A substrate-driven allosteric switch that enhances PDI catalytic activity

Protein Disulfide Isomerase (PDI) is a prothrombotic, multidomain enzyme with separate substrate binding and catalytic domains. Here, the authors identify a new class of compounds that target the PDI substrate binding site, inducing a conformational change in the catalytic domains and inhibiting thr...

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Autores principales:	Roelof H. Bekendam, Pavan K. Bendapudi, Lin Lin, Partha P. Nag, Jun Pu, Daniel R. Kennedy, Alexandra Feldenzer, Joyce Chiu, Kristina M. Cook, Bruce Furie, Mingdong Huang, Philip J. Hogg, Robert Flaumenhaft
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/98add86409e74be283e23770f1a6f0cb
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spelling	oai:doaj.org-article:98add86409e74be283e23770f1a6f0cb2021-12-02T17:33:20ZA substrate-driven allosteric switch that enhances PDI catalytic activity10.1038/ncomms125792041-1723https://doaj.org/article/98add86409e74be283e23770f1a6f0cb2016-08-01T00:00:00Zhttps://doi.org/10.1038/ncomms12579https://doaj.org/toc/2041-1723Protein Disulfide Isomerase (PDI) is a prothrombotic, multidomain enzyme with separate substrate binding and catalytic domains. Here, the authors identify a new class of compounds that target the PDI substrate binding site, inducing a conformational change in the catalytic domains and inhibiting thrombosis.Roelof H. BekendamPavan K. BendapudiLin LinPartha P. NagJun PuDaniel R. KennedyAlexandra FeldenzerJoyce ChiuKristina M. CookBruce FurieMingdong HuangPhilip J. HoggRobert FlaumenhaftNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Roelof H. Bekendam Pavan K. Bendapudi Lin Lin Partha P. Nag Jun Pu Daniel R. Kennedy Alexandra Feldenzer Joyce Chiu Kristina M. Cook Bruce Furie Mingdong Huang Philip J. Hogg Robert Flaumenhaft A substrate-driven allosteric switch that enhances PDI catalytic activity
description	Protein Disulfide Isomerase (PDI) is a prothrombotic, multidomain enzyme with separate substrate binding and catalytic domains. Here, the authors identify a new class of compounds that target the PDI substrate binding site, inducing a conformational change in the catalytic domains and inhibiting thrombosis.
format	article
author	Roelof H. Bekendam Pavan K. Bendapudi Lin Lin Partha P. Nag Jun Pu Daniel R. Kennedy Alexandra Feldenzer Joyce Chiu Kristina M. Cook Bruce Furie Mingdong Huang Philip J. Hogg Robert Flaumenhaft
author_facet	Roelof H. Bekendam Pavan K. Bendapudi Lin Lin Partha P. Nag Jun Pu Daniel R. Kennedy Alexandra Feldenzer Joyce Chiu Kristina M. Cook Bruce Furie Mingdong Huang Philip J. Hogg Robert Flaumenhaft
author_sort	Roelof H. Bekendam
title	A substrate-driven allosteric switch that enhances PDI catalytic activity
title_short	A substrate-driven allosteric switch that enhances PDI catalytic activity
title_full	A substrate-driven allosteric switch that enhances PDI catalytic activity
title_fullStr	A substrate-driven allosteric switch that enhances PDI catalytic activity
title_full_unstemmed	A substrate-driven allosteric switch that enhances PDI catalytic activity
title_sort	substrate-driven allosteric switch that enhances pdi catalytic activity
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/98add86409e74be283e23770f1a6f0cb
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A substrate-driven allosteric switch that enhances PDI catalytic activity

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