Zobrazeno 1 - 10
of 10
pro vyhledávání: '"María del Carmen Fernández-Ramírez"'
Autor:
Rubén Hervás, María del Carmen Fernández-Ramírez, Albert Galera-Prat, Mari Suzuki, Yoshitaka Nagai, Marta Bruix, Margarita Menéndez, Douglas V. Laurents, Mariano Carrión-Vázquez
Publikováno v:
BMC Biology, Vol 19, Iss 1, Pp 1-14 (2021)
Abstract Background Amyloids are ordered, insoluble protein aggregates, characterized by a cross-β sheet quaternary structure in which molecules in a β-strand conformation are stacked along the filament axis via intermolecular interactions. While a
Externí odkaz:
https://doaj.org/article/424f921c44eb4d14bf0ae0e29dc08050
Autor:
Rubén Hervás, Liying Li, Amitabha Majumdar, María Del Carmen Fernández-Ramírez, Jay R Unruh, Brian D Slaughter, Albert Galera-Prat, Elena Santana, Mari Suzuki, Yoshitaka Nagai, Marta Bruix, Sergio Casas-Tintó, Margarita Menéndez, Douglas V Laurents, Kausik Si, Mariano Carrión-Vázquez
Publikováno v:
PLoS Biology, Vol 14, Iss 1, p e1002361 (2016)
Amyloids are ordered protein aggregates that are typically associated with neurodegenerative diseases and cognitive impairment. By contrast, the amyloid-like state of the neuronal RNA binding protein Orb2 in Drosophila was recently implicated in memo
Externí odkaz:
https://doaj.org/article/77f95cb5f9284cf6befdeef4b438bc58
Autor:
María del Carmen Fernández‐Ramírez, Kevin Kan‐Shing Ng, Margarita Menéndez, Douglas V. Laurents, Rubén Hervás, Mariano Carrión‐Vázquez
Publikováno v:
Angewandte Chemie (International ed. in English).
11 pags., 5 figs.
Understanding early amyloidogenesis is key to rationally develop therapeutic strategies. Tau protein forms well-characterized pathological deposits but its aggregation mechanism is still poorly understood. Using single-molecule
Understanding early amyloidogenesis is key to rationally develop therapeutic strategies. Tau protein forms well-characterized pathological deposits but its aggregation mechanism is still poorly understood. Using single-molecule
Autor:
Mari Suzuki, Douglas V. Laurents, Albert Galera-Prat, Yoshitaka Nagai, Mariano Carrión-Vázquez, Marta Bruix, Margarita Menéndez, Rubén Hervás, María del Carmen Fernández-Ramírez
Publikováno v:
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
BMC Biology
BMC Biology, Vol 19, Iss 1, Pp 1-14 (2021)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Consejo Superior de Investigaciones Científicas (CSIC)
BMC Biology
BMC Biology, Vol 19, Iss 1, Pp 1-14 (2021)
Digital.CSIC. Repositorio Institucional del CSIC
instname
14 pags., 4 figs.
Background: Amyloids are ordered, insoluble protein aggregates, characterized by a cross-β sheet quaternary structure in which molecules in a β-strand conformation are stacked along the filament axis via intermolecular intera
Background: Amyloids are ordered, insoluble protein aggregates, characterized by a cross-β sheet quaternary structure in which molecules in a β-strand conformation are stacked along the filament axis via intermolecular intera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::920c6b7a6e21dc19b043268434fc4ce3
http://hdl.handle.net/10261/248470
http://hdl.handle.net/10261/248470
Autor:
Binh An Nguyen, Virender Singh, Shumaila Afrin, Anna Yakubovska, Lanie Wang, Yasmin Ahmed, Rose Pedretti, Maria del Carmen Fernandez-Ramirez, Preeti Singh, Maja Pękała, Luis O. Cabrera Hernandez, Siddharth Kumar, Andrew Lemoff, Roman Gonzalez-Prieto, Michael R. Sawaya, David S. Eisenberg, Merrill Douglas Benson, Lorena Saelices
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)
Abstract ATTR amyloidosis is caused by the deposition of transthyretin in the form of amyloid fibrils in virtually every organ of the body, including the heart. This systemic deposition leads to a phenotypic variability that has not been molecularly
Externí odkaz:
https://doaj.org/article/60a20b40007f4acdaf11442427648360
Autor:
Margarita Menéndez, Douglas V. Laurents, María del Carmen Fernández-Ramírez, Mariano Carrión-Vázquez, Rubén Hervás
Knowledge on the molecular bases of early amyloid assembly is fundamental to understand its structure-dysfunction relationship during disease progression. Tauopathies, a well-defined set of neurodegenerative disorders that includes Alzheimer’s dise
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::23f80f99dc417e0a6482382f9b57def5
https://doi.org/10.1101/2020.06.18.158923
https://doi.org/10.1101/2020.06.18.158923
Autor:
