Optimization of fluorescently labeled Nrf2 peptide probes and the development of a fluorescence polarization assay for the discovery of inhibitors of Keap1-Nrf2 interaction. (Q35842879)

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scientific article published on 7 December 2011

Language	Label	Description	Also known as
English	Optimization of fluorescently labeled Nrf2 peptide probes and the development of a fluorescence polarization assay for the discovery of inhibitors of Keap1-Nrf2 interaction.	scientific article published on 7 December 2011

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scholarly article

1 reference

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18 January 2020

Optimization of fluorescently labeled Nrf2 peptide probes and the development of a fluorescence polarization assay for the discovery of inhibitors of Keap1-Nrf2 interaction (English)

1 reference

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18 January 2020

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18 January 2020

Ah-Ng Tony Kong

5

object named as

Ah-Ng Tony Kong

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18 January 2020

author name string

Daigo Inoyama

1

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18 January 2020

Yu Chen

2

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18 January 2020

Xinyi Huang

3

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18 January 2020

Lesa J Beamer

4

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18 January 2020

publication date

7 December 2011

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18 January 2020

Journal of Biomolecular Screening

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18 January 2020

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18 January 2020

435-447

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18 January 2020

4

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18 January 2020

Kinetic analyses of Keap1-Nrf2 interaction and determination of the minimal Nrf2 peptide sequence required for Keap1 binding using surface plasmon resonance

1 reference

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Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1

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Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2

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Crystallization and initial crystallographic analysis of the Kelch domain from human Keap1

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Evolutionary conserved N-terminal domain of Nrf2 is essential for the Keap1-mediated degradation of the protein by proteasome

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Nrf2-Keap1 defines a physiologically important stress response mechanism

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Crystal structure of the Kelch domain of human Keap1

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12 December 2020

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12 December 2020

based on heuristic

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Identifiers

10.1177/1087057111430124

1 reference

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18 January 2020

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18 January 2020

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18 January 2020

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