DOI: 10.1016/s0969-2126(01)00192-7. Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine

Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine

10.1016/s0969-2126(01)00192-7

Crossref journal-article

Elsevier BV

Structure (78)

Bibliography

Baldwin, E. T., Bhat, T. N., Gulnik, S., Liu, B., Topol, I. A., Kiso, Y., Mimoto, T., Mitsuya, H., & Erickson, J. W. (1995). Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine. Structure, 3(6), 581â590.

Authors 9

Eric T Baldwin (first)
T.Narayana Bhat (additional)
Sergei Gulnik (additional)
Beishan Liu (additional)
Igor A Topol (additional)
Yoshiaki Kiso (additional)
Tsutomu Mimoto (additional)
Hiroaki Mitsuya (additional)
John W Erickson (additional)

References 34 Referenced 142

10.1089/aid.1992.8.153 / AIDS Res. Hum. Retroviruses / The HIV-1 protease as a therapeutic target for AIDS by Debouck (1992)
10.1021/jm00112a001 / J. Med. Chem / HIV protease: a novel chemotherapeutic target for AIDS by Huff (1991)
10.3109/14756369209041357 / J. Enzym. Inhib / Inhibitors of HIV-1 protease by Meek (1992)
{'key': '10.1016/S0969-2126(01)00192-7_BIB4', 'first-page': '6', 'article-title': 'The complexities of AIDS: an assessment of the HIV protease as a therapeutic target', 'volume': '9', 'author': 'Tomasselli', 'year': '1991', 'journal-title': 'Chimica Oggi'} / Chimica Oggi / The complexities of AIDS: an assessment of the HIV protease as a therapeutic target by Tomasselli (1991)
10.1007/BF02171658 / Perspect. Drug Discov. Des / Design and structure of symmetry-based inhibitors of HIV-1 protease by Erickson (1993)
10.1146/annurev.bi.62.070193.002551 / Annu. Rev. Biochem / Structure-based inhibitors of HIV-1 protease by Wlodawer (1993)
10.1007/BF02171654 / Perspect. Drug Discov. Des / Crystal structures of HIV-1 protease–inhibitor complexes by Appelt (1993)
10.1016/0959-440X(93)90150-J / Curr. Opin. Struct. Biol / HIV protease–ligand complexes by Fitzgerald (1993)
10.1248/cpb.39.2465 / Chem. Pharm. Bull / Rational design and synthesis of a novel class of active site-targeted HIV protease inhibitors containing a hydroxymethylcarbonyl isostere, use of phenylnorstatine or allophenylnorstatine as a transition-state mimic by Mimoto (1991)
10.1248/cpb.39.3088 / Chem. Pharm. Bull / KNI-102, a novel tripeptide HIV protease inhibitor containing allophenylnorstatine as a transition-state mimic by Mimoto (1991)
10.1248/cpb.40.2251 / Chem. Pharm. Bull / Kynostatin (KNI)-227 and -272, highly potent anti-HIV agents: conformationally-constrained tripeptide inhibitors of HIV protease containing allophenylnorstatine by Mimoto (1992)
10.1128/AAC.37.4.810 / Antimicrob. Agents Chemother / In vitro anti-human immunodeficiency virus (HIV) activities of transition state mimetic HIV protease inhibitors containing allophenylnorstatine by Kageyama (1993)
{'key': '10.1016/S0969-2126(01)00192-7_BIB13', 'series-title': 'Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications', 'first-page': 'in press', 'article-title': 'Structure of HIV-1 protease with KNI-272: a transition state mimetic inhibitor containing allophenylnorstatine', 'author': 'Baldwin', 'year': '1994'} / Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications / Structure of HIV-1 protease with KNI-272: a transition state mimetic inhibitor containing allophenylnorstatine by Baldwin (1994)
10.1126/science.8278812 / Science / Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors by Lam (1994)
10.1002/pro.5560010811 / Protein Sci / Crystal structure of a complex of HIV-1 protease with a dihydroxyethylene-containing inhibitor: comparisons with molecular modeling by Thanki (1992)
