Degradation of Ornithine Decarboxylase in Reticulocyte Lysate Is ATP-dependent but Ubiquitin-independent

This publication has 18 references indexed in Scilit:

• Amino Acid Sequences Common to Rapidly Degraded Proteins: The PEST Hypothesis
  Science, 1986
• The Ubiquitin Pathway for the Degradation of Intracellular Proteins
  Progress in Nucleic Acid Research and Molecular Biology, 1986
• Isolation of cloned cDNA encoding mammalian ornithine decarboxylase.
  Proceedings of the National Academy of Sciences, 1984
• ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin.
  The Journal of cell biology, 1983
• Mechanisms of Intracellular Protein Breakdown
  Annual Review of Biochemistry, 1982
• Role for the Adenosine Triphosphate-Dependent Proteolytic Pathway in Reticulocyte Maturation
  Science, 1982
• ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation.
  Proceedings of the National Academy of Sciences, 1980
• A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes
  Biochemical and Biophysical Research Communications, 1978
• A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes.
  Proceedings of the National Academy of Sciences, 1977
• Intracellular Protein Degradation in Mammalian and Bacterial Cells: Part 2
  Annual Review of Biochemistry, 1976