Zobrazeno 1 - 10
of 171
pro vyhledávání: '"Bruno Guigliarelli"'
Autor:
Annalisa Pierro, Ketty Concetta Tamburrini, Hugo Leguenno, Guillaume Gerbaud, Emilien Etienne, Bruno Guigliarelli, Valérie Belle, Barbara Zambelli, Elisabetta Mileo
Publikováno v:
iScience, Vol 26, Iss 10, Pp 107855- (2023)
Summary: UreG is a cytosolic GTPase involved in the maturation network of urease, an Ni-containing bacterial enzyme. Previous investigations in vitro showed that UreG features a flexible tertiary organization, making this protein the first enzyme dis
Externí odkaz:
https://doaj.org/article/1fcbd728d8274d93bed40ddbbb2e6bae
Autor:
Majid Haddad Momeni, Folmer Fredslund, Bastien Bissaro, Olanrewaju Raji, Thu V. Vuong, Sebastian Meier, Tine Sofie Nielsen, Vincent Lombard, Bruno Guigliarelli, Frédéric Biaso, Mireille Haon, Sacha Grisel, Bernard Henrissat, Ditte Hededam Welner, Emma R. Master, Jean-Guy Berrin, Maher Abou Hachem
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Microbial oxidoreductases are key in biomass breakdown. Here, the authors expand the specificity and redox scope within fungal auxiliary activity 7 family (AA7) enzymes and show that AA7 oligosaccharide dehydrogenases can directly fuel cellulose degr
Externí odkaz:
https://doaj.org/article/0da8e321f452495c9a48a6a598783fe7
Autor:
Laura Prioretti, Giulia D’Ermo, Pascale Infossi, Arlette Kpebe, Régine Lebrun, Marielle Bauzan, Elisabeth Lojou, Bruno Guigliarelli, Marie-Thérèse Giudici-Orticoni, Marianne Guiral
Publikováno v:
Life, Vol 13, Iss 3, p 627 (2023)
Aquifex aeolicus is a microaerophilic hydrogen- and sulfur -oxidizing bacterium that assimilates CO2 via the reverse tricarboxylic acid cycle (rTCA). Key enzymes of this pathway are pyruvate:ferredoxin oxidoreductase (PFOR) and 2-oxoglutarate:ferredo
Externí odkaz:
https://doaj.org/article/0a5d4ac7e1c94ea1be917d66c7ecfd3c
Autor:
Marlène Martinho, Diane Allegro, Isabelle Huvent, Charlotte Chabaud, Emilien Etienne, Hervé Kovacic, Bruno Guigliarelli, Vincent Peyrot, Isabelle Landrieu, Valérie Belle, Pascale Barbier
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
Abstract Tau is a Microtubule-associated protein that induces and stabilizes the formation of the Microtubule cytoskeleton and plays an important role in neurodegenerative diseases. The Microtubules binding region of Tau has been determined for a lon
Externí odkaz:
https://doaj.org/article/f38fd31e0683461fb98ee95d22a0e5fa
Autor:
Marta Palombo, Alessio Bonucci, Emilien Etienne, Stefano Ciurli, Vladimir N. Uversky, Bruno Guigliarelli, Valérie Belle, Elisabetta Mileo, Barbara Zambelli
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
Abstract A growing body of literature on intrinsically disordered proteins (IDPs) led scientists to rethink the structure-function paradigm of protein folding. Enzymes are often considered an exception to the rule of intrinsic disorder (ID), believed
Externí odkaz:
https://doaj.org/article/a1b925d80cc8421faa70d4865663e6ce
Autor:
Annalisa Pierro, Emilien Etienne, Guillaume Gerbaud, Bruno Guigliarelli, Stefano Ciurli, Valérie Belle, Barbara Zambelli, Elisabetta Mileo
Publikováno v:
Biomolecules, Vol 10, Iss 7, p 1062 (2020)
UreG is a P-loop GTP hydrolase involved in the maturation of nickel-containing urease, an essential enzyme found in plants, fungi, bacteria, and archaea. This protein couples the hydrolysis of GTP to the delivery of Ni(II) into the active site of apo
Externí odkaz:
https://doaj.org/article/fcf84cad7814432c9d23ec55260d4a8e
Autor:
Magali Lorenzi, Léa Sylvi, Guillaume Gerbaud, Elisabetta Mileo, Frédéric Halgand, Anne Walburger, Hervé Vezin, Valérie Belle, Bruno Guigliarelli, Axel Magalon
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e49523 (2012)
Molecular recognition is central to all biological processes. Understanding the key role played by dedicated chaperones in metalloprotein folding and assembly requires the knowledge of their conformational ensembles. In this study, the NarJ chaperone
Externí odkaz:
https://doaj.org/article/ca9cd4e43624482d8e17231992861254
Autor:
Batoul Srour, Sylvain Gervason, Maren Hellen Hoock, Beata Monfort, Kristian Want, Djabir Larkem, Nadine Trabelsi, Gautier Landrot, Andrea Zitolo, Emiliano Fonda, Emilien Etienne, Guillaume Gerbaud, Christina Sophia Müller, Jonathan Oltmanns, Jesse B. Gordon, Vishal Yadav, Malgorzata Kleczewska, Marcin Jelen, Michel B. Toledano, Rafal Dutkiewicz, David P. Goldberg, Volker Schünemann, Bruno Guigliarelli, Bénédicte Burlat, Christina Sizun, Benoit D’Autréaux
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, 2022, 144 (38), pp.17496-17515. ⟨10.1021/jacs.2c06338⟩
Journal of the American Chemical Society, 2022, 144 (38), pp.17496-17515. ⟨10.1021/jacs.2c06338⟩
International audience; Iron−sulfur (Fe−S) clusters are prosthetic groups of proteins biosynthesized on scaffold proteins by highly conserved multi-protein machineries. Biosynthesis of Fe−S clusters into the ISCU scaffold protein is initiated b
Autor:
Ana Rita Oliveira, Cristiano Mota, Kateryna Klymanska, Frédéric Biaso, Maria João Romão, Bruno Guigliarelli, Inês Cardoso Pereira
Publikováno v:
ACS Chemical Biology. 17:1901-1909
Funding Information: This work was financially supported by Fundação para a Ciência e Tecnologia (FCT, Portugal) through fellowship SFRH/BD/116515/2016, COVID/BD/151766/2021, grant PTDC/BII-BBF/2050/2020, R&D units MOSTMICRO-ITQB (UIDB/04612/2020
Autor:
Pierre Nabokoff, Guillaume Brulay, Cyrielle Dol, Guillaume Gerbaud, Bruno Guigliarelli, Emilien Etienne, Emily Bloch, Fabio Ziarelli, Eric Besson, Stéphane Gastaldi
Publikováno v:
Journal of Physical Chemistry C
Journal of Physical Chemistry C, 2023, 127 (20), pp.9699-9706. ⟨10.1021/acs.jpcc.3c01550⟩
Journal of Physical Chemistry C, 2023, 127 (20), pp.9699-9706. ⟨10.1021/acs.jpcc.3c01550⟩
International audience; Recent applications of bi-, oligo-or polyradicals to spin sciences have generated considerable interest in the design of new bi/oligoradical organic molecules. Nevertheless, studies of physicochemical properties open shell sys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::460a712661f6d2e074093d23f29e0f78
https://hal-amu.archives-ouvertes.fr/hal-04114864/document
https://hal-amu.archives-ouvertes.fr/hal-04114864/document