{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T01:40:24Z","timestamp":1790646024212,"version":"4.1.0"},"reference-count":91,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2022,5,4]],"date-time":"2022-05-04T00:00:00Z","timestamp":1651622400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Fabry disease is caused by a deficiency of lysosomal alpha galactosidase and has a very large genotypic and phenotypic spectrum. Some patients who carry hypomorphic mutations can benefit from oral therapy with a pharmacological chaperone. The drug requires a very precise regimen because it is a reversible inhibitor of alpha-galactosidase. We looked for molecules that can potentiate this pharmacological chaperone, among drugs that have already been approved for other diseases. We tested candidate molecules in fibroblasts derived from a patient carrying a large deletion in the gene GLA, which were stably transfected with a plasmid expressing hypomorphic mutants. In our cell model, three drugs were able to potentiate the action of the pharmacological chaperone. We focused our attention on one of them, acetylsalicylic acid. We expect that acetylsalicylic acid can be used in synergy with the Fabry disease pharmacological chaperone and prolong its stabilizing effect on alpha-galactosidase.<\/jats:p>","DOI":"10.3390\/ijms23095105","type":"journal-article","created":{"date-parts":[[2022,5,4]],"date-time":"2022-05-04T08:21:25Z","timestamp":1651652485000},"page":"5105","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Drug Repositioning for Fabry Disease: Acetylsalicylic Acid Potentiates the Stabilization of Lysosomal Alpha-Galactosidase by Pharmacological Chaperones"],"prefix":"10.3390","volume":"23","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3136-2138","authenticated-orcid":false,"given":"Maria","family":"Monticelli","sequence":"first","affiliation":[{"name":"Department Biology, University of Napoli \u00ab Federico II \u00bb, Complesso Universitario Monte Sant\u2019Angelo, Via Cinthia, 80126 Napoli, Italy"},{"name":"Department Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania \u201cLuigi Vanvitelli\u201d, Via Vivaldi 43, 81100 Caserta, Italy"},{"name":"Institute of Biomolecular Chemistry ICB, CNR, Via Campi Flegrei 34, 80078 Pozzuoli, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8480-0501","authenticated-orcid":false,"given":"Ludovica","family":"Liguori","sequence":"additional","affiliation":[{"name":"Department Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania \u201cLuigi Vanvitelli\u201d, Via Vivaldi 43, 81100 Caserta, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3693-2515","authenticated-orcid":false,"given":"Mariateresa","family":"Allocca","sequence":"additional","affiliation":[{"name":"Department Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania \u201cLuigi Vanvitelli\u201d, Via Vivaldi 43, 81100 Caserta, Italy"},{"name":"Institute of Biomolecular Chemistry ICB, CNR, Via Campi Flegrei 34, 80078 Pozzuoli, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2360-300X","authenticated-orcid":false,"given":"Andrea","family":"Bosso","sequence":"additional","affiliation":[{"name":"Department Biology, University of Napoli \u00ab Federico II \u00bb, Complesso Universitario Monte Sant\u2019Angelo, Via Cinthia, 80126 Napoli, Italy"},{"name":"Institute of Biochemistry and Cellular Biology, National Research Council, Via Pietro Castellino 111, 80131 Napoli, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1594-0156","authenticated-orcid":false,"given":"Giuseppina","family":"Andreotti","sequence":"additional","affiliation":[{"name":"Institute of Biomolecular Chemistry ICB, CNR, Via Campi Flegrei 34, 80078 Pozzuoli, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan","family":"Lukas","sequence":"additional","affiliation":[{"name":"Translational Neurodegeneration Section \u201cAlbrecht-Kossel\u201d, Department of Neurology, University Medical Center Rostock, 18147 Rostock, Germany"},{"name":"Center for Transdisciplinary Neurosciences Rostock (CTNR), University Medical Center Rostock, 18147 Rostock, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1337-2909","authenticated-orcid":false,"given":"Maria Chiara","family":"Monti","sequence":"additional","affiliation":[{"name":"Department of Pharmacy, University of