Search Results - "Le Meur, Remy"

A key interaction with RPA orients XPA in NER complexes by Topolska-Woś, Agnieszka M, Sugitani, Norie, Cordoba, John J, Le Meur, Kateryna V, Le Meur, Rémy A, Kim, Hyun Suk, Yeo, Jung-Eun, Rosenberg, Daniel, Hammel, Michal, Schärer, Orlando D, Chazin, Walter J

“…The XPA protein functions together with the single-stranded DNA (ssDNA) binding protein RPA as the central scaffold to ensure proper positioning of repair…”
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RADX Promotes Genome Stability and Modulates Chemosensitivity by Regulating RAD51 at Replication Forks by Dungrawala, Huzefa, Bhat, Kamakoti P., Le Meur, Rémy, Chazin, Walter J., Ding, Xia, Sharan, Shyam K., Wessel, Sarah R., Sathe, Aditya A., Zhao, Runxiang, Cortez, David

“…RAD51 promotes homology-directed repair (HDR), replication fork reversal, and stalled fork protection. Defects in these functions cause genomic instability and…”
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DNA-binding mechanism and evolution of replication protein A by Madru, Clément, Martínez-Carranza, Markel, Laurent, Sébastien, Alberti, Alessandra C., Chevreuil, Maelenn, Raynal, Bertrand, Haouz, Ahmed, Le Meur, Rémy A., Delarue, Marc, Henneke, Ghislaine, Flament, Didier, Krupovic, Mart, Legrand, Pierre, Sauguet, Ludovic

“…Replication Protein A (RPA) is a heterotrimeric single stranded DNA-binding protein with essential roles in DNA replication, recombination and repair. Little…”
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Liquid Native MALDI Mass Spectrometry for the Detection of Protein-Protein Complexes by Beaufour, Martine, Ginguené, David, Le Meur, Rémy, Castaing, Bertrand, Cadene, Martine

“…Native mass spectrometry (MS) encompasses methods to keep noncovalent interactions of biomolecular complexes intact in the gas phase throughout the instrument…”
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Identification of Chemical Probes Targeting MBD2 by Erdmann, Diane, Contreras, Jean, Le Meur, Rémy A., Vitorge, Bruno, Saverat, Vincent, Tafit, Ambre, Jallet, Corinne, Cadet-Daniel, Véronique, Bon, Corentin, Phansavath, Phannarath, Ratovelomanana-Vidal, Virginie, Jeltsch, Albert, Vichier-Guerre, Sophie, Guijarro, J. Iñaki, Arimondo, Paola B.

“…Epigenetics has received much attention in the past decade. Many insights on epigenetic (dys)­regulation in diseases have been obtained, and clinical therapies…”
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The CaMKII inhibitor KN93-calmodulin interaction and implications for calmodulin tuning of NaV1.5 and RyR2 function by Johnson, Christopher N., Pattanayek, Rekha, Potet, Franck, Rebbeck, Robyn T., Blackwell, Daniel J., Nikolaienko, Roman, Sequeira, Vasco, Le Meur, Remy, Radwański, Przemysław B., Davis, Jonathan P., Zima, Aleksey V., Cornea, Razvan L., Damo, Steven M., Györke, Sandor, George, Alfred L., Knollmann, Björn C.

“…[Display omitted] •Ca2+ /Calmodulin (CaM) binds the CaM dependent kinase II inhibitor (CaMKII) KN93.•KN93 modifies NaV1.5 and RyR2 function independent of…”
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Conidium Specific Polysaccharides in Aspergillus fumigatus by Liu, Zhonghua, Valsecchi, Isabel, Le Meur, Rémy A, Simenel, Catherine, Guijarro, J Iñaki, Comte, Catherine, Muszkieta, Laetitia, Mouyna, Isabelle, Henrissat, Bernard, Aimanianda, Vishukumar, Latgé, Jean-Paul, Fontaine, Thierry

