Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Alexis Nazabal"'
Autor:
Xibei Dang, Lars Guelen, David Lutje Hulsik, Grigori Ermakov, Edward J. Hsieh, Joost Kreijtz, Judith Stammen-Vogelzangs, Imke Lodewijks, Astrid Bertens, Arne Bramer, Marco Guadagnoli, Alexis Nazabal, Andrea van Elsas, Thierry Fischmann, Veronica Juan, Amy Beebe, Maribel Beaumont, Hans van Eenennaam
Publikováno v:
mAbs, Vol 15, Iss 1 (2023)
ABSTRACTMonoclonal antibodies have become an important class of therapeutics in the last 30 years. Because the mechanism of action of therapeutic antibodies is intimately linked to their binding epitopes, identification of the epitope of an antibody
Externí odkaz:
https://doaj.org/article/23e30f5d2f8c4516bac906e80f9ad9d7
Autor:
Sneha Singh, Alexis Nazabal, Senthilvelrajan Kaniyappan, Jean-Luc Pellequer, Alisa S. Wolberg, Diana Imhof, Johannes Oldenburg, Arijit Biswas
Publikováno v:
Biomolecules, Vol 9, Iss 12, p 765 (2019)
Factor XIII (FXIII) is a predominant determinant of clot stability, strength, and composition. Plasma FXIII circulates as a pro-transglutaminase with two catalytic A subunits and two carrier-protective B subunits in a heterotetramer (FXIII-A2B2). FXI
Externí odkaz:
https://doaj.org/article/fdcfd7a4dfd149b29f9ac532128b4fb1
Autor:
Benoit Maillot, Nicolas Lévy, Sylvia Eiler, Corinne Crucifix, Florence Granger, Ludovic Richert, Pascal Didier, Julien Godet, Karine Pradeau-Aubreton, Stéphane Emiliani, Alexis Nazabal, Paul Lesbats, Vincent Parissi, Yves Mely, Dino Moras, Patrick Schultz, Marc Ruff
Publikováno v:
PLoS ONE, Vol 8, Iss 4, p e60734 (2013)
Integration of the HIV-1 cDNA into the human genome is catalyzed by the viral integrase (IN) protein. Several studies have shown the importance of cellular cofactors that interact with integrase and affect viral integration and infectivity. In this s
Externí odkaz:
https://doaj.org/article/ae47d79f1a22403bb64619739332bb21
Autor:
Senthilvelrajan Kaniyappan, Alexis Nazabal, Alisa S. Wolberg, Sneha Singh, Jean-Luc Pellequer, Diana Imhof, Arijit Biswas, Johannes Oldenburg
Publikováno v:
Biomolecules
Biomolecules, 2019, 9 (12), pp.765. ⟨10.3390/biom9120765⟩
Volume 9
Issue 12
Biomolecules, MDPI, 2019, 9 (12), pp.765. ⟨10.3390/biom9120765⟩
Biomolecules, Vol 9, Iss 12, p 765 (2019)
Biomolecules 9(12), 765 (2019). doi:10.3390/biom9120765
Biomolecules, 2019, 9 (12), pp.765. ⟨10.3390/biom9120765⟩
Volume 9
Issue 12
Biomolecules, MDPI, 2019, 9 (12), pp.765. ⟨10.3390/biom9120765⟩
Biomolecules, Vol 9, Iss 12, p 765 (2019)
Biomolecules 9(12), 765 (2019). doi:10.3390/biom9120765
Factor XIII (FXIII) is a predominant determinant of clot stability, strength, and composition. Plasma FXIII circulates as a pro-transglutaminase with two catalytic A subunits and two carrier-protective B subunits in a heterotetramer (FXIII-A2B2). FXI
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56bc67ee039e72970e7eb9710e96eaa2
https://hal.science/hal-02413110
https://hal.science/hal-02413110
Autor:
V. Ivaškevičius, Jean-Luc Pellequer, Arijit Biswas, Diana Imhof, S. Singh, Alexis Nazabal, J. Oldenburg, S. Kanniyappan
Publikováno v:
Science meets clinical practice.
