Neutrophil Elastase Cleaves PML-RARα and Is Important for the Development of Acute Promyelocytic Leukemia in Mice

This publication has 39 references indexed in Scilit:

• Recurring chromosomal abnormalities in leukemia in PML-RARA transgenic mice identify cooperating events and genetic pathways to acute promyelocytic leukemia
  Blood, 2003
• The cleavage product ΔPML–RARα contributes to all-trans retinoic acid-mediated differentiation in acute promyelocytic leukemia cells
  Oncogene, 2003
• Proteolytic Cleavage of MLL Generates a Complex of N- and C-Terminal Fragments That Confers Protein Stability and Subnuclear Localization
  Molecular and Cellular Biology, 2003
• Leukemia proto-oncoprotein MLL is proteolytically processed into 2 fragments with opposite transcriptional properties
  Blood, 2002
• Human acute myeloid leukemia is organized as a hierarchy that originates from a primitive hematopoietic cell
  Nature Medicine, 1997
• Localization of Granzyme B in the Nucleus
  Published by Elsevier ,1996
• Analysis of the Growth and Transformation Suppressor Domains of Promyelocytic Leukemia Gene, PML
  Journal of Biological Chemistry, 1996
• Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases.
  The Journal of cell biology, 1995
• Human leukocyte and porcine pancreatic elastase: x-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors
  Biochemistry, 1989
• 12-o-Tetradecanoyl-phorbol-13-acetate-differentiated U937 cells express a macrophage-like profile of neutral proteinases. High levels of secreted collagenase and collagenase inhibitor accompany low levels of intracellular elastase and cathepsin G.
  Journal of Clinical Investigation, 1986