Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants
about
sameAs
Structural basis for cooperative RNA binding and export complex assembly by HIV RevImplications of the HIV-1 Rev dimer structure at 3.2 A resolution for multimeric binding to the Rev response elementHIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexesA solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNAResistance to RevM10 inhibition reflects a conformational switch in the HIV-1 Rev response element.HIV-1 Rev protein assembles on viral RNA one molecule at a time.A structurally plastic ribonucleoprotein complex mediates post-transcriptional gene regulation in HIV-1The Arginine-Rich RNA-Binding Motif of HIV-1 Rev Is Intrinsically Disordered and Folds upon RRE BindingRoles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactionsAnalysis of the EIAV Rev-responsive element (RRE) reveals a conserved RNA motif required for high affinity Rev binding in both HIV-1 and EIAVRecruitment of the Crm1 nuclear export factor is sufficient to induce cytoplasmic expression of incompletely spliced human immunodeficiency virus mRNAsProtein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes.Computational modeling suggests dimerization of equine infectious anemia virus Rev is required for RNA binding.A long-awaited structure is rev-ealed.Single-nucleotide changes in the HIV Rev-response element mediate resistance to compounds that inhibit Rev functionThe HIV-2 Rev-response element: determining secondary structure and defining folding intermediates.Cooperativity among Rev-associated nuclear export signals regulates HIV-1 gene expression and is a determinant of virus species tropismGeneration and characterization of a chimeric rabbit/human Fab for co-crystallization of HIV-1 Rev.A cell-penetrating antibody fragment against HIV-1 Rev has high antiviral activity: characterization of the paratopeAn intrabody based on a llama single-domain antibody targeting the N-terminal alpha-helical multimerization domain of HIV-1 rev prevents viral production.Formation of trans-activation competent HIV-1 Rev:RRE complexes requires the recruitment of multiple protein activation domains.Mapping the binding interface between an HIV-1 inhibiting intrabody and the viral protein RevHIV-1 regulatory proteins: targets for novel drug development.Measuring cooperative Rev protein-protein interactions on Rev responsive RNA by fluorescence resonance energy transfer.RNA-directed remodeling of the HIV-1 protein Rev orchestrates assembly of the Rev-Rev response element complexHIV Rev Assembly on the Rev Response Element (RRE): A Structural PerspectiveCooperative dimerization of a stably folded protein directed by a flexible RNA in the assembly of the HIV Rev dimer-RRE stem II complex.Identification and Optimization of Thienopyridine Carboxamides as Inhibitors of HIV Regulatory Complexes.The structural biology of HIV-1: mechanistic and therapeutic insightsThermodynamics of Rev-RNA interactions in HIV-1 Rev-RRE assembly.Rapid and efficient purification of RNA-binding proteins: application to HIV-1 Rev.The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE AssemblyTreatment with the fusion inhibitor enfuvirtide influences the appearance of mutations in the human immunodeficiency virus type 1 regulatory protein rev.Effects of human T-cell leukemia virus type 1 (HTLV-1) p13 on mitochondrial K+ permeability: A new member of the viroporin family?Strategies to inhibit viral protein nuclear import: HIV-1 as a target.Role of Nucleocytoplasmic RNA Transport during the Life Cycle of Retroviruses.RNA triplexes: from structural principles to biological and biotech applications.DDX1 is an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication.A Survey of DDX21 Activity During Rev/RRE Complex Formation.No longer a nuisance: long non-coding RNAs join CENP-A in epigenetic centromere regulation.
P2860
Q24569707-C7F04574-E906-4713-994D-847DD04B5B9BQ24600547-75D7896C-A35E-41B9-898D-8AC378517A54Q24606750-D20EF28A-67F3-4DE6-88C7-6CDD84802D3BQ24644716-4D2EB7DB-7209-48D5-AFF8-CF7CA2B19E32Q24652856-327EB8AC-B8A0-404E-8A5A-2ED911B4AC0EQ24658214-9606D471-A191-42C2-AB71-EE16CA200627Q26765389-DD992E5B-62F5-4D7B-B95E-BF2EC477C589Q27679793-D94BF4F7-BF48-4361-84A1-CAED2DA5DA33Q28286819-44A4547B-E424-4AA8-8AA1-A8AE11D916D7Q28472824-B634679C-7664-4D10-853B-EC3469C027BAQ28646696-470C7D5B-33D3-4B8A-964E-871C6A6D3A86Q30367347-C8DA740E-0E5C-43EB-BDE1-CF77C9BAFD55Q30370048-A528E885-BA3A-4A5D-8050-C93145EB0550Q30407389-030DD55E-7AF8-4943-A15F-744B64A56577Q30430496-239D8A2A-6D32-47A6-A2D8-3C3FA024B957Q30541486-A6D21C38-F994-4835-A1E3-F4F70A50A2C1Q30603666-0EAE54F5-C634-4BC1-922E-0772371D2E52Q33529946-08C819AF-2A75-475B-81F0-5DD28F7EDF96Q33931214-8A5DB474-9EEF-4013-AE69-48B6E149FD40Q33967157-3E73DF40-47DA-4145-B278-93F77CA7607BQ34295820-A1597984-DFAA-417C-88EE-3AC8FDC330C7Q34658271-A5E6B885-3896-4EF8-8524-70FB5BBB3D2FQ34768563-04FF092A-5D4A-4519-BD6C-77BCFF4D35D1Q35079170-7E046D84-D1DD-4250-A901-090E7CE367ABQ35179371-EC133866-924A-4ACE-BEE1-1A95040F0B8BQ35808679-9B3FCC08-E78E-469C-82FD-BAC5C7FC0B55Q35856263-77F96591-5CF6-45D0-A035-32D11B9206F8Q36349096-A33D5350-76EA-45F2-8874-F1E7B4CE08C5Q36656440-D5D8CD9E-471B-4B02-87F7-978742702146Q36711096-B3214975-FED8-40BB-8D28-4B801CFCEDC2Q37057990-1C299E2A-5F70-40E0-BF44-31A72F2DFE0DQ37079662-AADD426A-3655-41E3-B375-A1A369A4E816Q37247695-9006F19D-06C7-4901-B29D-9999B002F951Q37695355-E6B10405-49C1-4D12-8ECB-D61900A7145CQ37780819-316AA14A-A8B3-4258-AB35-AF4D606AC1DBQ38025392-53BAE01A-9F11-484E-BDD1-30311F10DE6DQ38242065-03B28415-AD35-44A0-9409-4D3601050D41Q38330601-B6539484-5248-4510-886D-65574BBCC708Q38680199-58BB0398-6274-4197-A2EA-475C97F68922Q38691266-FCA1BA21-8E98-4DE4-A588-AD9EC080D331
P2860
Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants
description
2001 nî lūn-bûn
@nan
2001 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մարտին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Structural model for the coope ...... of assembly-defective mutants
@ast
Structural model for the coope ...... of assembly-defective mutants
@en
Structural model for the coope ...... of assembly-defective mutants
@nl
type
label
Structural model for the coope ...... of assembly-defective mutants
@ast
Structural model for the coope ...... of assembly-defective mutants
@en
Structural model for the coope ...... of assembly-defective mutants
@nl
prefLabel
Structural model for the coope ...... of assembly-defective mutants
@ast
Structural model for the coope ...... of assembly-defective mutants
@en
Structural model for the coope ...... of assembly-defective mutants
@nl
P1433
P1476
Structural model for the coope ...... of assembly-defective mutants
@en
P2093
P304
P356
10.1016/S1097-2765(01)00207-6
P407
P577
2001-03-01T00:00:00Z