A template-based approach to inhibitors of calpain 2, 20S proteasome, and HIV-1 protease

Seth Adam Jones; Paul M Neilsen; Limei Siew; David Frederick Callen; Nathan E Goldfarb; Ben M Dunn; A D Abell

doi:10.1002/cmdc.201300387

A template-based approach to inhibitors of calpain 2, 20S proteasome, and HIV-1 protease

Seth Adam Jones, Paul M Neilsen, Limei Siew, David Frederick Callen, Nathan E Goldfarb, Ben M Dunn, A D Abell

Research output: Contribution to journal › Article › Research › peer-review

9 Citations (Scopus)

Abstract

Specificity counts: A template-based approach to protease inhibitors is presented using a core macrocycle that presents a generic ?-strand template for binding to protease active sites. This is then specifically functionalized at P2, and the C and N termini to give inhibitors of calpain 2, 20S proteasome, and HIV-1 protease.

Original language	English
Pages (from-to)	1918 - 1921
Number of pages	4
Journal	ChemMedChem
Volume	8
Issue number	12
DOIs	https://doi.org/10.1002/cmdc.201300387
Publication status	Published - 2013
Externally published	Yes

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This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1002/cmdc.201300387

Cite this

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title = "A template-based approach to inhibitors of calpain 2, 20S proteasome, and HIV-1 protease",

abstract = "Specificity counts: A template-based approach to protease inhibitors is presented using a core macrocycle that presents a generic ?-strand template for binding to protease active sites. This is then specifically functionalized at P2, and the C and N termini to give inhibitors of calpain 2, 20S proteasome, and HIV-1 protease.",

author = "Jones, {Seth Adam} and Neilsen, {Paul M} and Limei Siew and Callen, {David Frederick} and Goldfarb, {Nathan E} and Dunn, {Ben M} and Abell, {A D}",

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AU - Goldfarb, Nathan E

AU - Dunn, Ben M

AU - Abell, A D

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AB - Specificity counts: A template-based approach to protease inhibitors is presented using a core macrocycle that presents a generic ?-strand template for binding to protease active sites. This is then specifically functionalized at P2, and the C and N termini to give inhibitors of calpain 2, 20S proteasome, and HIV-1 protease.

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