Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first ArgRha specific antibody-Reference-Cited by-同舟云学术

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Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first ArgRha specific antibody

Published:2016 Issue:12 Volume:7 Page:6995-7001
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Li Xiang¹²³⁴⁵,Krafczyk Ralph⁶⁷⁸⁹¹⁰,Macošek Jakub¹¹¹²¹³⁹,Li Yu-Lei¹²³⁴⁵,Zou Yan¹²³⁴⁵,Simon Bernd¹¹¹²¹³⁹,Pan Xing¹⁴¹⁵¹⁶¹⁷⁵,Wu Qiu-Ye¹²³⁴⁵,Yan Fang²¹⁸⁵,Li Shan¹⁴¹⁵¹⁶¹⁷⁵,Hennig Janosch¹¹¹²¹³⁹^ORCID,Jung Kirsten⁶⁷⁸⁹¹⁰,Lassak Jürgen⁶⁷⁸⁹¹⁰,Hu Hong-Gang¹²³⁴⁵

Affiliation:

1. Department of Organic Chemistry

2. School of Pharmacy

3. Second Military Medical University

4. Shanghai 200433

5. China

6. Department of Biology I, Microbiology

7. Ludwig Maximilians-Universität München

8. Munich

9. Germany

10. Center for Integrated Protein Science Munich

11. Structural and Computational Biology Unit

12. EMBL Heidelberg

13. Heidelberg 69117

14. Institute of Infection and Immunity

15. Taihe Hospital

16. Hubei University of Medicine

17. Shiyan

18. Wei Fang Medical University

Abstract

Here we describe a potent tool to investigate arginine rhamnosylation and develop novel antibiotics.

Funder

Deutsche Forschungsgemeinschaft

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/SC/C6SC02889F

Reference44 articles.

1. Phosphofructokinase 1 Glycosylation Regulates Cell Growth and Metabolism

2. Futile Protein Folding Cycles in the ER Are Terminated by the Unfolded Protein O-Mannosylation Pathway

3. Glycosylation to Adapt to Stress

4. Protein Native-State Stabilization by Placing Aromatic Side Chains in N-Glycosylated Reverse Turns

5. Sweet Talk: Protein Glycosylation in Bacterial Interaction With the Host

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