Zobrazeno 1 - 10 of 60 pro vyhledávání: '"MESH: Protein Interaction Domains and Motifs"'
1
The coordinated replication of Vibrio cholerae’s two chromosomes required the acquisition of a unique domain by the RctB initiator
Autor: Fournes, Florian, Niault, Theophile, Czarnecki, Jakub, Tissier-Visconti, Alvise, Mazel, Didier, Val, Marie-Eve
Publikováno v: Nucleic Acids Research
Nucleic Acids Research, 2021, 49 (19), pp.11119-11133. ⟨10.1093/nar/gkab903⟩
Nucleic Acids Research, Oxford University Press, 2021, 49 (19), pp.11119-11133. ⟨10.1093/nar/gkab903⟩
International audience; Vibrio cholerae, the pathogenic bacterium that causes cholera, has two chromosomes (Chr1, Chr2) that replicate in a well-orchestrated sequence. Chr2 initiation is triggered only after the replication of the crtS site on Chr1.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::78989246a70ed6b9797197547822388d
http://europepmc.org/articles/PMC8565311
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2
Characterization of the Interaction Domains between the Phosphoprotein and the Nucleoprotein of Human Metapneumovirus
Autor: Jean-François Eléouët, Monika Bajorek, Luis Checa Ruano, Marie Galloux, Jenna Fix, Charles-Adrien Richard, Hortense Decool, Olivier Sperandio, Irina Gutsche, Benjamin Bardiaux
Publikováno v: J Virol
Journal of Virology
Journal of Virology, 2022, 96 (2), pp.e0090921. ⟨10.1128/JVI.00909-21⟩
Human metapneumovirus (HMPV) causes severe respiratory diseases in young children. The HMPV RNA genome is encapsidated by the viral nucleoprotein (N), forming an RNA-N complex (N(Nuc)), which serves as the template for genome replication and mRNA tra
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f7efcc80720167008066e4d77c332fd
https://europepmc.org/articles/PMC8791268/
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3
MAD2L2 dimerization and TRIP13 control shieldin activity in DNA repair
Autor: de Krijger, Inge, Föhr, Bastian, Pérez, Santiago Hernández, Vincendeau, Estelle, Serrat, Judit, Thouin, Alexander Marc, Susvirkar, Vivek, Lescale, Chloé, Paniagua, Inés, Hoekman, Liesbeth, Kaur, Simranjeet, Altelaar, Maarten, Deriano, Ludovic, Faesen, Alex C, Jacobs, Jacqueline J L, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics
Publikováno v: Nature Communications
Nature Communications, Nature Publishing Group, 2021, 12 (1), pp.5421. ⟨10.1038/s41467-021-25724-y⟩
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Nature Communications, 12(1). Nature Publishing Group
Nature Communications, 2021, 12 (1), pp.5421. ⟨10.1038/s41467-021-25724-y⟩
Nature Communications, Nature Publishing Group, 2021, 12 (1), ⟨10.1038/s41467-021-25724-y⟩
MAD2L2 (REV7) plays an important role in DNA double-strand break repair. As a member of the shieldin complex, consisting of MAD2L2, SHLD1, SHLD2 and SHLD3, it controls DNA repair pathway choice by counteracting DNA end-resection. Here we investigated
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e0eef28d1f10f82de63f851b152c960
https://hdl.handle.net/21.11116/0000-000A-7D73-921.11116/0000-000A-7D6F-F
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4
The steroid derivative 6-aminocholestanol inhibits the DEAD-box helicase eIF4A (LieIF4A) from the Trypanosomatid parasite Leishmania by perturbing the RNA and ATP binding sites
Autor: N. Kyle Tanner, Mourad Barhoumi, Emna Harigua-Souiai, Arnaud Blondel, Josette Banroques, Yosser Zina Abdelkrim, Ikram Guizani
Publikováno v: Molecular and Biochemical Parasitology
Molecular and Biochemical Parasitology, 2018, 226, pp.9-19. ⟨10.1016/j.molbiopara.2018.10.001⟩
Molecular and Biochemical Parasitology, Elsevier, 2018, 226, pp.9-19. ⟨10.1016/j.molbiopara.2018.10.001⟩
International audience; The antifungal agent 6-aminocholestanol targets the production of ergosterol, which is the principle sterol in many fungi and protozoans; ergosterol serves many of the same roles as cholesterol in animals. We found that it als
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d1cab00f461442b882b9cc5b78e1a41
https://doi.org/10.1016/j.molbiopara.2018.10.001
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5
Novel ribonucleotide discrimination in the RNA polymerase-like two-barrel catalytic core of Family D DNA polymerases
Autor: Thomas C. Evans, Andrew F. Gardner, Ece Alpaslan, Kelly M Zatopek, Ludovic Sauguet
Publikováno v: Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2020, 48 (21), pp.12204-12218. ⟨10.1093/nar/gkaa986⟩
Nucleic Acids Research, 2020, 48 (21), pp.12204-12218. ⟨10.1093/nar/gkaa986⟩
Family D DNA polymerase (PolD) is the essential replicative DNA polymerase for duplication of most archaeal genomes. PolD contains a unique two-barrel catalytic core absent from all other DNA polymerase families but found in RNA polymerases (RNAPs).
