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29 results on '"Arteni, Ana Andreea"'

1. Low-boiling-point perfluorocarbon nanodroplets for adaptable ultrasound-induced blood-brain barrier opening

Author

Dauba, Ambre, Spitzlei, Claire, Bautista, Kathlyne Jayne B., Jourdain, Laurène, Selingue, Erwan, VanTreeck, Kelly E., Mattern, Jacob A., Denis, Caroline, Ouldali, Malika, Arteni, Ana-Andreea, Truillet, Charles, Larrat, Benoit, Tsuruta, James, Durham, Phillip G., Papadopoulou, Virginie, Dayton, Paul A., Tsapis, Nicolas, and Novell, Anthony

Published
2024
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2. Dynamic BTB-domain filaments promote clustering of ZBTB proteins

Author

Mance, Lucija, Bigot, Nicolas, Zhamungui Sánchez, Edison, Coste, Franck, Martín-González, Natalia, Zentout, Siham, Biliškov, Marin, Pukało, Zofia, Mishra, Aanchal, Chapuis, Catherine, Arteni, Ana-Andreea, Lateur, Axelle, Goffinont, Stéphane, Gaudon, Virginie, Talhaoui, Ibtissam, Casuso, Ignacio, Beaufour, Martine, Garnier, Norbert, Artzner, Franck, Cadene, Martine, Huet, Sébastien, Castaing, Bertrand, and Suskiewicz, Marcin Józef

Published
2024
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8. Insight into microtubule nucleation from tubulin-capping proteins

Author

Campanacci, Valérie, Urvoas, Agathe, Cantos-Fernandes, Soraya, Aumont-Nicaise, Magali, Arteni, Ana-Andreea, Velours, Christophe, Valerio-Lepiniec, Marie, Dreier, Birgit, Plückthun, Andreas, Pilon, Antoine, Poüs, Christian, Minard, Philippe, and Gigant, Benoît

Published
2019

9. BRCA2-HSF2BP oligomeric ring disassembly by BRME1 promotes homologous recombination

Author

Ghouil, Rania, primary, Miron, Simona, additional, Sato, Koichi, additional, Ristic, Dejan, additional, van Rossum-Fikkert, Sari E., additional, Legrand, Pierre, additional, Ouldali, Malika, additional, Winter, Jean-Marie, additional, Ropars, Virginie, additional, David, Gabriel, additional, Arteni, Ana-Andreea, additional, Wyman, Claire, additional, Knipscheer, Puck, additional, Kanaar, Roland, additional, Zelensky, Alex N., additional, and Zinn-Justin, Sophie, additional

Published
2023
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10. BRCA2-HSF2BP oligomeric ring assembly is implicated in the regulation of homologous recombination during meiosis

Author

Ghouil, Rania, primary, Miron, Simona, additional, Legrand, Pierre, additional, Sato, Koichi, additional, Ristic, Dejan, additional, van Rossum-Fikkert, Sari E., additional, Ouldali, Malika, additional, Winter, Jean-Marie, additional, Ropars, Virginie, additional, David, Gabriel, additional, Arteni, Ana-Andreea, additional, Wyman, Claire, additional, Knipscheer, Puck, additional, Kanaar, Roland, additional, Zelensky, Alex N., additional, and Zinn-Justin, Sophie, additional

Published
2023
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11. BRCA2-HSF2BP oligomeric ring disassembly by BRME1 promotes homologous recombination

Author

Ghouil, Rania, Miron, Simona, Sato, Koichi, Ristic, Dejan, van Rossum-Fikkert, Sari E., Legrand, Pierre, Ouldali, Malika, Winter, Jean Marie, Ropars, Virginie, David, Gabriel, Arteni, Ana Andreea, Wyman, Claire, Knipscheer, Puck, Kanaar, Roland, Zelensky, Alex N., Zinn-Justin, Sophie, Ghouil, Rania, Miron, Simona, Sato, Koichi, Ristic, Dejan, van Rossum-Fikkert, Sari E., Legrand, Pierre, Ouldali, Malika, Winter, Jean Marie, Ropars, Virginie, David, Gabriel, Arteni, Ana Andreea, Wyman, Claire, Knipscheer, Puck, Kanaar, Roland, Zelensky, Alex N., and Zinn-Justin, Sophie

