Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Diane Cala de Paepe"'
Autor:
Emilie Layre, Diane Cala-De Paepe, Gérald Larrouy-Maumus, Julien Vaubourgeix, Sathish Mundayoor, Buko Lindner, Germain Puzo, Martine Gilleron
Publikováno v:
Journal of Lipid Research, Vol 52, Iss 6, Pp 1098-1110 (2011)
For 4 decades, in vivo and in vitro studies have suggested that sulfoglycolipids (SGLs) play a role in the virulence or pathogenesis of the tubercle bacilli. However, the SGL structure and biosynthesis pathway remain only partially elucidated. Using
Externí odkaz:
https://doaj.org/article/6cffcb1741c849c18d92489ca6e1b3f8
Autor:
Tanguy Le Marchand, Wolfgang Bermel, Claire Ollier, Jan Stanek, Henry W. Orton, Guido Pintacuda, Isabella C. Felli, Diane Cala de Paepe, Dylan Foucaudeau, Adrian W. Draney, Sebastian Hiller, Tobias Schubeis, Roberta Pierattelli
Publikováno v:
Angewandte Chemie. 132:2400-2405
Autor:
Nicola Salvi, Jayasubba Reddy Yarava, Baptiste Busi, Józef R. Lewandowski, Lyndon Emsley, Diane Cala de Paepe, Martin Blackledge, Albert Hofstetter
Publikováno v:
Journal of Physical Chemistry B
Journal of Physical Chemistry B, 2018, 122 (42), pp.9697-9702. ⟨10.1021/acs.jpcb.8b08578⟩
Journal of Physical Chemistry B, American Chemical Society, 2018, 122 (42), pp.9697-9702. ⟨10.1021/acs.jpcb.8b08578⟩
Journal of Physical Chemistry B, 2018, 122 (42), pp.9697-9702. ⟨10.1021/acs.jpcb.8b08578⟩
Journal of Physical Chemistry B, American Chemical Society, 2018, 122 (42), pp.9697-9702. ⟨10.1021/acs.jpcb.8b08578⟩
International audience; Understanding the interplay between protein function and dynamics is currently one of the fundamental challenges of physical biology. Recently, a method using variable temperature solid-state nuclear magnetic resonance relaxat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5542b1ef625fce271753a4cd53d7199
https://hal.science/hal-01995907
https://hal.science/hal-01995907
Autor:
Olivier Ouari, Diane Cala de Paepe, Inara Akopjana, Svetlana Kotelovica, G. Pintacuda, Anne Lesage, Andrea Pica, Andrew J. Pell, Kristaps Jaudzems, Andrea Bertarello, Sachin Rama Chaudhari, Emeline Barbet-Massin, Kaspars Tars, David Gajan
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2018, 57 (25), pp.7458-7462. ⟨10.1002/anie.201801016⟩
Angewandte Chemie International Edition, 2018, 57 (25), pp.7458-7462. ⟨10.1002/anie.201801016⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2018, 57 (25), pp.7458-7462. ⟨10.1002/anie.201801016⟩
Angewandte Chemie International Edition, 2018, 57 (25), pp.7458-7462. ⟨10.1002/anie.201801016⟩
International audience; Dynamic nuclear polarization (DNP) is a powerful way to overcome the sensitivity limitation of magic-angle-spinning (MAS) NMR experiments. However, the resolution of the DNPNMR spectra of proteins is compromised by severe line
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cc9e0d62449bc45746e65fcdc1af98e
https://hal.archives-ouvertes.fr/hal-01859534
https://hal.archives-ouvertes.fr/hal-01859534
Autor:
James A. Shayman, Lucia Mori, Diane Cala-De Paepe, Martine Gilleron, Emilie Layre, Gennaro De Libero, Frédéric Carrière, Naila Mebarek, Germain Puzo, Stéphane Canaan, Marco Lepore
Publikováno v:
Cell Chemical Biology
Cell Chemical Biology, Cell Press, 2016, 23 (9), pp.1147-1156. ⟨10.1016/j.chembiol.2016.07.021⟩
Cell Chemical Biology, Cell Press, 2016, pp.1147-1156. ⟨10.1016/j.chembiol.2016.07.021⟩
Cell Chemical Biology, 2016, 23 (9), pp.1147-1156. ⟨10.1016/j.chembiol.2016.07.021⟩
Cell Chemical Biology, Cell Press, 2016, 23 (9), pp.1147-1156. ⟨10.1016/j.chembiol.2016.07.021⟩
Cell Chemical Biology, Cell Press, 2016, pp.1147-1156. ⟨10.1016/j.chembiol.2016.07.021⟩
Cell Chemical Biology, 2016, 23 (9), pp.1147-1156. ⟨10.1016/j.chembiol.2016.07.021⟩
International audience; Complex antigens require processing within antigen-presenting cells (APCs) to form T cell stimulatory complexes with CD1 antigen-presenting molecules. It remains unknown whether lipids with multi-acylated moieties also necessi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5099f3d38c6f493b2974e80f30588bc9
https://hal.archives-ouvertes.fr/hal-03096294
https://hal.archives-ouvertes.fr/hal-03096294
Autor:
Emilie Layre, Diane Cala-De Paepe, Luis F. Garcia-Alles, Lucia Mori, Germain Puzo, Gaëlle Giacometti, Daniel Hanau, Martine Gilleron, Gennaro De Libero
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (37), pp.31494-31502. ⟨10.1074/jbc.M112.386300⟩
