Processing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates.
about
The prototype HIV-1 maturation inhibitor, bevirimat, binds to the CA-SP1 cleavage site in immature Gag particlesThe choreography of HIV-1 proteolytic processing and virion assemblyHIV-1 protease and reverse transcriptase control the architecture of their nucleocapsid partnerA Single-Cell Platform for Monitoring Viral Proteolytic Cleavage in Different Cellular CompartmentsCrystal structure of an FIV/HIV chimeric protease complexed with the broad-based inhibitor, TL-3Structural, kinetic, and thermodynamic studies of specificity designed HIV-1 proteaseHIV-1 Protease-Substrate Coevolution in Nelfinavir ResistanceStructural Maturation of HIV-1 Reverse Transcriptase-A Metamorphic Solution to Genomic InstabilityDrug-class specific impact of antivirals on the reproductive capacity of HIVAn assay to monitor HIV-1 protease activity for the identification of novel inhibitors in T-cellsGag-Pol processing during HIV-1 virion maturation: a systems biology approachHIV-1 Nef inhibits Protease activity and its absence alters protein content of mature viral particlesMechanistic Studies and Modeling Reveal the Origin of Differential Inhibition of Gag Polymorphic Viruses by HIV-1 Maturation InhibitorsRole of the SP2 domain and its proteolytic cleavage in HIV-1 structural maturation and infectivityUnderstanding HIV-1 protease autoprocessing for novel therapeutic development.The Second-Generation Maturation Inhibitor GSK3532795 Maintains Potent Activity Toward HIV Protease Inhibitor-Resistant Clinical IsolatesInhibition of human immunodeficiency virus type 1 by triciribine involves the accessory protein nefFeline immunodeficiency virus (FIV) as a model for study of lentivirus infections: parallels with HIV.Selective killing of human immunodeficiency virus infected cells by non-nucleoside reverse transcriptase inhibitor-induced activation of HIV protease.Structural basis and distal effects of Gag substrate coevolution in drug resistance to HIV-1 proteaseThe nature of the N-terminal amino acid residue of HIV-1 RNase H is critical for the stability of reverse transcriptase in viral particles.New findings in cleavage sites variability across groups, subtypes and recombinants of human immunodeficiency virus type 1The p66 immature precursor of HIV-1 reverse transcriptase.Gag-Pol Transframe Domain p6* Is Essential for HIV-1 Protease-Mediated Virus Maturation.Structural integrity of the ribonuclease H domain in HIV-1 reverse transcriptase.Context surrounding processing sites is crucial in determining cleavage rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol polyprotein precursors by viral protease.Identification and Characterization of BMS-955176, a Second-Generation HIV-1 Maturation Inhibitor with Improved Potency, Antiviral Spectrum, and Gag Polymorphic Coverage.A proposal for a new HIV-1 DLS structural model.The Race against Protease Activation Defines the Role of ESCRTs in HIV BuddingHIV Assembly and Budding: Ca(2+) Signaling and Non-ESCRT Proteins Set the Stage.Efavirenz enhances HIV-1 gag processing at the plasma membrane through Gag-Pol dimerizationMolecular mechanisms of FIV infection.HIV-1 drug resistance mutations: an updated framework for the second decade of HAARTSuboptimal inhibition of protease activity in human immunodeficiency virus type 1: effects on virion morphogenesis and RNA maturationFunctional consequences of human immunodeficiency virus escape from an HLA-B*13-restricted CD8+ T-cell epitope in p1 Gag protein.Mutations in HIV-1 reverse transcriptase cause misfolding and miscleavage by the viral protease.HIV-1 Gag processing intermediates trans-dominantly interfere with HIV-1 infectivity.New small-molecule inhibitor class targeting human immunodeficiency virus type 1 virion maturation.Targeting human immunodeficiency virus type 1 assembly, maturation and budding.Human Immunodeficiency Virus Gag and protease: partners in resistance.
