human immunodeficiency virus type 1 protease
mutant T31S, V32I, L33V, E34A, E35G, M36I, S37E
mutant T31S, L33V, E34T, E35G, M36I, S37E
mutant Q7K, L33I, L63I, C67A, L90M, C95A
Activated dynamics of flap opening in HIV-1 protease.
Molecular dynamics of HIV-1 protease in complex with a difluoroketone-containing inhibitor: implications for the catalytic mechanism.
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 69-167.
X-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes.
3D-STRUCTURE MODELING OF PROTEASE DOMAIN.
Molecular modeling of the HIV-1 protease and its substrate binding site.
Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0-A resolution.
Domain communication in the dynamical structure of human immunodeficiency virus 1 protease.
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 69-167.
Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor complexed to HIV-1 protease.
The three-dimensional x-ray crystal structure of HIV-1 protease complexed with a hydroxyethylene inhibitor.
Human immunodeficiency virus-1 protease. 2. Use of pH rate studies and solvent kinetic isotope effects to elucidate details of chemical mechanism.
Structure at 2.5-A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor.
Kinetic studies of human immunodeficiency virus type 1 protease and its active-site hydrogen bond mutant A28S.
Novel binding mode of highly potent HIV-proteinase inhibitors incorporating the (R)-hydroxyethylamine isostere.
The crystal structures at 2.2-A resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations.
Crystal structure of a complex of HIV-1 protease with a dihydroxyethylene-containing inhibitor: comparisons with molecular modeling.
Structure-based inhibitors of HIV-1 protease.
Inhibition of human immunodeficiency virus-1 protease by a C2-symmetric phosphinate. Synthesis and crystallographic analysis.
An orally bioavailable HIV-1 protease inhibitor containing an imidazole-derived peptide bond replacement: crystallographic and pharmacokinetic analysis.
X-ray crystallographic studies of a series of penicillin-derived asymmetric inhibitors of HIV-1 protease.
Influence of stereochemistry on activity and binding modes for C2 symmetry-based diol inhibitors of HIV-1 protease.
Rational design, synthesis, and crystallographic analysis of a hydroxyethylene-based HIV-1 protease inhibitor containing a heterocyclic P1'--P2' amide bond isostere.
Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors.
X-ray structure of a tethered dimer for HIV-1 protease.
Molecular recognition of the inhibitor AG-1343 by HIV-1 protease: conformationally flexible docking by evolutionary programming.
Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme.
Three-dimensional structure of a mutant HIV-1 protease displaying cross-resistance to all protease inhibitors in clinical trials.
A check on rational drug design: crystal structure of a complex of human immunodeficiency virus type 1 protease with a novel gamma-turn mimetic inhibitor.
Flexibility and function in HIV-1 protease.
Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine.
Comparative analysis of the X-ray structures of HIV-1 and HIV-2 proteases in complex with CGP 53820, a novel pseudosymmetric inhibitor.
Regulation of HIV-1 protease activity through cysteine modification.
Crystal structures of complexes of a peptidic inhibitor with wild-type and two mutant HIV-1 proteases.
Human immunodeficiency virus protease ligand specificity conferred by residues outside of the active site cavity.
Three-dimensional structures of HIV-1 and SIV protease product complexes.
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.
Improved cyclic urea inhibitors of the HIV-1 protease: synthesis, potency, resistance profile, human pharmacokinetics and X-ray crystal structure of DMP 450.
Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration.
Cyclic HIV protease inhibitors: synthesis, conformational analysis, P2/P2' structure-activity relationship, and molecular recognition of cyclic ureas.
Preparation and structure-activity relationship of novel P1/P1'-substituted cyclic urea-based human immunodeficiency virus type-1 protease inhibitors.
Inhibition and catalytic mechanism of HIV-1 aspartic protease.
Ionization states of the catalytic residues in HIV-1 protease.
Empirical free energy calculations of human immunodeficiency virus type 1 protease crystallographic complexes. II. Knowledge-based ligand-protein interaction potentials applied to thermodynamic analysis of hydrophobic mutations.
Molecular mechanics calculations on HIV-1 protease with peptide substrates correlate with experimental data.
Structural Analysis of the Native and Drug-Resistant HIV-1 Proteinases Complexed with an Aminodiol Inhibitor.
Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy.
Molecular basis of HIV-1 protease drug resistance: structural analysis of mutant proteases complexed with cyclic urea inhibitors.
Structure of HOE/BAY 793 complexed to human immunodeficiency virus (HIV-1) protease in two different crystal forms--structure/function relationship and influence of crystal packing.
Conformational selectivity of HIV-1 protease cleavage of X-Pro peptide bonds and its implications.
Unexpected binding mode of a cyclic sulfamide HIV-1 protease inhibitor.
Cyclic urea amides: HIV-1 protease inhibitors with low nanomolar potency against both wild type and protease inhibitor resistant mutants of HIV.
An orally bioavailable pyrrolinone inhibitor of HIV-1 protease: computational analysis and X-ray crystal structure of the enzyme complex.
Analysis of the structure of chemically synthesized HIV-1 protease complexed with a hexapeptide inhibitor. Part I: Crystallographic refinement of 2 A data.
