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kynostatin 272

Known as: 4-Thiazolidinecarboxamide, N-(1,1-dimethylethyl)-3- [2-hydroxy-3-[[2-[[(5-isoquinolinyloxy)acetyl]amino]-3- (methylthio)-1-oxopropyl]amino]-1-oxo-4-phenylbutyl]-,[4R-[3[2S*, 3S*(R*)],4R*]], KNI-272, kynostatin-272 
A synthetic peptide-based antiviral agent. As a peptidomimetic substrate containing an unnatural amino acid, allophenylnorstatine, KNI-272… Expand
National Institutes of Health

Related topics

Related topics

3 relations

Broader (3)

Anti-HIV AgentsHIV Protease InhibitorsOligopeptides

Papers overview

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Highly Cited
2009
Highly Cited
2009
Structure of HIV-1 protease in complex with potent inhibitor KNI-272 determined by high-resolution X-ray and neutron crystallography
HIV-1 protease is a dimeric aspartic protease that plays an essential role in viral replication. To further understand the… Expand
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Highly Cited
2002
Highly Cited
2002
Amino Acid Substitutions in Gag Protein at Non-cleavage Sites Are Indispensable for the Development of a High Multitude of HIV-1 Resistance against Protease Inhibitors*
Amino acid substitutions in human immunodeficiency virus type 1 (HIV-1) Gag cleavage sites have been identified in HIV-1 isolated… Expand
Highly Cited
2000
Highly Cited
2000
Thermodynamic dissection of the binding energetics of KNI‐272, a potent HIV‐1 protease inhibitor
KNI‐272 is a powerful HIV‐1 protease inhibitor with a reported inhibition constant in the picomolar range. In this paper, a… Expand
Highly Cited
1999
Highly Cited
1999
JE-2147: a dipeptide protease inhibitor (PI) that potently inhibits multi-PI-resistant HIV-1.
We designed, synthesized, and identified JE-2147, an allophenylnorstatine-containing dipeptide HIV protease inhibitor (PI), which… Expand
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Highly Cited
1999
Highly Cited
1999
Thermodynamic linkage between the binding of protons and inhibitors to HIV‐1 protease
The aspartyl dyad of free HIV‐1 protease has apparent pKas of ∼3 and ∼6, but recent NMR studies indicate that the aspartyl dyad… Expand
Highly Cited
1998
Highly Cited
1998
Relative potency of protease inhibitors in monocytes/macrophages acutely and chronically infected with human immunodeficiency virus.
The activity of three human immunodeficiency virus (HIV) protease inhibitors was investigated in human primary monocytes… Expand
Highly Cited
1996
Highly Cited
1996
Solution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272.
In order to improve the design of HIV-1 protease inhibitors, it is essential to understand how they interact with active site… Expand
Highly Cited
1995
Highly Cited
1995
Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure.
Eleven different recombinant, drug-resistant HIV-1 protease (HIV PR) mutants--R8Q, V32I, M46I, V82A, V82F, V82I, I84V, V32I/I84V… Expand
Highly Cited
1995
Highly Cited
1995
Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine.
BACKGROUND HIV-1 protease (HIV PR), an aspartic protease, cleaves Phe-Pro bonds in the Gag and Gag-Pol viral polyproteins… Expand
Highly Cited
1992
Highly Cited
1992
Kynostatin (KNI)-227 and -272, highly potent anti-HIV agents: conformationally constrained tripeptide inhibitors of HIV protease containing allophenylnorstatine.
Selective and potent HIV protease inhibitors containing allophenylnorstatine [Apns; (2S, 3S)-3-amino-2-hydroxy-4-phenylbutyric… Expand
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