IP-LC-MSMS Enables Identification of Three Tau O-GlcNAcylation Sites as O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau
Bijttebier S, Rodrigues Martins D, Mertens L, Grauwen K, Bruinzeel W, Willems R, Bartolomé-Nebreda JM, Theunis C, Bretteville A, Ebneth A, Dillen L.
DOI: 10.1021/acs.jproteome.2c00822
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O-GlcNAc modification forces the formation of an α-Synuclein amyloid-strain with notably diminished seeding activity and pathology
Balana AT , Mahul-Mellier AL, Nguyen BA , Horvath M, Javed A, Hard E R, Jasiqi Y, Singh P, Afrin S, Pedretti R, Singh V, Lee V MY , Luk KC, Saelices , Lashuel HA , Pratt MR
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O-GlcNAcase Inhibitor ASN90 is a Multimodal Drug Candidate for Tau and α-Synuclein Proteinopathies
Permanne B, Sand A, Ousson S, Nény M, Hantson J, Schubert R, Wiessner C, Quattropani A, Beher*
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Current directions in tau research: Highlights from Tau 2020
Sexton C, Snyder H, Beher D, Boxer A, Brannelly P, Brion JP, Buée L, Cacace A, Chételat G, Citron M, DeVos S, Diaz K, Feldman H, Frost B, Goate A, Gold M, Hyman B, Johnson K, Karch C, Kerwin D, Koroshetz W, Litvan I, Morris H, Mummery C, Mutamba J, Patterson M, Quiroz Y, Rabinovici G, Rommel A, Shulman M, Toledo-Sherman L, Weninger S, Wildsmith K, Worley S, Carrillo M.
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O-GlcNAcylation regulates dopamine neuron function, survival and degeneration in Parkinson disease.
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Inhibition of O-GlcNAcase leads to elevation of O-GlcNAc tau and reduction of tauopathy and cerebrospinal fluid tau in rTg4510 mice.
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Increased O-GlcNAcylation reduces pathological tau without affecting its normal phosphorylation in a mouse model of tauopathy.
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Generation and characterization of a rabbit monoclonal antibody site-specific for tau O-GlcNAcylated at serine 400.
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Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation.
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