Publikováno v:
Journal of Mass Spectrometry. 44:965-977
Understanding the structural basis that distinguishes the amyloid form of the prion protein from its monomeric homologue is of crucial importance to elucidate the mechanism of the lethal diseases related to this protein. Recently, an in vitro convers
Autor:
Uwe Riek, Marianne Suter, Michael Hennig, Philippe Ringler, Alexis Nazabal, Renato Zenobi, Peter V. Konarev, Roland W. Scholz, Arne C. Rufer, D. I. Svergun, Uwe Schlattner, Michael Forstner, Theo Wallimann, Andreas Engel, Mohamed Chami, Dietbert Neumann, Shirley A. Müller
Publikováno v:
Journal of Biological Chemistry. 283:18331-18343
Heterotrimeric AMP-activated protein kinase (AMPK) is crucial for energy homeostasis of eukaryotic cells and organisms. Here we report on (i) bacterial expression of untagged mammalian AMPK isoform combinations, all containing gamma(1), (ii) an autom
Autor:
Eléonore Lepvrier, Vincent Peyrot, Renan Goude, Daniel Thomas, Alexis Nazabal, Diane Allegro, Laura Moullintraffort, Pascale Barbier, Michaël Nigen, Cyrille Garnier
Publikováno v:
Analytical Chemistry
Analytical Chemistry, American Chemical Society, 2015, 87 (14), pp.7043-7051. ⟨10.1021/acs.analchem.5b00051⟩
Analytical Chemistry, 2015, 87 (14), pp.7043-7051. ⟨10.1021/acs.analchem.5b00051⟩
Analytical Chemistry, American Chemical Society, 2015, 87 (14), pp.7043-7051. ⟨10.1021/acs.analchem.5b00051⟩
Analytical Chemistry, 2015, 87 (14), pp.7043-7051. ⟨10.1021/acs.analchem.5b00051⟩
International audience; The 90-kDa heat shock protein (Hsp90) is a highly flexible dimer able to self-associate in the presence of divalent cations or under heat shock. This study investigated the relationship between Hsp90 oligomers and the Hsp90 co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::941fbb2636812f153e41c130d929ff5a
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01175535
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01175535
Autor:
Eléonore Lepvrier, Alexis Nazabal, Sophie Chat, Daniel Thomas, Michaël Nigen, Cyrille Garnier, Diane Allegro, Laura Moullintraffort, Pascale Barbier
Publikováno v:
Biochimica et Biophysica Acta Proteins and Proteomics
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2015, 1854 (10), pp.1412-1424. ⟨10.1016/j.bbapap.2015.07.003⟩
Biochimica et Biophysica Acta Proteins and Proteomics, 2015, 1854 (10), pp.1412-1424. ⟨10.1016/j.bbapap.2015.07.003⟩
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2015, 1854 (10), pp.1412-1424. ⟨10.1016/j.bbapap.2015.07.003⟩
Biochimica et Biophysica Acta Proteins and Proteomics, 2015, 1854 (10), pp.1412-1424. ⟨10.1016/j.bbapap.2015.07.003⟩
International audience; The 90-kDa heat shock protein (Hsp90) is a highly flexible dimer that is able to self-associate in the presence of divalent cations or under heat shock. In a previous work, we focused on the Mg2+-induced oligomerization proces
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51787a00b44ee81f12a071bdc81b39cc
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01174219
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01174219
Autor:
Laura Moullintraffort, Eléonore Lepvrier, Cyrille Garnier, Alexis Nazabal, Cyrielle Doigneaux
Publikováno v:
Analytical Chemistry
Analytical Chemistry, American Chemical Society, 2014, 86 (21), pp.10524-10530. ⟨10.1021/ac502561e⟩
Analytical Chemistry, 2014, 86 (21), pp.10524-10530. ⟨10.1021/ac502561e⟩
Analytical Chemistry, American Chemical Society, 2014, 86 (21), pp.10524-10530. ⟨10.1021/ac502561e⟩
Analytical Chemistry, 2014, 86 (21), pp.10524-10530. ⟨10.1021/ac502561e⟩
Since noncovalent protein macrocomplexes are implicated in many cellular functions, their characterization is essential to understand how they drive several biological processes. Over the past 20 years, because of its high sensitivity, mass spectrome