(Q27732560)

1

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T N Bhat

2

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S Gulnik

3

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B Liu

4

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I A Topol

5

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Y Kiso

6

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T Mimoto

7

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H Mitsuya

8

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J W Erickson

The HIV-1 protease as a therapeutic target for AIDS

9

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publication date

15 June 1995

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published in

Structure

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volume

3

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page(s)

581-90

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issue

6

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cites work

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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

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KNI-102, a novel tripeptide HIV protease inhibitor containing allophenylnorstatine as a transition-state mimic

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Kynostatin (KNI)-227 and -272, highly potent anti-HIV agents: conformationally constrained tripeptide inhibitors of HIV protease containing allophenylnorstatine

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Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors

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Crystal structure of a complex of HIV‐1 protease with a dihydroxyethylene‐containing inhibitor: Comparisons with molecular modeling

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Crystal structure of a tethered dimer of HIV-1 proteinase complexed with an inhibitor

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Discovery of a novel class of potent HIV-1 protease inhibitors containing the (R)-(hydroxyethyl)urea isostere

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Bound water molecules and conformational stabilization help mediate an antigen-antibody association

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