Real-time surface plasmon resonance monitoring of site-specific phosphorylation of p53 protein and its interaction with MDM2 protein-Reference-Cited by-同舟云学术

Real-time surface plasmon resonance monitoring of site-specific phosphorylation of p53 protein and its interaction with MDM2 protein

Published:2019 Issue:20 Volume:144 Page:6033-6040
ISSN:0003-2654
Container-title:The Analyst
language:en
Short-container-title:Analyst

Author:

Wu Ling¹²³⁴,He Yuhan¹²³⁴,Hu Yuqing¹²³⁴,Lu Hanwen¹²³⁴,Cao Zhong⁵⁶⁷³⁸^ORCID,Yi Xinyao¹²³⁴,Wang Jianxiu¹²³⁴⁹^ORCID

Affiliation:

1. College of Chemistry and Chemical Engineering

2. Central South University

3. Changsha

4. P. R. China 410083

5. Hunan Provincial Key Laboratory of Materials Protection for Electric Power and Transportation

6. School of Chemistry and Biological Engineering

7. Changsha University of Science and Technology

8. P. R. China 410114

9. Key Laboratory of Hunan Province for Water Environment and Agriculture Product Safety

Abstract

Real-time monitoring of site-specific phosphorylation of p53 protein and its binding to MDM2 is conducted using dual-channel surface plasmon resonance (SPR).

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Electrochemistry,Spectroscopy,Environmental Chemistry,Biochemistry,Analytical Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/AN/C9AN01121H

Reference60 articles.

1. The cellular response to p53: the decision between life and death

2. Inhibiting the p53–MDM2 interaction: an important target for cancer therapy

3. In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2

4. Extended String Binding Mode of the Phosphorylated Transactivation Domain of Tumor Suppressor p53

5. Multiplexed Quantitation of Protein Expression and Phosphorylation Based on Functionalized Soluble Nanopolymers

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