Single-cell absolute contact probability detection reveals chromosomes are organized by multiple low-frequency yet specific interactions

Autor: Diego I. Cattoni, Andrés M. Cardozo Gizzi, Mariya Georgieva, Marco Di Stefano, Alessandro Valeri, Delphine Chamousset, Christophe Houbron, Stephanie Déjardin, Jean-Bernard Fiche, Inma González, Jia-Ming Chang, Thomas Sexton, Marc A. Marti-Renom, Frédéric Bantignies, Giacomo Cavalli, Marcelo Nollmann

Publikováno v: Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)

Eukaryotic genomes are partitioned into self-interacting modules or topologically associated domains (TADs) that exist at the kilo-megabase scale. Here Cattoni et al. combine super-resolution microscopy with DNA-labeling methods to quantify absolute

Externí odkaz: https://doaj.org/article/e60cd11935584fd2817e693003fc822f

Diagnosis of Fanconi anemia in patients with bone marrow failure

Autor: Fernando O. Pinto, Thierry Leblanc, Delphine Chamousset, Gwenaelle Le Roux, Benoit Brethon, Bruno Cassinat, Jérôme Larghero, Jean-Pierre de Villartay, Dominique Stoppa-Lyonnet, André Baruchel, Gérard Socié, Eliane Gluckman, Jean Soulier

Publikováno v: Haematologica, Vol 94, Iss 4 (2009)

Background Patients with bone marrow failure and undiagnosed underlying Fanconi anemia may experience major toxicity if given standard-dose conditioning regimens for hematopoietic stem cell transplant. Due to clinical variability and/or potential eme

Externí odkaz: https://doaj.org/article/99fc0290295643a597fd4104449471a0

The ribosomal RNA processing 1B:protein phosphatase 1 holoenzyme reveals non-canonical PP1 interaction motifs

Autor: Gautam Srivastava, Rakhi Bajaj, Ganesan Senthil Kumar, Antoine Gaudreau-Lapierre, Hannah Nicolas, Delphine Chamousset, Dale Kreitler, Wolfgang Peti, Laura Trinkle-Mulcahy, Rebecca Page

Publikováno v: Cell Reports. 41:111726

The serine/threonine protein phosphatase 1 (PP1) dephosphorylates hundreds of substrates by associating with200 regulatory proteins to form specific holoenzymes. The major PP1 targeting protein in the nucleolus is RRP1B (ribosomal RNA processing 1B).

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b21a522b3d0b36cab385ccaf9728f566
https://doi.org/10.1016/j.celrep.2022.111726

Impact of fluorescent protein fusions on the bacterial flagellar motor

Autor: Francesco Pedaci, Bertus J. E. Beaumont, Minyoung Heo, Ashley L. Nord, Erwin van Rijn, Delphine Chamousset

Publikováno v: Scientific Reports, 7(1)
Scientific Reports
Scientific Reports, Nature Publishing Group, 2017, 7 (1), ⟨10.1038/s41598-017-11241-w⟩
Scientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)

Fluorescent fusion proteins open a direct and unique window onto protein function. However, they also introduce the risk of perturbation of the function of the native protein. Successful applications of fluorescent fusions therefore rely on a careful

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7a76f4ac3e05a96ba28968cd9f57646
http://resolver.tudelft.nl/uuid:60a7431d-155b-42f9-9d41-31b51001e251

RRP1B Targets PP1 to Mammalian Cell Nucleoli and Is Associated with Pre-60S Ribosomal Subunits

Autor: Veerle De Wever, Delphine Chamousset, François-Michel Boisvert, Greg B. G. Moorhead, Yan Chen, Angus I. Lamond, Laura Trinkle-Mulcahy

Publikováno v: Molecular Biology of the Cell

Protein phosphatase 1 (PP1) accumulates within the nucleolus, which plays a central role in regulation of cell growth and proliferation. Using a powerful combination of imaging and quantitative proteomics, we identify RRP1B as a nucleolar PP1 targeti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a82ac8a13569aece0908544ab1035a6
https://doi.org/10.1091/mbc.e10-04-0287