Interaction of HIV-1 reverse transcriptase with a synthetic form of its replication primer, tRNA(Lys,3)
about
Primer tRNAs for reverse transcriptionSelection of functional tRNA primers and primer binding site sequences from a retroviral combinatorial library: identification of new functional tRNA primers in murine leukemia virus replication.Functional domains of Tat required for efficient human immunodeficiency virus type 1 reverse transcription.Structural and dynamic characterization of the aromatic amino acids of the human immunodeficiency virus type I nucleocapsid protein zinc fingers and their involvement in heterologous tRNA(Phe) binding: a steady-state and time-resolved fluorescence sAssembly, purification and crystallization of an active HIV-1 reverse transcriptase initiation complex.Two step synthesis of (-) strong-stop DNA by avian and murine reverse transcriptases in vitro.Characterization of a nucleocapsid-like region and of two distinct primer tRNALys,2 binding sites in the endogenous retrovirus Gypsy.Retrons and multicopy single-stranded DNAHuman immunodeficiency virus type 1 can use different tRNAs as primers for reverse transcription but selectively maintains a primer binding site complementary to tRNA(3Lys)Specific initiation and switch to elongation of human immunodeficiency virus type 1 reverse transcription require the post-transcriptional modifications of primer tRNA3Lys.Effects of modifying the tRNA(3Lys) anticodon on the initiation of human immunodeficiency virus type 1 reverse transcriptionRNase D, a reported new activity associated with HIV-1 reverse transcriptase, displays the same cleavage specificity as Escherichia coli RNase IIIA specific orientation of RNA secondary structures is required for initiation of reverse transcription.Minimal sequence requirements of a functional human immunodeficiency virus type 1 primer binding site.Basic amino acids flanking the zinc finger of Moloney murine leukemia virus nucleocapsid protein NCp10 are critical for virus infectivity.Analytical study of avian reticuloendotheliosis virus dimeric RNA generated in vivo and in vitro.Double-stranded RNA-dependent RNase activity associated with human immunodeficiency virus type 1 reverse transcriptase.Viral RNA annealing activities of human immunodeficiency virus type 1 nucleocapsid protein require only peptide domains outside the zinc fingersReverse transcriptase of human immunodeficiency virus can use either human tRNA(3Lys) or Escherichia coli tRNA(2Gln) as a primer in an in vitro primer-utilization assayMutation in the primer binding site of the type 1 human immunodeficiency virus genome affects virus production and infectivity.Site-specific crosslinking of 4-thiouridine-modified human tRNA(3Lys) to reverse transcriptase from human immunodeficiency virus type I.Structural requirements for the binding of tRNA Lys3 to reverse transcriptase of the human immunodeficiency virus type 1.The N-terminal domain of mammalian Lysyl-tRNA synthetase is a functional tRNA-binding domain.Multiple molecular determinants for retrotransposition in a primer tRNAMutated primer binding sites interacting with different tRNAs allow efficient murine leukemia virus replicationRole of post-transcriptional modifications of primer tRNALys,3 in the fidelity and efficacy of plus strand DNA transfer during HIV-1 reverse transcription.A HIV-1 minimal gag protein is superior to nucleocapsid at in vitro annealing and exhibits multimerization-induced inhibition of reverse transcription.Inhibition of HIV-1 replication using a mutated tRNALys-3 primer.Construction of a type 1 human immunodeficiency virus that maintains a primer binding site complementary to tRNA(His).Replication and pathogenicity of primer binding site mutants of SL3-3 murine leukemia viruses.Purification and characterization of recombinant equine infectious anemia virus reverse transcriptase.Analysis of the nucleic acid annealing activities of nucleocapsid protein from HIV-1.The multimerization state of retroviral RNA is modulated by ammonium ions and affects HIV-1 full-length cDNA synthesis in vitro.The hepatitis C virus Core protein is a potent nucleic acid chaperone that directs dimerization of the viral (+) strand RNA in vitro.Switching the in vitro tRNA usage of HIV-1 by simultaneous adaptation of the PBS and PAS.Binding of the HIV-1 nucleocapsid protein to the primer tRNA(3Lys), in vitro, is essentially not specific.
