Zobrazeno 1 - 10
of 14
pro vyhledávání: '"MESH: PDZ Domains"'
Publikováno v:
Journal of Chemical Physics
Journal of Chemical Physics, American Institute of Physics, 2018, 149 (7), pp.072302. ⟨10.1063/1.5022249⟩
Journal of Chemical Physics, American Institute of Physics, 2018, 149 (7), pp.072302. ⟨10.1063/1.5022249⟩
International audience; For the high throughput design of protein:peptide binding, one must explore a vast space of amino acid sequences in search of low binding free energies. This complex problem is usually addressed with either simple heuristic sc
Autor:
Christine Petit, Florent Delhommel, Benjamin Bardiaux, Julia Chamot-Rooke, Michael Nilges, Sébastien Brier, Florence Cordier, Amel Bahloul, Bertrand Raynal, Sylvie Nouaille, Nicolas Wolff, Baptiste Colcombet-Cazenave, Guillaume Bouvier
Publikováno v:
Structure
Structure, Elsevier (Cell Press), 2017, 25 (11), pp.1645-1656.e5. ⟨10.1016/j.str.2017.08.013⟩
Structure, 2017, 25 (11), pp.1645-1656.e5. ⟨10.1016/j.str.2017.08.013⟩
Structure, Elsevier (Cell Press), 2017, 25 (11), pp.1645-1656.e5. ⟨10.1016/j.str.2017.08.013⟩
Structure, 2017, 25 (11), pp.1645-1656.e5. ⟨10.1016/j.str.2017.08.013⟩
International audience; Hearing relies on the transduction of sound-evoked vibrations into electric signals, occurring in the stereocilia bundle of hair cells. The bundle is organized in a staircase pattern formed by rows of packed stereocilia. This
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf6c0f0829c16de0cf89456ba92ad039
https://hal-pasteur.archives-ouvertes.fr/pasteur-02883914
https://hal-pasteur.archives-ouvertes.fr/pasteur-02883914
Publikováno v:
Biomolecular NMR Assignments
Biomolecular NMR Assignments, Springer, 2016, 10 (2), pp.361-365. ⟨10.1007/s12104-016-9701-z⟩
Biomolecular NMR Assignments, 2016, 10 (2), pp.361-365. ⟨10.1007/s12104-016-9701-z⟩
Biomolecular NMR Assignments, Springer, 2016, 10 (2), pp.361-365. ⟨10.1007/s12104-016-9701-z⟩
Biomolecular NMR Assignments, 2016, 10 (2), pp.361-365. ⟨10.1007/s12104-016-9701-z⟩
International audience; Mammals perceive sounds thanks to mechanosensory hair cells located in the inner ear. The stereocilia of these cells are tightly bound together in bundles by a network of cadherins and scaffolding proteins. Stereocilia deflect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1aec6f36ec693bff9d4ead6a2825369
https://hal-pasteur.archives-ouvertes.fr/pasteur-02883932
https://hal-pasteur.archives-ouvertes.fr/pasteur-02883932
Autor:
Yves Nominé, Sebastian Charbonnier, Patricia Cassonnet, Anne Forster, Julie Abdat, Marilyne Blémont, Nicolas Wolff, Kevin Ricquier, Renaud Vincentelli, Katja Luck, Juline Poirson, Marie-Laure Straub, Jérôme Reboul, Jolanta Polanowska, Jeremy Turchetto, Gilles Travé, Francois, Jean-Paul Borg, Yves Jacob, Murielle Masson
Publikováno v:
Nature Methods
Nature Methods, Nature Publishing Group, 2015, 12 (8), pp.787-793. ⟨10.1038/nmeth.3438⟩
Nature Methods, Nature Publishing Group, 2015, 12 (8), pp.787-U154. ⟨10.1038/NMETH.3438⟩
Nature Methods, 2015, 12 (8), pp.787-793. ⟨10.1038/nmeth.3438⟩
Nature methods
Nature Methods, Nature Publishing Group, 2015, 12 (8), pp.787-793. ⟨10.1038/nmeth.3438⟩
Nature Methods, Nature Publishing Group, 2015, 12 (8), pp.787-U154. ⟨10.1038/NMETH.3438⟩
Nature Methods, 2015, 12 (8), pp.787-793. ⟨10.1038/nmeth.3438⟩
Nature methods
Many protein interactions are mediated by small linear motifs interacting specifically with defined families of globular domains. Quantifying the specificity of a motif requires measuring and comparing its binding affinities to all its putative targe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d23a387bd6b6333f1fd2c0becc6ef51
https://hal-pasteur.archives-ouvertes.fr/pasteur-02883959
https://hal-pasteur.archives-ouvertes.fr/pasteur-02883959
Autor:
Elouan Terrien, Nicolas Babault, Nicolas Wolff, Monique Lafon, Florence Cordier, Pierre Maisonneuve, Célia Caillet-Saguy, Florent Delhommel
Publikováno v:
Progress in Biophysics and Molecular Biology
Progress in Biophysics and Molecular Biology, 2015, 119 (1), pp.53-59. ⟨10.1016/j.pbiomolbio.2015.02.007⟩
Progress in Biophysics and Molecular Biology, Elsevier, 2015, 119 (1), pp.53-59. ⟨10.1016/j.pbiomolbio.2015.02.007⟩
Progress in Biophysics and Molecular Biology, 2015, 119 (1), pp.53-59. ⟨10.1016/j.pbiomolbio.2015.02.007⟩
Progress in Biophysics and Molecular Biology, Elsevier, 2015, 119 (1), pp.53-59. ⟨10.1016/j.pbiomolbio.2015.02.007⟩
International audience; PDZ (PSD-95/Dlg/ZO-1) domains play a major role in neuronal homeostasis in which they act as scaffold domains regulating cellular trafficking, self-association and catalytic activity of essential proteins such as kinases and p