Salerno, Via Giovanni Paolo II 132, 84084 Fisciano, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7244-0297","authenticated-orcid":false,"given":"Elva","family":"Morretta","sequence":"additional","affiliation":[{"name":"Department of Pharmacy, University of Salerno, Via Giovanni Paolo II 132, 84084 Fisciano, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6147-6553","authenticated-orcid":false,"given":"Maria Vittoria","family":"Cubellis","sequence":"additional","affiliation":[{"name":"Department Biology, University of Napoli \u00ab Federico II \u00bb, Complesso Universitario Monte Sant\u2019Angelo, Via Cinthia, 80126 Napoli, Italy"},{"name":"Institute of Biomolecular Chemistry ICB, CNR, Via Campi Flegrei 34, 80078 Pozzuoli, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5579-183X","authenticated-orcid":false,"given":"Bruno","family":"Hay Mele","sequence":"additional","affiliation":[{"name":"Department Biology, University of Napoli \u00ab Federico II \u00bb, Complesso Universitario Monte Sant\u2019Angelo, Via Cinthia, 80126 Napoli, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,5,4]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Tuttolomondo, A., Simonetta, I., Riolo, R., Todaro, F., Di Chiara, T., Miceli, S., and Pinto, A. (2021). Pathogenesis and Molecular Mechanisms of Anderson\u2013Fabry Disease and Possible New Molecular Addressed Therapeutic Strategies. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms221810088"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"s10","DOI":"10.1590\/1806-9282.66.s1.10","article-title":"Fabry disease: Genetics, pathology, and treatment","volume":"66","author":"Bernardes","year":"2020","journal-title":"Rev. Da Assoc. M\u00e9dica Bras."},{"key":"ref_3","first-page":"4","article-title":"A Review of Fabry Disease","volume":"23","author":"Chan","year":"2018","journal-title":"Ski. Ther. Lett."},{"key":"ref_4","unstructured":"Adam, M.P., Ardinger, H.H., Pagon, R.A., and Wallace, S.E. (2022, January 27). DA Fabry Disease, GeneReviews\u00ae, Available online: https:\/\/www.ncbi.nlm.nih.gov\/books\/NBK1292\/."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1002\/dta.1798","article-title":"Looking for protein stabilizing drugs with thermal shift assay","volume":"7","author":"Andreotti","year":"2015","journal-title":"Drug Test. Anal."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/j.amjms.2020.07.011","article-title":"When and How to Diagnose Fabry Disease in Clinical Pratice","volume":"360","author":"Michaud","year":"2020","journal-title":"Am. J. Med Sci."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1136\/postgradmedj-2018-136056","article-title":"Hot topics in Fabry disease","volume":"94","author":"Cairns","year":"2018","journal-title":"Postgrad. Med J."},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Citro, V., Cammisa, M., Liguori, L., Cimmaruta, C., Lukas, J., Cubellis, M.V., and Andreotti, G. (2016). The Large Phenotypic Spectrum of Fabry Disease Requires Graduated Diagnosis and Personalized Therapy: A Meta-Analysis Can Help to Differentiate Missense Mutations. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17122010"},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Lukas, J., Cimmaruta, C., Liguori, L., Pantoom, S., Iwanov, K., Petters, J., Hund, C., Bunschkowski, M., Hermann, A., and Cubellis, M.V. (2020). Assessment of Gene Variant Amenability for Pharmacological Chaperone Therapy with 1-Deoxygalactonojirimycin in Fabry Disease. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21030956"},{"key":"ref_10","first-page":"1","article-title":"DNA methylation impact on Fabry disease","volume":"13","author":"Vinciguerra","year":"2021","journal-title":"Clin. Epigenetics"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1111\/cge.12613","article-title":"X-chromosome inactivation in female patients with Fabry disease","volume":"89","author":"Echevarria","year":"2016","journal-title":"Clin. Genet."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.ymgme.2018.09.007","article-title":"The effect of enzyme replacement therapy on clinical outcomes in female patients with Fabry disease \u2013 A systematic literature review by a European panel of experts","volume":"126","author":"Germain","year":"2019","journal-title":"Mol. Genet. Metab."