9 results match your criteria: "Institute of Chemical and Physical Research (RIKEN)[Affiliation]"
J Chem Phys
June 2005
Surface Chemistry Laboratory, Institute of Chemical and Physical Research (RIKEN), Wako, Saitama, Japan.
The angular intensity distributions of CO and N(2) molecules scattered from a LiF(001) surface have been measured as functions of surface temperature, incident translational energy, and incident azimuthal direction affecting surface corrugation at a high resolution. Although both molecules have the same molecular mass and linear structure, only the CO molecule shows a rainbow feature in its scattering pattern, while the N(2) molecule shows a single peak distribution. From the comparisons of the obtained results with the calculated predictions based on the newly developed classical theory of the ellipsoid-washboard model, the differences in scattering distribution are attributed to the effects of molecular anisotropy and center-of-mass position.
View Article and Find Full Text PDFGenome Inform Ser Workshop Genome Inform
December 2001
SNP Research Center, Institute of Chemical and Physical Research (RIKEN), Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato, Tokyo 108-8639, Japan.
The most challenging strategy for analyzing genome-wide polymorphisms and/or expression profiles is to solve multi-factor causal-relationship simultaneously. As the first step, we propose a framework of association study using maximum likelihood method that simultaneously handles genetic polymorphisms and epi-genetic information, e.g.
View Article and Find Full Text PDFBiochem Mol Biol Int
May 1998
Laboratory for Cellular Glycobiology, The Institute of Chemical and Physical Research (RIKEN), Saitama, Japan.
Ceramide glucosyltransferase (EC 2.4.1.
View Article and Find Full Text PDFCytogenet Cell Genet
June 1998
Laboratory for Cellular Glycobiology, Frontier Research Program, The Institute of Chemical and Physical Research (RIKEN), Saitama, Japan.
Biochem Biophys Res Commun
October 1995
Laboratory for Cell Glycobiology, Institute of Chemical and Physical Research (RIKEN), Saitama, Japan.
In many tumor cell lines, tumor necrosis factor alpha (TNF alpha) causes profound alterations in nucleus including chromatin condensation and DNA fragmentation. However the mechanism is largely unknown. Here we demonstrate that TNF alpha treatment of U937 cells increased tyrosine phosphorylation of a 23-kDa nuclear protein (P23) maximally by 13-fold, which occurred after 2.
View Article and Find Full Text PDFBiochem Biophys Res Commun
July 1995
Laboratory for Glyco Cell Biology, Institute of Chemical and Physical Research (Riken), Saitama, Japan.
In many tumor cell lines, tumor necrosis factor alpha (TNF alpha) causes apoptosis with characteristic internucleosomal DNA fragmentation. However, the mechanism is largely unknown. Here we examined the involvement of protein tyrosine kinases by using their inhibitors.
View Article and Find Full Text PDFFEBS Lett
January 1995
Laboratory for Glyco Cell Biology, Institute of Chemical and Physical Research (RIKEN), Saitama, Japan.
We have found that a solvent mixture of ethanol and dodecane was able to disperse natural ceramide (Cer) into aqueous solution. In U937 cells, addition of natural Cer to medium caused a characteristic pattern of DNA fragmentation, which is indistinguishable from that caused by TNF alpha. The effective concentration of Cer is as low as 25 nM.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
March 1994
Laboratory for Glyco Cell Biology, Institute of Chemical and Physical Research (RIKEN), Saitama, Japan.
Mouse B16 melanoma cell line, GM-95 (formerly designated as MEC-4), deficient in sialyllactosylceramide was examined for its primary defect. Glycolipids from the mutant cells were analyzed by high-performance TLC. No glycolipid was detected in GM-95 cells, even when total lipid from 10(7) cells was analyzed.
View Article and Find Full Text PDFVision Res
December 1993
Laboratory for Photobiology, Institute of Chemical and Physical Research (RIKEN), Sendai, Japan.
Light-induced protein interaction as part of the process of visual transduction in arthropods with rhabdomeric photoreceptors was investigated biochemically by using crayfish retina. Two kinds of retinal buffer soluble proteins (one of 40 kDa and the other of 46 kDa) were found to bind to the irradiated rhabdomeric membranes both in vitro and in vivo. The proteins bound to the membranes in the presence of metarhodopsin.
View Article and Find Full Text PDF