Binding kinetics of darunavir to human immunodeficiency virus type 1 protease explain the potent antiviral activity and high genetic barrier. - Wikidata - awgldk - TriplyDB

Binding kinetics of darunavir to human immunodeficiency virus type 1 protease explain the potent antiviral activity and high genetic barrier.

Binding kinetics of darunavir to human immunodeficiency virus type 1 protease explain the potent antiviral activity and high genetic barrier.

http://www.wikidata.org/entity/Q42910400

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Rationale and clinical utility of the darunavir-cobicistat combination in the treatment of HIV/AIDS Unique Flap Conformation in an HIV-1 Protease with High-Level Darunavir Resistance.Extreme Multidrug Resistant HIV-1 Protease with 20 Mutations Is Resistant to Novel Protease Inhibitors with P1′-Pyrrolidinone or P2-Tris-tetrahydrofuran HIV-1 Protease with 20 Mutations Exhibits Extreme Resistance to Clinical Inhibitors through Coordinated Structural Rearrangements Gag-Pol processing during HIV-1 virion maturation: a systems biology approach Structural Studies of a Rationally Selected Multi-Drug Resistant HIV-1 Protease Reveal Synergistic Effect of Distal Mutations on Flap Dynamics Teaching foundational topics and scientific skills in biochemistry within the conceptual framework of HIV protease.Understanding ligand-receptor non-covalent binding kinetics using molecular modeling.Drug interactions with new and investigational antiretrovirals.Mechanism of the Association Pathways for a Pair of Fast and Slow Binding Ligands of HIV-1 Protease.Dimerization of HIV-1 protease occurs through two steps relating to the mechanism of protease dimerization inhibition by darunavir.Aliskiren displays long-lasting interactions with human renin.In vitro selection of highly darunavir-resistant and replication-competent HIV-1 variants by using a mixture of clinical HIV-1 isolates resistant to multiple conventional protease inhibitors.Solution kinetics measurements suggest HIV-1 protease has two binding sites for darunavir and amprenavir.Virologic response to tipranavir-ritonavir or darunavir-ritonavir based regimens in antiretroviral therapy experienced HIV-1 patients: a meta-analysis and meta-regression of randomized controlled clinical trials.Conformation of inhibitor-free HIV-1 protease derived from NMR spectroscopy in a weakly oriented solution Inhibition of autoprocessing of natural variants and multidrug resistant mutant precursors of HIV-1 protease by clinical inhibitors.Loss of protease dimerization inhibition activity of darunavir is associated with the acquisition of resistance to darunavir by HIV-1.Substituted Bis-THF Protease Inhibitors with Improved Potency against Highly Resistant Mature HIV-1 Protease PR20 Mechanism of dissociative inhibition of HIV protease and its autoprocessing from a precursor.Loss of the protease dimerization inhibition activity of tipranavir (TPV) and its association with the acquisition of resistance to TPV by HIV-1.Conformational variation of an extreme drug resistant mutant of HIV protease.Switches of hydrogen bonds during ligand-protein association processes determine binding kinetics.C-5-Modified Tetrahydropyrano-Tetrahydofuran-Derived Protease Inhibitors (PIs) Exert Potent Inhibition of the Replication of HIV-1 Variants Highly Resistant to Various PIs, including Darunavir A potent HIV protease inhibitor, darunavir, does not inhibit ZMPSTE24 or lead to an accumulation of farnesyl-prelamin A in cells.Binding of Clinical Inhibitors to a Model Precursor of a Rationally Selected Multidrug Resistant HIV-1 Protease Is Significantly Weaker Than That to the Released Mature Enzyme Managing treatment-experienced pediatric and adolescent HIV patients: role of darunavir.Enhanced stability of monomer fold correlates with extreme drug resistance of HIV-1 protease.HIV-1 drug resistance mutations emerging on darunavir therapy in PI-naive and -experienced patients in the UK.HIV resistance to raltegravir Computing Clinically Relevant Binding Free Energies of HIV-1 Protease Inhibitors.Ritonavir-boosted protease inhibitors in HIV therapy.Darunavir: an effective protease inhibitor for HIV-infected patients.Role of darunavir in the management of HIV infection.Darunavir: a review of its use in the management of HIV-1 infection.Darunavir: A Review in Pediatric HIV-1 Infection.Darunavir/cobicistat for the treatment of HIV-1: a new era for compact drugs with high genetic barrier to resistance.TMC647055, a potent nonnucleoside hepatitis C virus NS5B polymerase inhibitor with cross-genotypic coverage.Conformational adaptation in drug-target interactions and residence time.Intracellular and plasma steady-state pharmacokinetics of raltegravir, darunavir, etravirine and ritonavir in heavily pre-treated HIV-infected patients.

P2860

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P2860

Binding kinetics of darunavir to human immunodeficiency virus type 1 protease explain the potent antiviral activity and high genetic barrier.

http://www.wikidata.org/entity/Q42910400

description

2007 nî lūn-bûn

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Binding kinetics of darunavir ...... vity and high genetic barrier.

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Binding kinetics of darunavir ...... vity and high genetic barrier.

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type

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Binding kinetics of darunavir ...... vity and high genetic barrier.

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Binding kinetics of darunavir ...... vity and high genetic barrier.

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Binding kinetics of darunavir ...... vity and high genetic barrier.

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Binding kinetics of darunavir ...... vity and high genetic barrier.

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Journal of Virology

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Binding kinetics of darunavir ...... vity and high genetic barrier.

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P2093

Emmanuel Gustin

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Inge Dierynck

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Inge Keuleers

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Johan Vandersmissen

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Kurt Hertogs

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Mieke De Wit

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Sabine Hallenberger

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P2860

Lack of synergy for inhibitors targeting a multi-drug-resistant HIV-1 protease

Declining morbidity and mortality among patients with advanced human immunodeficiency virus infection. HIV Outpatient Study Investigators

Affinity analysis of non-steady-state data obtained under mass transport limited conditions using BIAcore technology.

BIACORE data processing: an evaluation of the global fitting procedure.

Determination of interaction kinetic constants for HIV-1 protease inhibitors using optical biosensor technology.

Kinetic determinations of molecular interactions using Biacore--minimum data requirements for efficient experimental design.

Kinetic and thermodynamic characterization of HIV-1 protease inhibitors.

Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114

Novel bis-tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI) UIC-94017 (TMC114) with potent activity against multi-PI-resistant human immunodeficiency virus in vitro.

Drug-target residence time and its implications for lead optimization.

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13845-13851

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scholarly article

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10.1128/JVI.01184-07

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P407

P433

24

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81

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5917545

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17928344

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2168871

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