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This study proposes low-resolution models of the MRPP1-MRPP2 and MRPP1-MRPP2-MRPP3 complexes that suggest the overall architecture, stoichiometry, and orientation of subunits and tRNA substrates.
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17beta-Hydroxysteroid dehydrogenase type 10 is a multifunctional, homotetrameric, mitochondrial protein encoded by the HSD17B10 gene at Xp 11.2. This protein, 17beta-HSD10, is overexpressed in brain cells of Alzheimer's disease (AD) patients. Analysis of the impact of 17beta-HSD10 and its inhibitor, amyloid-beta peptide (Abeta), on the metabolism of neuroactive steroids offers a new approach to AD pathogenesis.
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Authors report two patients with novel missense mutations in the HSD17B10 gene (c.34G>C and c.526G>A), resulting in the p.V12L and p.V176M substitutions. Val12 and Val176 are highly conserved residues located at different regions of the MRPP2 structure.
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in addition to being an essential component of the RNase P reaction, MRPP1/2 serves as a processing platform for several down-stream tRNA maturation steps in human mitochondria.
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The S-nitrosation of a cysteine residue distal to the 3-hydroxyacyl-CoA dehydrogenase type 2 (HADH2) active site impaired catalytic activity.
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A computational study and enzyme inhibition assay with full length human 17-beta-HSD10 identifies risperidone as enzyme inhibitor and possible antineoplastic agent.
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Data suggest that HSD10 plays a role in alterations of energy metabolism by regulating mtDNA content in colorectal carcinomas.
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upon exposure to E2, ERalpha rapidly localizes to mitochondria, in which it interacts with HSD17B10 to modulate the expression of mitochondrial RNA transcripts.
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Our findings demonstrate that overexpression of HSD10 accelerates pheochromocytoma cell growth, enhances cell respiration, and increases cellular resistance to cell death induction.
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Three HSD10 variants associated with neurodegenerative disorders are inactive with cardiolipin
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The authors demonstrate elevated amounts of unprocessed pre-tRNAs and mRNA transcripts encoding mitochondrial subunits indicating deficient RNase P activity in HSD10 disease.
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The study showed that pathogenic mutations impair SDR5C1-dependent dehydrogenation, tRNA processing and methylation.
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loss of HSD10 causes impaired mitochondrial precursor transcript processing which may explain mitochondrial dysfunction observed in HSD10 disease
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Defects in this gene are a cause of 17beta-hydroxysteroid dehydrogenase type 10 (HSD10) deficiency. The encoded protein does not exhibit generalized alcohol dehydrogenase activity as was previously thought.
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Significantly higher levels of SRD5A1, AKR1C2, AKR1C3, and HSD17B10 mRNA were however found in bone metastases than in non-malignant and/or malignant prostate tissue
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Inhibition of mitochondrial RNase P by beta-amyloid is an unspecific effect and is not mediated by beta-amyloid interaction with SDR5C1.
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Two major HSD17B10 transcription start sites were identified by primer extension at -37 and -6 as well as a minor start site at -12 nucleotides from the initiation codon ATG.
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A 5-methylcytosine is present in both active and inactive X chromosomes at + 2259 nucleotide from the initiation ATG of the HSD17B10 gene, explaining the prevalence of the p.R130C mutation among HSD10 deficiency patients.
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analysis of clinical consequences of mutations in the HSD17B10 gene
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The role of ABAD in amyloid beta toxicity, was investigated.
