ALLEGRO Diane
Onglets principaux
Team
Localisation
Faculté de médecine, 3ème étage, Aile Rouge
Fonctions
Production, purification et modifications de protéines
- Culture de cellules procaryotes ou eucaryotes
- extraction de protéines tissulaires ou recombinantes
- Chromatographie liquide
- SDS PAGE et Western Blot
Etudes d'interactions moléculaires
- Spectrophotométries
- Ultracentrifugation Analytique
- DLS, CD, DSC, nanoDSF
- Microscopie Electronique à Transmission
Responsables parc instrumental
- centrifugeuses
- ultracentrifugeuses
- spectrophotomètres
- spectrofluorimètre
- FPLC
- lyophilisateur
Assistante de Prévention
Domaines de recherche
Notre équipe s’attèle à déchiffrer les mécanismes moléculaires et cellulaires impliqués dans les maladies neurodégénératives telles que la Maladie d’Alzheimer et le glioblastome. Je suis la référente technique des études d’interactions protéines-ligands au niveau moléculaire, c'est à dire que j'élabore et mets en place différents protocoles que je développe, adapte et optimise.
Ces protocoles s'appliquent aux projets de recherche concernant les protéines d'intérêt Tau et Tubuline.
Enseignements
Encadrement de stagiaires et étudiants (3e, L2, L3, M1, M2, doctorants, élèves ingénieur)
Participation TP
Publications
http://api.archives-ouvertes.fr/search/?&fq=authLastNameFirstName_s:%28%22Allegro+Diane%22%29&fl=title_s,en_title_s,docid,label_s,en_label_s,authIdHal_s,halId_s,structId_i,uri_s,keyword_s,en_keyword_s,authLastNameFirstName_s,journalTitle_s,abstract_s,en_abstract_s,producedDate_tdate,producedDateY_i,language_s&sort=publicationDate_s+desc
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Structural Flexibility of Tau in Its Interaction with Microtubules as Viewed by Site-Directed Spin Labeling EPR SpectroscopyMethods in Molecular Biology2024
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Structural Flexibility of Tau in Its Interaction with Microtubules as Viewed by Site-Directed Spin Labeling EPR Spectroscopy2024
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2-Aminothiazole-Flavonoid Hybrid Derivatives Binding to Tau Protein and Responsible for Antitumor Activity in GlioblastomaInternational Journal of Molecular Sciences2023
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Binding of two zinc ions promotes liquid-liquid phase separation of TauInternational Journal of Biological Macromolecules2022
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Identification of the three zinc-binding sites on tau proteinInternational Journal of Biological Macromolecules2022
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Allocolchicinoids bearing a Michael acceptor fragment for possible irreversible binding of tubulinRSC Medicinal Chemistry2020
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Discovery of dihydrofuranoallocolchicinoids - Highly potent antimitotic agents with low acute toxicityEuropean Journal of Medicinal Chemistry2020
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Two Tau binding sites on tubulin revealed by thiol-disulfide exchangesScientific Reports2018
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Synthesis and biological evaluation of 4 arylcoumarin analogues as tubulin-targeting antitumor agentsBioorganic and Medicinal Chemistry2017
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Interactions of long-chain homologues of colchicine with tubulinEuropean Journal of Medicinal Chemistry2017
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Tau Interaction with Tubulin and Microtubules: From Purified Proteins to Cells2017
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Hsp90 Oligomers Interacting with the Aha1 Cochaperone: An Outlook for the Hsp90 Chaperone MachineriesAnalytical Chemistry2015
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Hsp90 Oligomerization Process: How Can p23 Drive the Chaperone Machineries?Biochimica et Biophysica Acta Proteins and Proteomics2015
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Synthesis and Biological Evaluation of FuranoallocolchicinoidsJournal of Medicinal Chemistry2014
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Quantitative Analysis of Tau-Microtubule Interaction Using FRETInternational Journal of Molecular Sciences2014
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Synthesis and biological evaluation of novel anticancer bivalent colchicine–tubulizine hybridsBioorganic and Medicinal Chemistry2012
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Biochemical and biophysical characterization of the Mg2+-induced 90-kDa heat shock protein oligomers.Journal of Biological Chemistry2010
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Caulerpenyne binding to tubulin: structural modifications by a non conventional pharmacological agent.Medicinal Chemistry2009
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Stathmin/Op18 is a novel mediator of vinblastine activityFEBS Letters2008
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Discovery of a new family of bis-8-hydroxyquinoline substituted benzylamines with pro-apoptotic activity in cancer cells: Synthesis, structure-activity relationship, and action mechanism studies.European Journal of Medicinal Chemistry2008
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Modulation of microtubule assembly by the HIV-1 Tat protein is strongly dependent on zinc binding to TatRetrovirology2008
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Modulation of microtubule assembly by the HIV-1 Tat protein is strongly dependent on zinc binding to Tat.Retrovirology2008
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Modulation of microtubule assembly by the HIV-1 Tat protein is strongly dependent on zinc binding to TatRetrovirology2008
