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AUTHOR

Annalisa Pastore

showing 3 related works from this author

The Ancient Neapolitan Sweet Lime and the Calabrian Lemoncetta Locrese Belong to the Same Citrus Species

2019

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PopulationBiodiversityPharmaceutical Scienceengineering.materialArticleAnalytical Chemistrylcsh:QD241-44103 medical and health sciencestaxonomy0404 agricultural biotechnologylcsh:Organic chemistryagrobiodiversityCitrus aurantiifoliaDrug DiscoveryBotanyneapolitan “four citrus fruits” liqueurPhysical and Theoretical Chemistryagrobiodiversity; lemoncetta Locrese; Mediterranean sweet lime; Neapolitan "four citrus fruits" liqueur; Neapolitan limmo; taxonomyeducationlemoncetta locrese030304 developmental biologyLime2. Zero hunger0303 health scienceseducation.field_of_studyneapolitan limmoOrganic ChemistryNeapolitan "four citrus fruits" liqueur04 agricultural and veterinary sciences040401 food scienceRandom Amplified Polymorphic DNA TechniqueGeographyItalyChemistry (miscellaneous)Fruitmediterranean sweet limeengineeringMolecular MedicineTaxonomy (biology)Molecules
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Recombinant mussel protein Pvfp-5β: A potential tissue bioadhesive

2019

During their lifecycle, many marine organisms rely on natural adhesives to attach to wet surfaces for movement and self-defence in aqueous tidal environments. Adhesive proteins from mussels are biocompatible and elicit only minimal immune responses in humans. Therefore these proteins have received increased attention for their potential applications in medicine, biomaterials and biotechnology. The Asian green mussel Perna viridis secretes several byssal plaque proteins, molecules that help anchor the mussel to surfaces. Among these proteins, protein-5β (Pvfp-5β) initiates interactions with the substrate, displacing interfacial water molecules before binding to the surface. Here, we establis…

0301 basic medicinemedicine.disease_causeBiochemistryepidermal growth factor (EGF)law.inventionMiceCell Movementlawbiophysicsstructural biologyrecombinantCells CulturedbiologyChemistryMarine proteinsAdhesionRecombinant ProteinsadhesionProtein Structure and FoldingRecombinant DNAadhesion proteinsbiomaterialsPernaCell SurvivalSurface PropertiesBioadhesivemussel03 medical and health sciencesmedicineAnimalsHumansMolecular BiologyEscherichia coliCell ProliferationTissue Engineering030102 biochemistry & molecular biologyProteinsCell BiologyMusselbiology.organism_classificationEGF-like motifs; Marine proteins; adhesion; adhesion proteins; biomaterials; biophysics; epidermal growth factor (EGF); structural biologyEGF-like motifs030104 developmental biologyStructural biologyCell cultureNIH 3T3 CellsBiophysicsTissue AdhesivesHeLa CellsPerna viridisJournal of Biological Chemistry
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Solution structure of recombinant Pvfp-5β reveals insights into mussel adhesion

2022

Solution structure of byssal plaque protein Pvfp-5 beta secreted by the Asian green mussel Perna viridis gives molecular insight into mussel adhesion on wet surfaces.Some marine organisms can resist to aqueous tidal environments and adhere tightly on wet surface. This behavior has raised increasing attention for potential applications in medicine, biomaterials, and tissue engineering. In mussels, adhesive forces to the rock are the resultant of proteinic fibrous formations called byssus. We present the solution structure of Pvfp-5 beta, one of the three byssal plaque proteins secreted by the Asian green mussel Perna viridis, and the component responsible for initiating interactions with the…

PernaEpidermal Growth FactorTissue EngineeringArtificial IntelligenceAdhesivesAnimalsMedicine (miscellaneous)Biocompatible MaterialsGeneral Agricultural and Biological SciencesGeneral Biochemistry Genetics and Molecular BiologyCommunications Biology
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