| scholarly article | Q13442814 |
| P2093 | author name string | J W Erickson | |
| S K Burt | |||
| I A Topol | |||
| S W Rick | |||
| P2860 | cites work | Novel binding mode of highly potent HIV-proteinase inhibitors incorporating the (R)-hydroxyethylamine isostere | Q27656274 |
| Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease | Q27696384 | ||
| Crystal structure at 1.9-A resolution of human immunodeficiency virus (HIV) II protease complexed with L-735,524, an orally bioavailable inhibitor of the HIV proteases | Q27730719 | ||
| Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences | Q27732090 | ||
| Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine | Q27732560 | ||
| In vitro selection and characterization of human immunodeficiency virus type 1 (HIV-1) isolates with reduced sensitivity to hydroxyethylamino sulfonamide inhibitors of HIV-1 aspartyl protease | Q28367941 | ||
| L-735,524: an orally bioavailable human immunodeficiency virus type 1 protease inhibitor | Q28369664 | ||
| Impaired fitness of human immunodeficiency virus type 1 variants with high-level resistance to protease inhibitors | Q28379411 | ||
| Solvent-accessible surfaces of proteins and nucleic acids | Q29614464 | ||
| In vivo emergence of HIV-1 variants resistant to multiple protease inhibitors | Q29620622 | ||
| Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size | Q36278258 | ||
| Relative differences in the binding free energies of human immunodeficiency virus 1 protease inhibitors: a thermodynamic cycle-perturbation approach | Q37623814 | ||
| Free energy via molecular simulation: applications to chemical and biomolecular systems | Q38648060 | ||
| Structural and genetic analysis of protein stability | Q40835248 | ||
| Structure-based inhibitors of HIV-1 protease | Q40835286 | ||
| Angströms and calories | Q41441731 | ||
| A short-term study of the safety, pharmacokinetics, and efficacy of ritonavir, an inhibitor of HIV-1 protease. European-Australian Collaborative Ritonavir Study Group | Q42274436 | ||
| Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure | Q42277211 | ||
| Escape mutants of HIV-1 proteinase: enzymic efficiency and susceptibility to inhibition | Q42549394 | ||
| Evaluating the energetics of empty cavities and internal mutations in proteins | Q42845592 | ||
| 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. | Q43452863 | ||
| Determination of the relative binding free energies of peptide inhibitors to the HIV-1 protease | Q46133892 | ||
| Conic: a fast renderer for space-filling molecules with shadows | Q46906153 | ||
| Internal cavities and buried waters in globular proteins. | Q52638970 | ||
| Application of free energy simulations to the binding of a transition-state-analogue inhibitor to HTV protease | Q68207882 | ||
| P433 | issue | 8 | |
| P304 | page(s) | 1750-1756 | |
| P577 | publication date | 1998-08-01 | |
| P1433 | published in | Protein Science | Q7251445 |
| P1476 | title | Molecular mechanisms of resistance: free energy calculations of mutation effects on inhibitor binding to HIV-1 protease | |
| P478 | volume | 7 |
| Q51609848 | Analysis of HIV protease binding pockets based on 3D shape and electrostatic potential descriptors. |
| Q37319797 | Conformational selection and adaptation to ligand binding in T4 lysozyme cavity mutants |
| Q46121038 | Drug-resistant molecular mechanism of CRF01_AE HIV-1 protease due to V82F mutation |
| Q44238646 | Effect of atomic charge, solvation, entropy, and ligand protonation state on MM-PB(GB)SA binding energies of HIV protease. |
| Q56394569 | Simulation of protein association: Kinetic pathways towards crystal contacts |
| Q57991346 | Theoretical study of the amino acid interactions in the binding region of the trypsin–pancreatic trypsin inhibitor complex |
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