Zobrazeno 1 - 8
of 8
pro vyhledávání: '"MESH: DNA Nucleotidylexotransferase"'
Autor:
Marc Delarue, Jérôme Loc’h
Publikováno v:
Current Opinion in Structural Biology
Current Opinion in Structural Biology, 2018, 53, pp.22-31. ⟨10.1016/j.sbi.2018.03.019⟩
Current Opinion in Structural Biology, Elsevier, 2018, 53, pp.22-31. ⟨10.1016/j.sbi.2018.03.019⟩
Current Opinion in Structural Biology, 2018, 53, pp.22-31. ⟨10.1016/j.sbi.2018.03.019⟩
Current Opinion in Structural Biology, Elsevier, 2018, 53, pp.22-31. ⟨10.1016/j.sbi.2018.03.019⟩
International audience; Terminal deoxynucleotidyltransferase (TdT) is a member of the polX family which is involved in DNA repair. It has been known for years as an untemplated DNA polymerase used during V(D)J recombination to generate diversity at t
Publikováno v:
Structure
Structure, Elsevier (Cell Press), 2016, 24 (9), pp.1452-1463. ⟨10.1016/j.str.2016.06.014⟩
Structure, 2016, 24 (9), pp.1452-1463. ⟨10.1016/j.str.2016.06.014⟩
Structure, Elsevier (Cell Press), 2016, 24 (9), pp.1452-1463. ⟨10.1016/j.str.2016.06.014⟩
Structure, 2016, 24 (9), pp.1452-1463. ⟨10.1016/j.str.2016.06.014⟩
International audience; Eukaryotic DNA polymerase of the polX family, such as pol μ and terminal deoxynucleotidyl transferase (TdT), are key components of the non-homologous end-joining or V(D)J recombination machinery, respectively. The established
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2013, 425 (22), pp.4334-4352. ⟨10.1016/j.jmb.2013.07.009⟩
Journal of Molecular Biology, 2013, 425 (22), pp.4334-4352. ⟨10.1016/j.jmb.2013.07.009⟩
Journal of Molecular Biology, Elsevier, 2013, 425 (22), pp.4334-4352. ⟨10.1016/j.jmb.2013.07.009⟩
Journal of Molecular Biology, 2013, 425 (22), pp.4334-4352. ⟨10.1016/j.jmb.2013.07.009⟩
International audience; Terminal deoxynucleotidyltransferase (Tdt) is a non-templated eukaryotic DNA polymerase of the polX family that is responsible for the random addition of nucleotides at the V(D)J junctions of immunoglobulins and T-cell recepto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59028c68803a9c52064bd4a85d088521
https://hal-pasteur.archives-ouvertes.fr/pasteur-02174639
https://hal-pasteur.archives-ouvertes.fr/pasteur-02174639
Autor:
Roberta Costi, Luca Pescatori, Jerome Gouge, Pietro Campiglia, Bruno Maresca, Giuliana Cuzzucoli Crucitti, Marc Delarue, Luigi Scipione, Giovanni Maga, Ettore Novellino, Antonella Messore, Silvano Tortorella, Ilaria Granata, Amalia Porta, Roberto Di Santo, Alessandra Amoroso, Emmanuele Crespan
Publikováno v:
Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, American Chemical Society, 2013, 56 (18), pp.7431-41. ⟨10.1021/jm4010187⟩
Journal of Medicinal Chemistry, 2013, 56 (18), pp.7431-41. ⟨10.1021/jm4010187⟩
Journal of Medicinal Chemistry, American Chemical Society, 2013, 56 (18), pp.7431-41. ⟨10.1021/jm4010187⟩
Journal of Medicinal Chemistry, 2013, 56 (18), pp.7431-41. ⟨10.1021/jm4010187⟩
International audience; Terminal deoxynucletidyl transferase (TdT) is overexpressed in some cancer types, where it might compete with pol μ during the mutagenic repair of double strand breaks (DSBs) through the nonhomologous end joining (NHEJ) pathw
Autor:
Jean-Luc Jestin, Sophie Vichier-Guerre
Publikováno v:
Research in Microbiology
