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Advances in Protein Chemistry and Structural Biology|June 25, 2013
Anomalous protein-DNA interactions behind neurological disordersSergio Camero, María J Benítez, Juan S Jiménez
International Journal of Biological Macromolecules|January 29, 2013
Specific binding of DNA to aggregated forms of Alzheimer's disease amyloid peptidesSergio Camero, Jose M Ayuso, Alejandro Barrantes, et al.
Chemical Communications (Cambridge, England)|February 19, 2020
Vescalagin and castalagin reduce the toxicity of amyloid-beta42 oligomers through the remodelling of its secondary structureAna R Araújo, Sergio Camero, Pablo Taboada, et al.
Chemical Communications (Cambridge, England)|March 17, 2021
Correction: Vescalagin and castalagin reduce the toxicity of amyloid-beta42 oligomers through the remodelling of its secondary structureAna R Araújo, Sergio Camero, Pablo Taboada, et al.
Plos One|August 16, 2014
Thermodynamics of the interaction between Alzheimer's disease related tau protein and DNASergio Camero, María J Benítez, Raquel Cuadros, et al.
RNA Biology|August 23, 2021
The RBS1 domain of Gemin5 is intrinsically unstructured and interacts with RNA through conserved Arg and aromatic residuesAzman Embarc-Buh, Rosario Francisco-Velilla, Sergio Camero, et al.
Current Alzheimer Research|May 29, 2012
Alzheimer's disease amyloid peptides interact with DNA, as proved by surface plasmon resonanceAlejandro Barrantes, Sergio Camero, Angel Garcia-Lucas, et al.
Journal of Alzheimer'S Disease : JAD|November 21, 2013
Tau protein provides DNA with thermodynamic and structural features which are similar to those found in histone-DNA complexSergio Camero, María J Benítez, Alejandro Barrantes, et al.
Frontiers in Molecular Biosciences|October 10, 2022
eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assemblyBelén Chaves-Arquero, Santiago Martínez-Lumbreras, Nathalie Sibille, et al.
Life Science Alliance|January 13, 2022
Structural basis of Nrd1-Nab3 heterodimerizationBelén Chaves-Arquero, Santiago Martínez-Lumbreras, Sergio Camero, et al.
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