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"100454","DOI":"10.1016\/j.ymgmr.2019.100454","article-title":"The effect of enzyme replacement therapy on clinical outcomes in male patients with Fabry disease: A systematic literature review by a European panel of experts","volume":"19","author":"Germain","year":"2019","journal-title":"Mol. Genet. Metab. Rep."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1002\/jimd.12167","article-title":"Fabry disease genotype, phenotype, and migalastat amenability: Insights from a national cohort","volume":"43","author":"Nowak","year":"2019","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1038\/gim.2016.122","article-title":"The validation of pharmacogenetics for the identification of Fabry patients to be treated with migalastat","volume":"19","author":"Benjamin","year":"2017","journal-title":"Genet. Med."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1186\/1750-1172-8-111","article-title":"Fabry_CEP: A tool to identify Fabry mutations responsive to pharmacological chaperones","volume":"8","author":"Cammisa","year":"2013","journal-title":"Orphanet J. Rare Dis."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1007\/s10545-009-1077-0","article-title":"The pharmacological chaperone 1-deoxygalactonojirimycin increases \u03b1-galactosidase A levels in Fabry patient cell lines","volume":"32","author":"Benjamin","year":"2009","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1097\/FPC.0b013e32830500f4","article-title":"Prediction of response of mutated alpha-galactosidase A to a pharmacological chaperone","volume":"18","author":"Shin","year":"2008","journal-title":"Pharmacogenetics Genom."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.bbrc.2007.05.082","article-title":"Screening for pharmacological chaperones in Fabry disease","volume":"359","author":"Shin","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1042\/BJ20070479","article-title":"Mutant \u03b1-galactosidase A enzymes identified in Fabry disease patients with residual enzyme activity: Biochemical characterization and restoration of normal intracellular processing by 1-deoxygalactonojirimycin","volume":"406","author":"Ishii","year":"2007","journal-title":"Biochem. J."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1086\/504601","article-title":"High Incidence of Later-Onset Fabry Disease Revealed by Newborn Screening*","volume":"79","author":"Spada","year":"2006","journal-title":"Am. J. Hum. Genet."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1002\/humu.22910","article-title":"Functional and Clinical Consequences of Novel \u03b1-Galactosidase A Mutations in Fabry Disease","volume":"37","author":"Lukas","year":"2016","journal-title":"Hum. Mutat."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1006\/abbi.2000.1743","article-title":"Role of Ser-65 in the Activity of \u03b1-Galactosidase A: Characterization of a Point Mutation (S65T) Detected in a Patient with Fabry Disease","volume":"377","author":"Ishii","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1002\/humu.21530","article-title":"A pharmacogenetic approach to identify mutant forms of \u03b1-galactosidase a that respond to a pharmacological chaperone for Fabry disease","volume":"32","author":"Wu","year":"2011","journal-title":"Hum. Mutat."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1186\/1750-1172-6-66","article-title":"Therapy of Fabry disease with pharmacological chaperones: From in silico predictions to in vitro tests","volume":"6","author":"Andreotti","year":"2011","journal-title":"Orphanet J. Rare Dis."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3858\/emm.2009.41.1.001","article-title":"Effects of a chemical chaperone on genetic mutations in \u03b1-galactosidase A in Korean patients with Fabry disease","volume":"41","author":"Park","year":"2009","journal-title":"Exp. Mol. Med."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.ymgme.2013.01.009","article-title":"A Phase 2 study of migalastat hydrochloride in females with Fabry disease: Selection of population, safety and pharmacodynamic effects","volume":"109","author":"Giugliani","year":"2013","journal-title":"Mol. Genet. Metab."