Interactions of different inhibitors with active-site aspartyl residues of HIV-1 protease and possible relevance to pepsin.
about
Autocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: Relevance to drug resistanceThe L76V Drug Resistance Mutation Decreases the Dimer Stability and Rate of Autoprocessing of HIV-1 Protease by Reducing Internal Hydrophobic ContactsHIV-1 Protease with 20 Mutations Exhibits Extreme Resistance to Clinical Inhibitors through Coordinated Structural RearrangementsThe role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamicsRevealing the dimer dissociation and existence of a folded monomer of the mature HIV-2 proteaseDimerization of HIV-1 protease occurs through two steps relating to the mechanism of protease dimerization inhibition by darunavir.Inhibition of autoprocessing of natural variants and multidrug resistant mutant precursors of HIV-1 protease by clinical inhibitors.Dynamics of thermodynamically stable, kinetically trapped, and inhibitor-bound states of pepsinEvolution under Drug Pressure Remodels the Folding Free-Energy Landscape of Mature HIV-1 ProteaseMutations Proximal to Sites of Autoproteolysis and the α-Helix That Co-evolve under Drug Pressure Modulate the Autoprocessing and Vitality of HIV-1 Protease.Amide hydrogen exchange in HIV-1 subtype B and C proteases--insights into reduced drug susceptibility and dimer stability.Ribosomal synthesis of backbone-macrocyclic peptides containing γ-amino acids.
P2860
Q27664164-8F2FF577-60A5-44AD-8847-250C5CF34C6EQ27667353-7B37ED08-BBE5-49D3-AF29-E0296C16B5BDQ27677952-FED5F653-864C-4193-955E-8EAB462DB9D5Q28238412-53D4A34A-8AE1-434F-9748-865866F27E86Q33650307-37871548-1C54-472E-A6A6-61A0CC2DE786Q34082661-E8D4FE6F-F9CD-4372-8986-C0AA8FED35DCQ35022049-F6676442-3405-4DBE-AF0C-D6A2F6ACC173Q35246265-EAF54A23-B148-4A6D-AFB7-750DA8DDF580Q36999137-ADC6AB93-8C6D-4758-9490-54AA5675B681Q41490002-9DD68460-2D01-4E97-B5A0-441FE4471DA7Q42184665-0B0064F6-6CA5-422A-90BD-6D5C03754C56Q43770371-DC810E41-933F-4AB2-8AB9-A92584FCA103
P2860
Interactions of different inhibitors with active-site aspartyl residues of HIV-1 protease and possible relevance to pepsin.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Interactions of different inhi ...... possible relevance to pepsin.
@en
Interactions of different inhi ...... possible relevance to pepsin.
@nl
type
label
Interactions of different inhi ...... possible relevance to pepsin.
@en
Interactions of different inhi ...... possible relevance to pepsin.
@nl
prefLabel
Interactions of different inhi ...... possible relevance to pepsin.
@en
Interactions of different inhi ...... possible relevance to pepsin.
@nl
P2860
P356
P1433
P1476
Interactions of different inhi ...... possible relevance to pepsin.
@en
P2093
Jane M Sayer
John M Louis
P2860
P304
P356
10.1002/PROT.22271
P407
P577
2009-05-01T00:00:00Z