An activity-dependent proximity ligation platform for spatially resolved quantification of active enzymes in single cells

The interrogation of enzyme activity involves the ensemble averaging of many cells, loss of spatial relationships and is often biased to abundant proteins. Here the authors develop activity-dependent proximity ligation to quantify enzyme activity at the cellular and sub-cellular level in relevant bi...

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Autores principales: Gang Li, Jeffrey E. Montgomery, Mark A. Eckert, Jae Won Chang, Samantha M. Tienda, Ernst Lengyel, Raymond E. Moellering
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/4e4b7627eb0e4daf97d1194c3f8abb64
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spelling oai:doaj.org-article:4e4b7627eb0e4daf97d1194c3f8abb642021-12-02T17:06:10ZAn activity-dependent proximity ligation platform for spatially resolved quantification of active enzymes in single cells10.1038/s41467-017-01854-02041-1723https://doaj.org/article/4e4b7627eb0e4daf97d1194c3f8abb642017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01854-0https://doaj.org/toc/2041-1723The interrogation of enzyme activity involves the ensemble averaging of many cells, loss of spatial relationships and is often biased to abundant proteins. Here the authors develop activity-dependent proximity ligation to quantify enzyme activity at the cellular and sub-cellular level in relevant biological contexts.Gang LiJeffrey E. MontgomeryMark A. EckertJae Won ChangSamantha M. TiendaErnst LengyelRaymond E. MoelleringNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Gang Li
Jeffrey E. Montgomery
Mark A. Eckert
Jae Won Chang
Samantha M. Tienda
Ernst Lengyel
Raymond E. Moellering
An activity-dependent proximity ligation platform for spatially resolved quantification of active enzymes in single cells
description The interrogation of enzyme activity involves the ensemble averaging of many cells, loss of spatial relationships and is often biased to abundant proteins. Here the authors develop activity-dependent proximity ligation to quantify enzyme activity at the cellular and sub-cellular level in relevant biological contexts.
format article
author Gang Li
Jeffrey E. Montgomery
Mark A. Eckert
Jae Won Chang
Samantha M. Tienda
Ernst Lengyel
Raymond E. Moellering
author_facet Gang Li
Jeffrey E. Montgomery
Mark A. Eckert
Jae Won Chang
Samantha M. Tienda
Ernst Lengyel
Raymond E. Moellering
author_sort Gang Li
title An activity-dependent proximity ligation platform for spatially resolved quantification of active enzymes in single cells
title_short An activity-dependent proximity ligation platform for spatially resolved quantification of active enzymes in single cells
title_full An activity-dependent proximity ligation platform for spatially resolved quantification of active enzymes in single cells
title_fullStr An activity-dependent proximity ligation platform for spatially resolved quantification of active enzymes in single cells
title_full_unstemmed An activity-dependent proximity ligation platform for spatially resolved quantification of active enzymes in single cells
title_sort activity-dependent proximity ligation platform for spatially resolved quantification of active enzymes in single cells
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/4e4b7627eb0e4daf97d1194c3f8abb64
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