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Lukas, J., Giese, A.K., Markoff, A., Grittner, U., Kolodny, E., Mascher, H., Lackner, K.J., Meyer, W., Wree, P., and Saviouk, V. (2013). Functional Characterisation of Alpha-Galactosidase A Mutations as a Basis for a New Classification System in Fabry Disease. PLoS Genet., 9.","DOI":"10.1371\/journal.pgen.1003632"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.biochi.2015.03.018","article-title":"Taming molecular flexibility to tackle rare diseases","volume":"113","author":"Cubellis","year":"2015","journal-title":"Biochimie"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1186\/1750-1172-5-36","article-title":"Prediction of the responsiveness to pharmacological chaperones: Lysosomal human alpha-galactosidase, a case of study","volume":"5","author":"Andreotti","year":"2010","journal-title":"Orphanet J. Rare Dis."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.ymgme.2011.01.013","article-title":"Molecular mechanism for stabilization of a mutant \u03b1-galactosidase A involving M51I amino acid substitution by imino sugars","volume":"103","author":"Tsukimura","year":"2011","journal-title":"Mol. Genet. Metab."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"e0165463","DOI":"10.1371\/journal.pone.0165463","article-title":"Identification of an Allosteric Binding Site on Human Lysosomal Alpha-Galactosidase Opens the Way to New Pharmacological Chaperones for Fabry Disease","volume":"11","author":"Citro","year":"2016","journal-title":"PLoS ONE"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"eaat7467","DOI":"10.1126\/scitranslmed.aat7467","article-title":"Repurposing ciclopirox as a pharmacological chaperone in a model of congenital erythropoietic porphyria","volume":"10","author":"Urquiza","year":"2018","journal-title":"Sci. Transl. Med."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1007\/s40265-016-0607-y","article-title":"Migalastat: First Global Approval","volume":"76","author":"Markham","year":"2016","journal-title":"Drugs"},{"key":"ref_35","unstructured":"(2018). Pharmacoeconomic Review Report: Migalastat (Galafold): (Amicus Therapeutics): Indication: Fabry Disease [Internet], Canadian Agency for Drugs and Technologies in Healt."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1007\/s40265-019-01090-4","article-title":"Migalastat: A Review in Fabry Disease","volume":"79","author":"McCafferty","year":"2019","journal-title":"Drugs"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1038\/mt.2009.220","article-title":"The Pharmacological Chaperone 1-Deoxygalactonojirimycin Reduces Tissue Globotriaosylceramide Levels in a Mouse Model of Fabry Disease","volume":"18","author":"Khanna","year":"2010","journal-title":"Mol. Ther."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Liguori, L., Monticelli, M., Allocca, M., Mele, B.H., Lukas, J., Cubellis, M.V., and Andreotti, G. (2020). Pharmacological Chaperones: A Therapeutic Approach for Diseases Caused by Destabilizing Missense Mutations. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21020489"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2062","DOI":"10.1016\/S0021-9258(18)61618-7","article-title":"Synthesis and processing of alpha-galactosidase A in human fibroblasts. Evidence for different mutations in Fabry disease","volume":"262","author":"Lemansky","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1093\/glycob\/8.4.329","article-title":"Human -galactosidase A: Characterization of the N-linked oligosaccharides on the intracellular and secreted glycoforms overexpressed by Chinese hamster ovary cells","volume":"8","author":"Matsuura","year":"1998","journal-title":"Glycobiology"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/j.jmb.2004.01.035","article-title":"The Molecular Defect Leading to Fabry Disease: Structure of Human \u03b1-Galactosidase","volume":"337","author":"Garman","year":"2004","journal-title":"J. Mol. Biol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"448","DOI":"10.3389\/fphar.2017.00448","article-title":"Pharmaceutical Chaperones and Proteostasis Regulators in the Therapy of Lysosomal Storage Disorders: Current Perspective and Future Promises","volume":"8","author":"Mohamed","year":"2017","journal-title":"Front. Pharmacol."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Wang, F., and Segatori, L. (2013). Remodeling the Proteostasis Network to Rescue Glucocerebrosidase Variants by Inhibiting ER-Associated Degradation and Enhancing ER Folding. