Tau protein provides DNA with thermodynamic and structural features which are similar to those found in histone-DNA complex

S Camero, MJ Benítez, A Barrantes… - Journal of …, 2014 - content.iospress.com
Tau protein has been proposed as a trigger of Alzheimer's disease once it is hyperphosphorylated.
However, the role that native tau forms play inside the neuronal nucleus remains …

[HTML][HTML] Thermodynamics of the interaction between Alzheimer's disease related tau protein and DNA

S Camero, MJ Benítez, R Cuadros, F Hernandez… - PLoS …, 2014 - journals.plos.org
Tau hyperphosphorylation can be considered as one of the hallmarks of Alzheimer's disease
and other tauophaties. Besides its well-known role as a microtubule associated protein, …

Specific binding of DNA to aggregated forms of Alzheimer's disease amyloid peptides

S Camero, JM Ayuso, A Barrantes, MJ Benítez… - International journal of …, 2013 - Elsevier
Anomalous protein aggregation is closely associated to age-related mental illness.
Extraneuronal plaques, mainly composed of aggregated amyloid peptides, are considered as …

The RBS1 domain of Gemin5 is intrinsically unstructured and interacts with RNA through conserved Arg and aromatic residues

A Embarc-Buh, R Francisco-Velilla, S Camero… - RNA biology, 2021 - Taylor & Francis
Gemin5 is a multifaceted RNA-binding protein that comprises distinct structural domains,
including a WD40 and TPR-like for which the X-ray structure is known. In addition, the protein …

Structural basis of Nrd1–Nab3 heterodimerization

…, S Martínez-Lumbreras, S Camero… - Life science …, 2022 - life-science-alliance.org
Heterodimerization of RNA binding proteins Nrd1 and Nab3 is essential to communicate the
RNA recognition in the nascent transcript with the Nrd1 recognition of the Ser 5 -…

Vescalagin and castalagin reduce the toxicity of amyloid-beta42 oligomers through the remodelling of its secondary structure

AR Araújo, S Camero, P Taboada, RL Reis… - Chemical …, 2020 - pubs.rsc.org
The isomers vescalagin and castalagin protect SH-SY5Y cells from Aβ42-mediated death.
This is achieved better by vescalagin due to the spatial organization of its OH group at the C1 …

Alzheimer's disease amyloid peptides interact with DNA, as proved by surface plasmon resonance

A Barrantes, S Camero, A Garcia-Lucas… - Current Alzheimer …, 2012 - ingentaconnect.com
According to the amyloid hypothesis, abnormal processing of the β-amyloid precursor protein
in Alzheimer's disease patients increases the production of β-amyloid toxic peptides, which…

Anomalous Protein–DNA Interactions Behind Neurological Disorders

S Camero, MJ Benítez, JS Jiménez - Advances in protein chemistry and …, 2013 - Elsevier
Aggregation, nuclear location, and nucleic acid interaction are common features shared by
a number of proteins related to neurodegenerative diseases, including Alzheimer’s disease, …

[HTML][HTML] eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly

…, S Martínez-Lumbreras, N Sibille, S Camero… - Frontiers in molecular …, 2022 - frontiersin.org
Yeast eIF4G1 interacts with RNA binding proteins (RBPs) like Pab1 and Pub1 affecting its
function in translation initiation and stress granules formation. We present an NMR and SAXS …

Multivalent interactions between eIF4G1, Pub1 and Pab1 drive the formation of protein condensates

…, S Martínez-Lumbreras, N Sibille, S Camero… - bioRxiv, 2020 - biorxiv.org
Yeast eIF4G1 interacts with RNA binding proteins (RBPs) like Pab1 and Pub1 affecting its
function in translation initiation and stress granules formation. We present an NMR and SAXS …