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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

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3 relations

Broader (3)

Anti-HIV AgentsHIV Protease InhibitorsOligopeptides

Papers overview

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Highly Cited
2012
Highly Cited
2012
Placevent: An algorithm for prediction of explicit solvent atom distribution - Application to HIV-1 protease and F-ATP synthase
We have created a simple algorithm for automatically predicting the explicit solvent atom distribution of biomolecules. 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
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2000
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
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1999
1999
Thermodynamic linkage between the binding of protons and inhibitors to HIV-1 protease.
The aspartyl dyad of free HIV-1 protease has apparent pK(a)s of approximately 3 and approximately 6, but recent NMR studies… Expand
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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
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1996
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
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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
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1995
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
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1994
1994
Protein binding of human immunodeficiency virus protease inhibitor KNI-272 and alteration of its in vitro antiretroviral activity in the presence of high concentrations of proteins.
KNI-272 represents a peptide-based protease inhibitor having potent antiretroviral activity against human immunodeficiency virus… Expand
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1992
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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