Research in Microbiology, 2005, 156 (10), pp.961-6. ⟨10.1016/j.resmic.2005.09.004⟩
Research in Microbiology, Elsevier, 2005, 156 (10), pp.961-6. ⟨10.1016/j.resmic.2005.09.004⟩
Research in Microbiology, 2005, 156 (10), pp.961-6. ⟨10.1016/j.resmic.2005.09.004⟩
Research in Microbiology, Elsevier, 2005, 156 (10), pp.961-6. ⟨10.1016/j.resmic.2005.09.004⟩
For identification of mutations associated with the broadening of enzyme substrate specificity, three strategies, including directed enzyme evolution, are described for selected examples. Implications concerning enzyme models are highlighted. Applica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d971b6da786bf48cefbdbf8a5ea6a1b
https://hal-pasteur.archives-ouvertes.fr/pasteur-00166275
https://hal-pasteur.archives-ouvertes.fr/pasteur-00166275
Autor:
Thierry Kortulewski, Pierre Vaigot, Pascal Soularue, Olivier Alibert, Alexandre Pawlik, Diana Tronik-Le Roux, Beatrice Jacquelin, Xavier Gidrol, Christophe Joubert, Gaëtan Gruel
Publikováno v:
Blood
Blood, 2005, 106 (6), pp.1965-1974. ⟨10.1182/blood-2004-10-3975⟩
Blood, American Society of Hematology, 2005, 106 (6), pp.1965-1974. ⟨10.1182/blood-2004-10-3975⟩
Blood, 2005, 106 (6), pp.1965-1974. ⟨10.1182/blood-2004-10-3975⟩
Blood, American Society of Hematology, 2005, 106 (6), pp.1965-1974. ⟨10.1182/blood-2004-10-3975⟩
Our knowledge of the molecular mechanisms that regulate hematopoiesis in physiologic and pathologic conditions is limited. Using a molecular approach based on cDNA microarrays, we demonstrated the emergence of an alternative pathway for mature bone m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce1baebfd8aadf84afd6872961147eda
https://hal-pasteur.archives-ouvertes.fr/pasteur-02618902
https://hal-pasteur.archives-ouvertes.fr/pasteur-02618902
Autor:
N. Jourdan, Julien Lescar, Catherine Papanicolaou, Marc Delarue, Jean-Baptiste Boulé, N. Sukumar, François Rougeon, N. Expert-Bezancon
Publikováno v:
EMBO Journal
EMBO Journal, 2002, 21 (3), pp.427-439. ⟨10.1093/emboj/21.3.427⟩
EMBO Journal, 2002, 21 (3), pp.427-439. ⟨10.1093/emboj/21.3.427⟩
International audience; The crystal structure of the catalytic core of murine terminal deoxynucleotidyltransferase (TdT) at 2.35 A resolution reveals a typical DNA polymerase beta-like fold locked in a closed form. In addition, the structures of two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ee33bdb2d6c21f43af771a47b7975b5
https://hal-pasteur.archives-ouvertes.fr/pasteur-04089359
https://hal-pasteur.archives-ouvertes.fr/pasteur-04089359
Publikováno v:
Immunity
Immunity, Elsevier, 2006, 25 (1), pp.31-41. 〈10.1016/j.immuni.2006.04.013〉
Immunity, 2006, 25 (1), pp.31-41. ⟨10.1016/j.immuni.2006.04.013⟩
Immunity, Elsevier, 2006, 25 (1), pp.31-41. ⟨10.1016/j.immuni.2006.04.013⟩
Immunity, Elsevier, 2006, 25 (1), pp.31-41. 〈10.1016/j.immuni.2006.04.013〉
Immunity, 2006, 25 (1), pp.31-41. ⟨10.1016/j.immuni.2006.04.013⟩
Immunity, Elsevier, 2006, 25 (1), pp.31-41. ⟨10.1016/j.immuni.2006.04.013⟩
International audience; DNA polymerases mu (pol mu), lambda (pol lambda), and terminal deoxynucleotidyltransferase (TdT) are enzymes of the pol X family that share homology in sequence and functional domain organization. We showed previously that pol