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0061418"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1042\/BCJ20190513","article-title":"Proteostasis regulators modulate proteasomal activity and gene expression to attenuate multiple phenotypes in Fabry disease","volume":"477","author":"Seemann","year":"2020","journal-title":"Biochem. J."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1038\/mt.2014.224","article-title":"Enzyme Enhancers for the Treatment of Fabry and Pompe Disease","volume":"23","author":"Lukas","year":"2015","journal-title":"Mol. Ther."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/j.bbrc.2007.06.048","article-title":"4-Phenylbutyrate rescues trafficking incompetent mutant \u03b1-galactosidase A without restoring its functionality","volume":"360","author":"Yam","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.phrs.2019.04.002","article-title":"Lipid-regulating properties of butyric acid and 4-phenylbutyric acid: Molecular mechanisms and therapeutic applications","volume":"144","author":"He","year":"2019","journal-title":"Pharmacol. Res."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"6015","DOI":"10.1016\/j.bmcl.2013.08.001","article-title":"4-Phenylbutyric acid protects against neuronal cell death by primarily acting as a chemical chaperone rather than histone deacetylase inhibitor","volume":"23","author":"Mimori","year":"2013","journal-title":"Bioorganic Med. Chem. Lett."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.omtm.2020.08.012","article-title":"In Vitro and In Vivo Amenability to Migalastat in Fabry Disease","volume":"19","author":"Lenders","year":"2020","journal-title":"Mol. Ther. - Methods Clin. Dev."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1002\/cpt.1832","article-title":"Treatment of Fabry\u2019s Disease With Migalastat: Outcome From a Prospective Observational Multicenter Study (FAMOUS)","volume":"108","author":"Lenders","year":"2020","journal-title":"Clin. Pharmacol. Ther."},{"key":"ref_51","first-page":"533","article-title":"Does Aspirin Acetylate Multiple Cellular Proteins?","volume":"2","author":"Alfonso","year":"2009","journal-title":"Mol. Med. Rep."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1089\/ars.2016.6978","article-title":"Aspirin-Mediated Acetylation Protects Against Multiple Neurodegenerative Pathologies by Impeding Protein Aggregation","volume":"27","author":"Ayyadevara","year":"2017","journal-title":"Antioxidants Redox Signal."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Morretta, E., D\u2019Agostino, A., Cassese, E., Maglione, B., Petrella, A., Schiraldi, C., and Monti, M.C. (2022). Label-Free Quantitative Proteomics to Explore the Action Mechanism of the Pharmaceutical-Grade Triticum vulgare Extract in Speeding Up Keratinocyte Healing. Molecules, 27.","DOI":"10.3390\/molecules27031108"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1074\/mcp.M200008-MCP200","article-title":"Discordant Protein and mRNA Expression in Lung Adenocarcinomas","volume":"1","author":"Chen","year":"2002","journal-title":"Mol. Cell. Proteom."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1186\/1471-2164-9-246","article-title":"Correlation of mRNA and protein levels: Cell type-specific gene expression of cluster designation antigens in the prostate","volume":"9","author":"True","year":"2008","journal-title":"BMC Genom."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1720","DOI":"10.1128\/MCB.19.3.1720","article-title":"Correlation between Protein and mRNA Abundance in Yeast","volume":"19","author":"Gygi","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1002\/anie.201005969","article-title":"Genome-wide Correlation between mRNA and Protein in a Single Cell","volume":"50","author":"Yeung","year":"2011","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Ghazalpour, A., Bennett, B., Petyuk, V.A., Orozco, L., Hagopian, R., Mungrue, I.N., Farber, C.R., Sinsheimer, J., Kang, H.M., and Furlotte, N. (2011). Comparative Analysis of Proteome and Transcriptome Variation in Mouse. PLoS Genet., 7.","DOI":"10.1371\/journal.pgen.1001393"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1002\/pro.3978","article-title":"TheBioGRIDdatabase: A comprehensive biomedical resource of curated protein, genetic, and chemical interactions","volume":"30","author":"Oughtred","year":"2020","journal-title":"Protein Sci."