Search Results - "Lolicato, Fabio"
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Lipid-Chaperone Hypothesis: A Common Molecular Mechanism of Membrane Disruption by Intrinsically Disordered Proteins
Published in ACS chemical neuroscience (16-12-2020)“…An increasing number of human diseases has been shown to be linked to aggregation and amyloid formation by intrinsically disordered proteins (IDPs). Amylin,…”
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SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions
Published in eLife (27-02-2024)“…SNAP25 is one of three neuronal SNAREs driving synaptic vesicle exocytosis. We studied three mutations in SNAP25 that cause epileptic encephalopathy: V48F, and…”
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The Role of Cholesterol in Driving IAPP-Membrane Interactions
Published in Biophysical journal (12-07-2016)“…Our knowledge of the molecular events underlying type 2 diabetes mellitus—a protein conformational disease characterized by the aggregation of islet amyloid…”
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Dimerization of the pulmonary surfactant protein C in a membrane environment
Published in PloS one (27-04-2022)“…Surfactant protein C (SP-C) has several functions in pulmonary surfactant. These include the transfer of lipids between different membrane structures, a role…”
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Lipid-assisted protein transport: A diffusion-reaction model supported by kinetic experiments and molecular dynamics simulations
Published in The Journal of chemical physics (14-05-2016)“…The protein transport inside a cell is a complex phenomenon that goes through several difficult steps. The facilitated transport requires sophisticated…”
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A Role for Liquid-Ordered Plasma Membrane Nanodomains Coordinating the Unconventional Secretory Pathway of Fibroblast Growth Factor 2?
Published in Frontiers in cell and developmental biology (01-04-2022)“…Fibroblast growth factor 2 (FGF2) is a tumor cell survival factor that belongs to a subgroup of extracellular proteins lacking N-terminal signal peptides…”
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Disulfide bridge-dependent dimerization triggers FGF2 membrane translocation into the extracellular space
Published in eLife (22-01-2024)“…Fibroblast growth factor 2 (FGF2) exits cells by direct translocation across the plasma membrane, a type I pathway of unconventional protein secretion. This…”
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Negatively Charged Gangliosides Promote Membrane Association of Amphipathic Neurotransmitters
Published in Neuroscience (01-08-2018)“…[Display omitted] •Anionic ganglioside GM1 facilitates membrane association of amphipathic histamine.•GM1 promotes membrane association of amphipathic…”
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Overlay databank unlocks data-driven analyses of biomolecules for all
Published in Nature communications (07-02-2024)“…Tools based on artificial intelligence (AI) are currently revolutionising many fields, yet their applications are often limited by the lack of suitable…”
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Symmetry-breaking transitions in the early steps of protein self-assembly
Published in European biophysics journal (01-03-2020)“…Protein misfolding and subsequent self-association are complex, intertwined processes, resulting in development of a heterogeneous population of aggregates…”
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Key steps in unconventional secretion of fibroblast growth factor 2 reconstituted with purified components
Published in eLife (19-07-2017)“…FGF2 is secreted from cells by an unconventional secretory pathway. This process is mediated by direct translocation across the plasma membrane. Here, we…”
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In vivo characterization of the bacterial intramembrane-cleaving protease RseP using the heme binding tag-based assay iCliPSpy
Published in Communications biology (18-03-2023)“…Regulated intramembrane proteolysis (RIP) describes the protease-dependent cleavage of transmembrane proteins within the hydrophobic core of cellular…”
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The Na,K-ATPase acts upstream of phosphoinositide PI(4,5)P2 facilitating unconventional secretion of Fibroblast Growth Factor 2
Published in Communications biology (25-03-2020)“…FGF2 is a tumor cell survival factor that is exported from cells by an ER/Golgi-independent secretory pathway. This unconventional mechanism of protein…”
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Phosphoinositide switches in cell physiology - From molecular mechanisms to disease
Published in The Journal of biological chemistry (01-03-2024)“…Phosphoinositides are amphipathic lipid molecules derived from phosphatidylinositol that represent low abundance components of biological membranes. Rather…”
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The role of alpha-helix on the structure-targeting drug design of amyloidogenic proteins
Published in Chemistry and physics of lipids (01-05-2021)“…The most accredited hypothesis links the toxicity of amyloid proteins to their harmful effects on membrane integrity through the formation of…”
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A unifying framework for amyloid-mediated membrane damage: The lipid-chaperone hypothesis
Published in Biochimica et biophysica acta. Proteins and proteomics (01-04-2022)“…Over the past thirty years, researchers have highlighted the role played by a class of proteins or polypeptides that forms pathogenic amyloid aggregates in…”
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doGlycans–Tools for Preparing Carbohydrate Structures for Atomistic Simulations of Glycoproteins, Glycolipids, and Carbohydrate Polymers for GROMACS
Published in Journal of chemical information and modeling (23-10-2017)“…Carbohydrates constitute a structurally and functionally diverse group of biological molecules and macromolecules. In cells they are involved in, e.g., energy…”
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Resveratrol interferes with the aggregation of membrane-bound human-IAPP: A molecular dynamics study
Published in European journal of medicinal chemistry (06-03-2015)“…Amyloid aggregation of islet amyloid polypeptide (IAPP) in pancreatic tissues is a typical feature of type 2 diabetes mellitus. Resveratrol, a natural product…”
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A critical role for cholesterol in PI(4,5)P2-dependent unconventional secretion of fibroblast growth factor 2
Published in Biophysical journal (11-02-2022)Get full text
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Phospholipids Critical Micellar Concentrations Trigger Different Mechanisms of Intrinsically Disordered Proteins Interaction with Model Membranes
Published in The journal of physical chemistry letters (06-09-2018)“…Amyloidogenic proteins are involved in many diseases, including Alzheimer’s, Parkinson’s, and type II diabetes. These proteins are thought to be toxic for…”
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