Abnormal glycosylation of procathepsin l due to n-terminal point mutations correlates with failure to sort to lysosomes*

HIGHLIGHTS

• who: Richard L. Chapman from the (UNIVERSITY) have published the Article: Abnormal Glycosylation of Procathepsin L Due to N-terminal Point Mutations Correlates with Failure to Sort to Lysosomes*, in the Journal: (JOURNAL) of June/24,/1996
• what: Roles of the LIS Residues-This study has produced four single LIS mutants (H36A, R38A, Y40A, and Y40F) of mouse procatL that undergo cotranslational misfolding, substantial glycosylation at Asn268, and subsequent secretion.
• how: Before this structure became available the authors explored the physiological function of this mannose 6-phosphate-independent membrane as- H36A R37A R38A . . .
  

   

  

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