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    K-theory for group C*-algebras

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    These notes are based on a lecture course given by the first author in the Sedano Winter School on K-theory held in Sedano, Spain, on January 22-27th of 2007. They aim at introducing K-theory of C*-algebras, equivariant K-homology and KK-theory in the context of the Baum-Connes conjectur

    Yi-Fang Lin Piano Recital Program Notes

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    This report is Yi-Fang Lin Piano Recital Program Notes on April., 23, 2019. The two pieces on the program include Piano Sonata in C minor, K.457 by W.A. Mozart, and Piano Concerto No.1 in F-Sharp minor, Op.1 by S. Rachmaninoff. The note will introduce the life of two composers, the compositional background of individual work, and the analysis of the structure, including tonal design and thematic material in each work

    Search for eta(c) decays into pi pi and K(K)over-bar

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    Using 58 million J/psi) events taken with the BESII detector, a search for eta(c) CP violating decays into pi pi and K (K) over bar has been performed. No clear 77, signal is observed, and upper limits for B(eta(c) -> pi pi) and B(eta(c) -> K (K) over bar) are given at the 90% confidence level, B(J/psi -> gamma eta(c)) center dot B(eta(c) -> pi(+)pi(-)) < 1.1 x 10(-5), B(J/psi -> gamma eta(c)) center dot B(eta(c) -> pi(0)pi(0)) < 0.71 x 10(-5), B(J/psi -> gamma(eta c)) center dot B(eta(c) -> K+K-) < 0.96 x 10(-5), and B(J/psi -> gamma eta(c)) center dot B(eta(c) (KSKS0)-K-0) < 0.53 x 10(-5).Physics, Particles & FieldsSCI(E)1ARTICLE2337-3414

    Posttranslational modification of serine to formylglycine in bacterial sulfatases - Recognition of the modification motif by the iron-sulfur protein AtsB

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    Marquordt C, Fang QH, Will E, Peng JH, Figura von K, Dierks T. Posttranslational modification of serine to formylglycine in bacterial sulfatases - Recognition of the modification motif by the iron-sulfur protein AtsB. JOURNAL OF BIOLOGICAL CHEMISTRY. 2003;278(4):2212-2218.Calpha-formylglycine is the catalytic residue of sulfatases. Formylglycine is generated by posttranslational modification of a cysteine (pro- and eukaryotes) or serine (pro-karyotes) located in a conserved (C/S)XPXR motif. The modifying enzymes are unknown. AtsB, an iron-sulfur protein, is strictly required for modification of Se-72 in the periplasmic sulfatase AtsA of Klebsiella pneumoniae. Here we show W that AtsB is a cytosolic protein acting on newly synthesized serine-type sulfatases, (ii) that AtsB-mediated FGly formation is dependent on AtsA's signal peptide, and (iii) that the cytosolic cysteine-type sulfatase of Pseudomonas aeruginosa can be converted into a substrate of AtsB if the cysteine is substituted by serine and a signal peptide is added. Thus, formylglycine formation in serine-type sulfatases depends both on AtsB and on the presence of a signal peptide, and AtsB can act on sulfatases of other species. AtsB physically interacts with AtsA in a Ser(72)-dependent manner, as shown in yeast two-hybrid and GST pulldown experiments. This strongly suggests that AtsB is the serine-modifying enzyme and that AtsB relies on a cytosolic function of the sulfatase's signal peptide
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