Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry

There is growing evidence that the kinetics of interactions between inhibitors and their targets can strongly impact therapeutic efficacy. Here the authors describe an isothermal titration calorimetry-based method that can rapidly quantify inhibition kinetics and measure sub-nM binding affinities.

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Autores principales:	Justin M. Di Trani, Stephane De Cesco, Rebecca O’Leary, Jessica Plescia, Claudia Jorge do Nascimento, Nicolas Moitessier, Anthony K. Mittermaier
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/695ef23f7e8d4d87a44cc9ad450d7ebc
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spelling	oai:doaj.org-article:695ef23f7e8d4d87a44cc9ad450d7ebc2021-12-02T17:32:31ZRapid measurement of inhibitor binding kinetics by isothermal titration calorimetry10.1038/s41467-018-03263-32041-1723https://doaj.org/article/695ef23f7e8d4d87a44cc9ad450d7ebc2018-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03263-3https://doaj.org/toc/2041-1723There is growing evidence that the kinetics of interactions between inhibitors and their targets can strongly impact therapeutic efficacy. Here the authors describe an isothermal titration calorimetry-based method that can rapidly quantify inhibition kinetics and measure sub-nM binding affinities.Justin M. Di TraniStephane De CescoRebecca O’LearyJessica PlesciaClaudia Jorge do NascimentoNicolas MoitessierAnthony K. MittermaierNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-7 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Justin M. Di Trani Stephane De Cesco Rebecca O’Leary Jessica Plescia Claudia Jorge do Nascimento Nicolas Moitessier Anthony K. Mittermaier Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry
description	There is growing evidence that the kinetics of interactions between inhibitors and their targets can strongly impact therapeutic efficacy. Here the authors describe an isothermal titration calorimetry-based method that can rapidly quantify inhibition kinetics and measure sub-nM binding affinities.
format	article
author	Justin M. Di Trani Stephane De Cesco Rebecca O’Leary Jessica Plescia Claudia Jorge do Nascimento Nicolas Moitessier Anthony K. Mittermaier
author_facet	Justin M. Di Trani Stephane De Cesco Rebecca O’Leary Jessica Plescia Claudia Jorge do Nascimento Nicolas Moitessier Anthony K. Mittermaier
author_sort	Justin M. Di Trani
title	Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry
title_short	Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry
title_full	Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry
title_fullStr	Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry
title_full_unstemmed	Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry
title_sort	rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/695ef23f7e8d4d87a44cc9ad450d7ebc
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Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry

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