Polar Recognition Group Study of Keap1-Nrf2 Protein-Protein Interaction Inhibitors

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Polar Recognition Group Study of Keap1-Nrf2 Protein-Protein Interaction Inhibitors

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

@zh-sg

2016年學術文章

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2016年學術文章

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2016年學術文章

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Polar Recognition Group Study of Keap1-Nrf2 Protein-Protein Interaction Inhibitors

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label

Polar Recognition Group Study of Keap1-Nrf2 Protein-Protein Interaction Inhibitors

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prefLabel

Polar Recognition Group Study of Keap1-Nrf2 Protein-Protein Interaction Inhibitors

@en

P1476

Polar Recognition Group Study of Keap1-Nrf2 Protein-Protein Interaction Inhibitors

@en

P2093

Jian-Ai Ji

http://www.w3.org/2001/XMLSchema#string

Meng-Chen Lu

http://www.w3.org/2001/XMLSchema#string

Qi-Dong You

http://www.w3.org/2001/XMLSchema#string

Shi-Jie Tan

http://www.w3.org/2001/XMLSchema#string

Zhen-Wei Yuan

http://www.w3.org/2001/XMLSchema#string

Zhi-Yun Chen

http://www.w3.org/2001/XMLSchema#string

P2860

Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex.

Small molecules inhibit the interaction of Nrf2 and the Keap1 Kelch domain through a non-covalent mechanism

Binding mode and structure-activity relationships around direct inhibitors of the Nrf2-Keap1 complex

Monoacidic Inhibitors of the Kelch-like ECH-Associated Protein 1: Nuclear Factor Erythroid 2-Related Factor 2 (KEAP1:NRF2) Protein-Protein Interaction with High Cell Potency Identified by Fragment-Based Discovery

Small molecule modulators of Keap1-Nrf2-ARE pathway as potential preventive and therapeutic agents

Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model

Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway

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

Peptide inhibitors of the Keap1-Nrf2 protein-protein interaction.

Discovery of a small-molecule inhibitor and cellular probe of Keap1-Nrf2 protein-protein interaction

P304

835-840

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P31

scholarly article

P356

10.1021/ACSMEDCHEMLETT.5B00407

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Zhengyu Jiang

P577

2016-07-05T00:00:00Z

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P698

27660687

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P932

5018864

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