Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease
about
Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymesProcessing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates.HIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchStructural implications of drug-resistant mutants of HIV-1 protease: high-resolution crystal structures of the mutant protease/substrate analogue complexesCombining mutations in HIV-1 protease to understand mechanisms of resistanceSolution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursorAutocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: Relevance to drug resistanceVitAL: Viterbi algorithm for de novo peptide designAnalysis and prediction of highly effective antiviral peptides based on random forestsIntegrated analysis of residue coevolution and protein structures capture key protein sectors in HIV-1 proteinsRelationships of gag-pol diversity between Ty3/Gypsy and Retroviridae LTR retroelements and the three kings hypothesis.Signal propagation in proteins and relation to equilibrium fluctuationsDrug-associated changes in amino acid residues in Gag p2, p7(NC), and p6(Gag)/p6(Pol) in human immunodeficiency virus type 1 (HIV-1) display a dominant effect on replicative fitness and drug response.Effects of HIV-1 protease on cellular functions and their potential applications in antiretroviral therapy.Inhibitor design by wrapping packing defects in HIV-1 proteins.Proline residues within spacer peptide p1 are important for human immunodeficiency virus type 1 infectivity, protein processing, and genomic RNA dimer stability.HIPdb: a database of experimentally validated HIV inhibiting peptides.Gag-Pol Transframe Domain p6* Is Essential for HIV-1 Protease-Mediated Virus Maturation.Structural studies on molecular mechanisms of Nelfinavir resistance caused by non-active site mutation V77I in HIV-1 protease.Mutations in multiple domains of Gag drive the emergence of in vitro resistance to the phosphonate-containing HIV-1 protease inhibitor GS-8374.Water at biomolecular binding interfaces.Solid-phase glycan isolation for glycomics analysisBioinformatic flowchart and database to investigate the origins and diversity of clan AA peptidasesBinding 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 EnzymeUncoupling human immunodeficiency virus type 1 Gag and Pol reading frames: role of the transframe protein p6* in viral replication.Protein intrinsic disorder as a flexible armor and a weapon of HIV-1.C-Terminal HIV-1 Transframe p6* Tetrapeptide Blocks Enhanced Gag Cleavage Incurred by Leucine Zipper Replacement of a Deleted p6* Domain.Human immunodeficiency virus type 1 protease cleavage site mutations associated with protease inhibitor cross-resistance selected by indinavir, ritonavir, and/or saquinavir.The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage.Trp42 rotamers report reduced flexibility when the inhibitor acetyl-pepstatin is bound to HIV-1 protease.Interactions of a novel inhibitor from an extremophilic Bacillus sp. with HIV-1 protease: implications for the mechanism of inactivation.Efavirenz enhances the proteolytic processing of an HIV-1 pol polyprotein precursor and reverse transcriptase homodimer formation.Competitive inhibition of human immunodeficiency virus type-1 protease by the Gag-Pol transframe protein.Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.Interchain hydrophobic clustering promotes rigidity in HIV-1 protease flap dynamics: new insights from molecular dynamics.Desolvation shell of hydrogen bonds in folded proteins, protein complexes and folding pathways
P2860
Q24549622-1211A3FF-D7E5-44E1-814A-CAC31F7E2C07Q24812175-BDC6E3C0-D0A8-47A0-8ACD-EF76D27DCE18Q26746070-F1976B35-4E8D-4A53-9C03-3AFACED0D788Q27631613-9F2E49F6-94F0-4ADE-B43C-E9CB940359B1Q27638993-9FE4FEE0-6199-4713-958B-6D83F39F2767Q27641889-54014B15-0910-40D3-BE46-387CA05FD8F1Q27664164-FC6A930B-68A1-4CE2-AB55-22EC7CB07DA9Q28474154-333E4618-3DF2-4229-9504-633E792AD799Q28535105-85641296-6024-4EBD-9D17-B40BEEAC30B6Q28543396-A0918A23-DD3D-4553-9CD4-D1AD48AA4308Q28756671-022C253C-A9EA-4571-A388-C9E70C4ADD62Q33300127-48717FA9-10C9-46D1-A7D1-308F5BF5DEF0Q34012585-2A4D897F-EA38-4037-9FA5-F653348DA0E5Q34033572-CDE72EB2-7B50-4054-B244-AE1EDAF294F7Q34338157-038EEC20-10B3-4847-8420-111EED3CEA9FQ34354549-B443B4A6-31FC-452B-9649-4A3A38D29E3BQ34566584-FAE92392-ECEC-47C9-A81E-A7D6BFCB1556Q35672342-32BEC2A4-FA7B-4137-B3BA-9C3C9A82723DQ35875761-2D3E2D04-2486-4227-A344-F5D27511A84DQ36506829-37886D26-8784-4972-8D08-E824AD9A6881Q36715297-88FA46B9-EF62-4A85-A429-A616BCFB7AF2Q36908318-6CD01B47-9F0D-429F-88FF-6A541CB18DA9Q37097414-B11053AC-23D7-4B94-8C30-35CC78CB3B6DQ37237447-B8F0E5C0-B629-4658-ABC8-75385D7F671CQ37248021-3E2031B7-FF3A-44B1-AA8F-778CF21A20E2Q37950254-DBFD0490-D512-4A6B-862E-B663E8980FADQ38934936-C7130BDB-687F-47F5-9090-774F0A40A909Q39601382-FCEFDE01-8034-406B-AF58-99877A43F968Q39698249-BBE74059-5303-4240-9B8D-FDEC6B6D2713Q42059363-AF16941C-C3A7-4C5B-82F7-E578D6725009Q43508565-13A2969A-A1A7-48FC-B5B3-D3248959FDEFQ45218379-DD1BB0D0-13E0-4514-8A89-CF3CFD82D25CQ45748209-4C0BF248-DB60-4B98-9F63-A295C552309FQ47940296-B6B545C3-3E40-413D-8098-52451AEA2694Q50894892-46514C9C-94B1-453B-A063-9C85AD2661A8Q56970620-A837030D-D781-4EF4-82D6-F074342CDB0F
P2860
Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease
description
1998 nî lūn-bûn
@nan
1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Hydrophilic peptides derived f ...... Pol inhibit the HIV-1 protease
@ast
Hydrophilic peptides derived f ...... Pol inhibit the HIV-1 protease
@en
Hydrophilic peptides derived f ...... Pol inhibit the HIV-1 protease
@nl
type
label
Hydrophilic peptides derived f ...... Pol inhibit the HIV-1 protease
@ast
Hydrophilic peptides derived f ...... Pol inhibit the HIV-1 protease
@en
Hydrophilic peptides derived f ...... Pol inhibit the HIV-1 protease
@nl
prefLabel
Hydrophilic peptides derived f ...... Pol inhibit the HIV-1 protease
@ast
Hydrophilic peptides derived f ...... Pol inhibit the HIV-1 protease
@en
Hydrophilic peptides derived f ...... Pol inhibit the HIV-1 protease
@nl
P2093
P356
P1433
P1476
Hydrophilic peptides derived f ...... Pol inhibit the HIV-1 protease
@en
P2093
P304
P356
10.1021/BI972059X
P407
P577
1998-02-24T00:00:00Z