Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Ernesto Arias‐Palomo"'
Autor:
Mercedes Spínola-Amilibia, Lidia Araújo-Bazán, Álvaro de la Gándara, James M. Berger, Ernesto Arias-Palomo
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Abstract Transposases are ubiquitous enzymes that catalyze DNA rearrangement events with broad impacts on gene expression, genome evolution, and the spread of drug-resistance in bacteria. Here, we use biochemical and structural approaches to define t
Externí odkaz:
https://doaj.org/article/580142f5ed3e4930a5687d19c91c0d29
Autor:
Maria Lázaro‐Berenguer, Francisco Paredes‐Martínez, Yolanda Bel, Rafael Núñez‐Ramírez, Ernesto Arias‐Palomo, Patricia Casino, Juan Ferré
Publikováno v:
Microbial Biotechnology, Vol 15, Iss 10, Pp 2607-2618 (2022)
Abstract Vip3 proteins are produced by Bacillus thuringiensis and are toxic against lepidopterans, reason why the vip3Aa gene has been introduced into cotton and corn to control agricultural pests. Recently, the structure of Vip3 proteins has been de
Externí odkaz:
https://doaj.org/article/750c753fd82b45f4b733c694992139d9
Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis
Autor:
Rafael Núñez-Ramírez, Juanjo Huesa, Yolanda Bel, Juan Ferré, Patricia Casino, Ernesto Arias-Palomo
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Bacillus thuringiensis Vip3 (Vegetative Insecticidal Protein 3) toxins are widely used in biotech crops to control Lepidopteran pests. Here authors present the cryo-EM structures of the protoxin and the protease-activated state of Vip3Aa which shed l
Externí odkaz:
https://doaj.org/article/f4448b8a86204737aec24834ae368c1f
Publikováno v:
PLoS Genetics, Vol 15, Iss 12, p e1008557 (2019)
TRAnsport Protein Particle complexes (TRAPPs) are ubiquitous regulators of membrane traffic mediating nucleotide exchange on the Golgi regulatory GTPases RAB1 and RAB11. In S. cerevisiae and metazoans TRAPPs consist of two large oligomeric complexes:
Externí odkaz:
https://doaj.org/article/7e38bee368c147c69f6c8aaab27422df
The type V myosin-containing complex HUM is a RAB11 effector powering movement of secretory vesicles
Autor:
Mario Pinar, Ana Alonso, Vivian de los Ríos, Ignacio Bravo-Plaza, Álvaro de la Gandara, Antonio Galindo, Ernesto Arias-Palomo, Miguel Á. Peñalva
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
59 p.- 7 fig.-1 tab. 1 graph abst.
In the apex-directed RAB11 exocytic pathway of Aspergillus nidulans, kinesin-1/KinA conveys secretory vesicles (SVs) to the hyphal tip, where they are transferred to the type V myosin MyoE. MyoE concentrates SV
In the apex-directed RAB11 exocytic pathway of Aspergillus nidulans, kinesin-1/KinA conveys secretory vesicles (SVs) to the hyphal tip, where they are transferred to the type V myosin MyoE. MyoE concentrates SV
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::498f9788ebfa4eb3a094baa9a679bc59
http://hdl.handle.net/10261/271772
http://hdl.handle.net/10261/271772
Autor:
Corentin Claeys Bouuaert, Scott Keeney, Stephen Pu, Sam E. Tischfield, Ernesto Arias-Palomo, Eleni P. Mimitou, James M. Berger
Publikováno v:
Nature Structural & Molecular Biology
Nature structural & molecular biology
Nature Structural and Molecular Biology, Vol. 22, p. 92-102 (2021)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Nature structural & molecular biology
Nature Structural and Molecular Biology, Vol. 22, p. 92-102 (2021)
Digital.CSIC. Repositorio Institucional del CSIC
instname
54 p.-8 fig.
Spo11, which makes DNA double-strand breaks (DSBs) that are essential for meiotic recombination, has long been recalcitrant to biochemical study. We provide molecular analysis of Saccharomyces cerevisiae Spo11 purified with partners
Spo11, which makes DNA double-strand breaks (DSBs) that are essential for meiotic recombination, has long been recalcitrant to biochemical study. We provide molecular analysis of Saccharomyces cerevisiae Spo11 purified with partners
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97a4dd7153933c8a1e0db46177b0da8e
Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis
Autor:
Ernesto Arias-Palomo, Rafael Núñez-Ramírez, Patricia Casino, Yolanda Bel, Juanjo Huesa, Juan Ferré
Publikováno v:
Núñez-Ramírez, Rafael Huesa, Juanjo Bel Cortés, Yolanda Ferré Manzanero, Juan Casino Ferrando, Patricia Arias-Palomo, Ernesto 2020 Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis Nature Communications 11 3974 1 9
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
RODERIC. Repositorio Institucional de la Universitat de Valéncia
instname
RODERIC: Repositorio Institucional de la Universitat de Valéncia
Nature Communications
Digital.CSIC. Repositorio Institucional del CSIC
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
RODERIC. Repositorio Institucional de la Universitat de Valéncia
instname
RODERIC: Repositorio Institucional de la Universitat de Valéncia
Nature Communications
Digital.CSIC. Repositorio Institucional del CSIC
9 p.-5 fig.
Bacillus thuringiensis Vip3 (Vegetative Insecticidal Protein 3) toxins are widely used in biotech crops to control Lepidopteran pests. These proteins are produced as inactive protoxins that need to be activated by midgut proteases to
Bacillus thuringiensis Vip3 (Vegetative Insecticidal Protein 3) toxins are widely used in biotech crops to control Lepidopteran pests. These proteins are produced as inactive protoxins that need to be activated by midgut proteases to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c464e8a1f8c9b6875933dc11d0bc93ba
https://hdl.handle.net/10550/78230
https://hdl.handle.net/10550/78230
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
81 p.- 7 fig.-1 tab.-7 fig. supl.-6 vid.
In cells, dedicated AAA+ ATPases deposit hexameric, ring-shaped helicases onto DNA to initiate chromosomal replication. To better understand the mechanisms by which helicase loading can occur, we used cry
In cells, dedicated AAA+ ATPases deposit hexameric, ring-shaped helicases onto DNA to initiate chromosomal replication. To better understand the mechanisms by which helicase loading can occur, we used cry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7844c8e3a0ee9261f0f7dfd57ea2367
https://europepmc.org/articles/PMC6450724/
https://europepmc.org/articles/PMC6450724/
Autor:
Ernesto Arias-Palomo, Valerie L. O’Shea, Jan P. Erzberger, Melania S. Strycharska, James M. Berger, Artem Y. Lyubimov, Carlos Bustamante
Publikováno v:
Molecular cell, vol 52, iss 6
Summary Cellular replication forks are powered by ring-shaped, hexameric helicases that encircle and unwind DNA. To better understand the molecular mechanisms and control of these enzymes, we used multiple methods to investigate the bacterial replica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2b0b2d0e439312cf72397b79a6cd182
https://doi.org/10.1016/j.molcel.2013.11.016
https://doi.org/10.1016/j.molcel.2013.11.016
Publikováno v:
Cell. 153:438-448
Dedicated AAA+ ATPases help deposit hexameric ring-shaped helicases onto DNA to promote replication in cellular organisms. To understand how loading occurs, we used negative-stain electron microscopy and small-angle X-ray scattering to determine the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9d9c43b9cc6efda832d6fbf45b79003
https://doi.org/10.1016/j.cell.2013.03.006
https://doi.org/10.1016/j.cell.2013.03.006