Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease (Q24563308)

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Language	Label	Description	Also known as
English	Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease	scientific article

Statements

instance of

scholarly article

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title

Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease (English)

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author name string

C Brenner

series ordinal

1

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R S Fuller

series ordinal

2

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original language of film or TV show

English

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publication date

1 February 1992

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published in

Proceedings of the National Academy of Sciences of the United States of America

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volume

89

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issue

3

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page(s)

922-6

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cites work

Structural homology between the human fur gene product and the subtilisin-like protease encoded by yeast KEX2

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PubMed Central

Human fur gene encodes a yeast KEX2-like endoprotease that cleaves pro-beta-NGF in vivo

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stated in

PubMed Central

Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor

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stated in

PubMed Central

Yeast α factor is processed from a larger precursor polypeptide: The essential role of a membrane-bound dipeptidyl aminopeptidase

1 reference

stated in

PubMed Central

Structure, biosynthesis, and localization of dipeptidyl aminopeptidase B, an integral membrane glycoprotein of the yeast vacuole

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stated in

PubMed Central

Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease

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PubMed Central

Localization of components involved in protein transport and processing through the yeast Golgi apparatus

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stated in

PubMed Central

Hormone processing and membrane-bound proteinases in yeast

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stated in

PubMed Central

Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases

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stated in

PubMed Central

Characterization of KEX2-encoded endopeptidase from yeast Saccharomyces cerevisiae

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stated in

PubMed Central

Serine Proteases: Structure and Mechanism of Catalysis

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stated in

PubMed Central

Identifiers

DOI

10.1073/PNAS.89.3.922

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PMC publication ID

48357

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PubMed publication ID

1736307

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