Nonhuman cells correctly sort and process the human lysosomal enzyme cathepsin D
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00434a057
Reference26 articles.
1. Carboxyl-terminal proteolytic processing during biosynthesis of the lysosomal enzymes .beta.-glucuronidase and cathepsin D
2. Biosynthesis of a lysosomal enzyme. Partial structure of two transient and functionally distinct NH2-terminal sequences in cathepsin D.
3. Cloning and sequence analysis of cDNA for human cathepsin D.
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1. Similarities and differences in the biogenesis, processing and lysosomal targeting between zebrafish and human pro-Cathepsin D: Functional implications;The International Journal of Biochemistry & Cell Biology;2013-02
2. Cathepsins: Getting in Shape for Lysosomal Proteolysis;Proteases: Structure and Function;2013
3. Folding, activity and targeting of mutated human cathepsin D that cannot be processed into the double-chain form;The International Journal of Biochemistry & Cell Biology;2007
4. Comparative study of cathepsins D and S in rat IPE and RPE cells;Experimental Eye Research;2003-08
5. Novel Cathepsin D Inhibitors Block the Formation of Hyperphosphorylated Tau Fragments in Hippocampus;Journal of Neurochemistry;2002-01-18
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