pubmed-article:14742682 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14742682 | lifeskim:mentions | umls-concept:C0019169 | lld:lifeskim |
pubmed-article:14742682 | lifeskim:mentions | umls-concept:C0012892 | lld:lifeskim |
pubmed-article:14742682 | lifeskim:mentions | umls-concept:C0006933 | lld:lifeskim |
pubmed-article:14742682 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:14742682 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
pubmed-article:14742682 | lifeskim:mentions | umls-concept:C2257391 | lld:lifeskim |
pubmed-article:14742682 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
pubmed-article:14742682 | lifeskim:mentions | umls-concept:C0146894 | lld:lifeskim |
pubmed-article:14742682 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:14742682 | pubmed:dateCreated | 2004-1-26 | lld:pubmed |
pubmed-article:14742682 | pubmed:abstractText | The use of L(-)SddC [beta-L-2',3'-dideoxy-3'-thiacytidine (lamivudine, 3TC)] for the treatment of Herpes B virus (HBV) infection is hindered by the emergence of drug-resistance associated with the L526M, L550V, and L526M/M550V mutations of the viral DNA polymerase (DP). The interactions of the anti-HBV compounds 2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorode-oxycytidine and 2'-fluoro-5-methyl-beta-L-arabinofuranosyluracil triphosphate with HBV DP and its L(-)SddC-associated mutants have not been studied. The e antigen-negative variant of HBV associated with the G1896A mutation in the precore region has a high prevalence. Its effect on HBV DP is unclear. Because HBV DNA synthesis occurs in the nucleocapsid, we examined the kinetics of the reverse transcriptase activity from wild-type (wt) and mutated DPs with the wt or G1896A-mutated RNA template in the nucleocapsid. The effects of this template mutation on the activities of these L-nucleoside triphosphates were also examined. Results indicated that these DP mutations increased the Km values of deoxy-NTPs and decreased the efficiencies (Vmax/Km) of DPs. The additional L526M mutation increased the efficiency of the M550V-mutated DP but no more than that of the L526M-mutated DP. The G1896A mutation had impacts on the interactions between different DPs and deoxy-NTPs, except dCTP. It also had different impacts on the actions of the L-nucleoside triphosphates toward DPs. The L526M and M550V mutations caused a greater decrease in the Vmax using the wt RNA template compared with the G1896A-mutated template. The L526M, M550V, and L526M/M550V mutations caused varying degrees of resistance to the different M-nucleoside triphosphates. | lld:pubmed |
pubmed-article:14742682 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14742682 | pubmed:language | eng | lld:pubmed |
pubmed-article:14742682 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14742682 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14742682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14742682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14742682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14742682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14742682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14742682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14742682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14742682 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14742682 | pubmed:month | Feb | lld:pubmed |
pubmed-article:14742682 | pubmed:issn | 0026-895X | lld:pubmed |
pubmed-article:14742682 | pubmed:author | pubmed-author:LamWingW | lld:pubmed |
pubmed-article:14742682 | pubmed:author | pubmed-author:LiouJieh-Yuan... | lld:pubmed |
pubmed-article:14742682 | pubmed:author | pubmed-author:YingLiL | lld:pubmed |
pubmed-article:14742682 | pubmed:author | pubmed-author:ChengYung-chi... | lld:pubmed |
pubmed-article:14742682 | pubmed:author | pubmed-author:DutschmanGing... | lld:pubmed |
pubmed-article:14742682 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14742682 | pubmed:volume | 65 | lld:pubmed |
pubmed-article:14742682 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14742682 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14742682 | pubmed:pagination | 400-6 | lld:pubmed |
pubmed-article:14742682 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:14742682 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:14742682 | pubmed:articleTitle | Reverse transcriptase activity of hepatitis B virus (HBV) DNA polymerase within core capsid: interaction with deoxynucleoside triphosphates and anti-HBV L-deoxynucleoside analog triphosphates. | lld:pubmed |
pubmed-article:14742682 | pubmed:affiliation | Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520, USA. | lld:pubmed |
pubmed-article:14742682 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14742682 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14742682 | lld:pubmed |