β1,4-N-Acetylgalactosaminyltransferase (GM2 Synthase) Is Released from Golgi Membranes as a Neuraminidase-sensitive, Disulfide-bonded Dimer by a Cathepsin D-like Protease

This publication has 40 references indexed in Scilit:

• Porcine Submaxillary Mucin Forms Disulfide-bonded Dimers between Its Carboxyl-terminal Domains
  Journal of Biological Chemistry, 1996
• Substrate Specificity of β1,4-N-Acetylgalactosaminyltransferase in Vitro and in cDNA-transfected Cells
  Journal of Biological Chemistry, 1995
• Retention of p63 in an ER-Golgi intermediate compartment depends on the presence of all three of its domains and on its ability to form oligomers.
  The Journal of cell biology, 1994
• Isolation of a matrix that binds medial Golgi enzymes
  The Journal of cell biology, 1994
• Kin recognition
  FEBS Letters, 1993
• Mechanisms of membrane protein turnover
  Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1990
• Cloning of cDNA encoding the membrane‐bound form of bovine β1,4‐galactosyltransferase
  European Journal of Biochemistry, 1989
• Identification of the full-length coding sequence for human galactosyltransferase (β-N-acetylglucosaminide: β1,4-galactosyltransferase)
  Biochemical and Biophysical Research Communications, 1988
• Two integral membrane proteins located in the cis-middle and trans-part of the Golgi system acquire sialylated N-linked carbohydrates and display different turnovers and sensitivity to cAMP-dependent phosphorylation.
  The Journal of cell biology, 1987
• Reconstitution of the transport of protein between successive compartments of the golgi measured by the coupled incorporation of N-acetylglucosamine
  Cell, 1984