Search for TeV-scale gravity signatures in high-mass final states with leptons and jets with the ATLAS detector at sqrt [ s ] = 13TeV

A search for physics beyond the Standard Model, in final states with at least one high transverse momentum charged lepton (electron or muon) and two additional high transverse momentum leptons or jets, is performed using 3.2 fb−1 of proton–proton collision data recorded by the ATLAS detector at the Large Hadron Collider in 2015 at √s = 13 TeV. The upper end of the distribution of the scalar sum of the transverse momenta of leptons and jets is sensitive to the production of high-mass objects. No excess of events beyond Standard Model predictions is observed. Exclusion limits are set for models of microscopic black holes with two to six extra dimensions

Search for high-mass new phenomena in the dilepton final state using proton–proton collisions at View the MathML sources=13TeV with the ATLAS detector

A search is conducted for both resonant and non-resonant high-mass new phenomena in dielectron and dimuon final states. The search uses View the MathML source3.2fb−1 of proton–proton collision data, collected at View the MathML sources=13TeV by the ATLAS experiment at the LHC in 2015. The dilepton invariant mass is used as the discriminating variable. No significant deviation from the Standard Model prediction is observed; therefore limits are set on the signal model parameters of interest at 95% credibility level. Upper limits are set on the cross-section times branching ratio for resonances decaying to dileptons, and the limits are converted into lower limits on the resonance mass, ranging between 2.74 TeV and 3.36 TeV, depending on the model. Lower limits on the ℓℓqqℓℓqq contact interaction scale are set between 16.7 TeV and 25.2 TeV, also depending on the mode

Measurement of the top quark mass in the tt→ dilepton channel from √s = 8 TeV ATLAS data

The top quark mass is measured in the tt¯ → dilepton channel (lepton = e,μ) using ATLAS data recorded in the year 2012 at the LHC. The data were taken at a proton proton centre-of-mass energy of √s = 8 TeV and correspond to an integrated luminosity of about 20.2 fb−1. Exploiting the template method, and using the distribution of invariant masses of lepton–b-jet pairs, the top quark mass is measured to be mtop = 172.99±0.41 (stat) ±0.74 (syst) GeV, with a total uncertainty of 0.84 GeV. Finally, a combination with previous ATLAS mtop measurements from √s = 7 TeV data in the tt¯ → dilepton and tt¯ → lepton + jets channels results in mtop = 172.84±0.34 (stat)±0.61 (syst) GeV, with a total uncertainty of 0.70 GeV

Search for heavy long-lived charged R-hadrons with the ATLAS detector in 3.2 fb(-1) of proton-proton collision data at root s=13 TeV

A search for heavy long-lived charged R-hadrons is reported using a data sample corresponding to 3.2 fb−1 of proton–proton collisions at √s = 13 TeV collected by the ATLAS experiment at the Large Hadron Collider at CERN. The search is based on observables related to large ionisation losses and slow propagation velocities, which are signatures of heavy charged particles travelling significantly slower than the speed of light. No significant deviations from the expected background are observed. Upper limits at 95% confidence level are provided on the production cross section of long-lived R-hadrons in the mass range from 600 GeV to 2000 GeV and gluino, bottom and top squark masses are excluded up to 1580 GeV, 805 GeV and 890 GeV, respectively

The Thomsen-Friedenreich (TF) antigen: a critical review on the structural, biosynthetic and histochemica aspects of a pancarcinoma-associated antigen

Within the family of blood-group related carbohydrate antigens the Thomsen-Friedenreich (TF) antigen (or T antigen) is an outstanding member by attracting scientific interest for more than 65 years and by having retained its significance as object of current biomedical research; in particular, as a pancarcinoma-associated antigen. In accordance with its constant or even growing attraction scientists have searched for specific reagents which would allow the unambiguous and sensitive detection of the Thomsen-Friedenreich antigen on cells or tissues. While at the beginning, immunohistochemical work on TF antigen expression was restricted by the limited specificity of plant lectins (peanut lectin) a significant progress has been possible since the introduction of the hybridoma technique. The respective monoclonal antibodies display distinct fine specificities and cellular staining patterns in immunohistochemistry and have contributed to controversia1 discussions on the organ-characteristic and tumor-associated expression of the TF antigen in some organs. It is the aim of this survey to summarize in the context of its structural and biosynthetic aspects the current knowledge on the tissue expression of the TF antigen as based on the use of peanut agglutinin and monoclonal antibodies and to discuss the findings with regard to their biomedical relevance, in particular, with emphasis on their value in tumor diagnosis

Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo

Since there is no consensus sequence directing the initial GalNAc incorporation into mucin peptides, O-glycosylation sites are not reliably predictable. We have developed a mass spectrometric sequencing strategy that allows the identification of in vivo O-glycosylation sites on mucin-derived glycopeptides. Lactation-associated MUC1 was isolated from human milk and partially deglycosylated by trifluoromethanesulfonic acid to the level of core GalNAc residues. The product was fragmented by the Arg-C-specific endopeptidase clostripain to yield tandem repeat icosapeptides starting with the PAP motif. PAP20 glycopeptides were subjected to sequencing by post-source decay matrix-assisted laser desorption ionization mass spectrometry or by solid phase Edman degradation to localize the glycosylation sites. The masses of C- or N-terminal fragments registered for the mono- to pentasubstituted PAP20 indicated that GalNAc was linked to the peptide at Ser5,Thr6 (GSTA) and Thr14 (VTSA) but contrary to previous in vitro glycosylation studies also at Thr19 and Ser15 located within the PDTR or VTSA motifs, respectively. Quantitative data from solid phase Edman sequencing revealed no preferential glycosylation of the threonines. These discrepancies between in vivo and in vitro glycosylation patterns may be explained by assuming that O-glycosylation of adjacent peptide positions is a dynamically regulated process that depends on changes of the substrate qualities induced by glycosylation at vicinal sites