Daniel Ramírez de Mingo, Douglas V. Laurents, María del Carmen Fernández-Ramírez, Rubén Hervás, Mariano Carrión-Vázquez, Miguel Mompeán
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
Transactive Response DNA-Binding Protein of 43 kDa (TDP-43) is an essential human protein implicated in Amyotrophic Lateral Sclerosis (ALS) and common dementias. Its C-terminal disordered region, composed of residues 264–414 includes a hydrophobic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::540aebb92fcbe1aaa1f4fc5e56954568
http://hdl.handle.net/10261/206121
http://hdl.handle.net/10261/206121
Autor:
María del Carmen Fernández-Ramírez, Rubén Hervás, Albert Galera-Prat, Mariano Carrión-Vázquez, Douglas V. Laurents
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
Intrinsically disordered proteins (IDPs) lack a tertiary structure. Amyloidogenic IDPs (aIDPs) in particular have attracted great interest due to their implication in several devastating diseases as well as in critical biological functions. However,
Autor:
Marie-Isabel Aguilar, Maria Andreasen, Neil R. Anthony, Fernando Teran Arce, Florian Arnhold, Shruti Arya, Aida Attar, Silvia Barbosa, Manja A. Behrens, Innocent B. Bekard, Georges Belfort, Martin L. Bennink, Magdalena Bereza, Keith M. Berland, Gal Bitan, Mischa Bonn, Hugo M. Botelho, Joana Branco dos Santos, Leonid Breydo, Yi Cao, Roberto Cappai, Isabel Cardoso, Mariano Carrión-Vázquez, Sofia B. Carvalho, John A. Carver, Fiona T.S. Chan, W. Seth Childers, Jason C. Collins, Laura Connelly, Cyril Curtain, Vijit Dalal, Alfonso De Simone, Athene M. Donald, Dave E. Dunstan, Heath Ecroyd, Jan Johannes Enghild, Laura Esther Abelleira, Marcus Fändrich, María del Carmen Fernández-Ramírez, Vito Foderà, Günter Fritz, Yoshiaki Furukawa, Shirin D. Ghodke, Stefano Gianni, Armin Giese, Cláudio M. Gomes, Susana Gonçalves, Lesley H. Greene, Michael D.W. Griffin, Amy M. Griggs, Christian Haass, Per Hammarström, J. Robin Harris, Federico Herrera, Rubén Hervás, Shannon E. Hill, Xu Hou, Geoffrey J. Howlett, Tsuneya Ikezu, Hyunbum Jang, Grethe V. Jensen, Bruce L. Kagan, Clemens F. Kaminski, Shigeko Kawai-Noma, Alexei Klechikov, Gijsje H. Koenderink, Ratnesh Lal, Douglas V. Laurents, Chi Le Lan Pham, Harry LeVine, Dusan Losic, David G. Lynn, Kirsten G. Malmos, Lisandra L. Martin, Adam I. Mechler, Anil K. Mehta, Derya Meral, Nathaniel G.N. Milton, Yee-Foong Mok, Ludmilla A. Morozova-Roche, Víctor Mosquera, Samrat Mukhopadhyay, Mentor Mulaj, Martin Muschol, Niels Chr Nielsen, R. Nilsson, Georg Nübling, Ruth Nussinov, Daniel E. Otzen, Tiago Fleming Outeiro, Jan Skov Pedersen, Jesper Søndergaard Pedersen, K. Peter, Dorothea Pinotsi, Meng Qin, Srinivasan Ramachandran, Agata Rekas, Annalisa Relini, Jean-Christophe Rochet, Sophie Rothhämel, Nikita Rudinskiy, Markus Sauer, Gabriele S. Kaminski Schierle, Michael Schleeger, Bettina Schmid, David H. Small, Anne Søndergaard, Mirco Sorci, Tara L. Spires-Jones, Marcel Stenvang, Martin Stöckl, Katrin Strecker, Vinod Subramaniam, Anna S.P. Svane, Kim K.M. Sweers, Pablo Taboada, Hideki Taguchi, Chai Lean Teoh, David C. Thorn, Kiyotaka Tokuraku, Robert Tycko, Brigita Urbanc, Vladimir N. Uversky, Corianne C. van den Akker, Michele Vendruscolo, Anna von Mikecz, Vladana Vukojević, Wei Wang, Katrin Weise, Roland Winter, Jessica W. Wu, Wei-Feng Xue, Kiran Yanamandra, Daniel Ysselstein, Eva Žerovnik, Dawei Zou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3c175a1f0ef43b7e6a7630800263015e
https://doi.org/10.1016/b978-0-12-394431-3.01002-6
https://doi.org/10.1016/b978-0-12-394431-3.01002-6
Autor:
Jay R. Unruh, Douglas V. Laurents, Amitabha Majumdar, Mariano Carrión-Vázquez, Elena Santana, Liying Li, Brian D. Slaughter, Yoshitaka Nagai, María del Carmen Fernández-Ramírez, Marta Bruix, Rubén Hervás, Sergio Casas-Tintó, Mari Suzuki, Margarita Menéndez, Kausik Si, Albert Galera-Prat
Publikováno v:
Repositorio Institucional del Instituto Madrileño de Estudios Avanzados en Nanociencia
instname
Digital.CSIC. Repositorio Institucional del CSIC
PLoS Biology
PLoS Biology, Vol 14, Iss 1, p e1002361 (2016)
instname
Digital.CSIC. Repositorio Institucional del CSIC
PLoS Biology
PLoS Biology, Vol 14, Iss 1, p e1002361 (2016)
Amyloids are ordered protein aggregates that are typically associated with neurodegenerative diseases and cognitive impairment. By contrast, the amyloid-like state of the neuronal RNA binding protein Orb2 in Drosophila was recently implicated in memo