67,275 research outputs found
Personal Papers (MS 80-0002)
No full textLetter from James T. Baird to S. K. Cheng asking him to reserve a room for Harris and Ruth Kempner for when they are in Taipei
DNA fusion gene vaccination mobilizes effective anti-leukemic cytotoxic T lymphocytes from a tolerized repertoire
No full textThe majority of known human tumor-associated antigens derive from non-mutated self proteins. T cell tolerance, essential to prevent autoimmunity, must therefore be cautiously circumvented to generate cytotoxic T cell responses against these targets. Our strategy uses DNA fusion vaccines to activate high levels of peptide-specific CTL. Key foreign sequences from tetanus toxin activate tolerance-breaking CD4+ T cell help. Candidate MHC class Ibinding tumor peptide sequences are fused to the C terminus for optimal processing and presentation. To model performance against a leukemia-associated antigen in a tolerized setting, we constructed a fusion vaccine encoding an immunodominant CTL epitopederived from Friend murine leukemia virus gag protein (FMuLVgag) and vaccinated tolerant FMuLVgag-transgenic (gag-Tg) mice. Vaccination with the construct induced epitopespecificIFN-c-producing CD8+ T cells in normal and gag-Tg mice. The frequency and avidity of activated cells were reduced in gag-Tg mice, and no autoimmune injury resulted. However, these CD8+ T cells did exhibit gag-specific cytotoxicity in vitro and in vivo. Also, epitope-specific CTL killed FBL-3 leukemia cells expressing endogenous FMuLVgag antigen and protected against leukemia challenge in vivo. These results demonstrate a simple strategy to engage anti-microbial T cell help to activate epitope-specific polyclonal CD8+ T cell responses from a residual tolerized repertoire
Letter from Franklin K. Lane, Secretary of the Interior, to Representative Hayden
No full textLetter from Franklin K. Lane to Carl T. Hayden expressing his support for bill S.390 in establishing the Grand Canyon as a National Park
Measurement of the ratio of branching fractions B(B0→K∗0γ )/B(B0s→φγ ) and the directCP asymmetry inB 0→K∗0γ
Get PDFThe ratio of branching fractions of the radiative B decays B0→K⁎0γ and B0s→ϕγ has been measured using an integrated luminosity of 1.0 fb−1 of pp collision data collected by the LHCb experiment at a centre-of-mass energy of s√=7TeV. The value obtained is
B(B0→K⁎0γ)B(B0s→ϕγ)=1.23±0.06(stat.)±0.04(syst.)±0.10(fs/fd),
where the first uncertainty is statistical, the second is the experimental systematic uncertainty and the third is associated with the ratio of fragmentation fractions fs/fd. Using the world average value for B(B0→K⁎0γ), the branching fraction B(B0s→ϕγ) is measured to be (3.5±0.4)×10−5.
The direct CP asymmetry in B0→K⁎0γ decays has also been measured with the same data and found to be
ACP(B0→K⁎0γ)=(0.8±1.7(stat.)±0.9(syst.))%.
Both measurements are the most precise to date and are in agreement with the previous experimental results and theoretical expectations
Production of coloured glass-ceramics from incinerator ash using thermal plasma technology.
No full text
Binding and Membrane Damage Behaviors of Self-Aggregated Beta-Amyloid Oligomers on Lipid Raft Surfaces from Microsecond Molecular Dynamics Simulations
No full textOur hypothesis is that self-aggregated Beta-Amyloid Oligomers can bind to phase-separated lipid nanodomains and damage the membrane structures. The data were generated by microsecond molecular dynamics simulations of the binding events of beta-amyloid oligomers to phase-separated lipid rafts with or without glycolipid clusters, i.e., GM-raft or CO-raft. The lipid domain preference and binding energies of disordered amyloid aggregate to highly dynamic and heterogeneous lipid bilayers in structurally specific lipid nanodomains, e.g., glycolipid-clusters, cholesterol-enriched liquid-ordered (Lo) or cholesterol-depleted liquid-disordered (Ld), or mixed Lo/Ld (Lod) region, and annular lipid shells surrounding the membrane-bound protein, provide helpful insight into guiding future experiments to understand the regulation of lipid composition and structures on amyloid binding to cell membranes. The information is also helpful for the design of drug interventions and novel imaging markers targeting membrane-bound amyloidogenic oligomers. The results will guide the new design of single-molecule experiments aiming at understanding amyloidogenic proteins binding to complex but realistic lipid membranes, containing multiple lipid components and varying domain sizes and structures. The details of the procedures of modeling and simulations of beta-amyloid oligomers in lipid rafts have been described in a research article by Pham, T. and K.H. Cheng, Exploring the Binding Kinetics and Behaviors of Self-Aggregated Beta-Amyloid Oligomers to Phase-Separated Lipid Rafts with or without Ganglioside-Clusters. Biophysical Chemistry, 2022. (in press) . (https://www.sciencedirect.com/science/article/abs/pii/S0301462222001168?via%3Dihub)
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