Search for Exclusive Z-Boson Production and Observation of High-Mass pp̅ →pγγp̅ →pl+l-p̅ Events in pp̅ Collisions at √s=1.96 TeV

We present a search for exclusive Z boson production in proton-antiproton collisions at sqrt(s) = 1.96 TeV, using the CDF II detector at Fermilab. We observe no exclusive Z->ll candidates and place the first upper limit on the exclusive Z cross section in hadron collisions, sigma(exclu) gammagamma->p+ll+pbar, and measure the cross section for M(ll) > 40 GeV/c2 and |eta(l)|

Study of multi-muon events produced in p\bar{p} interactions at \sqrt{s}=1.96 TeV

We report the results of a study of multi-muon events produced at the Fermilab Tevatron collider and acquired with the CDF II detector using a dedicated dimuon trigger. The production cross section and kinematics of events in which both muon candidates are produced inside the beam pipe of radius 1.5 cm are successfully modeled by known processes which include heavy flavor production. In contrast, we are presently unable to fully account for the number and properties of the remaining events, in which at least one muon candidate is produced outside of the beam pipe, in terms of the same understanding of the CDF II detector, trigger, and event reconstruction.

Search for High-Mass e+e- Resonances in pp̅ Collisions at √s=1.96 TeV

A search for high-mass resonances in the $e^+e^-$ final state is presented based on 2.5 fb$^{-1}$ of $\sqrt{s}=$1.96 TeV $p\bar{p}$ collision data from the CDF II detector at the Fermilab Tevatron. The largest excess over the standard model prediction is at an $e^+e^-$ invariant mass of 240 GeV/$c^2$. The probability of observing such an excess arising from fluctuations in the standard model anywhere in the mass range of 150--1,000 GeV/$c^2$ is 0.6% (equivalent to 2.5 $\sigma$). We exclude the standard model coupling $Z'$ and the Randall-Sundrum graviton for $k/\overline{M}_{Pl}=0.1$ with masses below 963 and 848 GeV/$c^2$ at the 95% credibility level, respectively.

Generation of Flat and Curved Membranes by Inverse-BAR Domain Proteins

Biological membranes are tightly linked to the evolution of life, because they provide a way to concentrate molecules into partially closed compartments. The dynamic shaping of cellular membranes is essential for many physiological processes, including cell morphogenesis, motility, cytokinesis, endocytosis, and secretion. It is therefore essential to understand the structure of the membrane and recognize the players that directly sculpt the membrane and enable it to adopt different shapes. The actin cytoskeleton provides the force to push eukaryotic plasma membrane in order to form different protrusions or/and invaginations. It has now became evident that actin directly co-operates with many membrane sculptors, including BAR domain proteins, in these important events. However, the molecular mechanisms behind BAR domain function and the differences between the members of this large protein family remain largely unresolved. In this thesis, the structure and functions of the I-BAR domain family members IRSp53 and MIM were thoroughly analyzed. By using several methods such as electron microscopy and systematic mutagenesis, we showed that these I-BAR domain proteins bind to PI(4,5)P2-rich membranes, generate negative membrane curvature and are involved in the formation of plasma membrane protrusions in cells e.g. filopodia. Importantly, we characterized a novel member of the BAR-domain superfamily which we named Pinkbar. We revealed that Pinkbar is specifically expressed in kidney and epithelial cells, and it localizes to Rab13-positive vesicles in intestinal epithelial cells. Remarkably, we learned that the I-BAR domain of Pinkbar does not generate membrane curvature but instead stabilizes planar membranes. Based on structural, mutagenesis and biochemical work we present a model for the mechanism of the novel membrane deforming activity of Pinkbar. Collectively, this work describes the mechanism by which I-BAR domain proteins deform membranes and provides new information about the biological roles of these proteins. Intriguingly, this work also gives evidence that significant functional plasticity exists within the I-BAR domain family. I-BAR proteins can either generate negative membrane curvature or stabilize planar membrane sheets, depending on the specific structural properties of their I-BAR domains. The results presented in this thesis expand our knowledge on membrane sculpting mechanisms and shows for the first time how flat membranes can be generated in cells.