Výsledky vyhledávání - "Gwénaël Rabut"

Protein-fragment complementation assays for large-scale analysis of protein-protein interactions

Autor: Gwénaël Rabut, Aswani Sudevan, Natalia Lazarewicz, Robert W. Wysocki, Ewa Blaszczak

Publikováno v: Biochemical Society Transactions
Biochemical Society Transactions, 2021, 49 (3), pp.1337-1348. ⟨10.1042/BST20201058⟩
Biochemical Society Transactions, Portland Press, 2021, 49 (3), pp.1337-1348. ⟨10.1042/BST20201058⟩

International audience; Protein-protein interactions (PPIs) orchestrate nearly all biological processes. They are also considered attractive drug targets for treating many human diseases, including cancers and neurodegenerative disorders. Protein-fra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a30892394c2f6c9cd90dcbe538a8a9c
https://pubmed.ncbi.nlm.nih.gov/34156434

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Correction: Sensitive detection of protein ubiquitylation using a protein fragment complementation assay

Autor: Sébastien Léon, Gwénaël Rabut, Marie Le Boulch, Gaëlle Le Dez, Audrey Brossard

Publikováno v: Journal of cell science. 133(15)

There was an error in [J. Cell Sci. (2020) 133, jcs240093][1] ([doi:10.1242/jcs.240093][2]). In their article, the authors omitted to mention ubiquitin-mediated fluorescence complementation (UbFC), a method previously designed to probe the conjugatio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4cf9cfc8958e253edf2112f15e0ecc8
https://pubmed.ncbi.nlm.nih.gov/32409563

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Sensitive detection of protein ubiquitylation using a protein-fragment complementation assay

Autor: Gaëlle Le Dez, Marie Le Boulch, Audrey Brossard, Gwénaël Rabut, Sébastien Léon

Publikováno v: Journal of Cell Science
Journal of Cell Science, Company of Biologists, 2020, 133 (12), pp.jcs240093. ⟨10.1242/jcs.240093⟩
Journal of Cell Science, 2020, 133 (12), pp.jcs240093. ⟨10.1242/jcs.240093⟩

Ubiquitylation is a reversible post-translational protein modification that regulates a multitude of cellular processes. Detection of ubiquitylated proteins is often challenging because of their low abundance. Here, we present NUbiCA, a sensitive pro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42e978e2593fc693753c0ba0fd183c75
https://hal-univ-rennes1.archives-ouvertes.fr/hal-02635146/document

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Bimolecular Fluorescence Complementation to Assay the Interactions of Ubiquitylation Enzymes in Living Yeast Cells

Autor: Ewa Blaszczak, Gwénaël Rabut, Claude Prigent

Publikováno v: Methods in Molecular Biology ISBN: 9781493937547

Ubiquitylation is a versatile posttranslational protein modification catalyzed through the concerted action of ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s). These enzymes form transient complexes with each other and their modificat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b327c9628bd242fc1f6abb14dcc88a57
https://doi.org/10.1007/978-1-4939-3756-1_13

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Function and regulation of protein neddylation

Autor: Matthias Peter, Gwénaël Rabut

Publikováno v: EMBO reports. 9:969-976

Neddylation is the post-translational protein modification that is most closely related to ubiquitination. However, ubiquitination is known to regulate a myriad of processes in eukaryotic cells, whereas only a limited number of neddylation substrates

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5b753287af61243d0a4c4e933e701dee
https://doi.org/10.1038/embor.2008.183

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Systematic kinetic analysis of mitotic dis- and reassembly of the nuclear pore in living cells

Autor: Lucia Sironi, Esther Zanin, Jan Ellenberg, Claudia Wurzenberger, Gwénaël Rabut, Marion Braun, Elisa Dultz

Publikováno v: The Journal of Cell Biology

During mitosis in higher eukaryotes, nuclear pore complexes (NPCs) disassemble in prophase and are rebuilt in anaphase and telophase. NPC formation is hypothesized to occur by the interaction of mitotically stable subcomplexes that form defined struc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc919d31989133ffe1900a8db0fa154e
https://doi.org/10.1083/jcb.200707026

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Mapping the dynamic organization of the nuclear pore complex inside single living cells

Autor: Valérie Doye, Gwénaël Rabut, Jan Ellenberg

Publikováno v: Nature Cell Biology. 6:1114-1121

Most cellular activities are executed by multi-protein complexes that form the basic functional modules of their molecular machinery. Proteomic approaches can provide an evermore detailed picture of their composition, but do not reveal how these mach

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3e5994c35ab7c101edf22e4504632fb
https://doi.org/10.1038/ncb1184

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The Entire Nup107-160 Complex, Including Three New Members, Is Targeted as One Entity to Kinetochores in Mitosis

Autor: Valérie Doye, Isabelle Loïodice, Jean-Baptiste Sibarita, Jan Ellenberg, Megan van Overbeek, Annabelle Alves, Gwénaël Rabut

Publikováno v: Molecular Biology of the Cell. 15:3333-3344

In eukaryotes, bidirectional transport of macromolecules between the cytoplasm and the nucleus occurs through elaborate supramolecular structures embedded in the nuclear envelope, the nuclear pore complexes (NPCs). NPCs are composed of multiple copie

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::748bf2d6bc5be4b35169224c4d47dc71
https://doi.org/10.1091/mbc.e03-12-0878

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Dynamics of nuclear pore complex organization through the cell cycle

Autor: Péter Lénárt, Gwénaël Rabut, Jan Ellenberg

Publikováno v: Current Opinion in Cell Biology. 16:314-321

In eukaryotic cells, all macromolecules that traffic between the nucleus and the cytoplasm cross the double nuclear membrane through nuclear pore complexes (NPCs). NPCs are elaborate gateways that allow efficient, yet selective, translocation of many

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e6748e76766071415c451f7a3df2d68
https://doi.org/10.1016/j.ceb.2004.04.001

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Protein quality control at the inner nuclear membrane

Autor: Ewa Blaszczak, Marina Pantazopoulou, Matthias Meurer, Per O. Ljungdahl, Deike J. Omnus, Gwénaël Rabut, Audrey Brossard, Joseph Barry, Bernd Fischer, Daniel Kirrmaier, Wolfgang Huber, Anton Khmelinskii, Gaëlle Le Dez, Charles Boone, Alexander Gunnarsson, Michael Knop

Publikováno v: Nature
Nature, Nature Publishing Group, 2014, 516 (7531), pp.410-3. ⟨10.1038/nature14096⟩
Nature, 2014, 516 (7531), pp.410-3. ⟨10.1038/nature14096⟩

International audience; The nuclear envelope is a double membrane that separates the nucleus from the cytoplasm. The inner nuclear membrane (INM) functions in essential nuclear processes including chromatin organization and regulation of gene express

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f009d2697ba3e69e96fb1ce19f10c8a
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01117232

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