Zobrazeno 1 - 7
of 7
pro vyhledávání: '"María Eugenia Llases"'
Autor:
Lucía Ana Curti, Ivana Primost, Sofia Valla, Daiana Ibañez Alegre, Cecilia Olguin Perglione, Guillermo Daniel Repizo, Julia Lara, Ivana Parcerisa, Antonela Palacios, María Eugenia Llases, Adriana Rinflerch, Melanie Barrios, Federico Pereyra Bonnet, Carla Alejandra Gimenez, Débora Natalia Marcone
Publikováno v:
Viruses, Vol 13, Iss 3, p 420 (2021)
We evaluated a lyophilized CRISPR-Cas12 assay for SARS-CoV-2 detection (Lyo-CRISPR SARS-CoV-2 kit) based on reverse transcription, isothermal amplification, and CRISPR-Cas12 reaction. From a total of 210 RNA samples extracted from nasopharyngeal swab
Externí odkaz:
https://doaj.org/article/953bfcaf716e4741964b7a99cd87ad6e
Autor:
Cecilia Olguin Perglione, Julia Lara, Carla Alejandra Gimenez, Daiana Macarena Ibáñez Alegre, Melanie Barrios, Federico Alberto Pereyra Bonnet, Ivana Parcerisa, Lucia Ana Curti, Antonela Palacios, Ivana Primost, Adriana Raquel Rinflerch, Débora Natalia Marcone, Guillermo Daniel Repizo, Sofia Valla, María Eugenia Llases
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Viruses
Volume 13
Issue 3
Viruses, Vol 13, Iss 420, p 420 (2021)
Viruses 13 (3) : 420 (Marzo 2021)
INTA Digital (INTA)
Instituto Nacional de Tecnología Agropecuaria
instacron:INTA
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Viruses
Volume 13
Issue 3
Viruses, Vol 13, Iss 420, p 420 (2021)
Viruses 13 (3) : 420 (Marzo 2021)
INTA Digital (INTA)
Instituto Nacional de Tecnología Agropecuaria
instacron:INTA
We evaluated a lyophilized CRISPR-Cas12 assay for SARS-CoV-2 detection (Lyo-CRISPR SARS-CoV-2 kit) based on reverse transcription, isothermal amplification, and CRISPR-Cas12 reaction. From a total of 210 RNA samples extracted from nasopharyngeal swab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aac8537ffe29c2bef0fb08ab65204d24
https://www.mdpi.com/1999-4915/13/3/420
https://www.mdpi.com/1999-4915/13/3/420
Autor:
María-Natalia Lisa, Marcos N. Morgada, Pedro M. Alzari, Alejandro J. Vila, Estefanía Giannini, María-Eugenia Llases
Publikováno v:
FEBS Journal
FEBS Journal, Wiley, 2020, 287 (4), pp.749-762. ⟨10.1111/febs.15016⟩
FEBS Journal, 2020, 287 (4), pp.749-762. ⟨10.1111/febs.15016⟩
FEBS Journal, Wiley, 2020, 287 (4), pp.749-762. ⟨10.1111/febs.15016⟩
FEBS Journal, 2020, 287 (4), pp.749-762. ⟨10.1111/febs.15016⟩
International audience; The assembly of the CuA site in Cytochrome c Oxidase (COX) is a critical step for aerobic respiration in COX-dependent organisms. Several gene products have been associated with the assembly of this copper site, the most conse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c348181ad2f281e82d06082a2669053
https://hal-pasteur.archives-ouvertes.fr/pasteur-03095808
https://hal-pasteur.archives-ouvertes.fr/pasteur-03095808
Autor:
Alejandro J. Vila, Daniel H. Murgida, María-Eugenia Llases, Estefanía Giannini, María-Natalia Lisa, Marcos N. Morgada, María A. Castro, Pedro M. Alzari
Publikováno v:
Chemical Communications
Chemical Communications, Royal Society of Chemistry, 2020, 56 (8), pp.1223-1226. ⟨10.1039/c9cc08883k⟩
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Chemical Communications, 2020, 56 (8), pp.1223-1226. ⟨10.1039/c9cc08883k⟩
Chemical Communications, Royal Society of Chemistry, 2020, 56 (8), pp.1223-1226. ⟨10.1039/c9cc08883k⟩
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Chemical Communications, 2020, 56 (8), pp.1223-1226. ⟨10.1039/c9cc08883k⟩
The CuA center is a paradigm for the study of long-range biological electron transfer. This metal center is an essential cofactor for terminal oxidases like cytochrome c oxidase, the enzymatic complex responsible for cellular respiration in eukaryote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c4b6c8756d542e6078ac4e28a120fe3
https://hal-pasteur.archives-ouvertes.fr/pasteur-03095789
https://hal-pasteur.archives-ouvertes.fr/pasteur-03095789
Autor:
Marcos N, Morgada, María-Eugenia, Llases, Estefanía, Giannini, María-Ana, Castro, Pedro M, Alzari, Daniel H, Murgida, María-Natalia, Lisa, Alejandro J, Vila
Publikováno v:
Chemical communications (Cambridge, England). 56(8)
The CuA center is a paradigm for the study of long-range biological electron transfer. This metal center is an essential cofactor for terminal oxidases like cytochrome c oxidase, the enzymatic complex responsible for cellular respiration in eukaryote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0f65a1155f6ce39d884a8c448cd8672f
https://pubmed.ncbi.nlm.nih.gov/31897463
https://pubmed.ncbi.nlm.nih.gov/31897463
Autor:
Ulises A. Zitare, Alejandro J. Vila, Jonathan Szuster, Marcos N. Morgada, María Eugenia Llases, María C. Santalla, Daniel H. Murgida
Publikováno v:
Inorganic Chemistry
Inorganic Chemistry, American Chemical Society, 2019, 58 (3), pp.2149-2157. ⟨10.1021/acs.inorgchem.8b03244⟩
Inorganic Chemistry, American Chemical Society, 2019, 58 (3), pp.2149-2157. ⟨10.1021/acs.inorgchem.8b03244⟩
Here we report the spectroscopic and electrochemical characterization of three novel chimeric CuA proteins in which either one or the three loops surrounding the metal ions in the Thermus thermophilus protein have been replaced by homologous human an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63d40987d96e3ce11423fd6fbe5fa35e
https://hal-univ-rennes1.archives-ouvertes.fr/hal-02051160
https://hal-univ-rennes1.archives-ouvertes.fr/hal-02051160
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 15, p 3830 (2019)
International Journal of Molecular Sciences
RepHipUNR (UNR)
Universidad Nacional de Rosario
instacron:UNR
International Journal of Molecular Sciences
RepHipUNR (UNR)
Universidad Nacional de Rosario
instacron:UNR
Copper is an essential cofactor for aerobic respiration, since it is required as a redox cofactor in Cytochrome c Oxidase (COX). This ancient and highly conserved enzymatic complex from the family of heme-copper oxidase possesses two copper sites: Cu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d11e5ca217595ca7c0b95f079391d988
https://doi.org/10.3390/ijms20153830
https://doi.org/10.3390/ijms20153830