Autor:
Alain Chaffotte, Henri Buc, Nicolas Wolff, Javier Pérez, Muriel Delepierre, Bernard Gilquin, Bertrand Raynal, Pierre Maisonneuve, Célia Caillet-Saguy, Sophie Zinn-Justin, Florence Cordier
Publikováno v:
FEBS Journal
FEBS Journal, Wiley, 2014, 281 (21), pp.4852-4865. ⟨10.1111/febs.13024⟩
FEBS Journal, 2014, 281 (21), pp.4852-4865. ⟨10.1111/febs.13024⟩
FEBS Journal, Wiley, 2014, 281 (21), pp.4852-4865. ⟨10.1111/febs.13024⟩
FEBS Journal, 2014, 281 (21), pp.4852-4865. ⟨10.1111/febs.13024⟩
The human protein tyrosine phosphatase non-receptor type 4 (PTPN4) prevents cells death. Targeting its PDZ domain abrogates this protection and triggers apoptosis. We demonstrate here that the PDZ domain inhibits the phosphatase activity of PTPN4. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb992ee779c4cbf09beff1c9a6ee9bbd
https://hal.archives-ouvertes.fr/hal-02545802
https://hal.archives-ouvertes.fr/hal-02545802
Publikováno v:
Protein Engineering, Design and Selection
Protein Engineering, Design and Selection, Oxford University Press (OUP), 2014, 27 (8), pp.249-53. ⟨10.1093/protein/gzu022⟩
Protein Engineering, Design and Selection, Oxford University Press (OUP), 2014, 27 (8), pp.249-53. ⟨10.1093/protein/gzu022⟩
International audience; Many biological processes are regulated by the interaction between protein domains and their corresponding binding partners. The PDZ domain is one of the most common protein-protein interaction modules in mammalian cells, whos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e827a3f3ff3ffd19d62807e484683b8f
https://hal-riip.archives-ouvertes.fr/pasteur-01181359/document
https://hal-riip.archives-ouvertes.fr/pasteur-01181359/document
Autor:
Muriel Delepierre, Nicolas Wolff, Zakir Khan, Monique Lafon, Henri Buc, Mireille Lafage, Elouan Terrien, Florence Cordier, Alain Chaffotte, Catherine Simenel, Christophe Prehaud
Publikováno v:
Science Signaling
Science Signaling, 2012, 5 (237), pp.ra58-ra58. ⟨10.1126/scisignal.2002941⟩
Science Signaling, American Association for the Advancement of Science, 2012, 5 (237), pp.ra58-ra58. ⟨10.1126/scisignal.2002941⟩
Science Signaling, 2012, 5 (237), pp.ra58-ra58. ⟨10.1126/scisignal.2002941⟩
Science Signaling, American Association for the Advancement of Science, 2012, 5 (237), pp.ra58-ra58. ⟨10.1126/scisignal.2002941⟩
International audience; PTEN (phosphatase and tensin homolog deleted on chromosome 10) and MAST2 (microtubule-associated serine and threonine kinase 2) interact with each other through the PDZ domain of MAST2 (MAST2-PDZ) and the carboxyl-terminal (C-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d935b97cfc47fe71634deb45f7f7532e
https://hal-pasteur.archives-ouvertes.fr/pasteur-02883992
https://hal-pasteur.archives-ouvertes.fr/pasteur-02883992
Autor:
Åke Engström, Jakob Dogan, Per Jemth, Stefano Gianni, Serena Rinaldo, Patrik Lundström, Francesca Cutruzzolà, Celestine N. Chi, S. Raza Haq
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2012, 51 (44), pp.8971-9. ⟨10.1021/bi300792h⟩
Biochemistry, American Chemical Society, 2012, 51 (44), pp.8971-9. ⟨10.1021/bi300792h⟩
The postsynaptic density protein-95/discs large/zonula occludens-1 (PDZ) domain is a protein-protein interaction module with a shallow binding groove where protein ligands bind. However, interactions that are not part of this canonical binding groove
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88f6e9456ab06c4c6aba15e4d3d5da8b
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-186213
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-186213
Autor:
Mireille Lafage, Joseph J.B. Cockburn, Monique Lafon, Christophe Prehaud, Nicolas Wolff, Ahmed Haouz, Florence Cordier, Nicolas Babault, Félix A. Rey, Henri Buc, Muriel Delepierre
Publikováno v:
Structure
Structure, 2011, 19 (10), pp.1518-1524. ⟨10.1016/j.str.2011.07.007⟩
Structure, Elsevier (Cell Press), 2011, 19 (10), pp.1518-1524. ⟨10.1016/j.str.2011.07.007⟩
Structure, 2011, 19 (10), pp.1518-1524. ⟨10.1016/j.str.2011.07.007⟩
Structure, Elsevier (Cell Press), 2011, 19 (10), pp.1518-1524. ⟨10.1016/j.str.2011.07.007⟩
Comment in : PDZ-peptide complexes: as exciting as ever./ Trave G. Structure. 2011 Oct 12;19(10):1350-1. doi: 10.1016/j.str.2011.09.008.PMID: 22000506; International audience; PTPN4, a human tyrosine phosphatase, protects cells against apoptosis. Thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e0e24e66b3993e6d468e4653dff6a72
https://hal-pasteur.archives-ouvertes.fr/pasteur-02883997
https://hal-pasteur.archives-ouvertes.fr/pasteur-02883997