Abstract

In meiotic homologous recombination (HR), BRCA2 facilitates loading of the recombinases RAD51 and DMC1 at the sites of double-strand breaks (DSBs). The HSF2BP-BRME1 complex interacts with BRCA2. Its absence causes a severe reduction in recombinase loading at meiotic DSB. We previously showed that, in somatic cancer cells ectopically producing HSF2BP, DNA damage can trigger HSF2BP-dependent degradation of BRCA2, which prevents HR. Here, we report that, upon binding to BRCA2, HSF2BP forms octameric rings that are able to interlock into a large ring-shaped 24-nucleotide oligomer. Addition of BRME1 leads to dissociation of both of these ring structures and cancels the disruptive effect of HSF2BP on cancer cell resistance to DNA damage. It also prevents BRCA2 degradation during interstrand DNA crosslink repair in Xenopus egg extracts. We propose that, during meiosis, the control of HSF2BP-BRCA2 oligomerization by BRME1 ensures timely assembly of the ring complex that concentrates BRCA2 and controls its turnover, thus promoting HR.

Published
2023

12. BRCA2-HSF2BP oligomeric ring disassembly by BRME1 promotes homologous recombination

Author

Hubrecht Institute with UMC, Ghouil, Rania, Miron, Simona, Sato, Koichi, Ristic, Dejan, van Rossum-Fikkert, Sari E., Legrand, Pierre, Ouldali, Malika, Winter, Jean Marie, Ropars, Virginie, David, Gabriel, Arteni, Ana Andreea, Wyman, Claire, Knipscheer, Puck, Kanaar, Roland, Zelensky, Alex N., Zinn-Justin, Sophie, Hubrecht Institute with UMC, Ghouil, Rania, Miron, Simona, Sato, Koichi, Ristic, Dejan, van Rossum-Fikkert, Sari E., Legrand, Pierre, Ouldali, Malika, Winter, Jean Marie, Ropars, Virginie, David, Gabriel, Arteni, Ana Andreea, Wyman, Claire, Knipscheer, Puck, Kanaar, Roland, Zelensky, Alex N., and Zinn-Justin, Sophie

Published
2023

13. The luminal domain of Toxoplasma gondii sortilin adopts a ring-shaped structure exhibiting motifs specific to apicomplexan parasites

Author

Honfozo, Ariane, primary, Ghouil, Rania, additional, Alayi, Tchilabalo Dilezitoko, additional, Ouldali, Malika, additional, Arteni, Ana-Andreea, additional, Atindehou, Cynthia Menonve, additional, Fanou, Lucie Ayi, additional, Hathout, Yetrib, additional, Zinn-Justin, Sophie, additional, and Tomavo, Stanislas, additional

Published
2023
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15. Structural analysis of Toxoplasma gondiisortilin

Author

Honfozo, Ariane, primary, Ghouil, Rania, additional, Alayi, Tchilabalo Dilezitoko, additional, Ouldali, Malika, additional, Arteni, Ana-Andreea, additional, Atindehou, Cynthia Menonve, additional, Fanou, Lucie Ayi, additional, Hathout, Yetrib, additional, Zinn-Justin, Sophie, additional, and Tomavo, Stanislas, additional

Published
2022
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16. Emerin self‐assembly mechanism: role of the LEM domain

Author

Samson, Camille, Celli, Florian, Hendriks, Kitty, Zinke, Maximilian, Essawy, Nada, Herrada, Isaline, Arteni, Ana‐Andreea, Theillet, François‐Xavier, Alpha‐Bazin, Béatrice, Armengaud, Jean, Coirault, Catherine, Lange, Adam, and Zinn‐Justin, Sophie

Published
2017
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18. Atomic structure of Lanreotide nanotubes revealed by cryo-EM

Author

Pieri, Laura, primary, Wang, Fengbin, additional, Arteni, Ana-Andreea, additional, Vos, Matthijn, additional, Winter, Jean-Marie, additional, Le Du, Marie-Hélène, additional, Artzner, Franck, additional, Gobeaux, Frédéric, additional, Legrand, Pierre, additional, Boulard, Yves, additional, Bressanelli, Stéphane, additional, Egelman, Edward H., additional, and Paternostre, Maité, additional

