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Inhibitors of HIV‐1 Protease by Using In Situ Click Chemistry
Author(s) -
Whiting Matthew,
Muldoon John,
Lin YingChuan,
Silverman Steven M.,
Lindstrom William,
Olson Arthur J.,
Kolb Hartmuth C.,
Finn M. G.,
Sharpless K. Barry,
Elder John H.,
Fokin Valery V.
Publication year - 2006
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200502161
Subject(s) - click chemistry , protease , human immunodeficiency virus (hiv) , in situ , chemistry , triazole , linkage (software) , azide , alkyne , protease inhibitor (pharmacology) , combinatorial chemistry , biochemistry , stereochemistry , virology , organic chemistry , enzyme , antiretroviral therapy , biology , catalysis , gene , viral load
Twice poor equals potent : HIV‐1 Protease assembles its own potent inhibitor through formation of the triazole linkage from azide‐ and alkyne‐containing fragments that are themselves poor binders.