Reverse transcription in hepatitis B viruses is primed by a tyrosine residue of the polymerase
about
Identification and characterization of avihepadnaviruses isolated from exotic anseriformes maintained in captivityHepatitis B virus replicationEvidence that the RNAseH activity of the duck hepatitis B virus is unable to act on exogenous substratesHepatitis B virus reverse transcriptase: diverse functions as classical and emerging targets for antiviral interventionDirect acting antivirals for the treatment of chronic viral hepatitisMolecular biology of hepatitis B virus infectionInhibition of episomal hepatitis B virus DNA in vitro by 2,4-diamino-7- (2-deoxy-2-fluoro-beta-D-arabinofuranosyl)-pyrrolo[2,3-d]pyrimidineReverse transcription of the pFOXC mitochondrial retroplasmids of Fusarium oxysporum is protein primedA bulged region of the hepatitis B virus RNA encapsidation signal contains the replication origin for discontinuous first-strand DNA synthesisHepatitis B virus molecular biology and pathogenesisNucleic acid chaperone activity associated with the arginine-rich domain of human hepatitis B virus core protein.Mechanism for CCC DNA synthesis in hepadnaviruses.Mapping of the hepatitis B virus reverse transcriptase TP and RT domains by transcomplementation for nucleotide priming and by protein-protein interactionInhibitory effect of 2'-fluoro-5-methyl-beta-L-arabinofuranosyl-uracil on duck hepatitis B virus replication.The duck hepatitis B virus polymerase is activated by its RNA packaging signal, epsilon.In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90.Serine phosphoacceptor sites within the core protein of hepatitis B virus contribute to genome replication pleiotropically.Human hepatitis B virus polymerase interacts with the molecular chaperonin Hsp60.Reconstitution of a functional duck hepatitis B virus replication initiation complex from separate reverse transcriptase domains expressed in Escherichia coliHepatitis B virus biology.The majority of duck hepatitis B virus reverse transcriptase in cells is nonencapsidated and is bound to a cytoplasmic structure.Sequences in the terminal protein and reverse transcriptase domains of the hepatitis B virus polymerase contribute to RNA binding and encapsidationHepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids.Interferon prevents formation of replication-competent hepatitis B virus RNA-containing nucleocapsids.Identification of an essential molecular contact point on the duck hepatitis B virus reverse transcriptaseCharacterization of the antiviral effect of 2',3'-dideoxy-2', 3'-didehydro-beta-L-5-fluorocytidine in the duck hepatitis B virus infection model.Human hepatitis B virus production in avian cells is characterized by enhanced RNA splicing and the presence of capsids containing shortened genomesIn vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins.Distinct requirement for two stages of protein-primed initiation of reverse transcription in hepadnaviruses.Hepatitis B virus reverse transcriptase and epsilon RNA sequences required for specific interaction in vitro.Base pairing between the 5' half of epsilon and a cis-acting sequence, phi, makes a contribution to the synthesis of minus-strand DNA for human hepatitis B virus.Heat shock protein 90-independent activation of truncated hepadnavirus reverse transcriptase.Evidence for multiple distinct interactions between hepatitis B virus P protein and its cognate RNA encapsidation signal during initiation of reverse transcription.Generation of stable cell lines expressing Lamivudine-resistant hepatitis B virus for antiviral-compound screening.The guanine nucleoside analog penciclovir is active against chronic duck hepatitis B virus infection in vivo.2',3'-dideoxy-beta-L-5-fluorocytidine inhibits duck hepatitis B virus reverse transcription and suppresses viral DNA synthesis in hepatocytes, both in vitro and in vivoCryptic protein priming sites in two different domains of duck hepatitis B virus reverse transcriptase for initiating DNA synthesis in vitro.Cytotoxic T lymphocyte responses and CTL epitope escape mutation in HBsAg, anti-HBe positive individuals.Does Tyrosyl DNA Phosphodiesterase-2 Play a Role in Hepatitis B Virus Genome Repair?Complementarity between epsilon and phi sequences in pregenomic RNA influences hepatitis B virus replication efficiency.
