Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Danièle Tharaud"'
Autor:
B. Delord, Gérard Déléris, Laura Tarrago-Litvak, M. C. Guillorit, Marie-Line Andreola, Danièle Tharaud, Hervé Fleury, J. Lafay
Publikováno v:
European Journal of Medicinal Chemistry. 31:111-122
Summary In order to prepare novel antiretroviral lead compounds active against human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT), a family of C-silylalkylated heterocyclic derivatives were synthesized. One of these derivatives 3 in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2002e011244ed39f953fbee6d58648bd
https://doi.org/10.1016/0223-5234(96)80444-2
https://doi.org/10.1016/0223-5234(96)80444-2
Autor:
Laura Tarrago-Litvak, Rim El Dirani-Diab, Philip J. Barr, Danièle Tharaud, G.A. Nevinsky, Marie-Line Andreola, Simon Litvak
Publikováno v:
FEBS Letters. 301:23-28
The biochemical properties of the p51 subunit of HIV-1 reverse transcriptase (RT) were studied in order to understand its role in the heterodimeric form p66/p51 found in virions. A recombinant form of RT, p51/p51, expressed in yeast, was purified and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e23844587917c143a0fddd218caee56
https://doi.org/10.1016/0014-5793(92)80202-r
https://doi.org/10.1016/0014-5793(92)80202-r
Autor:
Laura Tarrago-Litvak, Michel Fournier, Philip J. Barr, Danièle Tharaud, Marie-Line Sallafranque-Andreola, Leila Sarih-Cottin, Dominique Robert, Bruno Bordier, Simon Litvak
Publikováno v:
Nucleic Acids Research. 18:429-436
Human immunodeficiency virus (HIV) reverse transcriptase (RT) uses host tRNA(Lys) partially annealed to the primer binding site (PBS) as primer for the initiation of cDNA synthesis. When assaying cDNA synthesis with a template-primer complex formed b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38653b385d2ec61897cdcf4343963605
https://doi.org/10.1093/nar/18.3.429
https://doi.org/10.1093/nar/18.3.429
Publikováno v:
Biochimie. 75(1-2)
A recombinant homodimer p66/p66 of the HIV-1 reverse transcriptase (RT) was expressed in and purified from a protease-deficient strain of the yeast Saccharomyces cerevisiae. The RNase H activity associated with the homodimer was biochemically charact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1224136ed29ba60961b63160fbff758
https://pubmed.ncbi.nlm.nih.gov/7684932
https://pubmed.ncbi.nlm.nih.gov/7684932
Autor:
Simon Litvak, Philip J. Barr, Marie-Line Andreola, Asja S. Levina, Danièle Tharaud, Laura Tarrago-Litvak, Vitalyi I. Jamkovoy, G.A. Nevinsky
Publikováno v:
European journal of biochemistry. 207(1)
The kinetics of copying of poly(A) · (dT)n, poly(A) · (U)n, poly(dA) · (dT)n and poly(A) · (dT)9-U by reverse transcriptase of human immunodeficiency virus-1 (HIV-1) has been studied and the binding affinity of the enzyme, for template or primer,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27de923855471b7c9e2b6cc416d4ffaf
https://pubmed.ncbi.nlm.nih.gov/1378404
https://pubmed.ncbi.nlm.nih.gov/1378404
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 866:222-232
Diadenosine 5′,5‴- P 1 , P 4 -tetraphosphate (Ap 4 A) stimulates DNA synthesis in Xenopus laevis oocytes in the presence of activated DNA as template. Besides Ap 4 A, other analogues such as Ap 3 A, ATP and other derivatives are able to stimulate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3bc12f475c6778da8d3be8dcd3dbfb7f
https://doi.org/10.1016/0167-4781(86)90047-3
https://doi.org/10.1016/0167-4781(86)90047-3
Publikováno v:
Developmental biology. 103(2)
Ap4A stimulated DNA synthesis when injected into oocytes. The stimulation was dramatically increased when an exogenous template was microinjected. Aphidicolin inhibited the effect of Ap4A, supporting a role of DNA polymerase alpha in this process. No
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b7c98887988f12a43ad79d242fe29fd
https://pubmed.ncbi.nlm.nih.gov/6724135
https://pubmed.ncbi.nlm.nih.gov/6724135