Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation
Open Access
- 20 October 1993
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Vol. 1182 (3) , 264-274
- https://doi.org/10.1016/0925-4439(93)90068-c
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Expression of wild-type and mutant medium-chain acyl-CoA dehydrogenase (MCAD) cDNA in eucaryotic cellsBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1992
- Protein folding and chaperoninsPlant Molecular Biology, 1992
- Protein Folding in the Cell: The Role of Molecular Chaperones Hsp70 and Hsp60Annual Review of Biophysics, 1992
- Immunochemical Characterization of Variant Medium-Chain Acyl-CoA Dehydrogenase in Fibroblasts from Patients with Medium-Chain Acyl-CoA Dehydrogenase DeficiencyPediatric Research, 1992
- Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coliHuman Genetics, 1991
- Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation.Journal of Clinical Investigation, 1990
- Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiencyBiochemical and Biophysical Research Communications, 1990
- GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coliNature, 1989
- Homologous plant and bacterial proteins chaperone oligomeric protein assemblyNature, 1988
- Biosynthesis of four rat liver mitochondrial acyl-CoA dehydrogenases: In vitro synthesis, import into mitochondria, and processing of their precursors in a cell-free system and in cultured cellsArchives of Biochemistry and Biophysics, 1987