Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Miguel A. Treviño"'
Autor:
Rosa Antón, Miguel Á. Treviño, David Pantoja-Uceda, Sara Félix, María Babu, Eurico J. Cabrita, Markus Zweckstetter, Philip Tinnefeld, Andrés M. Vera, Javier Oroz
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract Abnormal trinucleotide repeat expansions alter protein conformation causing malfunction and contribute to a significant number of incurable human diseases. Scarce structural insights available on disease-related homorepeat expansions hinder
Externí odkaz:
https://doaj.org/article/3794aa1413964515962ab2aa2be23a71
Autor:
Nadide Altincekic, Sophie Marianne Korn, Nusrat Shahin Qureshi, Marie Dujardin, Martí Ninot-Pedrosa, Rupert Abele, Marie Jose Abi Saad, Caterina Alfano, Fabio C. L. Almeida, Islam Alshamleh, Gisele Cardoso de Amorim, Thomas K. Anderson, Cristiane D. Anobom, Chelsea Anorma, Jasleen Kaur Bains, Adriaan Bax, Martin Blackledge, Julius Blechar, Anja Böckmann, Louis Brigandat, Anna Bula, Matthias Bütikofer, Aldo R. Camacho-Zarco, Teresa Carlomagno, Icaro Putinhon Caruso, Betül Ceylan, Apirat Chaikuad, Feixia Chu, Laura Cole, Marquise G. Crosby, Vanessa de Jesus, Karthikeyan Dhamotharan, Isabella C. Felli, Jan Ferner, Yanick Fleischmann, Marie-Laure Fogeron, Nikolaos K. Fourkiotis, Christin Fuks, Boris Fürtig, Angelo Gallo, Santosh L. Gande, Juan Atilio Gerez, Dhiman Ghosh, Francisco Gomes-Neto, Oksana Gorbatyuk, Serafima Guseva, Carolin Hacker, Sabine Häfner, Bing Hao, Bruno Hargittay, K. Henzler-Wildman, Jeffrey C. Hoch, Katharina F. Hohmann, Marie T. Hutchison, Kristaps Jaudzems, Katarina Jović, Janina Kaderli, Gints Kalniņš, Iveta Kaņepe, Robert N. Kirchdoerfer, John Kirkpatrick, Stefan Knapp, Robin Krishnathas, Felicitas Kutz, Susanne zur Lage, Roderick Lambertz, Andras Lang, Douglas Laurents, Lauriane Lecoq, Verena Linhard, Frank Löhr, Anas Malki, Luiza Mamigonian Bessa, Rachel W. Martin, Tobias Matzel, Damien Maurin, Seth W. McNutt, Nathane Cunha Mebus-Antunes, Beat H. Meier, Nathalie Meiser, Miguel Mompeán, Elisa Monaca, Roland Montserret, Laura Mariño Perez, Celine Moser, Claudia Muhle-Goll, Thais Cristtina Neves-Martins, Xiamonin Ni, Brenna Norton-Baker, Roberta Pierattelli, Letizia Pontoriero, Yulia Pustovalova, Oliver Ohlenschläger, Julien Orts, Andrea T. Da Poian, Dennis J. Pyper, Christian Richter, Roland Riek, Chad M. Rienstra, Angus Robertson, Anderson S. Pinheiro, Raffaele Sabbatella, Nicola Salvi, Krishna Saxena, Linda Schulte, Marco Schiavina, Harald Schwalbe, Mara Silber, Marcius da Silva Almeida, Marc A. Sprague-Piercy, Georgios A. Spyroulias, Sridhar Sreeramulu, Jan-Niklas Tants, Kaspars Tārs, Felix Torres, Sabrina Töws, Miguel Á. Treviño, Sven Trucks, Aikaterini C. Tsika, Krisztina Varga, Ying Wang, Marco E. Weber, Julia E. Weigand, Christoph Wiedemann, Julia Wirmer-Bartoschek, Maria Alexandra Wirtz Martin, Johannes Zehnder, Martin Hengesbach, Andreas Schlundt
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
The highly infectious disease COVID-19 caused by the Betacoronavirus SARS-CoV-2 poses a severe threat to humanity and demands the redirection of scientific efforts and criteria to organized research projects. The international COVID19-NMR consortium
Externí odkaz:
https://doaj.org/article/201170fa84b8450e9b468d9fb4480774
Autor:
Miguel Á. Treviño, Rubén López-Sánchez, María Redondo Moya, David Pantoja-Uceda, Miguel Mompeán, Douglas V. Laurents
9 pags.
