Thermostability profiling of MHC-bound peptides: a new dimension in immunopeptidomics and aid for immunotherapy design

Thermostability of the peptide-MHC interaction is important for immunogenicity. Here the authors present a mass spectrometry method to measure thermostability among thousands of peptide-MHC complexes in parallel and a trained artificial neural network to predict immunogenenicity of cancer antigens.

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Auteurs principaux:	Emma C. Jappe, Christian Garde, Sri H. Ramarathinam, Ethan Passantino, Patricia T. Illing, Nicole A. Mifsud, Thomas Trolle, Jens V. Kringelum, Nathan P. Croft, Anthony W. Purcell
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2020
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/5cf6ee2c88c54b69ae8a7c1723f4491d
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spelling	oai:doaj.org-article:5cf6ee2c88c54b69ae8a7c1723f4491d2021-12-02T13:27:31ZThermostability profiling of MHC-bound peptides: a new dimension in immunopeptidomics and aid for immunotherapy design10.1038/s41467-020-20166-42041-1723https://doaj.org/article/5cf6ee2c88c54b69ae8a7c1723f4491d2020-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20166-4https://doaj.org/toc/2041-1723Thermostability of the peptide-MHC interaction is important for immunogenicity. Here the authors present a mass spectrometry method to measure thermostability among thousands of peptide-MHC complexes in parallel and a trained artificial neural network to predict immunogenenicity of cancer antigens.Emma C. JappeChristian GardeSri H. RamarathinamEthan PassantinoPatricia T. IllingNicole A. MifsudThomas TrolleJens V. KringelumNathan P. CroftAnthony W. PurcellNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Emma C. Jappe Christian Garde Sri H. Ramarathinam Ethan Passantino Patricia T. Illing Nicole A. Mifsud Thomas Trolle Jens V. Kringelum Nathan P. Croft Anthony W. Purcell Thermostability profiling of MHC-bound peptides: a new dimension in immunopeptidomics and aid for immunotherapy design
description	Thermostability of the peptide-MHC interaction is important for immunogenicity. Here the authors present a mass spectrometry method to measure thermostability among thousands of peptide-MHC complexes in parallel and a trained artificial neural network to predict immunogenenicity of cancer antigens.
format	article
author	Emma C. Jappe Christian Garde Sri H. Ramarathinam Ethan Passantino Patricia T. Illing Nicole A. Mifsud Thomas Trolle Jens V. Kringelum Nathan P. Croft Anthony W. Purcell
author_facet	Emma C. Jappe Christian Garde Sri H. Ramarathinam Ethan Passantino Patricia T. Illing Nicole A. Mifsud Thomas Trolle Jens V. Kringelum Nathan P. Croft Anthony W. Purcell
author_sort	Emma C. Jappe
title	Thermostability profiling of MHC-bound peptides: a new dimension in immunopeptidomics and aid for immunotherapy design
title_short	Thermostability profiling of MHC-bound peptides: a new dimension in immunopeptidomics and aid for immunotherapy design
title_full	Thermostability profiling of MHC-bound peptides: a new dimension in immunopeptidomics and aid for immunotherapy design
title_fullStr	Thermostability profiling of MHC-bound peptides: a new dimension in immunopeptidomics and aid for immunotherapy design
title_full_unstemmed	Thermostability profiling of MHC-bound peptides: a new dimension in immunopeptidomics and aid for immunotherapy design
title_sort	thermostability profiling of mhc-bound peptides: a new dimension in immunopeptidomics and aid for immunotherapy design
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/5cf6ee2c88c54b69ae8a7c1723f4491d
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Thermostability profiling of MHC-bound peptides: a new dimension in immunopeptidomics and aid for immunotherapy design

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