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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… (More)
National Institutes of Health

Topic mentions per year

Topic mentions per year

1992-2012
0519922012

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3 relations

Broader (3)

Anti-HIV AgentsHIV Protease InhibitorsOligopeptides

Related mentions per year

Related mentions per year

1954-2018
1960198020002020
kynostatin 272
Oligopeptides
HIV Protease Inhibitors
Anti-HIV Agents

Papers overview

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2006
2006
Binding free energy contributions of interfacial waters in HIV-1 protease/inhibitor complexes.
Water molecules are commonly observed in crystal structures of protein-ligand complexes where they mediate protein-ligand binding… (More)
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2002
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… (More)
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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… (More)
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1999
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… (More)
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1998
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… (More)
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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… (More)
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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… (More)
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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… (More)
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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… (More)
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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… (More)
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