Rapid X-ray diffraction analysis of HIV-1 protease-inhibitor complexes: inhibitor exchange in single crystals of the bound enzyme.
X-ray crystallographic studies of the structure-function relationships of HIV-1 protease.
Counteracting HIV-1 protease drug resistance: structural analysis of mutant proteases complexed with XV638 and SD146, cyclic urea amides with broad specificities.
Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease.
Structural role of the 30's loop in determining the ligand specificity of the human immunodeficiency virus protease.
Functional characterization of the protease of human endogenous retrovirus, K10: can it complement HIV-1 protease?
A quantitative structure-activity relationship study on some sulfolanes and arylthiomethanes acting as HIV-1 protease inhibitors.
Structural studies of HIV-1 protease-inhibiting antibodies.
Molecular recognition of cyclic urea HIV-1 protease inhibitors.
Nonpeptide cyclic cyanoguanidines as HIV-1 protease inhibitors: synthesis, structure-activity relationships, and X-ray crystal structure studies.
Active-site mobility in human immunodeficiency virus, type 1, protease as demonstrated by crystal structure of A28S mutant.
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 57-155.
Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV.
Reaction path and free energy calculations of the transition between alternate conformations of HIV-1 protease.
Structural and kinetic analysis of drug resistant mutants of HIV-1 protease.
Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.
Synthesis, stability, antiviral activity, and protease-bound structures of substrate-mimicking constrained macrocyclic inhibitors of HIV-1 protease.
Structural studies of FIV and HIV-1 proteases complexed with an efficient inhibitor of FIV protease.
Determining the 3D structure of HIV-1 protease.
NMR identification of local structural preferences in HIV-1 protease tethered heterodimer in 6 M guanidine hydrochloride.
Synthesis and comparative molecular field analysis (CoMFA) of symmetric and nonsymmetric cyclic sulfamide HIV-1 protease inhibitors.
Structural implications of drug-resistant mutants of HIV-1 protease: high-resolution crystal structures of the mutant protease/substrate analogue complexes.
1.9 A x-ray study shows closed flap conformation in crystals of tethered HIV-1 PR.
Structural basis of HIV-1 and HIV-2 protease inhibition by a monoclonal antibody.
Effects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR investigations.
Reboud-Ravaux M. Metal-organic compounds: a new approach for drug discovery
N1-(4-methyl-2-pyridyl)-2,3,6-trimethoxybenzamide copper(II) complex as an inhibitor of human immunodeficiency virus 1 protease.
HIV-1 protease: characterization of a catalytically competent enzyme-substrate intermediate.
Molecular dynamics simulations of the first steps of the reaction catalyzed by HIV-1 protease.
Hydroxyethylamine isostere of an HIV-1 protease inhibitor prefers its amine to the hydroxy group in binding to catalytic aspartates. A synchrotron study of HIV-1 protease in complex with a peptidomimetic inhibitor.
Role of conformational fluctuations in the enzymatic reaction of HIV-1 protease.
Relation between sequence and structure of HIV-1 protease inhibitor complexes: a model system for the analysis of protein flexibility.
A potent human immunodeficiency virus type 1 protease inhibitor, UIC-94003 (TMC-126), and selection of a novel (A28S) mutation in the protease active site.
Lack of synergy for inhibitors targeting a multi-drug-resistant HIV-1 protease.
Drug resistance in HIV-1 protease: Flexibility-assisted mechanism of compensatory mutations.
Combining mutations in HIV-1 protease to understand mechanisms of resistance.
Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes.
A major role for a set of non-active site mutations in the development of HIV-1 protease drug resistance.
Molecular dynamics study of the connection between flap closing and binding of fullerene-based inhibitors of the HIV-1 protease.
Improved prediction of HIV-1 protease-inhibitor binding energies by molecular dynamics simulations.
NMR elucidation of early folding hierarchy in HIV-1 protease.
Solution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursor.
Cooperative fluctuations of unliganded and substrate-bound HIV-1 protease: a structure-based analysis on a variety of conformations from crystallography and molecular dynamics simulations.
Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 3. The free energy contribution of structural water molecules in HIV-1 protease complexes.
The folding and dimerization of HIV-1 protease: evidence for a stable monomer from simulations.
High resolution crystal structures of HIV-1 protease with a potent non-peptide inhibitor (UIC-94017) active against multi-drug-resistant clinical strains.
Crystal structures of a multidrug-resistant human immunodeficiency virus type 1 protease reveal an expanded active-site cavity.
Inhibitor design by wrapping packing defects in HIV-1 proteins.
HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs.
The role of hydrogen bonding in the enzymatic reaction catalyzed by HIV-1 protease.
The protein, POL polyprotein from HIV-1, is composed of the following enzymes, protease (E.C. 3.4.23.16), reverse transcriptase (E.C. 2.7.7.49), ribonuclease H (E.C. 3.1.26.4) and integrase. This entry corresponds to the protease domain, which belongs to the peptidase family-A2. According to the literature, this enzyme has got a similar catalytic mechanism to that of pepsin (D00436 in EzCatDB).