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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…
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National Institutes of Health
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Related topics
Related topics
3 relations
Broader (3)
Anti-HIV Agents
HIV Protease Inhibitors
Oligopeptides
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
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*
H. Gatanaga
,
Yasuhiro Suzuki
,
+8 authors
H. Mitsuya
Journal of Biological Chemistry
2002
Corpus ID: 44684513
Amino acid substitutions in human immunodeficiency virus type 1 (HIV-1) Gag cleavage sites have been identified in HIV-1 isolated…
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Highly Cited
2000
Highly Cited
2000
Thermodynamic dissection of the binding energetics of KNI‐272, a potent HIV‐1 protease inhibitor
A. Velázquez‐Campoy
,
I. Luque
,
M. Todd
,
Mark Milutinovich
,
Y. Kiso
,
E. Freire
Protein Science
2000
Corpus ID: 23273317
KNI‐272 is a powerful HIV‐1 protease inhibitor with a reported inhibition constant in the picomolar range. In this paper, a…
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Highly Cited
1999
Highly Cited
1999
JE-2147: a dipeptide protease inhibitor (PI) that potently inhibits multi-PI-resistant HIV-1.
K. Yoshimura
,
R. Kato
,
+11 authors
H. Mitsuya
Proceedings of the National Academy of Sciences…
1999
Corpus ID: 19449573
We designed, synthesized, and identified JE-2147, an allophenylnorstatine-containing dipeptide HIV protease inhibitor (PI), which…
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Highly Cited
1999
Highly Cited
1999
Thermodynamic linkage between the binding of protons and inhibitors to HIV‐1 protease
J. Trylska
,
J. Antosiewicz
,
+4 authors
M. Gilson
Protein Science
1999
Corpus ID: 40660891
The aspartyl dyad of free HIV‐1 protease has apparent pKas of ∼3 and ∼6, but recent NMR studies indicate that the aspartyl dyad…
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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.
C. Perno
,
F. M. Newcomb
,
+4 authors
R. Yarchoan
Journal of Infectious Diseases
1998
Corpus ID: 26009521
The activity of three human immunodeficiency virus (HIV) protease inhibitors was investigated in human primary monocytes…
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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.
Y. Wang
,
D. Freedberg
,
+5 authors
D. Torchia
Biochemistry
1996
Corpus ID: 25269503
In order to improve the design of HIV-1 protease inhibitors, it is essential to understand how they interact with active site…
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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.
S. Gulnik
,
L. Suvorov
,
+4 authors
J. Erickson
Biochemistry
1995
Corpus ID: 35480324
Eleven different recombinant, drug-resistant HIV-1 protease (HIV PR) mutants--R8Q, V32I, M46I, V82A, V82F, V82I, I84V, V32I/I84V…
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Highly Cited
1995
Highly Cited
1995
Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine.
E. Baldwin
,
T. Bhat
,
+6 authors
J. Erickson
Structure
1995
Corpus ID: 6842232
Highly Cited
1993
Highly Cited
1993
In vitro anti-human immunodeficiency virus (HIV) activities of transition state mimetic HIV protease inhibitors containing allophenylnorstatine
S. Kageyama
,
T. Mimoto
,
+7 authors
H. Hayashi
Antimicrobial Agents and Chemotherapy
1993
Corpus ID: 36371031
Transition state mimetic tripeptide human immunodeficiency virus (HIV) protease inhibitors containing allophenylnorstatine [(2S…
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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.
T. Mimoto
,
J. Imai
,
+4 authors
Y. Kiso
Chemical and pharmaceutical bulletin
1992
Corpus ID: 21806919
Selective and potent HIV protease inhibitors containing allophenylnorstatine [Apns; (2S, 3S)-3-amino-2-hydroxy-4-phenylbutyric…
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