10.1021/ja00082a004 / J. Am. Chem. Soc / Influence of stereochemistry on activity and binding modes for C2 symmetric-based diol inhibitors of HIV-1 protease by Hosur (1994)
10.1021/ja00094a085 / J. Am. Chem. Soc / Novel series of achiral, low molecular weight, and potent HIV-1 protease inhibitors by Prasad (1994)
10.1038/nsb0894-552 / Nat. Struct. Biol / Crystal structure of a tethered dimer of HIV-1 by Bhat (1994)
10.1021/jm00054a014 / J. Med. Chem / Discovery of a novel class of potent HIV-1 protease inhibitors containing the (R)-(hydroxyethyl)urea isostere by Getman (1993)
10.1038/368469a0 / Nature / Determinants of repressor/operator recognition from the structure of the trp operator binding site by Shakked (1994)
10.1073/pnas.91.3.1089 / Proc. Natl. Acad. Sci. USA / Bound water molecules and conformational stabilization help mediate an antigen–antibody association by Bhat (1994)
10.1021/jm00107a049 / J. Med. Chem / Effect of hydroxyl group configuration in hydroxyethylamine dipeptide isosteres on HIV protease inhibition. Evidence for multiple binding modes by Rich (1991)
10.1021/jm00115a028 / J. Med. Chem / Novel binding mode of highly potent HIV-proteinase inhibitors incorporating the (R)-hydroxyethylamine isostere by Krohn (1991)
10.1002/jcc.540141206 / J. Comput. Chem / Conformational analysis of HIV protease inhibitors. I. Rotation of the amide group adjacent to the P1′ decahydroisoquinoline ring system in Ro-31-8959 and related systems by Murcko (1993)
10.1073/pnas.87.22.8805 / Proc. Natl. Acad. Sci. USA / X-ray crystallographic structure of a complex between a synthetic protease of human immunodeficiency virus 1 and a substrate-based hydroxyethylamine inhibitor by Swain (1990)
10.1128/JVI.68.1.233-239.1994 / J. Virol / Generation and characterization of a human immunodeficiency virus type 1 (HIV-1) mutant resistant to an HIV-1 protease inhibitor by El-Farrash (1994)
10.1038/nsb0395-244 / Nat. Struct. Biol / Structural basis of drug resistance for the V82A mutant of HIV-1 protease: backbone flexibility and subsite repacking by Baldwin (1995)
10.1128/JVI.68.3.2016-2020.1994 / J. Virol / Characterization of human immunodeficiency virus type 1 variants with increased resistance to a C2-symmetric protease inhibitor by Ho (1994)
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{'key': '10.1016/S0969-2126(01)00192-7_BIB32', 'series-title': 'Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications', 'first-page': 'in press', 'article-title': 'A quantum mechanical model of the hydration and acidity of the active site in aspartic proteases', 'author': 'Topol', 'year': '1994'} / Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications / A quantum mechanical model of the hydration and acidity of the active site in aspartic proteases by Topol (1994)
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Dates

Type	When
Created	21 years, 1 month ago (July 23, 2004, 3:10 p.m.)
Deposited	5 years, 4 months ago (April 2, 2020, 5:07 p.m.)
Indexed	1 month, 2 weeks ago (July 8, 2025, 10:07 a.m.)
Issued	30 years, 2 months ago (June 1, 1995)
Published	30 years, 2 months ago (June 1, 1995)
Published Print	30 years, 2 months ago (June 1, 1995)

Funders 0

None

BibTeX

@article{Baldwin_1995, title={Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine}, volume={3}, ISSN={0969-2126}, url={http://dx.doi.org/10.1016/s0969-2126(01)00192-7}, DOI={10.1016/s0969-2126(01)00192-7}, number={6}, journal={Structure}, publisher={Elsevier BV}, author={Baldwin, Eric T and Bhat, T.Narayana and Gulnik, Sergei and Liu, Beishan and Topol, Igor A and Kiso, Yoshiaki and Mimoto, Tsutomu and Mitsuya, Hiroaki and Erickson, John W}, year={1995}, month=jun, pages={581–590} }

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