huntington disease/пролин

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Decreased proline endopeptidase activity in the basal ganglia in Huntington's disease.

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Soluble proline endopeptidase (EC 3.4.21.26) activity was measured by a fluorometric assay in eight human brain areas (caudate nucleus, lateral globus pallidus, medial globus pallidus, substantia nigra-zona compacta, substantia nigra-zona reticulata, frontal cortex-Brodmann area 10, temporal

Comparison of proline endopeptidase activity in brain tissue from normal cases and cases with Alzheimer's disease, Lewy body dementia, Parkinson's disease and Huntington's disease.

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Neuronal death associated with plaque and tangle formation characteristic of Alzheimer's disease (AD) may result from an underlying defect of intracellular protein catabolism. In an attempt to identify the proteolytic enzyme types responsible for aberrant protein processing, we have composed the

The IGF-I amino-terminal tripeptide glycine-proline-glutamate (GPE) is neuroprotective to striatum in the quinolinic acid lesion animal model of Huntington's disease.

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Huntington's disease is an incurable genetic neurological disorder characterized by the relatively selective degeneration of the striatum. Lesioning of the striatum in rodents using the excitatory amino acid agonist, quinolinic acid (QA), effectively mimics the human neuropathology seen in

Autoinhibitory structure of the WW domain of HYPB/SETD2 regulates its interaction with the proline-rich region of huntingtin.

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Huntington's disease (HD) is an autosomally dominant neurodegenerative disorder caused by expansion of polyglutamine (polyQ) in the huntingtin (Htt) protein. Htt yeast two-hybrid protein B (HYPB/SETD2), a histone methyltransferase, directly interacts with Htt and is involved in HD pathology. Using

CCG polymorphisms in the huntingtin gene have no effect on the pathogenesis of patients with Huntington's disease in mainland Chinese families.

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Huntington's disease (HD) is caused by the abnormal expansion of CAG repeats in the huntingtin gene (HTT). The adjacent proline-rich region, which also has a CCG polymorphism among people of different races, may also affect the pathogenesis of HD. To study the effect of this polymorphism on patients

Sequence analysis of the CAG triplet repeats region in the Huntington disease gene (IT15) in several mammalian species.

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Huntington's disease (HD) is a progressive neurodegenerative disease linked to abnormally expanded CAG repeats in the first exon of the IT15 gene. Neither HD or other glutamine expansion triplet disease has not yet been described in other species as human. In this study, we sequenced the region

Differential hydrophobicity drives self-assembly in Huntington's disease.

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Identifying the driving forces and the mechanism of association of huntingtin-exon1, a close marker for the progress of Huntington's disease, is an important prerequisite to finding potential drug targets and, ultimately, a cure. We introduce here a modeling framework based on a key analogy of the

Novel nuclear shuttle proteins, HDBP1 and HDBP2, bind to neuronal cell-specific cis-regulatory element in the promoter for the human Huntington's disease gene.

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Huntington's disease (HD) is a neurodegenerative disease caused by a CAG repeat expansion in exon 1 of the HD gene, and the expression level of either normal or mutant huntingtin is implicated in the pathogenesis of HD. However, a molecular base of the HD gene transcription has not been elucidated

Decreased plasma alanine and isoleucine in Huntington's disease.

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Amino acid concentrations in plasma of patients with Huntington's disease (HD) were determined in 16 patients and 21 age- and sex-matched healthy controls. Alanine and isoleucine were significantly decreased in HD plasma whereas arginine, histidine, leucine, lysine, ornithine, proline, serine,

Intrabodies binding the proline-rich domains of mutant huntingtin increase its turnover and reduce neurotoxicity.

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Although expanded polyglutamine (polyQ) repeats are inherently toxic, causing at least nine neurodegenerative diseases, the protein context determines which neurons are affected. The polyQ expansion that causes Huntington's disease (HD) is in the first exon (HDx-1) of huntingtin (Htt). However,

What excitotoxin kills striatal neurons in Huntington's disease? Clues from neurochemical studies.

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Amino acid analyses of both caudate nucleus and putamen obtained at autopsy from patients dying with Huntington's disease (HD), and from control subjects, showed significantly decreased mean glutamate contents in the HD patients. In addition, the mean glutamate concentration was significantly

Interaction of huntingtin fragments with brain membranes--clues to early dysfunction in Huntington's disease.

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Abstract Huntingtin is a large, multi-domain protein of unknown function in the brain. An abnormally elongated polyglutamine stretch in its N-terminus causes Huntington's disease (HD), a progressive neurodegenerative disorder. Huntingtin has been proposed to play a functional role in membrane

Mapping of the epitope of monoclonal antibody 2B4 to the proline-rich region of human Huntingtin, a region critical for aggregation and toxicity.

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Huntington's disease is a neurodegenerative disease caused by a polyglutamine (polyQ) expansion in Huntingtin, which provokes aggregation of a proteolytic amino-terminal fragment of the affected protein encompassing the polyQ expansion. Accumulation of mutant Huntingtin somehow triggers cellular

Inhibition of polyglutamine aggregation by SIMILAR huntingtin N-terminal sequences: Prospective molecules for preclinical evaluation in Huntington's disease.

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The mutant huntingtin protein (mHtt) fragments with expanded polyglutamine sequence forms microscopically visible aggregates in neurons, a hallmark of Huntington's disease (HD). The aggregation process and aggregates are possible targets of therapeutic intervention in HD. Owing to the lack of

Evidence of the reduced abundance of proline cis conformation in protein poly-proline tracts.

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Proline is found in a cis conformation in proteins more often than other proteinogenic amino acids, where it influences structure and modulates function, being the focus of several high-resolution structural studies. However, until now, technical and methodological limitations have hampered the

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