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"2463","DOI":"10.1096\/fj.01-0259com","article-title":"Aspirin and salicylate bind to immunoglobulin heavy chain binding protein (BiP) and inhibit its ATPase activity in human fibroblasts","volume":"15","author":"Deng","year":"2001","journal-title":"FASEB J."},{"key":"ref_61","first-page":"1","article-title":"Drug repositioning can accelerate discovery of pharmacological chaperones","volume":"10","author":"Mele","year":"2015","journal-title":"Orphanet J. Rare Dis."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"2307","DOI":"10.1002\/ajmg.a.38326","article-title":"Drug discovery and development for rare genetic disorders","volume":"173","author":"Sun","year":"2017","journal-title":"Am. J. Med Genet. Part A"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1093\/bib\/bbr021","article-title":"Drug repositioning for orphan diseases","volume":"12","author":"Sardana","year":"2011","journal-title":"Briefings Bioinform."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1097\/00042560-199510050-00008","article-title":"The Tolerability and Pharmacokinetics of N-Butyl-deoxynojirimycin in Patients with Advanced HIV Disease (ACTG 100)","volume":"10","author":"Tierney","year":"1995","journal-title":"J. Acquir. Immune Defic. Syndr. Hum. Retrovirol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1111\/j.1651-2227.2005.tb02107.x","article-title":"Vascular Complications of Fabry Disease: Enzyme Replacement and Other Therapies","volume":"94","author":"Hughes","year":"2005","journal-title":"Acta Paediatrics"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1016\/j.ymgme.2014.01.014","article-title":"Outcomes of patients treated through the Canadian Fabry disease initiative","volume":"111","author":"Sirrs","year":"2014","journal-title":"Mol. Genet. Metab."},{"key":"ref_67","unstructured":"Arif, H. (2021). Salicylic Acid (Aspirin). StatPearls [Internet], StatPearls Publishing."},{"key":"ref_68","unstructured":"(2022, February 28). Aspirin Dosage. Available online: https:\/\/www.drugs.com\/dosage\/aspirin.html."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"7568","DOI":"10.1074\/jbc.M704097200","article-title":"The Dystonia-associated Protein TorsinA Modulates Synaptic Vesicle Recycling","volume":"283","author":"Granata","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.devcel.2015.02.011","article-title":"BORC, a Multisubunit Complex that Regulates Lysosome Positioning","volume":"33","author":"Pu","year":"2015","journal-title":"Dev. Cell"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"32736","DOI":"10.1074\/jbc.M505558200","article-title":"Genetic Analysis of the Subunit Organization and Function of the Conserved Oligomeric Golgi (COG) Complex","volume":"280","author":"Oka","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1975","DOI":"10.1681\/ASN.2008111190","article-title":"Decreased Nitric Oxide Bioavailability in a Mouse Model of Fabry Disease","volume":"20","author":"Shu","year":"2009","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"546","DOI":"10.2174\/157340607782360399","article-title":"A Salicylic Acid-Based Analogue Discovered from Virtual Screening as a Potent Inhibitor of Human 20\u03b1-Hydroxysteroid Dehydrogenase","volume":"3","author":"Dhagat","year":"2007","journal-title":"Med. Chem."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1007\/s12192-016-0676-6","article-title":"The human HSP70 family of chaperones: Where do we stand?","volume":"21","author":"Radons","year":"2016","journal-title":"Cell Stress Chaperones"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1402","DOI":"10.1074\/jbc.M113.521997","article-title":"Binding of Human Nucleotide Exchange Factors to Heat Shock Protein 70 (Hsp70) Generates Functionally Distinct Complexes in Vitro","volume":"289","author":"Rauch","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"112417","DOI":"10.1016\/j.yexcr.2020.112417","article-title":"Revealing functional insights into ER proteostasis through proteomics and interactomics","volume":"399","author":"Wright","year":"2020","journal-title":"Exp. Cell Res."