The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Editor

Share

Personal info

View

Links

Table of contents

About

Terms

 

Chemical Compound Review: 

AZT TP     [[2-[(2R,3S,5R)-3-azido-5-(5- methyl-2,4...

Synonyms: AC1L9RVF, AZTTP, 5'MePO3H2 deriv.
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of AZT TP

  • Carbovir-TP was a potent inhibitor of HIV-1 reverse transcriptase using either template with Ki values similar to that observed by AZT-TP, ddGTP, and ddTTP [1].
  • The effects of their anabolic products, AZT-triphosphate (AZT-TP) and ddCTP on human cellular DNA metabolic processes were studied using highly purified, structurally and enzymatically defined forms of the two major human host DNA polymerases, alpha and beta, and compared to those of the reverse transcriptase purified from HIV viron [2].
  • In addition, the reduced toxicity of 3a and 4a toward CEM cells relative to AZT correlated with reduced levels of total phosphorylated AZT and not AZT-TP [3].
  • In the present study, templates containing a specific segment of the G gamma-globin gene were constructed and incorporation of 3'-azido-3'-deoxythymidine 5'-triphosphate (AZT-TP) or 2',3'-dideoxythymidine 5'-triphosphate (ddTTP) into these templates was compared to that observed in M13 bacteriophage DNA [4].
  • The inhibition of HSV-1 DNA polymerase and HeLa DNA polymerases alpha and beta by diphosphoryl derivatives of acyclic phosphonylmethoxyalkyl nucleotide analogues was studied and compared with the inhibition by ACV-TP, araCTP, ddTTP and AZT-TP [5].
 

High impact information on AZT TP

  • The efficiency of dTTP incorporation was unchanged for the D246V enzyme, indicating that the substantial decrease in AZT-TP incorporation is responsible for its drug resistance [6].
  • In contrast to AZT-TP (control), none of these nucleosides displayed any significant inhibition of RT in the recombinant enzyme assay, indicating that phosphorylation is a necessary prerequisite for activity [7].
  • Pretreatment of HIV-1 virions with physiologic NERT-stimulants and 3'-azido-3'-deoxythymidine 5'-triphosphate (AZT-TP) or nevirapine potently inactivated cell-free HIV-1 virions and resulted in strong inhibition of the viral infectivity [8].
  • BACKGROUND: 3'-azido-2',3'-dideoxythymidine (AZT) is phosphorylated intracellularly to 3'-azido-3'-deoxythymidine-5'-triphosphate (AZT-TP), which is incorporated into telomeric DNA, thereby blocking chain elongation [9].
  • Telomerase inhibitors such as 7-deaza-dGTP and AZT-TP, when used with the cytoplasmic extract of gametocytes in the Pf-TRAP assay, efficiently inhibit the product, which confirms the presence of telomerase in the gametocytes [10].
 

Anatomical context of AZT TP

  • The assay constitutes a very convenient tool permitting easy, precise studies of the first step of the intracellular metabolism of AZT leading to the formation of AZT-TP in cultured cells [11].
 

Analytical, diagnostic and therapeutic context of AZT TP

  • The gel retardation assay was utilized to examine also the effect of various HIV-1 RT inhibitors (i.e., AZT-TP, ddTTP, TIBO, and 3,5,8-trihydroxy-4-quinolone) on the enzyme-DNA interaction [12].
  • In this paper, we first describe the development of two enzyme immunoassays (EIA) of AZT-TP in PBMCs: one directly measuring AZT-TP content; the other, measuring the nucleoside AZT after selective extraction of AZT-TP and dephosphorylation [13].

References

  1. Mechanism of inhibition of human immunodeficiency virus type 1 reverse transcriptase and human DNA polymerases alpha, beta, and gamma by the 5'-triphosphates of carbovir, 3'-azido-3'-deoxythymidine, 2',3'-dideoxyguanosine and 3'-deoxythymidine. A novel RNA template for the evaluation of antiretroviral drugs. Parker, W.B., White, E.L., Shaddix, S.C., Ross, L.J., Buckheit, R.W., Germany, J.M., Secrist, J.A., Vince, R., Shannon, W.M. J. Biol. Chem. (1991) [Pubmed]
  2. Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. Copeland, W.C., Chen, M.S., Wang, T.S. J. Biol. Chem. (1992) [Pubmed]
  3. Amino acid phosphoramidate monoesters of 3'-azido-3'-deoxythymidine: relationship between antiviral potency and intracellular metabolism. Chang , S., Griesgraber, G.W., Southern, P.J., Wagner, C.R. J. Med. Chem. (2001) [Pubmed]
  4. Influence of template primary structure on 3'-azido-3'-deoxythymidine triphosphate incorporation into DNA. Bridges, E.G., LeBoeuf, R.B., Weidner, D.A., Sommadossi, J.P. Antiviral Res. (1993) [Pubmed]
  5. Inhibition of herpes simplex virus DNA polymerase by diphosphates of acyclic phosphonylmethoxyalkyl nucleotide analogues. Merta, A., Votruba, I., Rosenberg, I., Otmar, M., Hrebabecký, H., Bernaerts, R., Holý, A. Antiviral Res. (1990) [Pubmed]
  6. 3'-Azido-3'-deoxythymidine-resistant mutants of DNA polymerase beta identified by in vivo selection. Kosa, J.L., Sweasy, J.B. J. Biol. Chem. (1999) [Pubmed]
  7. Preparation and anti-HIV activity of N-3-substituted thymidine nucleoside analogs. Adams, D.R., Perez, C., Maillard, M., Florent, J.C., Evers, M., Hénin, Y., Litvak, S., Litvak, L., Monneret, C., Grierson, D.S. J. Med. Chem. (1997) [Pubmed]
  8. Inhibition of endogenous reverse transcription of human and nonhuman primate lentiviruses: Potential for development of lentivirucides. Argyris, E.G., Dornadula, G., Nunnari, G., Acheampong, E., Zhang, C., Mehlman, K., Pomerantz, R.J., Zhang, H. Virology (2006) [Pubmed]
  9. Cyclic induction of senescence with intermittent AZT treatment accelerates both apoptosis and telomere loss. Ji, H.J., Rha, S.Y., Jeung, H.C., Yang, S.H., An, S.W., Chung, H.C. Breast Cancer Res. Treat. (2005) [Pubmed]
  10. Identification of telomerase activity in gametocytes of Plasmodium falciparum. Raj, D.K., Das, B.R., Dash, A.P., Supakar, P.C. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  11. Monitoring of intracellular levels of 5'-monophosphate-AZT using an enzyme immunoassay. Goujon, L., Brossette, T., Dereudre-Bosquet, N., Creminon, C., Clayette, P., Dormont, D., Mioskowski, C., Lebeau, L., Grassi, J. J. Immunol. Methods (1998) [Pubmed]
  12. Interaction of the reverse transcriptase of human immunodeficiency virus type 1 with DNA. Bakhanashvili, M., Hizi, A. Biochemistry (1994) [Pubmed]
  13. Development of a direct assay for measuring intracellular AZT triphosphate in humans peripheral blood mononuclear cells. Becher, F., Schlemmer, D., Pruvost, A., Nevers, M.C., Goujard, C., Jorajuria, S., Guerreiro, C., Brossette, T., Lebeau, L., Créminon, C., Grassi, J., Benech, H. Anal. Chem. (2002) [Pubmed]
Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
 
WikiGenes - Universities