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Structural effects on the phosphorylation of 3-substituted 1-β-d-ribofuranosyl-1,2,4-triazoles by human adenosine kinase

The conversion of ribavirin to the monophosphate by adenosine kinase is the rate-limiting step in activation of this broad spectrum antiviral drug. Variation of the 3-substituents in a series of bioisosteric and homologated 1-β-d-ribofuranosyl-1,2,4-triazoles has marked effects on activity with the...

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Detalles Bibliográficos
Autores principales: Kumarapperuma, Sidath C., Sun, Yanjie, Jeselnik, Marjan, Chung, Kiwon, Parker, William B., Jonsson, Colleen B., Arterburn, Jeffrey B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Ltd. 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7127453/
https://www.ncbi.nlm.nih.gov/pubmed/17379518
http://dx.doi.org/10.1016/j.bmcl.2007.03.018
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author Kumarapperuma, Sidath C.
Sun, Yanjie
Jeselnik, Marjan
Chung, Kiwon
Parker, William B.
Jonsson, Colleen B.
Arterburn, Jeffrey B.
author_facet Kumarapperuma, Sidath C.
Sun, Yanjie
Jeselnik, Marjan
Chung, Kiwon
Parker, William B.
Jonsson, Colleen B.
Arterburn, Jeffrey B.
author_sort Kumarapperuma, Sidath C.
collection PubMed
description The conversion of ribavirin to the monophosphate by adenosine kinase is the rate-limiting step in activation of this broad spectrum antiviral drug. Variation of the 3-substituents in a series of bioisosteric and homologated 1-β-d-ribofuranosyl-1,2,4-triazoles has marked effects on activity with the human adenosine kinase, and analysis of computational descriptors and binding models offers insight for the design of novel substrates.
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spelling pubmed-71274532020-04-08 Structural effects on the phosphorylation of 3-substituted 1-β-d-ribofuranosyl-1,2,4-triazoles by human adenosine kinase Kumarapperuma, Sidath C. Sun, Yanjie Jeselnik, Marjan Chung, Kiwon Parker, William B. Jonsson, Colleen B. Arterburn, Jeffrey B. Bioorg Med Chem Lett Article The conversion of ribavirin to the monophosphate by adenosine kinase is the rate-limiting step in activation of this broad spectrum antiviral drug. Variation of the 3-substituents in a series of bioisosteric and homologated 1-β-d-ribofuranosyl-1,2,4-triazoles has marked effects on activity with the human adenosine kinase, and analysis of computational descriptors and binding models offers insight for the design of novel substrates. Elsevier Ltd. 2007-06-01 2007-03-12 /pmc/articles/PMC7127453/ /pubmed/17379518 http://dx.doi.org/10.1016/j.bmcl.2007.03.018 Text en Copyright © 2007 Elsevier Ltd. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Kumarapperuma, Sidath C.
Sun, Yanjie
Jeselnik, Marjan
Chung, Kiwon
Parker, William B.
Jonsson, Colleen B.
Arterburn, Jeffrey B.
Structural effects on the phosphorylation of 3-substituted 1-β-d-ribofuranosyl-1,2,4-triazoles by human adenosine kinase
title Structural effects on the phosphorylation of 3-substituted 1-β-d-ribofuranosyl-1,2,4-triazoles by human adenosine kinase
title_full Structural effects on the phosphorylation of 3-substituted 1-β-d-ribofuranosyl-1,2,4-triazoles by human adenosine kinase
title_fullStr Structural effects on the phosphorylation of 3-substituted 1-β-d-ribofuranosyl-1,2,4-triazoles by human adenosine kinase
title_full_unstemmed Structural effects on the phosphorylation of 3-substituted 1-β-d-ribofuranosyl-1,2,4-triazoles by human adenosine kinase
title_short Structural effects on the phosphorylation of 3-substituted 1-β-d-ribofuranosyl-1,2,4-triazoles by human adenosine kinase
title_sort structural effects on the phosphorylation of 3-substituted 1-β-d-ribofuranosyl-1,2,4-triazoles by human adenosine kinase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7127453/
https://www.ncbi.nlm.nih.gov/pubmed/17379518
http://dx.doi.org/10.1016/j.bmcl.2007.03.018
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