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dc.contributor.authorGiusj Monia Pugliese
dc.contributor.authorSara Latini
dc.contributor.authorGiorgia Massacci
dc.contributor.authorLivia Perfetto
dc.contributor.authorFrancesca Sacco
dc.contributor.otherDepartment of Biology, University of Rome Tor Vergata, Via delle Ricerca Scientifica 1, 00133 Rome, Italy
dc.contributor.otherDepartment of Biology, University of Rome Tor Vergata, Via delle Ricerca Scientifica 1, 00133 Rome, Italy
dc.contributor.otherDepartment of Biology, University of Rome Tor Vergata, Via delle Ricerca Scientifica 1, 00133 Rome, Italy
dc.contributor.otherFondazione Human Technopole, Department of Biology, Via Cristina Belgioioso 171, 20157 Milan, Italy
dc.contributor.otherDepartment of Biology, University of Rome Tor Vergata, Via delle Ricerca Scientifica 1, 00133 Rome, Italy
dc.date.accessioned2021-04-28T00:04:21Z
dc.date.available2025-10-02T04:30:46Z
dc.date.issued01-04-2021
dc.identifier.issn-
dc.identifier.urihttps://www.mdpi.com/2227-7382/9/2/19
dc.description.abstractFLT3 mutations are the most frequently identified genetic alterations in acute myeloid leukemia (AML) and are associated with poor clinical outcome, relapse and chemotherapeutic resistance. Elucidating the molecular mechanisms underlying FLT3-dependent pathogenesis and drug resistance is a crucial goal of biomedical research. Given the complexity and intricacy of protein signaling networks, deciphering the molecular basis of FLT3-driven drug resistance requires a systems approach. Here we discuss how the recent advances in mass spectrometry (MS)-based (phospho) proteomics and multiparametric analysis accompanied by emerging computational approaches offer a platform to obtain and systematically analyze cell-specific signaling networks and to identify new potential therapeutic targets.
dc.format-
dc.language.isoEN
dc.publisherMDPI AG
dc.relation.uri['https://www.journals.elsevier.com/chemical-thermodynamics-and-thermal-analysis', 'https://www.elsevier.com/journals/chemical-thermodynamics-and-thermal-analysis/2667-3126/guide-for-authors', 'https://www.elsevier.com/authors/open-access/choice#waivers']
dc.rights['CC BY', 'CC BY-NC-ND', 'CC BY-NC']
dc.subject['phase equilibria', 'equations of state', 'calorimetry', 'thermodynamics', 'mixtures', 'kinetics', 'Thermodynamics', 'QC310.15-319']
dc.subject.lccMicrobiology
dc.titleCombining Mass Spectrometry-Based Phosphoproteomics with a Network-Based Approach to Reveal FLT3-Dependent Mechanisms of Chemoresistance
dc.typeArticle
dc.description.keywordsAML
dc.description.keywordsFLT3
dc.description.keywordsdrug-resistance
dc.description.keywords(phospho)proteomic
dc.description.keywordssignaling-network
dc.description.keywordslogic-model
dc.description.pages-
dc.description.doi10.3390/proteomes9020019
dc.title.journalProteomes
dc.identifier.e-issn2227-7382
dc.identifier.oaioai:doaj.org/journal:b9fd26c078284b38b726ed59b7ebe481
dc.journal.infoVolume 9, Issue 2


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