HIV-1 Rev regulation involves recognition of non-Watson-Crick base pairs in viral RNA.
about
A new nucleoporin-like protein interacts with both HIV-1 Rev nuclear export signal and CRM-1Identification of specific nucleotide sequences within the conserved 3'-SL in the dengue type 2 virus genome required for replicationCrfA, a small noncoding RNA regulator of adaptation to carbon starvation in Caulobacter crescentusStructural and functional analysis of the visna virus Rev-response elementThe neuronal RNA binding protein Nova-1 recognizes specific RNA targets in vitro and in vivoThe basic domain of Rev from human immunodeficiency virus type 1 specifically blocks the entry of U4/U6.U5 small nuclear ribonucleoprotein in spliceosome assemblyEukaryotic initiation factor 5A is a cellular target of the human immunodeficiency virus type 1 Rev activation domain mediating trans-activationChimeric RNase H-competent oligonucleotides directed to the HIV-1 Rev response elementIdentification of a 14mer RNA that recognizes and binds flavin mononucleotide with high affinity.RNA Fluorescence with Light-Up AptamersDerivation and characterization of a dengue type 1 host range-restricted mutant virus that is attenuated and highly immunogenic in monkeys.The crystal structure of the Rev binding element of HIV-1 reveals novel base pairing and conformational variabilityCrystal structure of an oligonucleotide duplex containing G.G base pairs: influence of mispairing on DNA backbone conformationA curved RNA helix incorporating an internal loop with G.A and A.A non-Watson-Crick base pairingReal-time kinetics of HIV-1 Rev-Rev response element interactions. Definition of minimal binding sites on RNA and protein and stoichiometric analysisDNA and mRNA sequence of the immune protective DNA ligase I gene match the rev response element of HIVDecoy approach using RNA-DNA chimera oligonucleotides to inhibit the regulatory function of human immunodeficiency virus type 1 Rev proteinIn vitro genetic selection analysis of alfalfa mosaic virus coat protein binding to 3'-terminal AUGC repeats in the viral RNAsCharacterization and in vitro activity of a branched peptide boronic acid that interacts with HIV-1 RRE RNAThe HIV-1 Rev response element (RRE) adopts alternative conformations that promote different rates of virus replication.Selection and characterization of human immunodeficiency virus type 1 mutants that are resistant to inhibition by the transdominant negative RevM10 proteinIn vitro selection of RNAs with increased tertiary structure stability.A novel 5 displacement spin-labeling technique for electron paramagnetic resonance spectroscopy of RNA3D RNA and Functional Interactions from Evolutionary CouplingsA long-awaited structure is rev-ealed.Single-nucleotide changes in the HIV Rev-response element mediate resistance to compounds that inhibit Rev functionSelection of an RNA molecule that mimics a major autoantigenic epitope of human insulin receptor.Laser-mediated, site-specific inactivation of RNA transcripts.In vitro selection of RNA aptamers that bind special elongation factor SelB, a protein with multiple RNA-binding sites, reveals one major interaction domain at the carboxyl terminusIn vitro selection of an RNA sequence that interacts with high affinity with thymidylate synthase.Sequence analysis of an artificial family of RNA-binding peptidesDNA ligands that bind tightly and selectively to cellobiose.Rec (formerly Corf) function requires interaction with a complex, folded RNA structure within its responsive element rather than binding to a discrete specific binding siteThe human endogenous retrovirus K Rev response element coincides with a predicted RNA folding region.Exploring the sequence space of a DNA aptamer using microarrays.Thermodynamic profiling of HIV RREIIB RNA-zinc finger interactions.Saccharide-RNA recognition.Polyvalent Rev decoys act as artificial Rev-responsive elements.Using in vitro selection to direct the covalent attachment of human immunodeficiency virus type 1 Rev protein to high-affinity RNA ligandsAnalysis of RNA-binding proteins by in vitro genetic selection: identification of an amino acid residue important for locking U1A onto its RNA target.