Published
2022
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22. Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

Author

Guerrero-Ferreira, Ricardo, primary, Taylor, Nicholas MI, additional, Arteni, Ana-Andreea, additional, Kumari, Pratibha, additional, Mona, Daniel, additional, Ringler, Philippe, additional, Britschgi, Markus, additional, Lauer, Matthias E, additional, Makky, Ali, additional, Verasdonck, Joeri, additional, Riek, Roland, additional, Melki, Ronald, additional, Meier, Beat H, additional, Böckmann, Anja, additional, Bousset, Luc, additional, and Stahlberg, Henning, additional

Published
2019
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23. Author response: Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

Author

Guerrero-Ferreira, Ricardo, primary, Taylor, Nicholas MI, additional, Arteni, Ana-Andreea, additional, Kumari, Pratibha, additional, Mona, Daniel, additional, Ringler, Philippe, additional, Britschgi, Markus, additional, Lauer, Matthias E, additional, Makky, Ali, additional, Verasdonck, Joeri, additional, Riek, Roland, additional, Melki, Ronald, additional, Meier, Beat H, additional, Böckmann, Anja, additional, Bousset, Luc, additional, and Stahlberg, Henning, additional

Published
2019
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26. Structure and Conformation of the Carotenoids in Human Retinal Macular Pigment

Author

Arteni , Ana-Andreea, Fradot , Mathias, Galzerano , Denise, Mendes-Pinto , Maria M., Sahel , José-Alain, Picaud , Serge, Robert , Bruno, Pascal , Andrew A., Institut de Biologie et de Technologies de Saclay ( IBITECS ), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ), Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Institut de la Vision, Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Institut de Biologie et de Technologies de Saclay (IBITECS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), and Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)

Subjects
[ SDV ] Life Sciences [q-bio], [SDV]Life Sciences [q-bio], Lutein, lcsh:R, Molecular Conformation, lcsh:Medicine, food and beverages, macromolecular substances, Spectrum Analysis, Raman, eye diseases, Zeaxanthins, Humans, lcsh:Q, Macular Pigment, sense organs, lcsh:Science, Retinal Pigments, Research Article
Abstract

International audience; Human retinal macular pigment (MP) is formed by the carotenoids lutein and zeaxanthin (including the isomer meso-zeaxanthin). MP has several functions in improving visual performance and protecting against the damaging effects of light, and MP levels are used as a proxy for macular health-specifically, to predict the likelihood of developing age-related macular degeneration. While the roles of these carotenoids in retinal health have been the object of intense study in recent years, precise mechanistic details of their protective action remain elusive. We have measured the Raman signals originating from MP carotenoids in ex vivo human retinal tissue, in order to assess their structure and conformation. We show that it is possible to distinguish between lutein and zeaxanthin, by their excitation profile (related to their absorption spectra) and the position of their ν1 Raman mode. In addition, analysis of the ν4 Raman band indicates that these carotenoids are present in a specific, constrained conformation in situ, consistent with their binding to specific proteins as postulated in the literature. We discuss how these conclusions relate to the function of these pigments in macular protection. We also address the possibilities for a more accurate, consistent measurement of MP levels by Raman spectroscopy.

Published
2015

27. Unraveling the structure of the photosynthetic membrane using electron microscopy approach

Author

Arteni, Ana Andreea, Arteni, Ana Andreea, Arteni, Ana Andreea, and Arteni, Ana Andreea