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85fbf1b87ad50a09fe8aa5c33da49784
https://hal-pasteur.archives-ouvertes.fr/pasteur-03086156/document
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6
Differential activity and selectivity of N‐terminal modified CXCL12 chemokines at the CXCR4 and ACKR3 receptors
Autor: Carmen Gallego, Françoise Bachelerie, Françoise Baleux, Erika Cecon, Agnieszka Jaracz-Ros, Pasquale Cutolo, Angélique Levoye, Irina Kufareva, Guillaume Bernadat, Martin Gustavsson, Tracy M. Handel
Publikováno v: Journal of Leukocyte Biology
Journal of Leukocyte Biology, Society for Leukocyte Biology, 2020, 107 (6), pp.1123-1135. ⟨10.1002/jlb.2ma0320-383rr⟩
J Leukoc Biol
Journal of Leukocyte Biology, 2020, 107 (6), pp.1123-1135. ⟨10.1002/jlb.2ma0320-383rr⟩
Journal of leukocyte biology, vol 107, iss 6
Chemokines play critical roles in numerous physiologic and pathologic processes through their action on seven-transmembrane (TM) receptors. The N-terminal domain of chemokines, which is a key determinant of signaling via its binding within a pocket f
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c8ab59a65992cf5ae58cc65116784d0
https://hal-pasteur.archives-ouvertes.fr/pasteur-03260272/document
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7
Methylcytosine dioxygenase TET3 interacts with thyroid hormone nuclear receptors and stabilizes their association to chromatin
Autor: Romain Guyot, Jacques Samarut, Karine Gauthier, Frédéric Flamant, Wenyue Guan, Jiemin Wong
Publikováno v: 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, National Academy of Sciences, 2017, 114 (31), pp.8229-8234. ⟨10.1073/pnas.1702192114⟩
Proceedings of the National Academy of Sciences of the United States of America, 2017, 114 (31), pp.8229-8234. ⟨10.1073/pnas.1702192114⟩
International audience; Thyroid hormone receptors (TRs) are members of the nuclear hormone receptor superfamily that act as ligand-dependent transcription factors. Here we identified the ten-eleven translocation protein 3 (TET3) as a TR interacting p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccf2b53766639fbc3f46a5f35c84cc8c
https://doi.org/10.1073/pnas.1702192114
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8
Functional recruitment of dynamin requires multimeric interactions for efficient endocytosis
Autor: David Perrais, Thi Nhu Ngoc Van, Matthieu Sainlos, Silvia Sposini, Daniel Choquet, Morgane Rosendale, Isabel Gauthereau, Léa Claverie, Dolors Grillo-Bosch, Stéphane Claverol
Publikováno v: Nature Communications
Nature Communications, Nature Publishing Group, 2019, 10 (1), ⟨10.1038/s41467-019-12434-9⟩
Nature Communications, Nature Publishing Group, 2019, 10 (1), pp.4462. ⟨10.1038/s41467-019-12434-9⟩
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
During clathrin mediated endocytosis (CME), the concerted action of dynamin and its interacting partners drives membrane scission. Essential interactions occur between the proline/arginine-rich domain of dynamin (dynPRD) and the Src-homology domain 3
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::180bae18dfce814aa64800866cdb861d
https://doi.org/10.1038/s41467-019-12434-9
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9
The reaction mechanism of metallo-lactamases is tuned by the conformation of an active-site mobile loop
Autor: Estefanía Giannini, Lisandro H. Otero, Antonela Rocio Palacios, Magdalena A. Taracila, Pedro M. Alzari, Sebastián Klinke, Christopher R. Bethel, Maria F. Mojica, Robert A. Bonomo, Leticia I. Llarrull, Alejandro J. Vila
Publikováno v: Repositorio U. El Bosque
Universidad El Bosque
instacron:Universidad El Bosque
Antimicrobial Agents and Chemotherapy
Antimicrobial Agents and Chemotherapy, American Society for Microbiology, 2019, 63 (1), ⟨10.1128/AAC.01754-18⟩
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Antimicrobial Agents and Chemotherapy, 2019, 63 (1), ⟨10.1128/AAC.01754-18⟩
Carbapenems are "last resort" β-lactam antibiotics used to treat serious and life-threatening health care-associated infections caused by multidrug-resistant Gram-negative bacteria. Unfortunately, the worldwide spread of genes coding for carbapenema
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07bd3a48e1f34836367d2f135f8ca8d6
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10
Camelid nanobodies used as crystallization chaperones for different constructs of PorM, a component of the type IX secretion system from Porphyromonas gingivalis
Autor: Christian Cambillau, Christine Kellenberger, Alain Roussel, Aline Desmyter, Anaïs Gaubert, Jennifer Roche, Philippe Leone, Thi Trang Nhung Trinh, Yoan Duhoo
Publikováno v: Acta crystallographica. Section F, Structural biology communications
Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd, 2017, 73 (5), pp.286-293. ⟨10.1107/S2053230X17005969⟩
Acta crystallographica Section F : Structural biology communications [2014-...]
Acta crystallographica Section F : Structural biology communications [2014-..], 2017, 73 (5), pp.286-293. ⟨10.1107/S2053230X17005969⟩
Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd, 2017, 73 (5), pp.286-293. 〈10.1107/S2053230X17005969〉
PorM is a membrane protein that is involved in the assembly of the type IX secretion system (T9SS) inPorphyromonas gingivalis, a major bacterial pathogen that is responsible for periodontal disease in humans. In the context of structural studies of P
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3536833fa425e3c63576ed23e2ee7679
https://hal.archives-ouvertes.fr/hal-01802819
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