Výsledky vyhledávání - "MESH: Peptidylprolyl Isomerase"

Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA

Autor: Isabelle Landrieu, Guy Lippens, Jean-Michel Wieruszeski, Caroline Smet-Nocca, Hélène Launay

Publikováno v: Journal of Biomolecular NMR
Journal of Biomolecular NMR, Springer Verlag, 2013, 55 (4), pp.323-37. ⟨10.1007/s10858-013-9716-z⟩
Journal of Biomolecular NMR, 2013, 55 (4), pp.323-37. ⟨10.1007/s10858-013-9716-z⟩

International audience; The Pin1 protein plays a critical role in the functional regulation of the hyperphosphorylated neuronal Tau protein in Alzheimer's disease and is by itself regulated by phosphorylation. We have used Nuclear Magnetic Resonance

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9db6701d5c139f85a4404f38fa1d7e68
https://hal.archives-ouvertes.fr/hal-00903359

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Cotranslational processing mechanisms: towards a dynamic 3D model

Autor: Carmela Giglione, Sonia Fieulaine, Thierry Meinnel

Publikováno v: Trends in Biochemical Sciences
Trends in Biochemical Sciences, Elsevier, 2009, 34 (8), pp.417-26. ⟨10.1016/j.tibs.2009.04.003⟩

International audience; Recent major advances have been made in understanding how cotranslational events are achieved in the course of protein biosynthesis. Specifically, several studies have shed light into the dynamic process of how nascent chains

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::524e2caae0c61abec95e371295960ff1
https://hal.archives-ouvertes.fr/hal-00853800

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The peptidyl-prolyl isomerase and chaperone Par27 of Bordetella pertussis as the prototype for a new group of parvulins

Autor: Magalie Sénéchal, Françoise Jacob-Dubuisson, Alexandre Wohlkonig, Hervé Drobecq, Isabelle Landrieu, Jean-Michel Wieruszeski, Hélène Hodak, Marc Jamin, Caroline Smet-Nocca, Camille Locht

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2008, 376 (2), pp.414-26. ⟨10.1016/j.jmb.2007.10.088⟩
Journal of Molecular Biology, 2008, 376 (2), pp.414-26. ⟨10.1016/j.jmb.2007.10.088⟩

Proteins that pass through the periplasm in an unfolded state are highly sensitive to proteolysis and aggregation and, therefore, often require protection by chaperone-like proteins. The periplasm of Gram-negative bacteria is well equipped with ATP-i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c1982bfb54c832a386b83ada541f0a9
https://hal.archives-ouvertes.fr/hal-00273348

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Synapsin associates with cyclophilin B in an ATP- and cyclosporin A-dependent manner

Autor: Lane-Guermonprez, Lydie, Morot-Gaudry-Talarmain, Yvette, Meunier, François-Marie, O'Regan, Seana, Onofri, Franco, Le Caer, Jean-Pierre, Benfenati, Fabio

Publikováno v: Journal of Neurochemistry
Journal of Neurochemistry, Wiley, 2005, 93 (6), pp.1401-11. ⟨10.1111/j.1471-4159.2005.03125.x⟩

Immunophilins are ubiquitous enzymes responsible for proline isomerisation during protein synthesis and for the chaperoning of several membrane proteins. These activities can be blocked by the immunosuppressants cyclosporin A, FK506 and rapamycin. It

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::e823f829cb81a358da08d0767d4f3b25
https://hal.archives-ouvertes.fr/hal-00084386

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Octasaccharide is the minimal length unit required for efficient binding of cyclophilin B to heparin and cell surface heparan sulphate

Autor: Fabrice Allain, Rachel Pakula, Agnès Denys, Joël Mazurier, Christophe Vanpouille, Mathieu Carpentier

Publikováno v: Biochemical Journal
Biochemical Journal, Portland Press, 2004, 382 (Pt 2), pp.733-40. ⟨10.1042/BJ20031453⟩
Biochemical Journal, 2004, 382 (Pt 2), pp.733-40. ⟨10.1042/BJ20031453⟩

Cyclophilin B (CyPB) is a heparin-binding protein first identified as a receptor for cyclosporin A. In previous studies, we reported that CyPB triggers chemotaxis and integrin-mediated adhesion of T-lymphocytes by way of interaction with two types of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a50615138a38789a96aebdde4c45364
https://hal.archives-ouvertes.fr/hal-00149442

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Involvement of GAGs in the activity of pro-inflammatory factors

Autor: Allain, Fabrice, Vanpouille, Christophe, Denys, Agnès, Pakula, Rachel, Carpentier, Mathieu, Mazurier, Joël

Publikováno v: Advances in Experimental Medicine and Biology
Advances in Experimental Medicine and Biology, Kluwer, 2003, 535, pp.95-106
Advances in Experimental Medicine and Biology, 2003, 535, pp.95-106

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::29a5904364d875644abfd7607ccf8b3e
https://hal.archives-ouvertes.fr/hal-00149475

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Receptor type I and type II binding regions and the peptidyl-prolyl isomerase site of cyclophilin B are required for enhancement of T-lymphocyte adhesion to fibronectin

Autor: Marie-Christine Slomianny, Sandrine Durieux, Mathieu Carpentier, Fabrice Allain, Geneviève Spik, Bernard Haendler, Christophe Vanpouille

Publikováno v: Biochemistry
Biochemistry, American Chemical Society, 2002, 41 (16), pp.5222-9
Biochemistry, 2002, 41 (16), pp.5222-9

Cyclophilin B (CyPB), a cyclosporin A (CsA) binding protein, interacts with two types of binding sites at the surface of T-lymphocytes. The type I sites correspond to functional receptors involved in endocytosis and the type II sites to sulfated glyc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1824f579f150315e8a245d266497ef94
https://hal.archives-ouvertes.fr/hal-00167220

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Interaction with glycosaminoglycans is required for cyclophilin B to trigger integrin-mediated adhesion of peripheral blood T lymphocytes to extracellular matrix

Autor: Marie-Christine Slomianny, Fabrice Allain, Sandrine Durieux, Geneviève Spik, Mathieu Carpentier, Christophe Vanpouille

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, 2002, 99 (5), pp.2714-9. ⟨10.1073/pnas.052284899⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2002, 99 (5), pp.2714-9. ⟨10.1073/pnas.052284899⟩

Cyclophilins A and B (CyPA and CyPB) are cyclosporin A-binding proteins that are involved in inflammatory events. We have reported that CyPB interacts with two types of cell-surface-binding sites. The first site corresponds to a functional receptor a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0f308b6227456c8d9cfe389b032cd8d
https://hal.science/hal-00167221

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Conformational polymorphism of cyclosporin A

Autor: Jean Claude Thierry, Malcolm D. Walkinshaw, Vincent Mikol, Kurt Wüthrich, Joerg Kallen, Danièle Altschuh, Olivier Vix, Werner Braun, Claus Spitzfaden

Publikováno v: Structure / Struct Fold Des; Structure (Camb )
Structure / Struct Fold Des; Structure (Camb ), 1994, 2 (10), pp.963-72

Background: Cyclosporin A (CsA) is a cyclic undecapeptide fungal metabolite with immunosuppressive properties, widely used in transplant surgery. It forms a tight complex with the ubiquitous 18 kDa cytosolic protein cyclophilin A (CypA). The conforma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d56c90fb049f6654cd2d20ee52286c75
https://hal.archives-ouvertes.fr/hal-00265271

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