A5051899114- Alzheimer's disease research and treatments
- Advanced Glycation End Products research
- Neuroscience and Neuropharmacology Research
- Biochemical effects in animals
- Acute Ischemic Stroke Management
- Blood properties and coagulation
- Endoplasmic Reticulum Stress and Disease
- Neuroinflammation and Neurodegeneration Mechanisms
- Adipokines, Inflammation, and Metabolic Diseases
- Neurological Disorders and Treatments
- RNA regulation and disease
- Metabolism, Diabetes, and Cancer
- Drug Transport and Resistance Mechanisms
- Williams Syndrome Research
- Barrier Structure and Function Studies
- Amino Acid Enzymes and Metabolism
- Cholinesterase and Neurodegenerative Diseases
- Nuclear Receptors and Signaling
- Protein Interaction Studies and Fluorescence Analysis
- Electron Spin Resonance Studies
- Receptor Mechanisms and Signaling
- HIV Research and Treatment
- Inflammatory Myopathies and Dermatomyositis
- Nitric Oxide and Endothelin Effects
- Nanoparticle-Based Drug Delivery
Universitat Pompeu Fabra
2011-2023
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by the pathological aggregation of amyloid-β peptide (Aβ). Monomeric soluble Aβ can switch from helicoidal to β-sheet conformation, promoting its assembly into oligomers and subsequently amyloid fibrils. Oligomers are highly toxic neurons have been reported induce synaptic transmission impairments. The progression fibrils forming senile plaques currently considered protective mechanism avoid presence oligomers. Protein...
Ischemic stroke is an acute vascular event that obstructs blood supply to the brain, producing irreversible damage affects neurons but also glial and brain vessel cells. Immediately after stroke, ischemic tissue produces nitric oxide (NO) recover perfusion superoxide anion. These compounds interact, peroxynitrite, which irreversibly nitrates protein tyrosines. The present study measured NO production in a human neuroblastoma (SH-SY5Y), murine (BV2), endothelial cell line (HUVEC), primary...
Glycation and nitrotyrosination are pathological posttranslational modifications that make proteins prone to losing their physiological properties. Since both increased in Alzheimer's disease (AD) due amyloid-β peptide (Aβ) accum
Amyloid-β peptide (Aβ) aggregates induce nitro-oxidative stress, contributing to the characteristic neurodegeneration found in Alzheimer's disease (AD). One of most strongly nitrotyrosinated proteins AD is triosephosphate isomerase (TPI) e
Aims: Hippocampus is the brain center for memory formation, a process that requires synaptogenesis. However, hippocampus dramatically compromised in Alzheimer's disease due to accumulation of amyloid β-peptide, whose production initiated by β-site APP Cleaving Enzyme 1 (BACE1). It known pathological stressors activate BACE1 translation through phosphorylation eukaryotic initiation factor-2α (eIF2α) GCN2, PERK, or PKR kinases, leading amyloidogenesis. physiological regulation still unclear....
Williams-Beuren syndrome (WBS) is a neurodevelopmental disorder caused by heterozygous deletion of 26–28 genes at chromosome band 7q11.23. The complete (CD) mouse model mimics the most common found in WBS patients and recapitulates neurologic features along with some cardiovascular manifestations leading to significant cardiac hypertrophy increased cardiomyocytes' size. Epigallocatechin-3-gallate (EGCG), abundant catechin green tea, has been associated potential health benefits, both on...
// Mònica Bosch-Morató 1 , Cinta Iriondo Biuse Guivernau Victòria Valls-Comamala Noemí Vidal 2 Montse Olivé Henry Querfurth 3 and Francisco J. Muñoz Laboratory of Molecular Physiology, Department Experimental Health Sciences, Universitat Pompeu Fabra, Barcelona, Spain Institut de Neuropatologia, Servei Anatomia Patològica, Hospital Bellvitge, Hospitalet Llobregat, Neurology, Rhode Island Hospital, Warren Alpert Medical School Brown University,...
// Eva Ramos-Fernández 1,* , Marta Tajes Gerard ILL-Raga 1 Lina Vargas 2 Arnau Busquets-García 3 Mònica Bosch-Morató Biuse Guivernau Victòria Valls-Comamala Maria Gomis Cristina Grau 6 César Fandos Mark D. Rosen 4 Michael H. Rabinowitz Nibaldo Inestrosa 5 Rafael Maldonado Xavier Altafaj Andrés Ozaita Alejandra Alvarez Rubén Vicente Miguel A. Valverde and Francisco J. Muñoz Laboratory of Molecular Physiology, Faculty Health Life Sciences, Universitat Pompeu Fabra, Barcelona, Catalonia, Spain...
// Victòria Valls-Comamala 1 , Biuse Guivernau Jaume Bonet 2 Marta Puig Alex Perálvarez-Marín 3 Ernest Palomer Xavier Fernàndez-Busquets 4, 5 Altafaj 6 Tajes 7 Albert Puig-Pijoan 8 Rubén Vicente Baldomero Oliva and Francisco J. Muñoz Laboratory of Molecular Physiology, Faculty Health Life Sciences, Universitat Pompeu Fabra, Barcelona, Spain Structural Bioinformatics (GRIB), Unitat de Biofísica, Departament Bioquímica i Biologia Molecular, Facultat Medicina, Autònoma 4 Institute for...
Alzheimer's disease (AD) is known to be caused by amyloid β-peptide (Aβ) misfolded into β-sheets, but this knowledge has not yet led treatments prevent AD. To identify novel molecular players in Aβ toxicity, we carried out a genome-wide screen Saccharomyces cerevisiae, using library of 5154 gene knock-out strains expressing Aβ1-42. We identified 81 mammalian orthologue genes that enhance Aβ1-42 while 157 were protective. Next, performed interactome and text-mining studies increase the number...
Alzheimer’s disease (AD) is a neurodegenerative characterized by senile plaques and neurofibrillary tangles. Senile are deposits of amyloid ß-peptide (Aß) produced the cleavage transmembrane protein termed Amyloid Precursor Protein (APP). The amyloidogenic APP performed γ-secretase complex ß-site cleaving enzyme 1 (BACE1), key in AD that can be activated different noxious stimuli. Interestingly, some viruses could activate double-stranded RNA-activated kinase (PKR), which phosphorylates...