An isoform of protein disulfide isomerase isolated from chronic myelogenous leukemia cells alters complex formation between nuclear proteins and regulatory regions of interferon-inducible genes.

This publication has 38 references indexed in Scilit:

• A metabolite of halothane covalently binds to an endoplasmic reticulum protein that is highly homologous to phosphatidylinositol-specific phospholipase C-α but has no activity
  Biochemical and Biophysical Research Communications, 1991
• A Genetic Tool Used to Identify Thioredoxin as a Mediator of a Growth Inhibitory Signal
  Science, 1991
• A phosphatase activity present in peripheral blood myeloid cells of chronic myelogenous leukemia patients but not normal individuals alters nuclear protein binding to transcriptional enhancers of interferon-inducible genes.
  Journal of Clinical Investigation, 1990
• In vivo and in vitro mutants of FNR the anaerobic transcriptional regulator of E.coli
  FEBS Letters, 1990
• Redox Regulation of Fos and Jun DNA-Binding Activity in Vitro
  Science, 1990
• Glucagon activation of the thiol:Protein disulfide oxidoreductase in isolated, rat, hepatic microsomes
  Life Sciences, 1986
• Hematologic Remission and Cytogenetic Improvement Induced by Recombinant Human Interferon Alpha_Ain Chronic Myelogenous Leukemia
  New England Journal of Medicine, 1986
• ROLE OF REVERSIBLE OXIDATION-REDUCTION OF ENZYME THIOLS-DISULFIDES IN METABOLIC REGULATION
  Annual Review of Biochemistry, 1985
• Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
  Proceedings of the National Academy of Sciences, 1979
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970