Zobrazeno 1 - 10
of 139
pro vyhledávání: '"Douglas V. Laurents"'
Publikováno v:
Communications Chemistry, Vol 7, Iss 1, Pp 1-11 (2024)
Abstract Hydrogen bond cooperativity (HBC) plays an important role in stabilizing protein assemblies built by α-helices and β-sheets, the most common secondary structures. However, whether HBC exists in other types of protein secondary structures s
Externí odkaz:
https://doaj.org/article/ec934708e4e44906951fafa5d735a60d
Autor:
Jaime Carrasco, Rosa Antón, Alejandro Valbuena, David Pantoja-Uceda, Mayur Mukhi, Rubén Hervás, Douglas V. Laurents, María Gasset, Javier Oroz
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
In this work, the authors show that metamorphism in the post-translationally modified TDP-43 prion-like domain encodes determinants that command mechanisms with major relevance in disease and stress the relevance of post-translationally modified chai
Externí odkaz:
https://doaj.org/article/9a9166e33ea74700a35643c8927458e0
Autor:
Pablo Gracia, David Polanco, Jorge Tarancón-Díez, Ilenia Serra, Maruan Bracci, Javier Oroz, Douglas V. Laurents, Inés García, Nunilo Cremades
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
Here, the authors report that α-synuclein phase-separates into liquid condensates with positively charged polypeptides such as Tau. The condensates undergo different maturation processes, including the formation of α-synuclein/Tau amyloid hetero-ag
Externí odkaz:
https://doaj.org/article/910d67f857ce4c4785141427b4af0177
Publikováno v:
FEBS Open Bio, Vol 11, Iss 9, Pp 2390-2399 (2021)
Biomolecular condensates are microdroplets that form inside cells and serve to selectively concentrate proteins, RNAs and other molecules for a variety of physiological functions, but can contribute to cancer, neurodegenerative diseases and viral inf
Externí odkaz:
https://doaj.org/article/41e87823236c4af5abb20f756f5283bd
Autor:
Douglas V. Laurents
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
The artificial intelligence program AlphaFold 2 is revolutionizing the field of protein structure determination as it accurately predicts the 3D structure of two thirds of the human proteome. Its predictions can be used directly as structural models
Externí odkaz:
https://doaj.org/article/00bd250852f64988802ea8feca6bddc9
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:
David Pantoja-Uceda, Cristiana Stuani, Douglas V Laurents, Ann E McDermott, Emanuele Buratti, Miguel Mompeán
Publikováno v:
PLoS Biology, Vol 19, Iss 4, p e3001198 (2021)
Transactive response DNA-binding Protein of 43 kDa (TDP-43) assembles various aggregate forms, including biomolecular condensates or functional and pathological amyloids, with roles in disparate scenarios (e.g., muscle regeneration versus neurodegene
Externí odkaz:
https://doaj.org/article/5c3974d5df084d1e8289dc404e4a15f8
Autor:
Sabrina Fasoli, Ilaria Bettin, Riccardo Montioli, Andrea Fagagnini, Daniele Peterle, Douglas V. Laurents, Giovanni Gotte
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 18, p 10068 (2021)
Human Angiogenin (hANG, or ANG, 14.1 kDa) promotes vessel formation and is also called RNase 5 because it is included in the pancreatic-type ribonuclease (pt-RNase) super-family. Although low, its ribonucleolytic activity is crucial for angiogenesis
Externí odkaz:
https://doaj.org/article/fbdb8c86383f490e916310fa40a0a33e
Autor:
Andrea Fagagnini, Miguel Garavís, Irene Gómez-Pinto, Sabrina Fasoli, Giovanni Gotte, Douglas V. Laurents
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 3, p 1439 (2021)
Protein oligomerization is key to countless physiological processes, but also to abnormal amyloid conformations implicated in over 25 mortal human diseases. Human Angiogenin (h-ANG), a ribonuclease A family member, produces RNA fragments that regulat
Externí odkaz:
https://doaj.org/article/0671f20e6b0e41619ad56c0fa19f3bd5
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