P2860
Q24556680-C629CA36-3A71-4330-AB06-CAF9B96814CAQ24563894-A44DC72B-EA55-466C-85AD-D7CE9C90C4F3Q24802171-AA6137FF-334F-4A3D-B1A0-A4D320C213E2Q27013849-1DE374BE-A3BA-4A97-9D2D-0E7E2E1B9107Q27022216-C44B6140-D70C-4051-9C50-9491BF053FDBQ28083478-902F151C-A5DD-41C3-8059-32298D92E873Q28378787-E65D56E9-BBBE-4FD2-8C17-D54A4A0C572DQ28742992-CCC64019-F8DA-47E8-A7CB-E14122DC23E7Q28775714-99239072-E0FB-485B-A040-FA5CBB8C2DE1Q28818406-3920ACB2-3DEC-4F17-915D-050CE000E081Q30357029-2D3EF532-B63E-437B-A712-8F12E3E867BEQ30943676-83980E02-E965-48F6-BC17-87298BBB1E21Q33652843-3749A9C8-C65A-4C2D-89D1-C160FD7147BFQ33689987-A7091224-724F-4AD5-B4C3-4A5B81099148Q33785615-97BA94FE-332F-49EC-8331-3B458017D276Q33812161-A60E17FC-6428-4E2D-BCAC-B4C274D02546Q33831725-5C61F8AA-D251-4F96-8C38-F1CBED7BEF89Q33844349-44133B27-8339-4F4F-BED8-82666CDA21F8Q33852684-5676AD03-1B94-49A6-8000-A9D716D1D5A8Q33855246-056A5485-BD00-440D-B393-9ACAD4C118BBQ33874395-EA0AAF9E-5892-4809-A8AD-FF9F2EE790DEQ33875691-1FA8EE1D-BD05-4D1C-B98A-1181AB4E791FQ33885913-E404550A-2B49-4452-94AC-A33C76FD5ABBQ33896072-68611157-8E2E-40D2-AB58-AF0580F7AADBQ33911921-8EE76645-4E1F-4133-9D33-FB2346F1090AQ33978482-5C206390-5C6E-4E09-9326-65A784ED53EEQ34279855-0195F244-4F61-4F07-A00A-6E7F6DC5F56EQ34327359-13B07522-02DF-443F-8BF3-4BD32A090F12Q34339499-3B3C1B28-09DC-4CC0-A059-AF157F2F4020Q34434801-BF6D2ECE-3601-48C3-BBF8-49B02EB1126DQ34647380-D8C7F087-06EC-4C98-BB85-3FAC04B60A0CQ34860763-D03E0215-0B66-4048-9B83-0366930A8ED5Q34974070-D3260258-EF0E-4D90-B6FE-6865F6634C95Q35014297-C06809AD-1AE9-49DE-B8C5-A4C3D6FEDAEFQ35122451-06746C75-9832-44C1-B09B-6BEBBBEE6B65Q35122499-94817AFE-DEC4-4D1D-8C2C-416916BE8944Q35140266-E992B301-E184-4DCD-984B-8A2D61FA6544Q35360487-E28D16E9-FE7C-4738-9CAF-41A4C4086AA2Q35664939-EEDA0E43-3B97-4DAD-A3E9-66163BF3B6EEQ35748415-AE5884B2-91F0-406E-9ED6-34742228027F
P2860
Reverse transcription in hepatitis B viruses is primed by a tyrosine residue of the polymerase
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Reverse transcription in hepat ...... sine residue of the polymerase
@ast
Reverse transcription in hepat ...... sine residue of the polymerase
@en
type
label
Reverse transcription in hepat ...... sine residue of the polymerase
@ast
Reverse transcription in hepat ...... sine residue of the polymerase
@en
prefLabel
Reverse transcription in hepat ...... sine residue of the polymerase
@ast
Reverse transcription in hepat ...... sine residue of the polymerase
@en
P2860
P1433
P1476
Reverse transcription in hepat ...... sine residue of the polymerase
@en
P2093
P2860
P407
P577
1994-01-01T00:00:00Z