6747128
Prospects for the measurement of the structure of the coupling of a Higgs boson to weak gauge bosons in weak boson fusion with the ATLAS detector
The prospects for the measurement of the tensor structure of the vertex between a standard model Higgs boson and two weak gauge bosons using the distribution of the azimuthal angles between the two tagging jets in the weak boson fusion channel are studied in a Monte Carlo analysis using the fast simulation of the ATLAS detector. The decay channels H→τ+τ-→ll+4ν, H→τ+τ-→lh+3ν at mH=120 GeV and H→W+W-→llνν at mH=160 GeV are used in the analysis. For a standard model Higgs boson it is found that purely anomalous couplings are expected to be excluded at a confidence level corresponding to 2σ or more at mH=120 GeV and more than 5σ at mH=160 GeV from 30 fb-1 of data. With a value of 1 roughly reproducing the standard model cross section for a purely anomalous coupling, the standard deviation in a measurement of a contribution of a CP even anomalous coupling in addition to the standard model coupling is estimated to be 0.20 at mH=120 GeV and 0.09 at mH=160 GeV.
119439280
Higgs Physics at a Future e+e- Linear Collider
This letter reviews the potential of a high luminosity e+e- linear collider (LC) in the precision study of the Higgs boson profile. The complementarity with the Large Hadron Collider (LHC) Higgs physics program is briefly discussed.
117815253
Higgs Boson Searches with ATLAS based on 2010 Data
The results of Higgs Boson searches with the ATLAS detector based on 2010 proton proton collision data corresponding to integrated luminosities of up to 39 pb-1are presented. Searches for H --> 2 photons, H --> W+W- --> l+l- 2 neutrinos and H --> ZZ --> l+l- 2 neutrinos / l+l- qqbar in the context of the Standard Model (SM), for H--> tau+ tau- in the context of the Minimal Supersymmetric Extension of the Standard Model (MSSM) and for a generic scalar at low mass in the vicinity of the Ypsilon resonance decaying to a pair of muons are discussed. All observations are in agreement with the expectations from the background-only hypothesis. Hence exclusion limits at 95% confidence level are derived
2506186
Model-independent determination of the top Yukawa coupling from LHC and ILC
We show how a measurement of the process pp→tt̄H0+X at the Large Hadron Collider (LHC) and a measurement of the Higgs boson branching ratios BR(H0→bb̄) and BR(H0→W+W-) at a future linear electron positron collider (ILC) can be combined to extract a value of the top quark Yukawa coupling in a model-independent way. We find that for masses with 120 GeV/c2<mH<200 GeV/c2 a measurement precision of 15% including systematic uncertainties can be achieved for integrated luminosities of 300 fb-1 at the LHC and 500 fb-1 at the ILC at a centre-of-mass energy of 350 GeV. 
139488231
LC TPC R & D: A proposal to the DESY PRC
117936692
TPC with GEM readout for TESLA
A Time Projection Chamber (TPC) is proposed as the main tracking device for the detector at the future e+e− linear accelerator now studied in Europe. The performance requirements and the basic design using a Gas Electron Multiplier (GEM) as the readout device are described. Some preliminary R&D results are discussed.
29559148
Structural basis for the recognition of a bisphosphorylated MAP kinase peptide by human VHR protein Phosphatase.
Human VHR (vaccinia H1 related phosphatase) is a member of the dual-specificity phosphatases (DSPs) that often act on bisphosphorylated protein substrates. Unlike most DSPs, VHR displays a strong preference for dephosphorylating phosphotyrosine residues over phosphothreonine residues. Here we describe the 2.75 A crystal structure of the C124S inactive VHR mutant in complex with a bisphosphorylated peptide corresponding to the MAP kinase activation lip. This structure and subsequent biochemical studies revealed the basis for the strong preference for hydrolyzing phosphotyrosine within bisphosphorylated substrates containing -pTXpY-. In the structure, the two phospho residues are oriented into distinct pockets; the phosphotyrosine is bound in the exposed yet deep active site cleft while the phosphothreonine is loosely tethered into a nearby basic pocket containing Arg(158). As this structure is the first substrate-enzyme complex reported for the DSP family of enzymes, these results provide the first glimpse into how DSPs bind their protein substrates.
22785877
Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein.
In prokaryotes, Hfq regulates translation by modulating the structure of numerous RNA molecules by binding preferentially to A/U-rich sequences. To elucidate the mechanisms of target recognition and translation regulation by Hfq, we determined the crystal structures of the Staphylococcus aureus Hfq and an Hfq-RNA complex to 1.55 and 2.71 A resolution, respectively. The structures reveal that Hfq possesses the Sm-fold previously observed only in eukaryotes and archaea. However, unlike these heptameric Sm proteins, Hfq forms a homo-hexameric ring. The Hfq-RNA structure reveals that the single-stranded hepta-oligoribonucleotide binds in a circular conformation around a central basic cleft, whereby Tyr42 residues from adjacent subunits stack with six of the bases, and Gln8, outside the Sm motif, provides key protein-base contacts. Such binding suggests a mechanism for Hfq function.
17287147
Structural Basis of Core Promoter Recognition in a Primitive Eukaryote
Transcription start site selection in eukaryotes is mediated through combinations of the TATA, initiator (Inr), and downstream promoter elements (DPE). In Trichomonas vaginalis, a parabasalian flagellate thought to represent an ancient eukaryote lineage, the Inr appears to be solely responsible for start site selection and is recognized by the initiator binding protein 39 kDa (IBP39). IBP39 contains an N-terminal Inr binding domain (IBD) connected via a flexible linker to a C-terminal domain (C domain). Here we present crystal structures of the apoIBD and IBD-Inr complexes and the C domain. The IBD structures reveal a winged-helix motif with prokaryotic and eukaryotic features and a scaffold similar to that of ETS-family proteins. The C domain structure and biochemical studies indicate that it interacts with the T. vaginalis RNAP II large subunit C-terminal domain. These data suggest that binding of IBP39 to the Inr directly recruits RNAP II and in this way initiates transcription.