Given a context passage, generate a question from the passage such that its answer is shortest continous span from the passage.

[Q]: Hermann Friedrich Kohlbrugge, or Kohlbrugge (August 15, 1803, Amsterdam - March 5, 1875, Elberfeld) was a Dutch (German father) minister.
[A]: Where did Hermann Friedrich Kohlbrugge live when he died?


[Q]: Ataxin-3 (AT3) is the protein that triggers the inherited neurodegenerative disorder spinocerebellar ataxia type 3 when its polyglutamine (polyQ) stretch close to the C-terminus exceeds a critical length. AT3 consists of the N-terminal globular Josephin domain (JD) and the C-terminal disordered one. It cleaves isopeptide bonds between ubiquitin monomers, an event involved in protein quality control mechanisms. AT3 has been implicated in the pathway that sorts aggregated protein to aggresomes via microtubules, in which dynein and histone deacetylase 6 (HDAC6) also seem to be involved. By taking advantage of small angle X-ray scattering (SAXS) and surface plasmon resonance (SPR), we have investigated the interaction of AT3 with tubulin and HDAC6. Based on SAXS results, the AT3 oligomer, consisting of 6-7 subunits, tightly binds to the tubulin hexameric oligomer in a "parallel" fashion. By SPR analysis we have demonstrated that AT3 binds to tubulin dimer with a 50nM affinity. Binding fits with a Langmuir 1:1 model and involves a single binding interface. Nevertheless, the interaction surface consists of three distinct, discontinuous tubulin-binding regions (TBR), one located in the JD, and the two others in the disordered domain, upstream and downstream of the polyQ stretch. In the absence of any of the three TBRs, the affinity is drastically reduced. By SPR we have also provided the first evidence of direct binding of AT3 to HDAC6, with affinity in the range 0.1-1M. These results shed light on the interactions among the components of the transport machinery that sorts aggregate protein to the aggresome, and pave the way to in vivo studies aimed at further clarifying their roles.
[A]: Which is the protein implicated in Spinocerebellar ataxia type 3?


[Q]: Chronic myeloid leukemia (CML) is arguably the best understood of all human malignancies. Its origins in the hematopoietic stem cell can be traced to a reciprocal translocation involving chromosomes 9 and 22, dubbed the Philadelphia chromosome, which is observed in essentially all patients. The resulting fusion gene, BCR/ABL, encodes an activated tyrosine kinase that can act alone to induce a CML-like syndrome in mouse models. These animal models have validated BCR/ABL as a target for the development of specific pharmaceutical inhibitors. The kinase inhibitor imatinib mesylate (Gleevec) is highly specific, effective, and minimally toxic, but may not effect cures as a single agent, particularly in patients with accelerated and blast-phase disease. Resistance to imatinib can confound therapy. Surprisingly, a high percentage of resistant cases manifest intact or augmented BCR/ABL signaling, suggesting that this oncoprotein, or signaling pathways emanating from it, remain viable targets. Combination chemotherapy is under active investigation, and among the most compelling strategies is dual treatment with agents that both target BCR/ABL signal transduction. BCR/ABL activates Ras, and compounds designed to antagonize Ras function called farnesyl transferase inhibitors (FTIs) have shown potent activity in vitro and in animal models of BCR/ABL-induced leukemia. Initial clinical trials in patients with refractory acute myeloid leukemia and CML in blast crisis have shown significant activity, suggesting that trials combining imatinib and FTIs are warranted.
[A]:
What tyrosine kinase, involved in a Philadelphia- chromosome positive chronic myelogenous leukemia, is the target of Imatinib (Gleevec)?