Folding regulates autoprocessing of HIV-1 protease precursor.
about
Visualization of early events in acetic acid denaturation of HIV-1 protease: a molecular dynamics study.Gag-Pol processing during HIV-1 virion maturation: a systems biology approachThe extremely slow-exchanging core and acid-denatured state of green fluorescent protein.Understanding HIV-1 protease autoprocessing for novel therapeutic development.Local structural preferences and dynamics restrictions in the urea-denatured state of SUMO-1: NMR characterization.Gag-Pol Transframe Domain p6* Is Essential for HIV-1 Protease-Mediated Virus Maturation.Atomistic simulations of the HIV-1 protease folding inhibition.NMR insights into a megadalton-size protein self-assembly.Uncoupling 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.Construction of a molecular clone of ovine enzootic nasal tumor virus.C-Terminal HIV-1 Transframe p6* Tetrapeptide Blocks Enhanced Gag Cleavage Incurred by Leucine Zipper Replacement of a Deleted p6* Domain.Importance of protease cleavage sites within and flanking human immunodeficiency virus type 1 transframe protein p6* for spatiotemporal regulation of protease activation.HIV-1 protease with leucine zipper fused at N-terminus exhibits enhanced linker amino acid-dependent activity.Presence of the propeptide on recombinant lysosomal dipeptidase controls both activation and dimerization.Thermodynamics of strongly allosteric inhibition: a model study of HIV-1 protease
P2860
Q21135453-4D6E1BED-26F7-43F1-9148-13C5DC982795Q28533696-AEDD3BD1-E22B-4848-866C-792DF3229D41Q30157256-AA56EB66-025C-41F3-BBCB-1E02D247EEFCQ33356201-F2690380-21B5-4E1B-BC5B-E566817F59DAQ34452373-6604C28B-EF0D-44FE-85F3-6F09FD2CA924Q35672342-781B6C72-552D-41A3-9E17-D57672404832Q36737204-F3735BA3-559E-491D-8FD0-232F234B69B6Q36803133-20346EA7-AE08-4BF9-8CCC-073CB17CE72BQ37248021-166470DF-EC2B-4B6A-AB5B-959A6EB04EA5Q37950254-6BFE19DD-E194-4875-BA3E-8D55F31B593AQ38723523-1BF5408E-85F4-46AD-981E-7A0270A39F5FQ38934936-28B650BA-7008-4CC8-B2C8-F0D830BB9524Q40005589-B21563D6-A12D-4A66-BBE4-C6CB2BC48F10Q52719399-E19D9FEE-FA99-4E9E-A4E9-AE053B2D0106Q54448759-94483171-3D31-4D39-8043-78FBEE2B18E1Q58882302-62E2203C-6C20-466D-BC35-4BFFA7496F70
P2860
Folding regulates autoprocessing of HIV-1 protease precursor.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունվարին 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
Folding regulates autoprocessing of HIV-1 protease precursor.
@ast
Folding regulates autoprocessing of HIV-1 protease precursor.
@en
type
label
Folding regulates autoprocessing of HIV-1 protease precursor.
@ast
Folding regulates autoprocessing of HIV-1 protease precursor.
@en
prefLabel
Folding regulates autoprocessing of HIV-1 protease precursor.
@ast
Folding regulates autoprocessing of HIV-1 protease precursor.
@en
P2093
P356
P1476
Folding regulates autoprocessing of HIV-1 protease precursor.
@en
P2093
Amarnath Chatterjee
Ram Kumar Mishra
Ramakrishna V Hosur
Rohit Mittal
P304
11369-11378
P356
10.1074/JBC.M412603200
P407
P577
2005-01-04T00:00:00Z