino acid identity are known to influence the efficacy of interspecific transmission.
D C, Krakauer, P M, Zanotto, M, Pagel
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Journal of Molecular Biology, 2010
The prion protein can exist both in a normal cellular isoform and in a pathogenic conformational isoform. The latter is responsible for the development of different neurodegenerative diseases, for example Creutzfeldt-Jakob disease or fatal familial insomnia.
Christian, Gerum +2 more
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The prion protein can exist both in a normal cellular isoform and in a pathogenic conformational isoform. The latter is responsible for the development of different neurodegenerative diseases, for example Creutzfeldt-Jakob disease or fatal familial insomnia.
Christian, Gerum +2 more
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The Prion Diseases: Creutzfeldt-Jakob, Gerstmann-Sträussler-Scheinker, and Related Disorders
Journal of Geriatric Psychiatry and Neurology, 1998The prion diseases are an interesting group of neurodegenerative disorders for a variety of reasons. The most obvious is their property of transmissibility, but beyond that they constitute a fascinating example of the diversity of disease expression possible from a common etiologic factor.
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British Journal of Neuroscience Nursing, 2022
Background: Most cases of dementia are due to Alzheimer's disease or vascular dementia, but attention on these disorders means that other important causes of dementia may be relatively neglected. About 10–15% of people with dementia have other diagnoses, and there are numerous causes of the less common types of dementia.
Laura Davis, Zarina Karim, Tom Dening
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Background: Most cases of dementia are due to Alzheimer's disease or vascular dementia, but attention on these disorders means that other important causes of dementia may be relatively neglected. About 10–15% of people with dementia have other diagnoses, and there are numerous causes of the less common types of dementia.
Laura Davis, Zarina Karim, Tom Dening
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Prion Protein-Related Diseases Of Man And Animals
1998Abstract Scrapie, Creutzfeldt-Jakob disease (CJD), Gerstmann- Straussler-Sheinker (GSS) syndrome and related diseases of mink (transmissible mink encephalopathy), mule deer, and elk (chronic wasting disease) are the founder members of a group of diseases called the transmissible degenerative (or spongiform) encephalopathies (TSE); the
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2000
In humans, familial forms of transmissible spongiform encephalopathies (TSE; "prion diseases") have been shown to segregate with the exchange of individual amino acids in the prion protein (PrP) sequence. We used the NMR structure of the globular domain of mouse PrP in the cellular form (PrP(C)) as a starting point for investigations by long-time ...
M, Billeter, K, Wüthrich
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In humans, familial forms of transmissible spongiform encephalopathies (TSE; "prion diseases") have been shown to segregate with the exchange of individual amino acids in the prion protein (PrP) sequence. We used the NMR structure of the globular domain of mouse PrP in the cellular form (PrP(C)) as a starting point for investigations by long-time ...
M, Billeter, K, Wüthrich
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Journal of the American Dietetic Association, 2011
The transmission of bovine spongiform encephalopathy (BSE) to human beings and the spread of chronic wasting disease (CWD) among cervids have prompted concerns about zoonotic transmission of prion diseases. Travel to the United Kingdom and other European countries, hunting for deer or elk, and venison consumption could result in the exposure of US ...
Joseph Y, Abrams +4 more
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The transmission of bovine spongiform encephalopathy (BSE) to human beings and the spread of chronic wasting disease (CWD) among cervids have prompted concerns about zoonotic transmission of prion diseases. Travel to the United Kingdom and other European countries, hunting for deer or elk, and venison consumption could result in the exposure of US ...
Joseph Y, Abrams +4 more
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