HIV-1 reverse transcriptase-associated RNase H cleaves RNA/RNA in arrested complexes: implications for the mechanism by which RNase H discriminates between RNA/RNA and RNA/DNA
about
Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNARNase H activity: structure, specificity, and function in reverse transcriptionRibonuclease H: properties, substrate specificity and roles in retroviral reverse transcriptionVirus-encoded RNA helicasesThe reverse transcriptase of the Tf1 retrotransposon has a specific novel activity for generating the RNA self-primer that is functional in cDNA synthesisInhibition of the ribonuclease H activity of HIV-1 reverse transcriptase by GSK5750 correlates with slow enzyme-inhibitor dissociation.The kissing-loop motif is a preferred site of 5' leader recombination during replication of SL3-3 murine leukemia viruses in mice.Structural basis for the specificity of the initiation of HIV-1 reverse transcription.Structure and function of HIV-1 reverse transcriptase: molecular mechanisms of polymerization and inhibition.Reverse transcriptase in motion: conformational dynamics of enzyme-substrate interactions.HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors.Sequence, distance, and accessibility are determinants of 5'-end-directed cleavages by retroviral RNases H.Cleavage of double-stranded RNA by RNase HI from a thermoacidophilic archaeon, Sulfolobus tokodaii 7.Fusion with an RNA binding domain to confer target RNA specificity to an RNase: design and engineering of Tat-RNase H that specifically recognizes and cleaves HIV-1 RNA in vitro.HIV-1 reverse transcriptase can simultaneously engage its DNA/RNA substrate at both DNA polymerase and RNase H active sites: implications for RNase H inhibition.Specific initiation and switch to elongation of human immunodeficiency virus type 1 reverse transcription require the post-transcriptional modifications of primer tRNA3Lys.Mutations in the U5 region adjacent to the primer binding site affect tRNA cleavage by human immunodeficiency virus type 1 reverse transcriptase in vivoAn unusual mechanism of self-primed reverse transcription requires the RNase H domain of reverse transcriptase to cleave an RNA duplex.Preferred sequences within a defined cleavage window specify DNA 3' end-directed cleavages by retroviral RNases HExtended minus-strand DNA as template for R-U5-mediated second-strand transfer in recombinational rescue of primer binding site-modified retroviral vectors.Complementation of a primer binding site-impaired murine leukemia virus-derived retroviral vector by a genetically engineered tRNA-like primer.Initiation of HIV reverse transcription: is enzyme flipping required?Entire-Dataset Analysis of NMR Fast-Exchange Titration Spectra: A Mg2+ Titration Analysis for HIV-1 Ribonuclease H Domain.Replication errors during in vivo Ty1 transposition are linked to heterogeneous RNase H cleavage sites.Mutational analysis of the reverse transcriptase and ribonuclease H domains of the human foamy virus.Connection domain mutations N348I and A360V in HIV-1 reverse transcriptase enhance resistance to 3'-azido-3'-deoxythymidine through both RNase H-dependent and -independent mechanisms.Delayed chain termination protects the anti-hepatitis B virus drug entecavir from excision by HIV-1 reverse transcriptase.Expression of an active form of recombinant Ty1 reverse transcriptase in Escherichia coli: a fusion protein containing the C-terminal region of the Ty1 integrase linked to the reverse transcriptase-RNase H domain exhibits polymerase and RNase H actiArchitecture of an HIV-1 reverse transcriptase initiation complex.
P2860
Q24545723-5A60098F-258D-4573-B4C6-7B9293E40659Q24643032-7B68D357-CCD9-4B62-A08D-62BF48921862Q24655903-7C026CC6-0734-428D-B9E9-8BEB15B99604Q27480799-476DEC20-58DA-4FBB-8FB1-D2A6D02C3B7DQ28756733-B7C814CE-8B40-4161-973B-C9406DFA6429Q33718515-7F5F0331-61DB-40B7-9400-138666458CE4Q33823773-1613105C-5718-410E-9998-64E71F1C8E58Q33890456-974F896B-A718-405F-9A73-E03387DAE8E9Q33896402-D118F0DE-5F03-4CBC-9857-07882E6156E9Q34092798-C1389ACF-DA37-4280-A44D-87AA9879D8B3Q34223771-F58629F1-C876-4168-A73E-F06D12C883CDQ34333528-F9E4A13B-DF65-4352-B253-8188A8C1DFF9Q34364175-FBFB3B19-0BAB-4DE1-B312-4C7397C03B63Q34595695-1BF69BF9-21BC-4885-8FA6-2C5CDF73909DQ34849844-94700CD8-F42B-4E22-95D8-A09A326196B9Q35853488-A9CCA8FB-E57A-4EED-8D8C-1FD6D0FE055CQ36424554-57765B66-941B-4A95-A839-1250CF3EEFF2Q36562838-5A5D25A1-A0BD-40B3-8946-DFB0603760AAQ37431890-7AE041CE-F271-46D9-BD6E-7B017865D720Q38339423-6FF7E5D2-51A7-49DD-83EF-B51598DF376FQ38349052-221C0A6D-8226-4CAC-B102-B4E982A823CCQ38615386-FC9610A3-136D-4854-B5CC-8F066BC5798CQ39101156-FE41361C-352D-4D09-8D2F-97ABB8DA4FCEQ39574404-B0DC7283-77D2-425F-AC7F-3921BEEC431EQ40394911-56C51816-67F2-4B61-8C75-0268144697A4Q41262484-95EB6DF2-4816-4B39-8532-1054133A8190Q41503130-64A9C09D-BF8F-4B93-B58F-2B278B0B4EE6Q41783121-E5433A19-AC10-4B1C-9FF0-C03D145815D4Q52309444-C7FA10B0-D27D-419D-8429-33263CB5932F
P2860
HIV-1 reverse transcriptase-associated RNase H cleaves RNA/RNA in arrested complexes: implications for the mechanism by which RNase H discriminates between RNA/RNA and RNA/DNA
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on February 1995
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
HIV-1 reverse transcriptase-as ...... es between RNA/RNA and RNA/DNA
@en
HIV-1 reverse transcriptase-as ...... s between RNA/RNA and RNA/DNA.
@nl
type
label
HIV-1 reverse transcriptase-as ...... es between RNA/RNA and RNA/DNA
@en
HIV-1 reverse transcriptase-as ...... s between RNA/RNA and RNA/DNA.
@nl
prefLabel
HIV-1 reverse transcriptase-as ...... es between RNA/RNA and RNA/DNA
@en
HIV-1 reverse transcriptase-as ...... s between RNA/RNA and RNA/DNA.
@nl
P2093
P2860
P1433
P1476
HIV-1 reverse transcriptase-as ...... es between RNA/RNA and RNA/DNA
@en
P2093
S F Le Grice
P2860
P304
P356
10.1002/J.1460-2075.1995.TB07061.X
P407
P577
1995-02-01T00:00:00Z