P2860
Q28775697-34B34E25-F065-45F7-B382-1E8F62DA7615Q30651852-3BAB87FE-5BC9-4BED-9E88-BB70A2E83611Q33654155-A7CC6EDF-2C65-4FE0-84E8-0B1554DBFC74Q34019828-57534BF2-AE2E-4849-8531-ABF025E1818AQ34369163-3E59DE3D-BF4A-40E2-BB80-6939779E5491Q34625646-AB50F724-E629-4A0C-979F-6824E3C6E494Q35128110-350CF89F-5988-49AB-9664-943B7EFD971BQ35313526-958974E1-6745-4315-BD31-52EB95B7500FQ35847385-B38A0D46-8567-4EBE-A1BB-60A875DE404BQ35853488-FC743D69-DB9B-439A-AD13-CAC8C6274FAEQ35864780-09AADB90-8FFA-4AEC-92DF-B10F5CFE3C38Q35933884-7DDB6B6D-9DA1-4A33-B5A5-94ACFFFFF554Q36626314-C2E48314-A146-4814-9300-6A618925BACAQ36629265-3AD9191A-9277-4648-BA0B-4C10FD38E67FQ36645128-EEB54B3E-F49B-48A2-9E13-AA6A1B2A8A28Q36687225-D3562B73-A52A-4FAA-AA11-874667B7E99BQ36810310-08DAD6EF-BAF5-4B4B-86E1-2491B446C63BQ37111477-DEADA595-AF71-4104-A869-8CC4E32034D8Q37248161-A21B5435-3890-4DED-8E4B-872816A35471Q37600218-0E9DB48E-C27C-46F2-B917-CF7F682D5CF7Q37698214-A8908289-1349-4D88-B501-D9F9006EE692Q38290548-C622FF5F-C66D-4439-9E2F-627E1BC9692CQ38294797-6820D0DC-1AB3-4F66-83D4-5EF7A33D727CQ38300846-2F21539C-4C30-4FD5-99AE-E3293CFB189BQ38314018-A357FB40-6172-461D-B4CB-F331EEFBCA24Q38328581-0C83C4B1-E3F0-45A8-8185-1840CC61E462Q38330143-585A4FDA-340E-4B84-AF03-7A3CE880977BQ38345179-9CE38FA2-501C-47BD-88C2-F4ABD5AE8D22Q38362410-95D80A22-0CB4-453A-80B9-94AAAB597F82Q39594951-20F8A5BD-B6E5-4EB6-B4AF-A414C8BBF783Q40115966-69097C89-172E-42F7-9033-5FA93F7A4051Q40394716-4B2403B4-FE0B-4FB0-831A-79586CBA1ADFQ40416681-05D468F0-3677-4305-A543-3BA5A7375343Q40899915-B8F98C77-4AA2-446C-B888-9423671B3101Q42107901-CE28521A-4D89-4771-8311-BF77A6DA5EE3Q44852086-F6973CDA-1207-42AE-9628-493141A12C39
P2860
Interaction of HIV-1 reverse transcriptase with a synthetic form of its replication primer, tRNA(Lys,3)
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
Interaction of HIV-1 reverse t ...... eplication primer, tRNA(Lys,3)
@en
type
label
Interaction of HIV-1 reverse t ...... eplication primer, tRNA(Lys,3)
@en
prefLabel
Interaction of HIV-1 reverse t ...... eplication primer, tRNA(Lys,3)
@en
P2093
P2860
P356
P1476
Interaction of HIV-1 reverse t ...... eplication primer, tRNA(Lys,3)
@en
P2093
P2860
P304
P356
10.1093/NAR/19.4.751
P407
P577
1991-02-01T00:00:00Z