The use of polyproline II (PPII) helices in protein design is currently hindered by limitations in our understanding of their conformational stability and folding. Recent studies of the snow flea antifreeze protein (sfAFP), a useful mode
The use of polyproline II (PPII) helices in protein design is currently hindered by limitations in our understanding of their conformational stability and folding. Recent studies of the snow flea antifreeze protein (sfAFP), a useful mode
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb1f5fdf07f0e90742f5678701e73592
http://hdl.handle.net/10261/303238
http://hdl.handle.net/10261/303238
Publikováno v:
European Biophysics Journal
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC. Repositorio Institucional del CSIC
instname
Intrinsically disordered proteins (IDPs) play essential roles in regulating physiological processes in eukaryotic cells. Many viruses use their own IDPs to “hack” these processes to deactivate host defenses and promote viral growth. Thus, viral I
Autor:
Miguel Á. Treviño, María Redondo Moya, Rubén López Sánchez, David Pantoja-Uceda, Miguel Mompeán, Douglas V. Laurents
The use of PPII helices in protein design is currently hindered by limitations in our understanding of their conformational stability and folding. Recent studies of the snow flea antifreeze protein (sfAFP), a useful model system composed of six PPII
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b6d3277686405f71725a6447b902600e
https://doi.org/10.1101/2022.03.10.483783
https://doi.org/10.1101/2022.03.10.483783
Autor:
María Flor García-Mayoral, Miguel Angel Treviño, Teresa Pérez-Piñar, María Luisa Caballero, Tobias Knaute, Ana Umpierrez, Marta Bruix, Rosa Rodríguez-Pérez
Publikováno v:
PLoS Neglected Tropical Diseases, Vol 8, Iss 3, p e2735 (2014)
BACKGROUND: Anisakiasis is a re-emerging global disease caused by consumption of raw or lightly cooked fish contaminated with L3 Anisakis larvae. This zoonotic disease is characterized by severe gastrointestinal and/or allergic symptoms which may mis
Externí odkaz:
https://doaj.org/article/ecc69fce2bc846f78476eaf7c5262cce
Autor:
Miguel Mompeán, Eurico J. Cabrita, S.S. Félix, Andrew J. Doig, Miguel A. Treviño, R. López-Sánchez, David Pantoja-Uceda, Javier Oroz, Bethan S. McAvan, Douglas V. Laurents
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
Supplementary data related to this article can be found at https://doi.org/10.1016/j.abb.2021.108867.
Many intrinsically disordered proteins contain Gly-rich regions which are generally assumed to be disordered. Such regions often form biomolecu
Many intrinsically disordered proteins contain Gly-rich regions which are generally assumed to be disordered. Such regions often form biomolecu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a2cd528d87d9cc3bf0eb95731d49b34
http://hdl.handle.net/10261/260140
http://hdl.handle.net/10261/260140
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
The SARS-CoV-2 Nsp8 protein is a critical component of the RNA replicase, as its N-terminal domain (NTD) anchors Nsp12, the RNA, and Nsp13. Whereas its C-terminal domain (CTD) structure is well resolved, there is an open debate regarding the conforma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0a3ee8bfd396ddb3d295397eb9e8faf
http://hdl.handle.net/10261/235013
http://hdl.handle.net/10261/235013
Autor:
Héctor Zamora-Carreras, Daniel Butrón, Ana Baamonde, Olga Abian, Isabel Devesa, Miguel A. Treviño, Sara González-Rodríguez, Adrián Velázquez-Campoy, Asia Fernández-Carvajal, Rosario González-Muñiz, Laura Lagartera, M. Angeles Bonache, M. Angeles Jiménez, Mercedes Martín-Martínez, Antonio Ferrer-Montiel
Publikováno v:
WOS:000704036500011
Digital.CSIC. Repositorio Institucional del CSIC
instname
RUO. Repositorio Institucional de la Universidad de Oviedo
Zaguán. Repositorio Digital de la Universidad de Zaragoza
Universitat Politècnica de Catalunya (UPC)
Digital.CSIC. Repositorio Institucional del CSIC
instname
RUO. Repositorio Institucional de la Universidad de Oviedo
Zaguán. Repositorio Digital de la Universidad de Zaragoza
Universitat Politècnica de Catalunya (UPC)
15 pags, 8 figs, 3 tabs. -- Supplementary data to this article can be found online at https://doi.org/10.1016/j.bioorg.2021.105231.
The analgesic peptide DD04107 (Pal-EEMQRR-NH2) and its acetylated analogue inhibit α-calcitonin gene-related pep
The analgesic peptide DD04107 (Pal-EEMQRR-NH2) and its acetylated analogue inhibit α-calcitonin gene-related pep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95760067d418a994b7877362c6cd4919
http://zaguan.unizar.es/record/117947
http://zaguan.unizar.es/record/117947
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
Intrinsically disordered proteins (IDPs) play essential roles in regulating physiological processes in eukaryotic cells. Many virus use their own IDPs to hack these processes to disactive host defenses and promote viral growth. Thus, viral IDPs are a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97c2fd873e402c25f7414305773f8c2c
http://hdl.handle.net/10261/222671
http://hdl.handle.net/10261/222671