A5052323656- Alzheimer's disease research and treatments
- Parkinson's Disease Mechanisms and Treatments
- Ginkgo biloba and Cashew Applications
- Lipid Membrane Structure and Behavior
- Mitochondrial Function and Pathology
- Tea Polyphenols and Effects
- Endoplasmic Reticulum Stress and Disease
- Enzyme Production and Characterization
- Neurological Disease Mechanisms and Treatments
- Neuroscience and Neuropharmacology Research
- Organ Transplantation Techniques and Outcomes
- African history and culture analysis
- Microbial Metabolism and Applications
- Computational Drug Discovery Methods
- Liver physiology and pathology
- Tryptophan and brain disorders
- biodegradable polymer synthesis and properties
- Botanical Research and Applications
- Biochemical and biochemical processes
- Liver Disease and Transplantation
- Cholinesterase and Neurodegenerative Diseases
- Middle East Politics and Society
- Language, Linguistics, Cultural Analysis
- Seaweed-derived Bioactive Compounds
- Natural product bioactivities and synthesis
University of Malta
2011-2021
University College London
1999
The Royal Free Hospital
1999
Alpha-synuclein binds to by biophysical (View Interaction 1, 2) Convergent genetic, biochemical and animal studies over the past decade strongly suggest that aggregation of 140-residue pre-synaptic alpha-synuclein (αS) protein plays a fundamental role in etiology pathogenesis Parkinson's disease (PD) related disorders [1]. These are fact collectively known as "α-synucleinopathies", with PD being most common movement disorder [2]. Motor symptoms reflect severe degeneration dopaminergic...
Aggregation of the amyloid-forming α-synuclein (αS) protein is closely associated with etiology Parkinson's disease (PD), most common motor neurodegenerative disorder. Many studies have shown that soluble aggregation intermediates αS, termed oligomers, permeabilize a variety phospholipid membranes; thus, membrane disruption may represent key pathogenic mechanism αS toxicity. Given centrality mitochondrial dysfunction in PD, we therefore probed formation ion-permeable pores by oligomers...
Research Article5 December 2017Open Access Transparent process The diphenylpyrazole compound anle138b blocks Aβ channels and rescues disease phenotypes in a mouse model for amyloid pathology Ana Martinez Hernandez Department Epigenetics Systems Medicine Neurodegenerative Diseases, German Center Diseases (DZNE), Göttingen, Germany Genes Behavior, Max Planck Institute Biophysical Chemistry, Search more papers by this author Hendrik Urbanke Alan L Gillman orcid.org/0000-0002-1312-047X of...
Amyloid-β (Aβ) aggregation is a recognized key process in the pathogenesis of Alzheimer's disease (AD). Misfolded Aβ peptides self-assemble into higher-order oligomers that compromise membrane integrity, leading to synaptic degeneration and neuronal cell death. The main aim this study was explore whether small-molecule compounds black tea extract can protect phospholipid membranes from disruption by aggregates. We first established robust protocol for aggregating Aβ₄₂ range efficiently...
Aggregation of α-synuclein is involved in the pathogenesis Parkinson's disease (PD). Studies vitro aggregation are rendered complex because formation a heterogeneous population oligomers. With use confocal single-molecule fluorescence techniques, we demonstrate that small aggregates (oligomers) formed from unbound monomeric species presence organic solvent (DMSO) and iron (Fe3+) ions have high affinity to bind model membranes, regardless lipid-composition or membrane curvature. This binding...
Abstract Studies on the amyloidogenic N-terminal domain of E. coli HypF protein (HypF-N) have contributed significantly to a detailed understanding pathogenic mechanisms in neurodegenerative diseases characterised by formation misfolded oligomers, proteins such as amyloid-β, α-synuclein and tau. Given that both cell membranes mitochondria are increasingly recognised key targets oligomer toxicity, we investigated damaging effects aggregates HypF-N mitochondrial membranes. Essentially, found...
The identification of compounds which protect the double-membrane mitochondrial organelles from disruption by toxic confomers amyloid proteins may offer a therapeutic strategy to combat human neurodegenerative diseases. Here, we exploited an extract marine brown seaweed Padina pavonica (PPE) as vital source natural bioactive membranes against insult oligomeric aggregates amyloidogenic amyloid-β (Aβ), α-synuclein (α-syn) and tau, are currently considered be major targets for drug discovery in...