Ribosomally synthesized peptides, foreground players in microbial interactions: recent developments and unanswered questions-Reference-Cited by-同舟云学术

Ribosomally synthesized peptides, foreground players in microbial interactions: recent developments and unanswered questions

Published:2022 Issue: Volume: Page:
ISSN:0265-0568
Container-title:Natural Product Reports
language:en
Short-container-title:Nat. Prod. Rep.

Author:

Rebuffat Sylvie¹^ORCID

Affiliation:

1. Laboratory Molecules of Communication and Adaptation of Microorganisms (MCAM, UMR 7245 CNRS-MNHN), National Museum of Natural History (MNHN), National Centre of Scientific Research (CNRS), CP 54, 57 rue Cuvier 75005, Paris, France

Abstract

This review unveils current knowledge on the complex interaction networks involving ribosomally synthesized peptides, either modified or not, being at play in microbial interactions and symbioses.

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Drug Discovery,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/NP/D1NP00052G

Reference280 articles.

1. Metaorganisms as the new frontier

2. Host-microbiota interactions: from holobiont theory to analysis

3. What is the hologenome concept of evolution?

4. The hologenome concept of evolution after 10 years

5. Microbiome definition re-visited: old concepts and new challenges

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