Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Davide Normanno"'
Autor:
Ineke Brouwer, Hongshan Zhang, Andrea Candelli, Davide Normanno, Erwin J.G. Peterman, Gijs J.L. Wuite, Mauro Modesti
Publikováno v:
Cell Reports, Vol 18, Iss 12, Pp 2845-2853 (2017)
Human RAD52 promotes annealing of complementary single-stranded DNA (ssDNA). In-depth knowledge of RAD52-DNA interaction is required to understand how its activity is integrated in DNA repair processes. Here, we visualize individual fluorescent RAD52
Externí odkaz:
https://doaj.org/article/154e78ea140f4d6d90e3c76e81e6b0e1
Autor:
Davide Normanno, Aurélie Négrel, Abinadabe J de Melo, Stéphane Betzi, Katheryn Meek, Mauro Modesti
Publikováno v:
eLife, Vol 6 (2017)
XRCC4 and DNA Ligase 4 (LIG4) form a tight complex that provides DNA ligase activity for classical non-homologous end joining (the predominant DNA double-strand break repair pathway in higher eukaryotes) and is stimulated by XLF. Independently of LIG
Externí odkaz:
https://doaj.org/article/25865395ffa34e55964879d1f42c49a0
Autor:
Patryk Poliński, Marta Miret Cuesta, Alfonsa Zamora-Moratalla, Federica Mantica, Gerard Cantero-Recasens, Davide Normanno, Luis Iñiguez Rabago, Cruz Morenilla-Palao, Patricia Ordoño, Sophie Bonnal, Raúl Gómez Riera, María Martínez De Lagrán Cabredo, Álvaro Fernández-Blanco, Cristina Rodríguez-Marin, Jon Permanyer, Orsolya Fölsz, Cesar Sierra, Diana Legutko, José Wojnacki, Juan Luis Musoles Lleo, Eloisa Herrera, Mara Dierssen, Manuel Irimia
Actin cytoskeleton dynamics is crucial for neurogenesis and neuronal function. Precise quantitative and qualitative regulation of actin polymerization is achieved by multiple actin-binding proteins, among which formins are particularly versatile. Her
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36c323d7dfd5e612f2958e4c1a1d2072
https://doi.org/10.1101/2023.01.12.523772
https://doi.org/10.1101/2023.01.12.523772
Autor:
Annalisa Pierro, Alessio Bonucci, Davide Normanno, Mireille Ansaldi, Eric Pilet, Olivier Ouari, Bruno Guigliarelli, Emilien Etienne, Guillaume Gerbaud, Axel Magalon, Valérie Belle, Elisabetta Mileo
Publikováno v:
Chemistry – A European Journal. 28
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::90803e8497ee8801aedc5161c51f6037
https://doi.org/10.1002/chem.202203489
https://doi.org/10.1002/chem.202203489
Autor:
Annalisa Pierro, Alessio Bonucci, Davide Normanno, Mireille Ansaldi, Eric Pilet, Olivier Ouari, Bruno Guigliarelli, Emilien Etienne, Guillaume Gerbaud, Axel Magalon, Valérie Belle, Elisabetta Mileo
Publikováno v:
Chemistry-A European Journal
Chemistry-A European Journal, 2022, ⟨10.1002/chem.202202249⟩
Chemistry-A European Journal, 2022, ⟨10.1002/chem.202202249⟩
International audience; One of the current greatest challenges in structural biology is to study protein dynamics over a wide range of time scales in complex environments, such as the cell. Among magnetic resonances suitable for this approach, Electr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fe464eeb70acd3e9cdf11ed22e208b6
https://hal.science/hal-03836431
https://hal.science/hal-03836431
Autor:
Benjamin J. LaFrance, Johanna Roostalu, Gil Henkin, Basil J. Greber, Rui Zhang, Davide Normanno, Chloe O. McCollum, Thomas Surrey, Eva Nogales
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 119, iss 2
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
