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Characterization of the yeast KEX1 gene product: a carboxypeptidase involved in processing secreted precursor proteins
scientific article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
2668738
retrieved
1 December 2016
title
Characterization of the yeast KEX1 gene product: a carboxypeptidase involved in processing secreted precursor proteins
(English)
1 reference
stated in
PubMed
PubMed ID
2668738
retrieved
1 December 2016
main subject
Serine-type carboxypeptidase YGL203C
1 reference
stated in
GOA release 2020-03-11
author name string
H Bussey
series ordinal
2
0 references
A Cooper
series ordinal
1
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language of work or name
English
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publication date
June 1989
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published in
Molecular and Cellular Biology
1 reference
stated in
PubMed
PubMed ID
2668738
retrieved
1 December 2016
volume
9
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page(s)
2706-14
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issue
6
0 references
cites work
Physiological characterization of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and alpha factor pheromones
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Order of events in the yeast secretory pathway
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Yeast α factor is processed from a larger precursor polypeptide: The essential role of a membrane-bound dipeptidyl aminopeptidase
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Saccharomyces cerevisiae contains two discrete genes coding for the alpha-factor pheromone
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Expression of cDNA encoding the human "protective protein" associated with lysosomal beta-galactosidase and neuraminidase: homology to yeast proteases
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A membrane glycoprotein, Sec12p, required for protein transport from the endoplasmic reticulum to the Golgi apparatus in yeast
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One-step gene disruption in yeast
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Hormone processing and membrane-bound proteinases in yeast
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Carboxypeptidase E
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Evidence for an essential histidine in carboxypeptidase Y. Reaction with the chloromethyl ketone derivative of benzyloxycarbonyl-L-phenylalanine
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Polyprotein gene expression: generation of diversity of neuroendocrine peptides
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Secretion of Saccharomyces cerevisiae Killer Toxin: Processing of the Glycosylated Precursor
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[12] One-step gene disruption in yeast
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Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus
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Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and alpha-factor precursor processing.
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Enzymes required for yeast prohormone processing
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Proteases and the processing of precursors to secreted proteins in yeast
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29 September 2017
Prohormone processing and the secretory pathway
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Sorting of soluble ER proteins in yeast
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Neuropeptides: multiple molecular forms, metabolic pathways, and receptors
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Two chromosomal genes required for killing expression in killer strains of Saccharomyces cerevisiae
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Structure of a yeast pheromone gene (MF alpha): a putative alpha-factor precursor contains four tandem copies of mature alpha-factor.
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Protein sorting by selective retention in the endoplasmic reticulum and Golgi stack
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Hormone (pheromone) processing enzymes in yeast. The carboxy-terminal processing enzyme of the mating pheromone alpha-factor, carboxypeptidase ysc alpha, is absent in alpha-factor maturation-defective kex1 mutant cells
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/2668738
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Glycosylation and processing of prepro-alpha-factor through the yeast secretory pathway
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/2668738
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Synthesis of human insulin gene VIII. Construction of expression vectors for fused proinsulin production in Escherichia coli
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/2668738
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Radiometric assay for carboxypeptidase H (EC 3.4.17.10) and other carboxypeptidase B-like enzymes
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/2668738
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Direct evidence for the presence of histidine in the active center of chymotrypsin
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/2668738
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/MCB.9.6.2706
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PMCID
362343
0 references
PubMed ID
2668738
1 reference
stated in
PubMed
PubMed ID
2668738
retrieved
1 December 2016
ResearchGate publication ID
20486970
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