P2860
Q21245046-CE6C1742-5B7B-4670-9C1A-94E1F139F214Q27009643-19F1D205-6057-4379-87A4-C397E9005165Q27302871-5A27DC54-12CD-412B-9FBD-F7EFCC4B08D8Q27468663-A90EBF4B-2AD2-4EA8-B0C0-59D0F89C0D4EQ27641090-30A2518B-8467-416C-8C56-C59B49D0D5A2Q27678853-D77F63BF-EA1F-498B-B238-8686F8388D22Q27683192-D4E4CA77-DFA5-4521-B2AF-7C513F454BC4Q28074527-7DD329F6-776D-4222-97B2-4E1E6F81E4BBQ28473451-EF2D3094-914D-44FA-8437-3F38FBB71F94Q28474218-1F145936-B5D7-46C1-BEF7-802D12457840Q28533696-5B81B0F1-3396-408E-BE0C-21B78260462FQ28538038-7778F6C2-A0D6-42AF-AA40-529448ACCF65Q28554482-F16246CD-0EB6-4A07-869E-1F65011A25C3Q28710568-2E218E63-8F63-4DC2-9775-F75D8BA7D5D3Q33356201-8A466A15-33CE-4D9F-8F1E-3BF2CD2638A5Q33557807-B6A18C3F-2F4F-4B8B-B205-18091AEAB0FFQ33768829-B015BF6E-0EEE-4DAA-8A3B-63DCC69B7DD0Q33786404-DC8BCC57-55BF-4DB4-898B-58F5EDB4789CQ34282609-BB83E614-1C74-4FDF-9E58-DD17E437720CQ34526179-889CFDC2-B95A-4F71-A3B0-578B14F5DC32Q34991047-8A173261-5376-4215-85FF-99D6E9EBF042Q35091548-713D1D50-D3A5-4564-A72B-620B21D14C37Q35638699-03ADD4F5-6173-4B29-9D02-2FC3BE6A3B9BQ35672342-764ACC77-E3A0-4D4C-83DD-D3BD29939737Q35875958-ED60A0BB-3334-4927-87B9-CDF031414591Q35921690-194E36A4-0390-45E6-95FC-7729C7D615FBQ35992805-EA8D1EA7-9FAB-466C-9F12-82E98A107004Q36008146-D0DA8576-9C6B-47BE-8314-BE3F29C9C895Q36046317-F558627B-BD1E-46A1-AF0F-8A5006EAC90AQ36063560-782B2184-C261-4FC4-83E3-B45B620A5C9AQ36667876-54DB4FF0-4054-48C2-BE01-B4D548AAE3E6Q36692802-77752BF5-D20C-4825-8395-D103EEF618D5Q36900010-A77D4155-1D44-4F77-A4FD-894F6BA5A498Q36958798-64B240E8-EB6E-470E-A381-70D875A0BF1DQ37033282-3E9CA800-E39E-4B65-A10E-C0EEE70FA2E4Q37244912-7AB8112C-564E-4BC8-995C-2333EBF6449BQ37447762-411C352B-8670-4D96-8713-5A57F75A22A7Q37450688-E3A60D71-0D0B-4204-B4BE-BA43958A5529Q37928913-494CE3D0-27C0-44A8-8228-C1079B7323F4Q38032330-224C45E2-F8A4-4CCF-82F0-9033DC346EC4
P2860
Processing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates.
description
2005 nî lūn-bûn
@nan
2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Processing sites in the human ...... al protease at different rates
@nl
Processing sites in the human ...... l protease at different rates.
@ast
Processing sites in the human ...... l protease at different rates.
@en
type
label
Processing sites in the human ...... al protease at different rates
@nl
Processing sites in the human ...... l protease at different rates.
@ast
Processing sites in the human ...... l protease at different rates.
@en
prefLabel
Processing sites in the human ...... al protease at different rates
@nl
Processing sites in the human ...... l protease at different rates.
@ast
Processing sites in the human ...... l protease at different rates.
@en
P2093
P2860
P3181
P356
P1433
P1476
Processing sites in the human ...... l protease at different rates.
@en
P2093
Andrew H Kaplan
Jeffrey N Lindquist
Steve C Pettit
P2860
P2888
P3181
P356
10.1186/1742-4690-2-66
P407
P577
2005-11-01T00:00:00Z
P5875
P6179
1038359461