Significance Microtubules (MTs) are nonequilibrium polymers that switch between states of growth and shrinkage. This property is critical for their function and is a consequence of GTP hydrolysis in the MT. The structure of the stable GTP part of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df3a0e31d8f85e82ce3cca49e683755b
https://escholarship.org/uc/item/76v8v4sc
https://escholarship.org/uc/item/76v8v4sc
Autor:
Chloe O. McCollum, Basil J. Greber, Johanna Roostalu, Davide Normanno, Benjamin LaFrance, Eva Nogales, Rui Zhang, Gil Henkin, Thomas Surrey
Microtubules (MTs) are polymers of α/β-tubulin heterodimers that stochastically switch between growth and shrinkage phases. This dynamic instability is critically important for MT function. It is believed that GTP hydrolysis within the MT lattice i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c10020c75e96341fd4b7aa3875fba79b
https://doi.org/10.1101/2021.08.13.456308
https://doi.org/10.1101/2021.08.13.456308
Gradual compaction of the central spindle decreases its dynamicity in PRC1 and EB1 gene-edited cells
Publikováno v:
Life Science Alliance
Although different anaphase proteins bind with characteristically different strength to the central spindle, the overall central spindle dynamicity slows down as mitosis proceeds.
During mitosis, the spindle undergoes morphological and dynamic c
During mitosis, the spindle undergoes morphological and dynamic c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39c87e64e9cd8fba140659a81c421161
During mitosis the spindle undergoes morphological and dynamic changes. It reorganizes at the onset of anaphase when the antiparallel bundler PRC1 accumulates and recruits central spindle proteins to the midzone. Little is known about how the dynamic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8cd758d43ab2234ed57962d701d92069
https://doi.org/10.1101/2020.07.09.195347
https://doi.org/10.1101/2020.07.09.195347
Autor:
Ineke Brouwer, Abinadabe J. Melo de, Andrea Candelli, Gerrit Sitters, Davide Normanno, Erwin J.G. Peterman, Mauro Modesti, Stephanie J. Heerema, Gijs J.L. Wuite, Hongshan Zhang, Iddo Heller
Publikováno v:
Nature
Nature, Nature Publishing Group, 2016, 535 (7613), pp.566-569. ⟨10.1038/nature18643⟩
Nature, 2016, 535 (7613), pp.566-569. ⟨10.1038/nature18643⟩
Nature, 535(7613). Nature Publishing Group
Brouwer, I, Sitters, G, Candelli, A, Heerema, S J, Heller, I, de Melo, A J, Zhang, H S, Normanno, D, Modesti, M, Peterman, E J G & Wuite, G J L 2016, ' Sliding sleeves of XRCC4-XLF bridge DNA and connect fragments of broken DNA ', Nature, vol. 535, no. 7613, pp. 566 . https://doi.org/10.1038/nature18643
Nature, Nature Publishing Group, 2016, 535 (7613), pp.566-569. ⟨10.1038/nature18643⟩
Nature, 2016, 535 (7613), pp.566-569. ⟨10.1038/nature18643⟩
Nature, 535(7613). Nature Publishing Group
Brouwer, I, Sitters, G, Candelli, A, Heerema, S J, Heller, I, de Melo, A J, Zhang, H S, Normanno, D, Modesti, M, Peterman, E J G & Wuite, G J L 2016, ' Sliding sleeves of XRCC4-XLF bridge DNA and connect fragments of broken DNA ', Nature, vol. 535, no. 7613, pp. 566 . https://doi.org/10.1038/nature18643
Non-homologous end joining (NHEJ) is the primary pathway for repairing DNA double-strand breaks (DSBs) in mammalian cells. Such breaks are formed, for example, during gene-segment rearrangements in the adaptive immune system or by cancer therapeutic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a90b2598b598cceba7c1a4bfd439727
https://doi.org/10.1038/nature18643
https://doi.org/10.1038/nature18643