Synthetic Transit Peptides Inhibit Import and Processing of Mitochondrial Precursor Proteins
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference30 articles.
1. Import of proteins into mitochondria. Partial purification of a matrix-located protease involved in cleavage of mitochondrial precursor polypeptides.
2. Phosphodiester bond cleavage outside mitochondria is required for the completion of protein import into the mitochondrial matrix
3. The role of arginine residues in the rat mitochondrial malate dehydrogenase transit peptide.
4. Mutation of a neutral amino acid in the transit peptide of rat mitochondrial malate dehydrogenase abolishes binding and import.
5. Structural identity between the NH2-terminal domain of the rat and human ornithine carbamyltransferase “targeting” sequences.
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1. A TAT–Frataxin fusion protein increases lifespan and cardiac function in a conditional Friedreich's ataxia mouse model;Human Molecular Genetics;2011-11-23
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3. Studies on Protein Processing for Membrane-Bound Spinach Leaf Mitochondrial Processing Peptidase Integrated into the Cytochrome bc1, Complex and the Soluble Rat Liver Matrix Mitochondrial Processing Peptidase;European Journal of Biochemistry;1996-11-15
4. Protein Import into Subsarcolemmal and Intermyofibrillar Skeletal Muscle Mitochondria;Journal of Biological Chemistry;1996-11
5. Proteolytic Processing of Mitochondrial Precursor Proteins;Protein Targeting to Mitochondria;1996
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