Zobrazeno 1 - 10
of 124
pro vyhledávání: '"Arturo Muga"'
Autor:
Lorea Velasco-Carneros, Jorge Cuéllar, Leire Dublang, César Santiago, Jean-Didier Maréchal, Jaime Martín-Benito, Moisés Maestro, José Ángel Fernández-Higuero, Natalia Orozco, Fernando Moro, José María Valpuesta, Arturo Muga
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-16 (2023)
Abstract J-domain proteins tune the specificity of Hsp70s, engaging them in precise functions. Despite their essential role, the structure and function of many J-domain proteins remain largely unknown. We explore human DNAJA2, finding that it reversi
Externí odkaz:
https://doaj.org/article/6cd9508201a643d8a30f5d1e3bb400ad
Autor:
Jon Olano-Bringas, Patricia Villegas-Zafra, Begum Kurt, Dalila Ciceri, Arturo Muga, Nora Bengoa-Vergniory
Publikováno v:
IBRO Neuroscience Reports, Vol 15, Iss , Pp S465- (2023)
Externí odkaz:
https://doaj.org/article/f7a0b919dd684fb990d1bcbd69ddbf17
Autor:
Lorea Velasco-Carneros, Jorge Cuéllar, Leire Dublang, César Santiago, Jean-Didier Maréchal, Jaime Martín-Benito, Moisés Maestro, José Ángel Fernández-Higuero, Natalia Orozco, Fernando Moro, José María Valpuesta, Arturo Muga
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-1 (2024)
Externí odkaz:
https://doaj.org/article/a222e6ad375d4e16b18188f55f5314a6
Autor:
Aitor Franco, Jorge Cuéllar, José Ángel Fernández-Higuero, Igor de la Arada, Natalia Orozco, José M. Valpuesta, Adelina Prado, Arturo Muga
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 23, p 12983 (2021)
The aggregation of α-synuclein is the hallmark of a collective of neurodegenerative disorders known as synucleinopathies. The tendency to aggregate of this protein, the toxicity of its aggregation intermediates and the ability of the cellular protei
Externí odkaz:
https://doaj.org/article/4aee3d07d70c4626ba48ad2d0283857c
Autor:
Aitor Franco, Lorea Velasco-Carneros, Naiara Alvarez, Natalia Orozco, Fernando Moro, Adelina Prado, Arturo Muga
Publikováno v:
Cells, Vol 10, Iss 10, p 2745 (2021)
Neurodegenerative diseases (NDs) are increasingly positioned as leading causes of global deaths. The accelerated aging of the population and its strong relationship with neurodegeneration forecast these pathologies as a huge global health problem in
Externí odkaz:
https://doaj.org/article/af47aa04988441bbb6c4d59e9dcde4e5
Autor:
Leire Dublang, Jarl Underhaug, Marte I. Flydal, Lorea Velasco-Carneros, Jean-Didier Maréchal, Fernando Moro, Maria Dolores Boyano, Aurora Martinez, Arturo Muga
Publikováno v:
Cancers, Vol 13, Iss 12, p 2936 (2021)
Heat shock protein (Hsp) synthesis is upregulated in a wide range of cancers to provide the appropriate environment for tumor progression. The Hsp110 and Hsp70 families have been associated to cancer cell survival and resistance to chemotherapy. In t
Externí odkaz:
https://doaj.org/article/e3ccec35180a4f7c93c03249759cde84
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 17, p 4122 (2019)
Proteins must fold into their native structure and maintain it during their lifespan to display the desired activity. To ensure proper folding and stability, and avoid generation of misfolded conformations that can be potentially cytotoxic, cells syn
Externí odkaz:
https://doaj.org/article/d713cae8eeb645d9ad803aa7b95ed7cd
Autor:
Lars Skjaerven, Barry Grant, Arturo Muga, Knut Teigen, J Andrew McCammon, Nathalie Reuter, Aurora Martinez
Publikováno v:
PLoS Computational Biology, Vol 7, Iss 3, p e1002004 (2011)
GroEL is an ATP dependent molecular chaperone that promotes the folding of a large number of substrate proteins in E. coli. Large-scale conformational transitions occurring during the reaction cycle have been characterized from extensive crystallogra
Externí odkaz:
https://doaj.org/article/4dd297e046af4b9990cbbd9c6db2f83c
Autor:
Jaime Santos, Jorge Cuellar, Irantzu Pallarès, Emily J Byrd, Alons Lends, Fernando Moro, Muhammed Bilal Abdul-Shukkoor, Jordi Pujols, Lorea Velasco-Carneros, Frank Sobott, Daniel E Otzen, Antonio N Calabrese, Arturo Muga, Jan Skov Pedersen, Antoine Loquet, Jose María Valpuesta, Sheena E Radford, Salvador Ventura
Oligomeric species populated during α-synuclein aggregation are considered key drivers of neurodegeneration in Parkinson’s disease. However, their structure and the molecular determinants driving their conversion to fibrils remain elusive. In this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cc5124549253e70a4832df8bf77b620a
https://doi.org/10.1101/2023.02.10.527650
https://doi.org/10.1101/2023.02.10.527650
Autor:
Michael J. Morten, Liina Sirvio, Huzefa Rupawala, Emma Mee Hayes, Aitor Franco, Carola Radulescu, Liming Ying, Samuel J. Barnes, Arturo Muga, Yu Ye
Protein aggregation is a hallmark of major neurodegenerative disorders. Increasing data suggest that smaller aggregates cause higher toxic response than filamentous aggregates (fibrils). However, the size of small aggregates has challenged their dete
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ca2ffcea7d7251652f565092d2ac05d
http://hdl.handle.net/10044/1/100274
http://hdl.handle.net/10044/1/100274