The PAX Toolkit and its Applications at Tevatron and LHC

At the CHEP03 conference we launched the Physics Analysis eXpert (PAX), a C++ toolkit released for the use in advanced high energy physics (HEP) analyses. This toolkit allows to define a level of abstraction beyond detector reconstruction by providing a general, persistent container model for HEP events. Physics objects such as particles, vertices and collisions can easily be stored, accessed and manipulated. Bookkeeping of relations between these objects (like decay trees, vertex and collision separation, etc.) including deep copies is fully provided by the relation management. Event container and associated objects represent a uniform interface for algorithms and facilitate the parallel development and evaluation of different physics interpretations of individual events. So-called analysis factories, which actively identify and distinguish different physics processes and study systematic uncertainties, can easily be realized with the PAX toolkit. PAX is officially released to experiments at Tevatron and LHC. Being explored by a growing user community, it is applied in a number of complex physics analyses, two of which are presented here. We report the successful application in studies of t-tbar production at the Tevatron and Higgs searches in the channel t-tbar-Higgs at the LHC and give a short outlook on further developments

Testing the bipartite model of the sulfonylurea receptor binding site: binding of A-, B-, and A + B-site ligands

ABSTRACT ATP-sensitive K ϩ (K ATP ) channels are composed of pore-forming subunits (Kir6.x) and of regulatory subunits, the sulfonylurea receptors (SURx). Subtypes of K ATP channels are expressed in different organs. The sulfonylureas and glinides (insulinotropes) close the K ATP channel in pancreatic ␤-cells and stimulate insulin secretion. The insulinotrope binding site of the pancreatic channel (Kir6.2/SUR1) consists of two overlapping (sub)-sites, site A, located on SUR1 and containing Ser1237 (which in SUR2 is replaced by Tyr1206), and site B, formed by SUR1 and Kir6.2. Insulinotropes bind to the A-, B-, or A ϩ B-site(s) and are grouped accordingly. A-ligands are highly selective in closing the pancreatic channel, whereas B-ligands are nonselective and insensitive to the mutation S1237Y. We have examined the binding of insulinotropes representative of the three groups in [ 3 H]glibenclamide competition experiments to determine the contribution of Kir6.x to binding affinity, the effect of the mutation Y1206S in site A of SUR2, and the subtype selectivity of the compounds. The results show that the bipartite nature of the SUR1 binding site applies also to SUR2. Kir6.2 as part of the B-site may interact directly or allosterically with structural elements common to all insulinotropes, i.e., the negative charge and/or the adjacent phenyl ring. The B-site confers a moderate subtype selectivity on B-ligands. The affinity of B-ligands is altered by the mutation SUR2(Y1206S), suggesting that the mutation affects the binding chamber of SUR2 as a whole or subsite A, including the region where the subsites overlap. Sulfonylureas and glinides (termed here insulinotropes) are used in the therapy of type 2 diabetes. They act by closing the ATP-sensitive K ϩ (K ATP ) channel in pancreatic ␤-cells, thereby inducing depolarization, Ca 2ϩ entry, and insulin secretion With the advent of the long-chain sulfonylureas such as glibenclamide, structure-activity relationships suggested that the binding site of the pancreatic channel for sulfonylureas had two attachment points, the "A-site" for the sulfonylurea part and the "B-site" for the new carboxamido part The short sulfonylureas bind to the A-site. A single amino acid in SUR1, Ser1237, which corresponds to Tyr1206 in SUR2 (mouse numbering), affords to these compounds an up This study was supported by the Deutsche Forschungsgemeinschaft (Qu 100/3-2). Article, publication date, and citation information can be found a

Measurements of branching fraction ratios and CP-asymmetries in suppressed B^- -> D(-> K^+ pi^-)K^- and B^- -> D(-> K^+ pi^-)pi^- decays

We report the first reconstruction in hadron collisions of the suppressed decays B^- -> D(-> K^+ pi^-)K^- and B^- -> D(-> K^+ pi^-)pi^-, sensitive to the CKM phase gamma, using data from 7 fb^-1 of integrated luminosity collected by the CDF II detector at the Tevatron collider. We reconstruct a signal for the B^- -> D(-> K^+ pi^-)K^- suppressed mode with a significance of 3.2 standard deviations, and measure the ratios of the suppressed to favored branching fractions R(K) = [22.0 \pm 8.6(stat)\pm 2.6(syst)]\times 10^-3, R^+(K) = [42.6\pm 13.7(stat)\pm 2.8(syst)]\times 10^-3, R^-(K)= [3.8\pm 10.3(stat)\pm 2.7(syst]\times 10^-3, as well as the direct CP-violating asymmetry A(K) = -0.82\pm 0.44(stat)\pm 0.09(syst) of this mode. Corresponding quantities for B^- -> D(-> K^+ pi^-)pi^- decay are also reported.Comment: 8 pages, 1 figure, accepted by Phys.Rev.D Rapid Communications for Publicatio