Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Ramalho, João J."'
Autor:
Castiglioni, Victoria G., Ramalho, João J., Kroll, Jason R., Stucchi, Riccardo, van Beuzekom, Hanna, Schmidt, Ruben, Altelaar, Maarten, Boxem, Mike
Publikováno v:
In Journal of Biological Chemistry April 2022 298(4)
Akademický článek
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Akademický článek
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Akademický článek
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Autor:
Remmelzwaal, Sanne, Geisler, Florian, Stucchi, Riccardo, van der Horst, Suzanne, Pasolli, Milena, Kroll, Jason R., Jarosinska, Olga D., Akhmanova, Anna, Richardson, Christine A., Altelaar, Maarten, Leube, Rudolf E., Ramalho, João J., Boxem, Mike, Developmental Biology, Sub Developmental Biology, Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Celbiologie, Biomolecular Mass Spectrometry and Proteomics
Publikováno v:
Current biology, 2021, Vol.31(11), pp.2334-2346 [Peer Reviewed Journal]
Current biology 31(11), 2334-2346.e9 (2021). doi:10.1016/j.cub.2021.03.069
Current Biology, 31(11), 2334. Cell Press
Current biology 31(11), 2334-2346.e9 (2021). doi:10.1016/j.cub.2021.03.069
Current Biology, 31(11), 2334. Cell Press
Current biology 31(11), 2334-2346.e9 (2021). doi:10.1016/j.cub.2021.03.069
Published by Current Biology Ltd., London
Published by Current Biology Ltd., London
Autor:
Ramalho, João J, Sepers, Jorian J, Nicolle, Ophélie, Schmidt, Ruben, Cravo, Janine, Michaux, Grégoire, Boxem, Mike, Sub Developmental Biology, Developmental Biology
Publikováno v:
Development (Cambridge), 147(14)
Development (Cambridge, England), 147(14). Company of Biologists Ltd
Development (Cambridge, England)
Development (Cambridge, England), 2020, 147 (14), pp.dev188011. ⟨10.1242/dev.188011⟩
Development (Cambridge, England), Company of Biologists, 2020, 147 (14), pp.dev188011. ⟨10.1242/dev.188011⟩
Development (Cambridge) 147 (2020) 14
Development (Cambridge, England), 147(14). Company of Biologists Ltd
Development (Cambridge, England)
Development (Cambridge, England), 2020, 147 (14), pp.dev188011. ⟨10.1242/dev.188011⟩
Development (Cambridge, England), Company of Biologists, 2020, 147 (14), pp.dev188011. ⟨10.1242/dev.188011⟩
Development (Cambridge) 147 (2020) 14
International audience; ERM proteins are conserved regulators of cortical membrane specialization, that function as membrane-actin linkers and molecular hubs. Activity of ERM proteins requires a conformational switch from an inactive cytoplasmic form
Akademický článek
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Autor:
Koorman, Thijs, Klompstra, Diana, van der Voet, Monique, Lemmens, Irma, Ramalho, João J., Nieuwenhuize, Susan, van den Heuvel, Sander, Tavernier, Jan, Nance, Jeremy, Boxem, Mike, Developmental Biology, Sub Developmental Biology
Publikováno v:
Nature Cell Biology, 18, 337-46
Nature Cell Biology, 18(3)
Nature cell biology
Nature Cell Biology, 18, 3, pp. 337-46
Nature Cell Biology, 18(3)
Nature cell biology
Nature Cell Biology, 18, 3, pp. 337-46
The establishment of cell polarity is an essential process for the development of multicellular organisms and the functioning of cells and tissues. Here, we combine large-scale protein interaction mapping with systematic phenotypic profiling to study
Autor:
Amendola, Pier Giorgio, Zaghet, Nico, Ramalho, João J., Vilstrup Johansen, Jens, Boxem, Mike, Salcini, Anna Elisabetta, Sub Developmental Biology, Developmental Biology
Publikováno v:
PLoS Genetics, 13(2), 1. Public Library of Science
PLoS Genetics, Vol 13, Iss 2, p e1006632 (2017)
PLoS Genetics
Amendola, P G, Zaghet, N, Ramalho, J J, Johansen, J V, Boxem, M & Salcini, A E 2017, ' JMJD-5/KDM8 regulates H3K36me2 and is required for late steps of homologous recombination and genome integrity ', P L o S Genetics, vol. 13, no. 2, e1006632 . https://doi.org/10.1371/journal.pgen.1006632
PLoS Genetics, Vol 13, Iss 2, p e1006632 (2017)
PLoS Genetics
Amendola, P G, Zaghet, N, Ramalho, J J, Johansen, J V, Boxem, M & Salcini, A E 2017, ' JMJD-5/KDM8 regulates H3K36me2 and is required for late steps of homologous recombination and genome integrity ', P L o S Genetics, vol. 13, no. 2, e1006632 . https://doi.org/10.1371/journal.pgen.1006632
The eukaryotic genome is organized in a three-dimensional structure called chromatin, constituted by DNA and associated proteins, the majority of which are histones. Post-translational modifications of histone proteins greatly influence chromatin str
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5f16fc323d4990561d4f8c1ded765d6
https://dspace.library.uu.nl/handle/1874/354812
https://dspace.library.uu.nl/handle/1874/354812
Autor:
Waaijers, Selma, Muñoz, Javier, Berends, Christian, Ramalho, João J, Goerdayal, Soenita S, Low, Teck Y, Zoumaro-Djayoon, Adja D, Hoffmann, Michael, Koorman, Thijs, Tas, Roderick P, Harterink, Martin, Seelk, Stefanie, Kerver - Stumpfova, J, Hoogenraad, Casper C, Bossinger, Olaf, Tursun, Baris, van den Heuvel, Sander, Heck, Albert J R, Boxem, Mike, Sub Developmental Biology, Sub Biomol.Mass Spect. and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Sub Cell Biology, Developmental Biology
Publikováno v:
BMC Biology, 14
BMC Biology
BMC Biology, 14. BioMed Central
BMC Biology
BMC Biology, 14. BioMed Central
Background Affinity purification followed by mass spectrometry (AP/MS) is a widely used approach to identify protein interactions and complexes. In multicellular organisms, the accurate identification of protein complexes by AP/MS is complicated by t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::958bac8324bfacbde9298c8806e4f817
https://hdl.handle.net/2066/172544
https://hdl.handle.net/2066/172544