P2860
Q22009935-9B1C7571-A07F-4F3B-8295-3AE20587BFFFQ24523550-B829B5C1-8EDE-4906-BCAB-91E6820EEB6FQ24612172-F686D7E9-9610-4B60-82BD-099BAA5AE2D4Q24645046-2F17E4FD-B639-4ABC-B09D-B58167F1E4C6Q24646213-23874B61-CAEA-46AC-A1CD-C2922DDB86FCQ24656044-15EE2A2C-2BEC-4B74-A724-CBFAA62619AFQ24657633-2A874DEE-1D2F-4ACF-B546-53EEA95929D9Q24682407-7909F1F6-8BD7-4C9C-B04F-8C5FCFF0C584Q25255133-B4419CBF-23F5-4278-A557-309E7B0A795DQ26742083-4D20A26F-4688-43D0-BFC2-2DAB99F8872EQ27472847-0C5C509B-F243-4C8F-BA21-AF1732C52F75Q27622350-D79F0BF7-4A5A-4506-A8A2-B6446D89817DQ27732084-A8A22751-59E8-4814-B68A-47155C19DDD5Q27733905-7C9F980D-CE9F-4B8A-88B2-61FC8A07DF4EQ28199340-F013DB07-941E-42F7-BED8-7CD76BCC3412Q28295971-204A7A19-0CEC-4D49-A1F8-A2F8490462B9Q28379462-B8203636-8293-4D14-B50D-45CF6779CC46Q28775709-E649119F-BB09-4ED8-92EE-276E8309447EQ30276963-FE03AC40-E3DA-4451-BBCB-4EAB18E49ADAQ30300217-82F09533-B7C2-408D-B276-5456106B454BQ30304057-8FF1B604-F0AF-412A-89BF-3FC3AE964C98Q30304206-97C4DDA8-6D1A-46B8-8BCA-9016F78B3A5BQ30322974-BB49F9DF-F57C-466D-9890-35A314EE01D2Q30387020-549A4012-9478-4E99-82A0-62E228251E2BQ30407389-8F343BC1-67B6-4C08-B5A1-A31BCA99A208Q30430496-A3DDFFE5-8408-4C9B-AC5B-89C221703C3EQ30463953-174A72B0-1CB3-4E77-91A2-1487BF427DAEQ30639723-2A03DCF9-B863-467A-A810-C8314E020223Q30778197-AE08CB66-4322-42A2-A924-FB0EBF7F197DQ30953700-D0C76E08-642F-4C7D-90B5-674F3130F827Q31114312-73798E17-B0DD-4861-AAF1-93AEB3020361Q32064796-388CA2B0-CD1C-4A90-B1EC-68016D00D8B5Q33292081-0D362CDB-C4BC-437A-81C6-B01547007255Q33292323-F5FF7F01-3892-461F-ADAD-EAE46FFC985AQ33304953-757EDBC9-CB07-4B68-A1D9-D88DA79CF6CCQ33489159-DBD614C9-E6B3-42AE-858C-497311D37118Q33638750-4F7E3DD6-61FB-4E4E-8A80-B23A8F524A23Q33648134-5A1F7D84-18AC-476E-A880-700E43A1AA8DQ33657353-2FFEBA00-C267-426B-A2B1-79DE152E728BQ33729059-E0808180-F7E1-40F3-B1AA-EDDA6DDBF823
P2860
HIV-1 Rev regulation involves recognition of non-Watson-Crick base pairs in viral RNA.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh
1991年學術文章
@zh-hant
name
HIV-1 Rev regulation involves recognition of non-Watson-Crick base pairs in viral RNA.
@en
type
label
HIV-1 Rev regulation involves recognition of non-Watson-Crick base pairs in viral RNA.
@en
prefLabel
HIV-1 Rev regulation involves recognition of non-Watson-Crick base pairs in viral RNA.
@en
P2093
P1433
P1476
HIV-1 Rev regulation involves recognition of non-Watson-Crick base pairs in viral RNA.
@en
P2093
P304
P356
10.1016/0092-8674(91)90527-6
P407
P50
P577
1991-11-01T00:00:00Z