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gerstmann-straussler-scheinker disease/пролин

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Prion Protein Prolines 102 and 105 and the Surrounding Lysine Cluster Impede Amyloid Formation.

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Human prion diseases can have acquired, sporadic, or genetic origins, each of which results in the conversion of prion protein (PrP) to transmissible, pathological forms. The genetic prion disease Gerstmann-Straussler-Scheinker syndrome can arise from point mutations of prolines 102 or 105. However,

p>1p> H NMR based Metabolic Signatures in Liver and Brain in Rat Model of Hepatic Encephalopathy

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Hepatic Encephalopathy (HE) is a debilitating neuropsychiatric complication associated with acute and chronic liver failure. It is characterized by diverse symptoms with variable severity that includes cognitive and motor deficits. The aim of the study is to assess metabolic alterations in brain and

Proton magnetic resonance spectroscopy of a patient with Gerstmann-Straussler-Scheinker disease.

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A 23-year-old woman with Gerstmann-Straussler-Scheinker disease (GSS) was investigated by 1H-magnetic resonance spectroscopy (1H-MRS). She developed gait ataxic at 22 years. The diagnosis was confirmed by DNA analysis showing a proline-to-leucine point mutation at codon 102 of the prion protein. On

Overestimation of serum concentrations of gamma-aminobutyric acid in patients with hepatic encephalopathy by the gamma-aminobutyric acid-radioreceptor assay.

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Sera of patients with hepatic encephalopathy strongly inhibit the specific binding of gamma-aminobutyric acid to synaptic membranes. In a previous study, this inhibition of specific gamma-aminobutyric acid binding was attributed to gamma-aminobutyric acid itself, and it was assumed that serum

Correlation between electroencephalographic and biochemical indices in acute hepatic encephalopathy in rats.

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Changes in biochemical and electroencephalographic parameters were followed over time during the development of acute hepatic encephalopathy (HE) in two different experimental models. In the rat, (sub)acute liver failure was obtained either by ligation of the hepatic artery in previously

Ovine prion protein variant A(136)R(154)L(168)Q(171) increases resistance to experimental challenge with bovine spongiform encephalopathy agent.

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Susceptibility and incubation periods of transmissible spongiform encephalopathies, such as scrapie in sheep, are modulated by the PrP gene. The standard model of association between ovine PrP genetics and classical scrapie susceptibility is based on PrP genotypes with respect to codons 136, 154 and

Atypical frontotemporal dementia as a new clinical phenotype of Gerstmann-Straussler-Scheinker disease with the PrP-P102L mutation. Description of a previously unreported Italian family.

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OBJECTIVE To describe a new dementia phenotype of Gerstmann-Straussler-Scheinker disease (GSS) in a previously unreported Italian family. Design Longitudinal clinical and neuropsychological assessment, combined with magnetic resonance imaging (MRI), single positron emission tomography (SPECT) and

Encephalopathy with neuroserpin inclusion bodies presenting as progressive myoclonus epilepsy and associated with a novel mutation in the Proteinase Inhibitor 12 gene.

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Neuroserpin encephalopathy is an autosomal-dominant degenerative disease associated with mutations in the Proteinase Inhibitor 12 (PI12) gene. A 26-year-old male presented with progressive myoclonus epilepsy and declining mental status. He had failed in university studies because of impaired

l-Serine dietary supplementation is associated with clinical improvement of loss-of-function GRIN2B-related pediatric encephalopathy.

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Autosomal dominant mutations in GRIN2B are associated with severe encephalopathy, but little is known about the pathophysiological outcomes and any potential therapeutic interventions. Genetic studies have described the association between de novo mutations of genes encoding the subunits of

Cell surface accumulation of a truncated transmembrane prion protein in Gerstmann-Straussler-Scheinker disease P102L.

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A familial prion disorder with a proline to leucine substitution at residue 102 of the prion protein (PrP(102L)) is typically associated with protease-resistant PrP fragments (PrP(Sc)) in the brain parenchyma that are infectious to recipient animals. When modeled in transgenic mice, a fatal

Contribution of the arterial blood ketone body ratio to elevate plasma amino acids in hepatic encephalopathy of surgical patients.

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To clarify the role of hepatic metabolic derangements in elevated plasma amino acid levels, the patterns of plasma amino acids in 17 surgical patients with hepatic failure were analyzed in relation to the blood ketone body ratio (acetoacetate to beta-hydroxybutyrate), which reflects the

Biochemical and clinical features of hereditary hyperprolinemia.

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There are two classifications of hereditary hyperprolinemia: type I (HPI) and type II (HPII). Each type is caused by an autosomal recessive inborn error of the proline metabolic pathway. HPI is caused by an abnormality in the proline-oxidizing enzyme (POX). HPII is caused by a deficiency of

Familial prion disease mutation alters the secondary structure of recombinant mouse prion protein: implications for the mechanism of prion formation.

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A considerable body of data supports the model that the infectious agent (called a prion) which causes the transmissible spongiform encephalopathies is a replicating polypeptide devoid of nucleic acid. Prions are believed to propagate by changing the conformation of the normal cellular prion protein

Polyanion induced fibril growth enables the development of a reproducible assay in solution for the screening of fibril interfering compounds, and the investigation of the prion nucleation site.

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The misfolded conformer of the prion protein (PrP) that aggregates into fibrils is believed to be the pathogenic agent in transmissible spongiform encephalopathies. In order to find fibril interfering compounds a screening assay in solution would be the preferred format to approximate more closely

Expression of prion protein is closely associated with pathological and clinical progression and abnormalities of p53 in head and neck squamous cell carcinomas.

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Prion protein (PrP) is a glycosyl-phosphatidylinositol (GPI)-anchored membrane protein that functions as a unique pathogenic agent in transmissible spongiform encephalopathy (TSE). In the past decade, overexpression of PrP was observed in a number of human malignant tumors, such as gastric, breast
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