Abstract

Cyanobacteriën of blauwalgen zijn foto-autotrofe bacteriën die leven van fotosynthese. Cyanobacterien hebben in tegenstelling tot hogere planten geen chloroplasten maar phycobilisomen, supramoleculaire aggregaten van fotosynthesemembranen. Fotosynthese vindt plaats door middel van pigment bevattende eiwitten die geassocieerd zijn met de fotosynthesemembranen. Fotosysteem I (PSI) en fotosysteem II (PSII) zijn beide belangrijke schakels in het omzetten van zonne-energie naar chemisch vastgelegde energie. Elektronenmicroscopie en beeldverwerking van losse deeltjes is gebruikt om de structuur van PSI en PSII nader te bestuderen. Door een systematische vergelijking te maken tussen op twee verschillende manieren gezuiverd PSII kon een 6.8 kDa kleine subeenheid (PsbZ) in het eiwit worden gelokaliseerd. Nieuw was de combinatie tussen massaspectrometrie en elektronenmicroscopie. NAD(P)H dehydrogenase type 1 (NDH-1) van cyanobacteriën werd bestudeerd na groei onder verschillende CO2 condities. Hierdoor konden twee kleinere eiwit complexen (NDH-1M en NDH-1I) worden geïdentificeerd zonder de NdhD1 en NdhF1 subeenheid. Verder werden eiwitcomplexen van NDH-1 gevonden met extra massa vergelijkbaar met complex-1 van E. coli en andere organisme. Cyanobacterie PSII ondergaat een structurele verandering als het organisme groeit bij gebrek aan ijzer. Onder deze condities bindt het IsiA (iron-stress-induced protein A) uitsluitend aan PSII dimeren en niet aan PSII monomeren. Mutanten van phycobilisomen werden gebruikt om de posities van een aantal eiwitten te bepalen. Door vergelijking van de projectiemappen van de wild-type en de mutanten die één of meerdere eiwitten missen kon de bindingspositie bepaald worden.

Published
2007

28. Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

Author

Guerrero-Ferreira, Ricardo, Taylor, Nicholas M.I., Arteni, Ana-Andreea, Kumari, Pratibha, Mona, Daniel, Ringler, Philippe, Britschgi, Markus, Lauer, Matthias E., Makky, Ali, Verasdonck, Joeri, Riek, Roland, Melki, Ronald, Meier, Beat H., Böckmann, Anja, Bousset, Luc, and Stahlberg, Henning

Subjects
3. Good health
Abstract

Intracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological diseases including Parkinson’s disease (PD). Previously, we reported the structure of alpha-synuclein fibrils (residues 1–121), composed of two protofibrils that are connected via a densely-packed interface formed by residues 50–57 (Guerrero-Ferreira, eLife 218;7:e36402). We here report two new polymorphic atomic structures of alpha-synuclein fibrils termed polymorphs 2a and 2b, at 3.0 Å and 3.4 Å resolution, respectively. These polymorphs show a radically different structure compared to previously reported polymorphs. The new structures have a 10 nm fibril diameter and are composed of two protofilaments which interact via intermolecular salt-bridges between amino acids K45, E57 (polymorph 2a) or E46 (polymorph 2b). The non-amyloid component (NAC) region of alpha-synuclein is fully buried by previously non-described interactions with the N-terminus. A hydrophobic cleft, the location of familial PD mutation sites, and the nature of the protofilament interface now invite to formulate hypotheses about fibril formation, growth and stability., eLife, 8, ISSN:2050-084X

29. Structure and Conformation of the Carotenoids in Human Retinal Macular Pigment.

Author

Arteni AA, Fradot M, Galzerano D, Mendes-Pinto MM, Sahel JA, Picaud S, Robert B, and Pascal AA

Subjects
Humans, Lutein metabolism, Molecular Conformation, Retinal Pigments metabolism, Spectrum Analysis, Raman, Zeaxanthins metabolism, Lutein chemistry, Macular Pigment analysis, Retinal Pigments chemistry, Zeaxanthins chemistry
Abstract

Human retinal macular pigment (MP) is formed by the carotenoids lutein and zeaxanthin (including the isomer meso-zeaxanthin). MP has several functions in improving visual performance and protecting against the damaging effects of light, and MP levels are used as a proxy for macular health-specifically, to predict the likelihood of developing age-related macular degeneration. While the roles of these carotenoids in retinal health have been the object of intense study in recent years, precise mechanistic details of their protective action remain elusive. We have measured the Raman signals originating from MP carotenoids in ex vivo human retinal tissue, in order to assess their structure and conformation. We show that it is possible to distinguish between lutein and zeaxanthin, by their excitation profile (related to their absorption spectra) and the position of their ν1 Raman mode. In addition, analysis of the ν4 Raman band indicates that these carotenoids are present in a specific, constrained conformation in situ, consistent with their binding to specific proteins as postulated in the literature. We discuss how these conclusions relate to the function of these pigments in macular protection. We also address the possibilities for a more accurate, consistent measurement of MP levels by Raman spectroscopy.

Published
2015
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