Výsledky vyhledávání - "Davide Normanno"

Akademický článek

Human RAD52 Captures and Holds DNA Strands, Increases DNA Flexibility, and Prevents Melting of Duplex DNA: Implications for DNA Recombination

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

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A novel regulatory mechanism of actin cytoskeleton dynamics through a neural microexon in DAAM1 is important for proper memory formation

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

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Cover Feature: Probing the Structural Dynamics of a Bacterial Chaperone in Its Native Environment by Nitroxide‐Based EPR Spectroscopy (Chem. Eur. J. 66/2022)

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

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Probing Structural Dynamics of a Bacterial Chaperone in Its Native Environment by Nitroxide-Based EPR Spectroscopy

Publikováno v: Chemistry-A European Journal
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

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Akademický článek

Mutational phospho-mimicry reveals a regulatory role for the XRCC4 and XLF C-terminal tails in modulating DNA bridging during classical non-homologous end joining

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

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Structural transitions in the GTP cap visualized by cryo-electron microscopy of catalytically inactive microtubules

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

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

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Structural transitions in the GTP cap visualized by cryo-EM of catalytically inactive microtubules

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

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Gradual compaction of the central spindle decreases its dynamicity in PRC1 and EB1 gene-edited cells

Autor: Nicholas I. Cade, Wei Ming Lim, Davide Normanno, Jayant Asthana, Thomas Surrey

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39c87e64e9cd8fba140659a81c421161

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Gradual Compaction of the Central Spindle Decreases its Dynamicity as Revealed in PRC1 and EB1 Gene-Edited Human Cells

Autor: Thomas Surrey, Wei Ming Lim, Davide Normanno, Nicholas I. Cade, Jayant Asthana

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

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Sliding sleeves of XRCC4–XLF bridge DNA and connect fragments of broken DNA

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

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

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