The duck hepatitis B virus reverse transcriptase functions as a full-length monomer. - Wikidata - awgldk - TriplyDB

The duck hepatitis B virus reverse transcriptase functions as a full-length monomer.

The duck hepatitis B virus reverse transcriptase functions as a full-length monomer.

http://www.wikidata.org/entity/Q40226948

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Hepatitis B virus reverse transcriptase: diverse functions as classical and emerging targets for antiviral intervention Encapsidated hepatitis B virus reverse transcriptase is poised on an ordered RNA lattice TP-RT domain interactions of duck hepatitis B virus reverse transcriptase in cis and in trans during protein-primed initiation of DNA synthesis in vitro.Functional and structural dynamics of hepadnavirus reverse transcriptase during protein-primed initiation of reverse transcription: effects of metal ions.Reverse transcriptase- and RNA packaging signal-dependent incorporation of APOBEC3G into hepatitis B virus nucleocapsids.trans-Complementation of HBV rtM204I mutant replication by HBV wild-type polymerase.Maturation-associated destabilization of hepatitis B virus nucleocapsid.Characterization of the pleiotropic effects of the genotype G-specific 36-nucleotide insertion in the context of other hepatitis B virus genotypes.Purification and enzymatic characterization of the hepatitis B virus ribonuclease H, a new target for antiviral inhibitors.Characterization of novel hepadnaviral RNA species accumulated in hepatoma cells treated with viral DNA polymerase inhibitors A Tyr residue in the reverse transcriptase domain can mimic the protein-priming Tyr residue in the terminal protein domain of a hepadnavirus P protein

P2860

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P2860

The duck hepatitis B virus reverse transcriptase functions as a full-length monomer.

http://www.wikidata.org/entity/Q40226948

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

2006年论文

@zh

2006年论文

@zh-cn

name

The duck hepatitis B virus reverse transcriptase functions as a full-length monomer.

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type

label

The duck hepatitis B virus reverse transcriptase functions as a full-length monomer.

@en

prefLabel

The duck hepatitis B virus reverse transcriptase functions as a full-length monomer.

@en

P1433

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P1433

Journal of Biological Chemistry

P1476

The duck hepatitis B virus reverse transcriptase functions as a full-length monomer.

@en

P2093

John E Tavis

http://www.w3.org/2001/XMLSchema#string

Zhian Zhang

http://www.w3.org/2001/XMLSchema#string

P2860

Epitope tagging and protein surveillance

Expression of the P-protein of the human hepatitis B virus in a vaccinia virus system and detection of the nucleocapsid-associated P-gene product by radiolabelling at newly introduced phosphorylation sites.

In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90.

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 coli

The majority of duck hepatitis B virus reverse transcriptase in cells is nonencapsidated and is bound to a cytoplasmic structure.

Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids.

Identification of an essential molecular contact point on the duck hepatitis B virus reverse transcriptase

HIV expression strategies: ribosomal frameshifting is directed by a short sequence in both mammalian and yeast systems.

Duck hepatitis B virus virion secretion requires a double-stranded DNA genome.

P304

35794-35801

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P31

scholarly article

P356

10.1074/JBC.M608031200

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P407

P433

47

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P478

281

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P577

2006-09-27T00:00:00Z

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P698

17005569

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