General rules of fragmentation evidencing lasso structures in CID and ETD-Reference-Cited by-同舟云学术

General rules of fragmentation evidencing lasso structures in CID and ETD

Published:2018 Issue:5 Volume:143 Page:1157-1170
ISSN:0003-2654
Container-title:The Analyst
language:en
Short-container-title:Analyst

Author:

Jeanne Dit Fouque K.¹²³⁴⁵^ORCID,Lavanant H.¹²³⁴⁵^ORCID,Zirah S.⁶⁷⁸⁹¹⁰^ORCID,Hegemann J. D.¹¹¹²¹³¹⁴¹⁵^ORCID,Fage C. D.¹²¹⁶¹⁷¹⁸¹⁹^ORCID,Marahiel M. A.¹²¹⁶¹⁷¹⁸¹⁹^ORCID,Rebuffat S.⁶⁷⁸⁹¹⁰^ORCID,Afonso C.¹²³⁴⁵^ORCID

Affiliation:

1. Normandie Univ

2. UNIROUEN

3. INSA Rouen

4. CNRS

5. COBRA

6. Muséum National d'Histoire Naturelle

7. Sorbonne Universités

8. Centre national de la Recherche scientifique

9. Laboratoire Molécules de Communication et Adaptation des Microorganismes

10. UMR 7245 CNRS-MNHN

11. Roger Adams Laboratory

12. Department of Chemistry

13. University of Illinois at Urbana–Champaign

14. Urbana

15. USA

16. Biochemistry; LOEWE Center for Synthetic Microbiology

17. Philipps-University Marburg

18. Marburg

19. Germany

Abstract

Lasso peptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) characterized by a mechanically interlocked structure in which the C-terminal tail of the peptide is threaded and trapped within an N-terminal macrolactam ring.

Funder

European Regional Development Fund

Conseil Régional de Haute Normandie

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

Electrochemistry,Spectroscopy,Environmental Chemistry,Biochemistry,Analytical Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2018/AN/C7AN02052J

Reference79 articles.

1. Y. Li , S.Zirah and S.Rebuffat , Lasso Peptides: Bacterial Strategies to Make and Maintain Bioactive Entangled Scaffolds , Springer , New York , 2015

2. Lasso peptides: structure, function, biosynthesis, and engineering

3. Microcin J25, from the Macrocyclic to the Lasso Structure: Implications for Biosynthetic, Evolutionary and Biotechnological Perspectives

4. Sungsanpin, a Lasso Peptide from a Deep-Sea Streptomycete

5. The glucagon receptor antagonist BI-32169 constitutes a new class of lasso peptides

Cited by 26 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The pearl jubilee of microcin J25: thirty years of research on an exceptional lasso peptide;Natural Product Reports;2024

2. Cloacaenodin, an Antimicrobial Lasso Peptide with Activity against Enterobacter;ACS Infectious Diseases;2022-12-15

3. Trapped Ion Mobility Spectrometry, Ultraviolet Photodissociation, and Time-of-Flight Mass Spectrometry for Gas-Phase Peptide Isobars/Isomers/Conformers Discrimination;Journal of the American Society for Mass Spectrometry;2022-06-06

4. Discovery and Characterization of Rubrinodin Provide Clues into the Evolution of Lasso Peptides;Biochemistry;2022-03-17

5. Spatially Resolved Neuropeptide Characterization from Neuropathological Formalin-Fixed, Paraffin-Embedded Tissue Sections by a Combination of Imaging MALDI FT-ICR Mass Spectrometry Histochemistry and Liquid Extraction Surface Analysis-Trapped Ion Mobility Spectrometry-Tandem Mass Spectrometry;Journal of the American Society for Mass Spectrometry;2022-03-08