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KNI 764
Known as:
KNI-764
, KNI764
National Institutes of Health
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Related topics
Related topics
2 relations
Broader (2)
Amides
Thiazoles
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2009
2009
Small-sized human immunodeficiency virus type-1 protease inhibitors containing allophenylnorstatine to explore the S2' pocket.
K. Hidaka
,
Tooru Kimura
,
+14 authors
Y. Kiso
Journal of Medicinal Chemistry
2009
Corpus ID: 19513299
A series of HIV protease inhibitor based on the allophenylnorstatine structure with various P(2)' moieties were synthesized…
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2007
2007
Synthesis and antiviral property of allophenylnorstatine-based HIV protease inhibitors incorporating D-cysteine derivatives as P2/P3 moieties.
E. Ami
,
Koichiro Nakahara
,
+7 authors
Y. Kiso
Bioorganic & Medicinal Chemistry Letters
2007
Corpus ID: 10953587
2006
2006
Optimization and Computational Evaluation of a Series of Potential Active Site Inhibitors of the V82F/I84V Drug‐resistant Mutant of HIV‐1 Protease: an Application of the Relaxed Complex Method of…
A. Perryman
,
Jung-Hsin Lin
,
J. Andrew McCammon
Chemical Biology and Drug Design
2006
Corpus ID: 20645049
The Relaxed Complex method, an approach to structure‐based drug design that incorporates the flexibilities of both the ligand and…
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2004
2004
Structure-activity and structure-metabolism relationships of HIV protease inhibitors containing the 3-hydroxy-2-methylbenzoyl-allophenylnorstatine structure.
T. Mimoto
,
K. Terashima
,
+5 authors
H. Hayashi
Bioorganic & Medicinal Chemistry
2004
Corpus ID: 44535278
Highly Cited
2004
Highly Cited
2004
A structural and thermodynamic escape mechanism from a drug resistant mutation of the HIV‐1 protease
S. Vega
,
L. Kang
,
A. Velázquez‐Campoy
,
Y. Kiso
,
L. Amzel
,
E. Freire
Proteins: Structure, Function, and Bioinformatics
2004
Corpus ID: 9439475
The efficacy of HIV‐1 protease inhibition therapies is often compromised by the appearance of mutations in the protease molecule…
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Highly Cited
2002
Highly Cited
2002
Overcoming drug resistance in HIV‐1 chemotherapy: The binding thermodynamics of Amprenavir and TMC‐126 to wild‐type and drug‐resistant mutants of the HIV‐1 protease
Hiroyasu Ohtaka
,
A. Velázquez‐Campoy
,
D. Xie
,
E. Freire
Protein Science
2002
Corpus ID: 20913948
Amprenavir is one of six protease inhibitors presently approved for clinical use in the therapeutic treatment of AIDS…
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Highly Cited
2002
Highly Cited
2002
Amplification of the effects of drug resistance mutations by background polymorphisms in HIV-1 protease from African subtypes.
A. Velázquez‐Campoy
,
S. Vega
,
E. Freire
Biochemistry
2002
Corpus ID: 39885753
The vast majority of HIV-1 infections worldwide are caused by the C and A viral subtypes rather than the B subtype prevalent in…
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Highly Cited
2001
Highly Cited
2001
The binding energetics of first- and second-generation HIV-1 protease inhibitors: implications for drug design.
A. Velázquez‐Campoy
,
Y. Kiso
,
E. Freire
Archives of Biochemistry and Biophysics
2001
Corpus ID: 41707983
KNI-764 is a powerful HIV-1 protease inhibitor with a reported low susceptibility to the effects of protease mutations commonly…
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