Commissioning Of The Kekb Rf System

KEKB has been operated since December, 1998, to deliver B B ̄ pairs for a physics detector. In this paper,we describe the commissioning procedure of KEKB

First measurement of the real part of a pp double-spin-flip amplitude

The asymmetry ANN for pp elastic scattering has been measured at 800 and 650 MeV in the region of Coulomb-nuclear interference. The data have been analyzed to extract the real part of a spin-spin scattering amplitude. Results are compared with the predictions of forward dispersion relations. They disagree significantly at 650 MeV

Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells

Huntington's disease is a progressive neurodegenerative disorder caused by a polyglutamine repeat expansion in the first exon of the huntingtin (Htt) protein. N-terminal Htt peptides with polyglutamine tracts in the pathological range (51–122 glutamines) form high-molecular-weight protein aggregates with fibrillar morphology in vitro, and they form discrete inclusion bodies in a cell-culture model. However, in some studies, formation of discrete Htt inclusions does not correlate well with cell death. We coexpressed N-terminal Htt fragments containing 91 glutamines fused to different affinity tags in HEK293 cells, and we isolated small aggregates by double sequential-affinity chromatography to assure the isolation of multimeric molecules. Transmission electron microscopy and atomic force microscopy revealed the isolated aggregates as globules or clusters of globules 4–50 nm in diameter without any detectable fibrillar species. Because small nonfibrillar oligomers, not mature fibrils, recently have been suggested to be the principal cytotoxic species in neurodegenerative disease, these Htt globular aggregates formed in cells may represent the pathogenic form of mutant Htt