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May 1, 1990Journal of Biological ChemistryOpen Access

Sulfated N-linked oligosaccharides affect secretion but are not essential for the transport, proteolytic processing, and sorting of lysosomal enzymes in Dictyostelium discoideum.

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Authors

JCJames A. CardelliBiparJBJohn M. BushUniversity of Arkansas at Little RockDEDavid L. EbertThe University of Melbourne

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Cite This Study

Cardelli et al. (1990) studied this question.

synapsesocial.com/papers/6a8a882ee0083a7c2c437e73https://doi.org/10.1016/s0021-9258(19)38965-3
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Inhibition of early but not late proteolytic processing events leads to the missorting and oversecretion of precursor forms of lysosomal enzymes in Dictyostelium discoideum.1988 · 46 citations
  2. 2Lysosomal enzymes in Dictyostelium discoideum are transported to lysosomes at distinctly different rates.1986 · 49 citations
  3. 3The high mannose oligosaccharides of Dictyostelium discoideum glycoproteins contain a novel intersecting N-acetylglucosamine residue.1987 · 45 citations
  4. 4Lysosomal enzymes possess a common antigenic determinant in the cellular slime mold, Dictyostelium discoideum.1981 · 71 citations
  5. 5Identification of methylphosphomannosyl residues as components of the high mannose oligosaccharides of Dictyostelium discoideum glycoproteins.1984 · 93 citations