Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Johann Stojko"'
Autor:
Frederik Rainer Ehrmann, Johann Stojko, Alexander Metz, François Debaene, Luzi Jakob Barandun, Andreas Heine, François Diederich, Sarah Cianférani, Klaus Reuter, Gerhard Klebe
Publikováno v:
PLoS ONE, Vol 12, Iss 4, p e0175723 (2017)
For the efficient pathogenesis of Shigella, the causative agent of bacillary dysentery, full functionality of tRNA-guanine transglycosylase (TGT) is mandatory. TGT performs post-transcriptional modifications of tRNAs in the anticodon loop taking impa
Externí odkaz:
https://doaj.org/article/daa5507fa1614209b8c0af23f4c2b513
Publikováno v:
Melatonin ISBN: 9781071625927
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::df2aeef1b824fb85d31010a98220c646
https://doi.org/10.1007/978-1-0716-2593-4_34
https://doi.org/10.1007/978-1-0716-2593-4_34
Autor:
Estelle Marcheteau, Anne Rouch, Jean A. Boutin, Sophie Landron, Johann Stojko, Gilles Ferry, Benjamin Fould, Elodie Jeantet, Alicia Schirer
Publikováno v:
Molecular biology reports. 49(1)
Posttranslational modifications of proteins are catalyzed by a large family of enzymes catalyzing many chemical modifications. One can hijack the natural use of those enzymes to modify targeted proteins with synthetic chemical moieties. The lipoic ac
Autor:
Estelle Marcheteau, Gilles Ferry, Charline Fagnen, Mathias Antoine, Eric Chabrol, Sophie Landron, Benjamin Fould, Jean A. Boutin, Catherine Vénien-Bryan, Johann Stojko, Sophie-Pénélope Guenin
Publikováno v:
Protein Science
Protein Science, 2021, 30 (9), pp.1946-1957. ⟨10.1002/pro.4147⟩
Protein Sci
Protein Science, 2021, 30 (9), pp.1946-1957. ⟨10.1002/pro.4147⟩
Protein Sci
International audience; VHH stands for the variable regions of heavy chain only of camelid IgGs. The VHH family forms a set of interesting proteins derived from antibodies that maintain their capacity to recognize the antigen, despite their relativel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::537c78ea89460cd53890faa14c59276d
https://hal.sorbonne-universite.fr/hal-03278612v1/document
https://hal.sorbonne-universite.fr/hal-03278612v1/document
Autor:
Gilles Ferry, Alexandre Nicolas, Mathias Antoine, Benjamin Fould, Eric Chabrol, Johann Stojko, Jean A. Boutin, Sarah Cianférani, Thomas Botzanowski
Publikováno v:
Analytical Biochemistry
Analytical Biochemistry, Elsevier Masson, 2020, 589, pp.113491. ⟨10.1016/j.ab.2019.113491⟩
Analytical Biochemistry, Elsevier Masson, 2020, 589, pp.113491. ⟨10.1016/j.ab.2019.113491⟩
International audience; Among the biological approaches to therapeutics, are the cells, such as CAR-T cells engineered or not, the antibodies armed or not, and the smaller protein scaffolds that can be modified to render them specific of other protei
Autor:
Aakash Patel, Hala Guedouari, Elzbieta Janda, Karine Reybier, Istvan Gacsalyi, Vishalgiri Goswami, Jean A. Boutin, Adeline Giganti, Mathias Antoine, Monivan Chhour, Marie-Claude Viaud-Massuard, Hervé Da Costa, Marc Bertrand, Pierre Ducrot, Jérôme Paysant, Patrick P. Michel, Gilles Ferry, Thierry Le Diguarher, Daniel A. Kane, Françoise Nepveu, Frédéric Bouillaud, Karen Brebner, Gérald Guillaumet, Etienne C. Hirsch, Philippe Dupuis, Johann Stojko
Publikováno v:
Molecular Pharmacology
Molecular Pharmacology, American Society for Pharmacology and Experimental Therapeutics, 2019, 95 (3), pp.269-285. ⟨10.1124/mol.118.114231⟩
Molecular Pharmacology, 2019, 95 (3), pp.269-285. ⟨10.1124/mol.118.114231⟩
