Regular ArticleEffect of PCCB Gene Mutations on the Heteromeric and Homomeric Assembly of Propionyl-CoA Carboxylase
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Cited by (20)
Protein profiles in zebrafish (Danio rerio) brains exposed to chronic microcystin-LR
2010, ChemosphereCitation Excerpt :Recent studies suggest that complex I is a potent source of ROS (Murphy, 2009), and the decrease of NDUFA10 abundance might decrease energy production from the respiratory chain, however, concomitantly releasing the brain from oxidative attack via decreasing ROS production. Propionyl-CoA carboxylase is involved in the catabolism of essential amino acids, odd-chain fatty acids, and side chains of cholesterol (Muro et al., 2001). 3-oxoacid CoA transferase transfers the CoA residue from succinyl-CoA to acetoacetate to form acetoacetyl-CoA as a mitochondrial energy source (Tildon and Sevdalian, 1972).
Cardiomyopathies in Propionic Aciduria are Reversible After Liver Transplantation
2010, Journal of PediatricsCitation Excerpt :Finally, the enzymatic activity in fibroblasts does not appear to be a determining factor for the development of cardiomyopathy because several patients of group 2 had severe activity impairment. This is in contrast to earlier reports suggesting some genotype-phenotype correlation, with patients carrying null mutations showing severe clinical presentation.19,21,22 In the series described by Perez-Cerda et al, cardiomyopathy appeared in 13.5% of cases (5/37), including a late-onset form with residual PCC activity and only 1 case with no activity, supporting our observations.
Characterization of four variant forms of human propionyl-CoA carboxylase expressed in Escherichia coli
2005, Journal of Biological ChemistryCitation Excerpt :Co-expression of human polypeptides with bacterial chaperone proteins has been shown to correct the misfolding of some mutant forms of phenylalanine hydroxylase (46). Misfolded proteins are typically destined for proteolytic degradation (20). Missense mutations not situated in the active site or cofactor binding site may have an effect on protein stability by producing nonfunctional conformations that lead to degradation or aggregation (44).
Towards a model to explain the intragenic complementation in the heteromultimeric protein propionyl-CoA carboxylase
2005, Biochimica et Biophysica Acta - Molecular Basis of DiseasePropionic acidemia: Mutation update and functional and structural effects of the variant alleles
2004, Molecular Genetics and MetabolismFunctional analysis of PCCB mutations causing propionic acidemia based on expression studies in deficient human skin fibroblasts
2003, Biochimica et Biophysica Acta - Molecular Basis of Disease
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To whom correspondence should be addressed at Dpto. Biologı́a Molecular, Centro de Biologı́a Molecular “Severo Ochoa,” CSIC-UAM, Universidad Autónoma de Madrid, Campus de Cantoblanco, 28049 Madrid, Spain. Fax: 341-7347797. E-mail: [email protected].