BSc3094 is used in tau protein amyloidogenicity/tauopathy research to study the processes of tau aggregation and cross-linking in neurodegenerative disease development.
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BSc3094 is a potent inhibitor of tau aggregation and dissolves preformed tau paired helical filaments. BSc3094 interacts closely with the tau protein at the edge involving protons I-IV, while the second attachment site seems to be at the nitro group. In N2A cells (model system for tau aggregation), BSc3094 exhibited low toxicity.
Current Alzheimer research, 4(4), 397-402 (2007-10-03)
Cell models of tauopathy were generated in order to study mechanisms of neurodegeneration involving abnormal changes of tau. They are based on neuroblastoma cell lines (N2a) that inducibly express different forms of the repeat domain of tau (tau(RD)), e.g. the
Biochemical Society transactions, 38(4), 967-972 (2010-07-28)
Tau pathology is characterized by intracellular aggregates of abnormally and hyperphosphorylated tau proteins. It is encountered in many neurodegenerative disorders, but also in aging. These neurodegenerative disorders are referred to as tauopathies. Comparative biochemistry of the tau aggregates shows that
Human molecular genetics, 21(16), 3587-3603 (2012-05-23)
Increased Tau protein amyloidogenicity has been causatively implicated in several neurodegenerative diseases, collectively called tauopathies. In pathological conditions, Tau becomes hyperphosphorylated and forms intracellular aggregates. The deletion of K280, which is a mutation that commonly appears in patients with frontotemporal
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