A novel robust quantitative Förster resonance energy transfer assay for protease SENP2 kinetics determination against its all natural substrates-Reference-Cited by-同舟云学术

A novel robust quantitative Förster resonance energy transfer assay for protease SENP2 kinetics determination against its all natural substrates

Published:2015 Issue:12 Volume:11 Page:3407-3414
ISSN:1742-206X
Container-title:Molecular BioSystems
language:en
Short-container-title:Mol. BioSyst.

Author:

Liu Yan¹²³⁴⁵,Shen Yali⁶⁷⁸⁹¹⁰,Zheng Shasha¹¹¹²¹³⁴⁵,Liao Jiayu¹²³⁴⁵

Affiliation:

1. Department of Bioengineering

2. Bourns College of Engineering

3. University of California, Riverside

4. Riverside

5. USA

6. Department of Radiation Oncology

7. Cancer Center

8. West China Hospital

9. Sichuan University

10. Chngdu 610041

11. Department of Health Sciences

12. College of Allied Health

13. California Baptist University

Abstract

SUMOylation (the process of adding the SUMO [small ubiquitin-like modifier] to substrates) is an important post-translational modification of critical proteins in multiple processes. The kinetics parameters of pre-SUMO1-3 by its protease SENP2 is determined by a quantitative FRET assay in real time.

Publisher

Royal Society of Chemistry (RSC)

Subject

Molecular Biology,Biotechnology

Link

http://pubs.rsc.org/en/content/articlepdf/2015/MB/C5MB00568J

Reference32 articles.

1. New approaches for dissecting protease functions to improve probe development and drug discovery

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