Molecular Pharmacology, American Society for Pharmacology and Experimental Therapeutics, 2019, 95 (3), pp.269-285. ⟨10.1124/mol.118.114231⟩
Molecular Pharmacology, 2019, 95 (3), pp.269-285. ⟨10.1124/mol.118.114231⟩
International audience; Quinone reductase 2 (QR2, E.C. 1.10.5.1) is an enzyme with a feature that has attracted attention for several decades: in standard conditions, instead of recognizing NAD(P)H as an electron donor, it recognizes putative metabol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c332ae7dd4579c5014783569d4574301
https://www.hal.inserm.fr/inserm-02334766
https://www.hal.inserm.fr/inserm-02334766
Autor:
Alain Van Dorsselaer, Sergii Kolodych, J.-Y. Bonnefoy, Sarah Cianférani, Alain Wagner, Jitka Eberova, Zoljargal Baatarkhuu, Johann Stojko, Oleksandr Koniev
Publikováno v:
Bioconjugate Chemistry. 26:1863-1867
Thiols are among the most frequently used functional groups in the field of bioconjugation. While there exists a variety of heterobifunctional reagents that allow for coupling thiols to other functions (e.g., amines, carboxylic acids), there is no sp
Autor:
Amélie Vallet-Courbin, Alain Van Dorsselaer, Sébastien Fribourg, Lionel Beaurepaire, Lionel Minvielle-Sebastia, Stéphane Chaignepain, Jean-Marie Schmitter, Sarah Cianférani, Adrien F. Dupin, Johann Stojko
Publikováno v:
International Journal of Mass Spectrometry
International Journal of Mass Spectrometry, Elsevier, 2017, 420, pp.57-66. ⟨10.1016/j.ijms.2016.08.005⟩
International Journal of Mass Spectrometry, Elsevier, 2017, 420, pp.57-66. ⟨10.1016/j.ijms.2016.08.005⟩
The cleavage/polyadenylation factor IA (CF IA) is a yeast multiprotein complex that consists of Rna14, Rna15, Pcf11 and Clp1 proteins, and is involved in the 3′-end maturation of mRNAs. Structural data have been reported for the individual protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afc462fab077b21cbb82c075634c8d72
https://hal.archives-ouvertes.fr/hal-02349738
https://hal.archives-ouvertes.fr/hal-02349738
Autor:
François Debaene, Johann Stojko, Andreas Heine, Luzi Jakob Barandun, F.R. Ehrmann, Alexander Metz, François Diederich, Gerhard Klebe, Sarah Cianférani, Klaus Reuter
Publikováno v:
PLoS ONE, Vol 12, Iss 4, p e0175723 (2017)
PLoS ONE
PLoS ONE, Public Library of Science, 2017, 26, pp.e0175723. ⟨10.1371/journal.pone.0175723.s010⟩
PLoS ONE, 12 (4)
PLoS ONE
PLoS ONE, Public Library of Science, 2017, 26, pp.e0175723. ⟨10.1371/journal.pone.0175723.s010⟩
PLoS ONE, 12 (4)
For the efficient pathogenesis of Shigella, the causative agent of bacillary dysentery, full functionality of tRNA-guanine transglycosylase (TGT) is mandatory. TGT performs post-transcriptional modifications of tRNAs in the anticodon loop taking impa
Autor:
Alan Kadek, Johann Stojko, Sarah Cianférani, Julien Marcoux, Daniel Kavan, Petr Halada, Roland Ludwig, Alfons K. G. Felice, Petr Man
Publikováno v:
Biochimica et Biophysica Acta (BBA)-General Subjects
Biochimica et Biophysica Acta (BBA)-General Subjects, Elsevier, 2017, 1861 (2), pp.157-167. ⟨10.1016/j.bbagen.2016.11.016⟩
Biochimica et Biophysica Acta (BBA)-General Subjects, Elsevier, 2017, 1861 (2), pp.157-167. ⟨10.1016/j.bbagen.2016.11.016⟩
Background Cellobiose dehydrogenase (CDH) is a fungal extracellular oxidoreductase which fuels lytic polysaccharide monooxygenase with electrons during cellulose degradation. Interdomain electron transfer between the flavin and cytochrome domain in C