Thermodynamic dissection of the binding energetics of KNI‐272, a potent HIV‐1 protease inhibitor-Reference-Cited by-同舟云学术

Thermodynamic dissection of the binding energetics of KNI‐272, a potent HIV‐1 protease inhibitor

Published:2000-01 Issue:9 Volume:9 Page:1801-1809
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Velazquez‐Campoy Adrian¹,Luque Irene¹,Todd Matthew J.¹,Milutinovich Mark¹,Kiso Yoshiaki²,Freire Ernesto¹

Affiliation:

1. Department of Biology and Biocalorimetry Center, The Johns Hopkins University, Baltimore, Maryland 21218

2. Department of Medicinal Chemistry, Center for Frontier Research in Medicinal Science, Kyoto Pharmaceutical University, Yamashina‐ku, Kyoto 607‐8412, Japan

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.9.9.1801

Reference33 articles.

1. Counteracting HIV-1 Protease Drug Resistance: Structural Analysis of Mutant Proteases Complexed with XV638 and SD146, Cyclic Urea Amides with Broad Specificities

2. Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry

3. Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine

4. Study of strong to ultratight protein interactions using differential scanning calorimetry

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