(Q44373795)

English

The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre

scientific article published in April 2003

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

author name string

Götz Hofhaus

1

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Jeung-Eun Lee

2

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Ivo Tews

3

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Beate Rosenberg

4

1 reference

Europe PubMed Central

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2 December 2017

Thomas Lisowsky

5

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

language of work or name

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publication date

1 April 2003

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Europe PubMed Central

PubMed publication ID

2 December 2017

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

270

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Europe PubMed Central

PubMed publication ID

2 December 2017

7

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

1528-1535

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Roles of thiol-redox pathways in bacteria

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

Functional comparison of the yeast scERV1 and scERV2 genes.

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

WHAT IF: a molecular modeling and drug design program

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

Impact of a plastid-bearing endocytobiont on apicomplexan genomes.

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

Removal of an intron with unique 3' branch site creates an amino-terminal protein sequence directing the scERV1 gene product to mitochondria

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2003.03519.X

21 January 2018

Identifiers

10.1046/J.1432-1033.2003.03519.X

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

ResearchGate publication ID

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