Dipeptide metalloendoprotease substrates are glucose transport inhibitors and membrane structure perturbants
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00361a031
Reference34 articles.
1. Unique cytochalasin B binding characteristics of the hepatic glucose carrier
2. Protease inhibitors implicate metalloendoprotease in synaptic transmission at the mammalian neuromuscular junction.
3. Proteolytic cleavage of influenza virus hemagglutinins: primary structure of the connecting peptide between HA1 and HA2 determines proteolytic cleavability and pathogenicity of avian influenza viruses
4. Rat myoblast fusion requires metalloendoprotease activity
5. Specific blockers of myoblast fusion inhibit a soluble and not the membrane-associated metalloendoprotease in myoblasts.
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