Exploring structural signatures of the lanthipeptide prochlorosin 2.8 using tandem mass spectrometry and trapped ion mobility-mass spectrometry-Reference-Cited by-同舟云学术

Exploring structural signatures of the lanthipeptide prochlorosin 2.8 using tandem mass spectrometry and trapped ion mobility-mass spectrometry

Published:2021-06-08 Issue:19 Volume:413 Page:4815-4824
ISSN:1618-2642
Container-title:Analytical and Bioanalytical Chemistry
language:en
Short-container-title:Anal Bioanal Chem

Author:

Jeanne Dit Fouque Kevin^ORCID,Hegemann Julian D.^ORCID,Santos-Fernandez Miguel,Le Tung T.,Gomez-Hernandez Mario,van der Donk Wilfred A.^ORCID,Fernandez-Lima Francisco^ORCID

Funder

Division of Chemistry

National Institute of General Medical Sciences

Publisher

Springer Science and Business Media LLC

Subject

Biochemistry,Analytical Chemistry

Link

https://link.springer.com/content/pdf/10.1007/s00216-021-03437-x.pdf

Reference68 articles.

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4. Ortiz-Lopez FJ, Carretero-Molina D, Sanchez-Hidalgo M, Martin J, Gonzalez I, Roman-Hurtado F, et al. Cacaoidin, first member of the new lanthidin RiPP family. Angew Chem Int Ed. 2020;59(31):12654–8.

5. Xu M, Zhang F, Cheng Z, Bashiri G, Wang J, Hong J, et al. Functional genome mining reveals a class V lanthipeptide containing a d-amino acid introduced by an F420 H2 -dependent reductase. Angew Chem Int Ed. 2020;59(41):18029–35.

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