The N-terminal portion of mature aldehyde dehydrogenase affects protein folding and assembly
Open Access
- 1 August 2001
- journal article
- Published by Wiley in Protein Science
- Vol. 10 (8) , 1490-1497
- https://doi.org/10.1110/ps.5301
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Human liver mitochondrial aldehyde dehydrogenase: Three‐dimensional structure and the restoration of solubility and activity of chimeric formsProtein Science, 1999
- Aminotransferase Variants as Probes for the Role of the N-terminal Region of a Mature Protein in Mitochondrial Precursor Import and ProcessingJournal of Biological Chemistry, 1998
- Conversion of a Nonprocessed Mitochondrial Precursor Protein into One That Is Processed by the Mitochondrial Processing PeptidasePublished by Elsevier ,1995
- Structural Features of the Precursor to Mitochondrial Aspartate Aminotransferase Responsible for Binding to hsp70Published by Elsevier ,1995
- Basis of unique red cell membrane properties in hereditary ovalocytosisJournal of Molecular Biology, 1992
- 2D NMR and structural model for a mitochondrial signal peptide bound to a micelleBiochemistry, 1990
- Signals guiding proteins to their correct locations in mitochondriaEuropean Journal of Biochemistry, 1987
- The amino terminus of the yeast F1-ATPase beta-subunit precursor functions as a mitochondrial import signal.The Journal of cell biology, 1986
- Mitochondrial aldehyde dehydrogenase from human liverEuropean Journal of Biochemistry, 1985
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970