(Q44738569)

English

A major peroxiredoxin-induced activation of Yap1 transcription factor is mediated by reduction-sensitive disulfide bonds and reveals a low level of transcriptional activation

scientific article

In more languages

default for all languages

No label defined

No description defined

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

A major peroxiredoxin-induced activation of Yap1 transcription factor is mediated by reduction-sensitive disulfide bonds and reveals a low level of transcriptional activation (English)

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

author name string

Tsuyoshi Tachibana

1

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

Shoko Okazaki

2

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

Asako Murayama

3

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

Akira Naganuma

4

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

Akio Nomoto

5

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

Shusuke Kuge

6

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

language of work or name

0 references

publication date

22 December 2008

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

284

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

7

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

4464-4472

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

Cell signaling. H2O2, a necessary evil for cell signaling

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Superoxide dismutase 1 (SOD1) is essential for H2O2-mediated oxidation and inactivation of phosphatases in growth factor signaling

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Activation of the OxyR transcription factor by reversible disulfide bond formation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

OxyR: a molecular code for redox-related signaling

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Structure, mechanism and regulation of peroxiredoxins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

GPX2, encoding a phospholipid hydroperoxide glutathione peroxidase homologue, codes for an atypical 2-Cys peroxiredoxin in Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Gpx1 is a stationary phase-specific thioredoxin peroxidase in fission yeast

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Oxidation of a eukaryotic 2-Cys peroxiredoxin is a molecular switch controlling the transcriptional response to increasing levels of hydrogen peroxide

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Crm1p mediates regulated nuclear export of a yeast AP-1-like transcription factor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

The redox domain of the Yap1p transcription factor contains two disulfide bonds

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

H2O2 sensing through oxidation of the Yap1 transcription factor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Thioredoxin deficiency causes the constitutive activation of Yap1, an AP-1-like transcription factor in Saccharomyces cerevisiae.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Regulation of yAP-1 nuclear localization in response to oxidative stress

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

The Skn7 response regulator controls gene expression in the oxidative stress response of the budding yeast Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Peroxiredoxin-mediated redox regulation of the nuclear localization of Yap1, a transcription factor in budding yeast

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Global analysis of protein expression in yeast

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Activation of the redox sensor Pap1 by hydrogen peroxide requires modulation of the intracellular oxidant concentration

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

A 2-Cys peroxiredoxin regulates peroxide-induced oxidation and activation of a stress-activated MAP kinase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Structural basis for redox regulation of Yap1 transcription factor localization

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M807583200

21 January 2018

Identifiers

10.1074/JBC.M807583200

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q44738569&oldid=2035638977"