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Title
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3.4.23.25
Characterization of proteinase A excretion from Saccharomyces cerevisiae in high sugar stress conditions
Saccharomyces cerevisiae
3.4.23.25
Decreased proteinase A excretion by strengthening its vacuolar sorting and weakening ist constitutive secretion in Saccharomyces cerevisiae
Saccharomyces cerevisiae
3.4.23.25
Decreased proteinase A excretion by strengthening its vacuolar sorting and weakening ist constitutive secretion in Saccharomyces cerevisiae
Saccharomyces cerevisiae W303-1A
3.4.23.25
Regulating the Golgi apparatus sorting of proteinase A to decrease its excretion in Saccharomyces cerevisiae
Saccharomyces cerevisiae
3.4.23.25
Regulating the Golgi apparatus sorting of proteinase A to decrease its excretion in Saccharomyces cerevisiae
Saccharomyces cerevisiae W303-1A
3.4.23.25
Saccharomyces cerevisiae proteinase A excretion and wine making
Saccharomyces cerevisiae
3.4.23.25
An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae
Saccharomyces cerevisiae
3.4.23.25
Analysis of a processing system for proteases using yeast cell surface engineering: conversion of precursor of proteinase A to active proteinase A
Saccharomyces cerevisiae
3.4.23.25
Analysis of proteinase A function in yeast
Saccharomyces cerevisiae
3.4.23.25
Aspartic proteinase inhibitors from tomato and potato are more potent against yeast proteinase A than cathepsin D
Saccharomyces cerevisiae
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