Xavier Fernàndez‐Busquets

ORCID: 0000-0002-4622-9631
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About
Contact & Profiles
Research Areas
  • Malaria Research and Control
  • Lipid Membrane Structure and Behavior
  • Mosquito-borne diseases and control
  • Marine Sponges and Natural Products
  • Alzheimer's disease research and treatments
  • RNA Interference and Gene Delivery
  • Advancements in Transdermal Drug Delivery
  • Computational Drug Discovery Methods
  • HIV Research and Treatment
  • Venomous Animal Envenomation and Studies
  • Force Microscopy Techniques and Applications
  • Invertebrate Immune Response Mechanisms
  • Nanoparticle-Based Drug Delivery
  • Advanced biosensing and bioanalysis techniques
  • DNA and Nucleic Acid Chemistry
  • Synthetic Organic Chemistry Methods
  • Advanced Glycation End Products research
  • Advanced Drug Delivery Systems
  • Complement system in diseases
  • Research on Leishmaniasis Studies
  • Antimicrobial Peptides and Activities
  • Supramolecular Self-Assembly in Materials
  • Marine Biology and Environmental Chemistry
  • RNA and protein synthesis mechanisms
  • Proteoglycans and glycosaminoglycans research

Institute for Bioengineering of Catalonia
2016-2025

Barcelona Institute for Global Health
2016-2025

Universitat de Barcelona
2016-2025

Institut de Nanociència i Nanotecnologia de la Universitat de Barcelona
2016-2025

Barcelona Institute for Science and Technology
2019-2022

Shanghai Institute for Science of Science
2019-2020

Institute of Science and Technology
2019-2020

FC Barcelona
2019-2020

Barcelona Centre for International Affairs
2013-2015

Marine Biological Laboratory
1996-2009

One of the hallmarks Alzheimer's disease is self-aggregation amyloid beta peptide (Abeta) in extracellular fibrils. Among different forms Abeta, 42-residue fragment (Abeta1-42) readily self-associates and nucleation centers from where fibrils can quickly grow. The strong tendency Abeta1-42 to aggregate one reasons for scarcity data on its fibril formation process. We have used atomic force microscopy (AFM) visualize liquid environment fibrillogenesis synthetic hydrophilic hydrophobic...

10.1096/fj.04-3137fje article EN The FASEB Journal 2005-05-26

Alzheimer's disease neuropathology is characterized by neuronal death, amyloid beta-peptide deposits and neurofibrillary tangles composed of paired helical filaments tau protein. Although crucial for our understanding the pathogenesis disease, molecular mechanisms linking remain unknown. Here, we show that beta-peptide-induced nitro-oxidative damage promotes nitrotyrosination glycolytic enzyme triosephosphate isomerase in human neuroblastoma cells. Consequently, nitro-triosephosphate was...

10.1093/brain/awp023 article EN cc-by Brain 2009-02-27

Abstract The antimalarial activity of heparin, against which there are no resistances known, has not been therapeutically exploited due to its potent anticoagulating activity. Here, we have explored the antiplasmodial capacity heparin-like sulfated polysaccharides from sea cucumbers Ludwigothurea grisea and Isostichopus badionotus , red alga Botryocladia occidentalis marine sponge Desmapsamma anchorata . In vitro experiments demonstrated for most compounds significant inhibition Plasmodium...

10.1038/srep24368 article EN cc-by Scientific Reports 2016-04-13

Abstract Plants produce diverse isoprenoids, which are synthesized in plastids, mitochondria, endoplasmic reticulum (ER), and the nonorganellar cytoplasm. 3-Hydroxy-3-methylglutaryl-coenzyme A reductase (HMGR) catalyzes synthesis of mevalonate, a rate-limiting step cytoplasmic pathway. Several branches pathway lead to structurally functionally varied, yet essential, isoprenoids. HMGR isoforms have been identified all plants examined. Studies based on gene expression fractionation enzyme...

10.1104/pp.104.050245 article EN PLANT PHYSIOLOGY 2004-12-24
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