“…Earlier studies have shown that the outer layers of the conidial and mycelial cell walls of are different. In this work, we analyzed the polysaccharidome of…”
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The nucleoid-associated protein HU enhances 8-oxoguanine base excision by the formamidopyrimidine-DNA glycosylase by Le Meur, Rémy, Culard, Françoise, Nadan, Virginie, Goffinont, Stéphane, Coste, Franck, Guerin, Martine, Loth, Karine, Landon, Céline, Castaing, Bertrand

“…The nucleoid-associated protein HU is involved in numerous DNA transactions and thus is essential in DNA maintenance and bacterial survival. The high affinity…”
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Molecular basis and functional consequences of the interaction between the base excision repair DNA glycosylase NEIL1 and RPA by Le Meur, Rémy A., Pecen, Turner J., Le Meur, Kateryna V., Nagel, Zachary D., Chazin, Walter J.

“…NEIL1 is a DNA glycosylase that recognizes and initiates base excision repair of oxidized bases. The ubiquitous ssDNA binding scaffolding protein, replication…”
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EXO5-DNA structure and BLM interactions direct DNA resection critical for ATR-dependent replication restart by Hambarde, Shashank, Tsai, Chi-Lin, Pandita, Raj K., Bacolla, Albino, Maitra, Anirban, Charaka, Vijay, Hunt, Clayton R., Kumar, Rakesh, Limbo, Oliver, Le Meur, Remy, Chazin, Walter J., Tsutakawa, Susan E., Russell, Paul, Schlacher, Katharina, Pandita, Tej K., Tainer, John A.

“…Stalled DNA replication fork restart after stress as orchestrated by ATR kinase, BLM helicase, and structure-specific nucleases enables replication, cell…”
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The CaMKII inhibitor KN93-calmodulin interaction and implications for calmodulin tuning of NaV1.5 and RyR2 function by Johnson, Christopher N., Pattanayek, Rekha, Potet, Franck, Rebbeck, Robyn T., Blackwell, Daniel J., Nikolaienko, Roman, Sequeira, Vasco, Le Meur, Remy, Radwański, Przemysław B., Davis, Jonathan P., Zima, Aleksey V., Cornea, Razvan L., Damo, Steven M., Györke, Sandor, George, Jr., Alfred L., Knollmann, Björn C.

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The CaMKII inhibitor KN93-calmodulin interaction and implications for calmodulin tuning of Na V 1.5 and RyR2 function by Johnson, Christopher N, Pattanayek, Rekha, Potet, Franck, Rebbeck, Robyn T, Blackwell, Daniel J, Nikolaienko, Roman, Sequeira, Vasco, Le Meur, Remy, Radwański, Przemysław B, Davis, Jonathan P, Zima, Aleksey V, Cornea, Razvan L, Damo, Steven M, Györke, Sandor, George, Jr, Alfred L, Knollmann, Björn C

“…Here we report the structure of the widely utilized calmodulin (CaM)-dependent protein kinase II (CaMKII) inhibitor KN93 bound to the Ca -sensing protein CaM…”
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Conidium Specific Polysaccharides in IAspergillus fumigatus/I by Liu, Zhonghua, Valsecchi, Isabel, Le Meur, Rémy A, Simenel, Catherine, Guijarro, J. Iñaki, Comte, Catherine, Muszkieta, Laetitia, Mouyna, Isabelle, Henrissat, Bernard, Aimanianda, Vishukumar, Latgé, Jean-Paul, Fontaine, Thierry

“…Earlier studies have shown that the outer layers of the conidial and mycelial cell walls of Aspergillus fumigatus are different. In this work, we analyzed the…”
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Backbone assignment of the three dimers of HU from Escherichia coli at 293 K: EcHUα2, EcHUβ2 and EcHUαβ by Le Meur, Rémy, Loth, Karine, Culard, Françoise, Castaing, Bertrand, Landon, Céline

“…HU is one of the major nucleoid-associated proteins involved in bacterial chromosome structure and in all DNA-dependent cellular activities. Similarly to…”
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