Thermodynamic dissection of the binding energetics of KNI-272, a potent HIV-1 protease inhibitor (Q28344884)

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I Luque

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M J Todd

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M Milutinovich

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Y Kiso

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E Freire

Small dipeptide-based HIV protease inhibitors containing the hydroxymethylcarbonyl isostere as an ideal transition-state mimic

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language of work or name

English

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publication date

September 2000

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published in

Protein Science

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volume

9

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issue

9

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page(s)

1801-9

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cites work

1 reference

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Structure-activity relationship of small-sized HIV protease inhibitors containing allophenylnorstatine

20 March 2017

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Counteracting HIV-1 protease drug resistance: structural analysis of mutant proteases complexed with XV638 and SD146, cyclic urea amides with broad specificities

20 March 2017

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Human immunodeficiency virus protease ligand specificity conferred by residues outside of the active site cavity

20 March 2017

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

20 March 2017

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Selection and analysis of human immunodeficiency virus type 1 variants with increased resistance to ABT-538, a novel protease inhibitor

20 March 2017

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JE-2147: a dipeptide protease inhibitor (PI) that potently inhibits multi-PI-resistant HIV-1.

20 March 2017

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Thermodynamic linkage between the binding of protons and inhibitors to HIV-1 protease

29 September 2017

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Structure-based prediction of binding affinities and molecular design of peptide ligands.

29 September 2017

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Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy.

29 September 2017

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Design and synthesis of substrate-based peptidomimetic human immunodeficiency virus protease inhibitors containing the hydroxymethylcarbonyl isostere

29 September 2017

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Study of strong to ultratight protein interactions using differential scanning calorimetry

29 September 2017

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Thermodynamics of structural stability and cooperative folding behavior in proteins

29 September 2017

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Molecular basis of resistance to HIV-1 protease inhibition: a plausible hypothesis.

29 September 2017

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The enthalpy change in protein folding and binding: refinement of parameters for structure-based calculations.

2 June 2018

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Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry

2 June 2018

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Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure

2 June 2018

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HIV-1 protease inhibitors: enthalpic versus entropic optimization of the binding affinity.

2 June 2018

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The effect of inhibitor binding on the structural stability and cooperativity of the HIV-1 protease.

27 November 2018

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Resistance to HIV protease inhibitors: a comparison of enzyme inhibition and antiviral potency.

27 November 2018

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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.

27 November 2018

1 reference

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Estimation of changes in side chain configurational entropy in binding and folding: general methods and application to helix formation.

27 November 2018

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Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin

27 November 2018

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12 December 2020

The heat capacity of proteins

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12 December 2020

The magnitude of the backbone conformational entropy change in protein folding

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12 December 2020

Structure-based thermodynamic scale of alpha-helix propensities in amino acids

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12 December 2020

The structural stability of the HIV-1 protease

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12 December 2020

Identifiers

DOI

10.1110/PS.9.9.1801

1 reference

release_uebzdjtbtzd3jj7z6myknitidq

5025936

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/uebzdjtbtzd3jj7z6myknitidq

24 November 2022

mapped directly with Wikidata item

5025936

1 reference

1 reference

1 reference