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"355ra118","DOI":"10.1126\/scitranslmed.aad9823","article-title":"Heat shock protein\u2013based therapy as a potential candidate for treating the sphingolipidoses","volume":"8","author":"Kirkegaard","year":"2016","journal-title":"Sci. Transl. Med."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/j.ebiom.2018.11.037","article-title":"The heat shock protein amplifier arimoclomol improves refolding, maturation and lysosomal activity of glucocerebrosidase","volume":"38","author":"Fog","year":"2018","journal-title":"EBioMedicine"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1038\/nbt1018-913","article-title":"FDA approves Galafold, a triumph for Amicus","volume":"36","author":"Moran","year":"2018","journal-title":"Nat. Biotechnol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1987","DOI":"10.1038\/s41436-019-0451-z","article-title":"Efficacy of the pharmacologic chaperone migalastat in a subset of male patients with the classic phenotype of Fabry disease and migalastat-amenable variants: Data from the phase 3 randomized, multicenter, double-blind clinical trial and extension study","volume":"21","author":"Germain","year":"2019","journal-title":"Genet. Med."},{"key":"ref_81","first-page":"1224","article-title":"Oral Chaperone Therapy Migalastat for Treating Fabry Disease: Enzymatic Response and Serum Biomarker Changes After 1 Year","volume":"105","author":"Gensler","year":"2018","journal-title":"Clin. Pharmacol. Ther."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1136\/jmedgenet-2017-104826","article-title":"Reduction of podocyte globotriaosylceramide content in adult male patients with Fabry disease with amenableGLAmutations following 6 months of migalastat treatment","volume":"54","author":"Mauer","year":"2017","journal-title":"J. Med Genet."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1002\/cpt.1536","article-title":"Oral Chaperone Therapy Migalastat for the Treatment of Fabry Disease: Potentials and Pitfalls of Real-World Data","volume":"106","author":"Svarstad","year":"2019","journal-title":"Clin. Pharmacol. Ther."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"2368","DOI":"10.1089\/scd.2012.0498","article-title":"MePR: A Novel Human Mesenchymal Progenitor Model with Characteristics of Pluripotency","volume":"22","author":"Miceli","year":"2013","journal-title":"Stem Cells Dev."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1006\/meth.2001.1262","article-title":"Analysis of relative gene expression data using real-time quantitative PCR and the 2\u2212\u0394\u0394CT Method","volume":"25","author":"Livak","year":"2001","journal-title":"Methods"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1093\/oxfordjournals.jbchem.a123749","article-title":"Specific Storage of Subunit c of Mitochondrial ATP Synthase in Lysosomes of Neuronal Ceroid Lipofuscinosis (Batten\u2019s Disease)","volume":"111","author":"Kominami","year":"1992","journal-title":"J. Biochem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1038\/nprot.2009.121","article-title":"Measurement of cytochrome P450 and NADPH\u2013cytochrome P450 reductase","volume":"4","author":"Guengerich","year":"2009","journal-title":"Nat. Protoc."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1139\/y59-099","article-title":"A rapid method of total lipid extraction and purification","volume":"37","author":"Bligh","year":"1959","journal-title":"Can. J. Biochem. Physiol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"2180","DOI":"10.1038\/s41467-021-22369-9","article-title":"The landscape of molecular chaperones across human tissues reveals a layered architecture of core and variable chaperones","volume":"12","author":"Shemesh","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2013\/637629","article-title":"Genetics of Proteasome Diseases","volume":"2013","author":"Gomes","year":"2013","journal-title":"Scientifica"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/23\/9\/5105\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T23:05:57Z","timestamp":1760137557000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/23\/9\/5105"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,5,4]]},"references-count":91,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2022,5]]}},"alternative-id":["ijms23095105"],"URL":"https:\/\/doi.org\/10.3390\/ijms23095105","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,5,4]]}}}