The Journal of biological chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (37), pp.31494-31502. ⟨10.1074/jbc.M112.386300⟩
The Journal of biological chemistry
International audience; Lipids are important antigens that induce T cell-mediated specific immune responses. They are presented to T lymphocytes by a specific class of MHC-I like proteins, termed CD1. The majority of the described CD1-presented mycob
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::428d4b782398e4680f77c76616e7fef8
https://hal.archives-ouvertes.fr/hal-03096337
https://hal.archives-ouvertes.fr/hal-03096337
Autor:
Diane Cala-De Paepe, Gerald Larrouy-Maumus, Germain Puzo, Martine Gilleron, Sathish Mundayoor, Buko Lindner, Emilie Layre, Julien Vaubourgeix
Publikováno v:
Journal of Lipid Research
Journal of Lipid Research, American Society for Biochemistry and Molecular Biology, 2011, 52 (6), pp.1098-1110. ⟨10.1194/jlr.M013482⟩
Journal of Lipid Research, Vol 52, Iss 6, Pp 1098-1110 (2011)
Journal of Lipid Research, American Society for Biochemistry and Molecular Biology, 2011, 52 (6), pp.1098-1110. ⟨10.1194/jlr.M013482⟩
Journal of Lipid Research, Vol 52, Iss 6, Pp 1098-1110 (2011)
For 4 decades, in vivo and in vitro studies have suggested that sulfoglycolipids (SGLs) play a role in the virulence or pathogenesis of the tubercle bacilli. However, the SGL structure and biosynthesis pathway remain only partially elucidated. Using
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20b1844ed8e6c127fb9da71cdab240f7
https://hal.archives-ouvertes.fr/hal-03096390/document
https://hal.archives-ouvertes.fr/hal-03096390/document
Autor:
Kristaps Jaudzems, Guido Pintacuda, Loren B. Andreas, Kaspars Tars, Diane Cala de Paepe, Jan Stanek
Publikováno v:
Solid State Nuclear Magnetic Resonance
Solid State Nuclear Magnetic Resonance, Elsevier, 2017, 87, pp.126-136. ⟨10.1016/j.ssnmr.2017.07.004⟩
Solid State Nuclear Magnetic Resonance, 2017, 87, pp.126-136. ⟨10.1016/j.ssnmr.2017.07.004⟩
Solid State Nuclear Magnetic Resonance, Elsevier, 2017, 87, pp.126-136. ⟨10.1016/j.ssnmr.2017.07.004⟩
Solid State Nuclear Magnetic Resonance, 2017, 87, pp.126-136. ⟨10.1016/j.ssnmr.2017.07.004⟩
We thank the members of technical staff of ISA for assistance with NMR spectrometers.; International audience; 1H-detection in solid-state NMR of proteins has been traditionally combined with deuteration for both resolution and sensitivity reasons, w
Autor:
Tanguy Le Marchand, Guido Pintacuda, Loren B. Andreas, Sebastian Wegner, Diane Cala de Paepe, Andrea Bertarello, Carl Öster, Isabella C. Felli, Torsten Herrmann, Nicholas E. Dixon, Camille Doyen, Lyndon Emsley, Roberta Pierattelli, Daniela Lalli, Magdaléna Krejčíková, Benno Knott, Frank Engelke, Jan Stanek
Publikováno v:
Journal of Biomolecular NMR
Journal of Biomolecular NMR, Springer Verlag, 2015, 62 (3), pp.253-261. ⟨10.1007/s10858-015-9956-1⟩
Journal of Biomolecular NMR, 2015, 62 (3), pp.253-261. ⟨10.1007/s10858-015-9956-1⟩
Journal of Biomolecular NMR, Springer Verlag, 2015, 62 (3), pp.253-261. ⟨10.1007/s10858-015-9956-1⟩
Journal of Biomolecular NMR, 2015, 62 (3), pp.253-261. ⟨10.1007/s10858-015-9956-1⟩
Here we introduce a new pulse sequence for resonance assignment that halves the number of data sets required for sequential linking by directly correlating sequential amide resonances in a single diagonal-free spectrum. The method is demonstrated wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55905408b5a1a9219019fce00e58eb22
https://infoscience.epfl.ch/record/212259
https://infoscience.epfl.ch/record/212259
Autor:
Torsten Herrmann, Guido Pintacuda, Inara Akopjana, Lyndon Emsley, Sebastian Wegner, Andrea Bertarello, Jan Stanek, Daniela Lalli, Loren B. Andreas, Kristaps Jaudzems, Tanguy Le Marchand, Diane Cala de Paepe, Svetlana Kotelovica, Benno Knott, Anne Lesage, Frank Engelke, Kaspars Tars
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2016, 113 (33), pp.9187-9192. ⟨10.1073/pnas.1602248113⟩
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2016, 113 (33), pp.9187-9192. ⟨10.1073/pnas.1602248113⟩
Proceedings of the National Academy of Sciences
International audience; Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has focused on highly deuterated samples, in which only a small number of protons are introduced and observation of signals from side chains is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::439c1fb5ce6afc4adee068c2f68c2355
https://infoscience.epfl.ch/record/222219
https://infoscience.epfl.ch/record/222219