Primary Folding of Aspartylglucosaminidase

This publication has 19 references indexed in Scilit:

• Large-scale purification and preliminary X-ray diffraction studies of human aspartylglucosaminidase
  Proteins-Structure Function and Bioinformatics, 1996
• Three-dimensional structure of human lysosomal aspartylglucosaminidase
  Nature Structural & Molecular Biology, 1995
• A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
  Nature, 1995
• Intracellular Sorting of Aspartylglucosaminidase: The Role ofN-Linked Oligosaccharides and Evidence of Man-6-P-Independent Lysosomal Targeting
  DNA and Cell Biology, 1995
• Immediate Interaction between the Nascent Subunits and Two Conserved Amino Acids Trp34 and Thr206 Are Needed for the Catalytic Activity of Aspartylglucosaminidase
  Published by Elsevier ,1995
• Dissection of the Molecular Consequences of a Double Mutation Causing a Human Lysosomal Disease
  DNA and Cell Biology, 1994
• In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation
  Genomics, 1991
• Human leucocyte aspartylglucosaminidase. Evidence for two different subunits in a more complex native structure
  Biochemical Journal, 1991
• High efficiency polyoma DNA transfection of chloroquine treated cells
  Nucleic Acids Research, 1983
• ASPARTYLGLYCOSAMINURIA
  The Lancet, 1968