Quaid-i-Azam University

About: Quaid-i-Azam University is a education organization based out in Islamabad, Pakistan. It is known for research contribution in the topics: Heat transfer & Nanofluid. The organization has 6577 authors who have published 16865 publications receiving 381678 citations. The organization is also known as: Islamabad University.

Inclusive search for a vector-like T quark with charge 2/3 in pp collisions at √s=8 TeV

Abstract: A search is performed for a massive new vector-like quark T, with charge (2/3), that is pair produced together with its antiparticle in proton–proton collisions. The data were collected by the CMS experiment at the Large Hadron Collider in 2012 at √s = 8 TeV and correspond to an integrated luminosity of 19.5 fb^(−1). The T quark is assumed to decay into three different final states, bW, tZ, and tH. The search is carried out using events with at least one isolated lepton. No deviations from standard model expectations are observed, and lower limits are set on the T quark mass at 95% confidence level. The lower limit lies between 687 and 782 GeV for all possible values of the branching fractions into the three different final states assuming strong production. These limits are the most stringent constraints to date on the existence of such a quark.

Mutations in Orthologous Genes in Human Spondyloepimetaphyseal Dysplasia and the Brachymorphic Mouse

Abstract: The osteochondrodysplasias are a genetically heterogeneous group of disorders affecting skeletal development, linear growth and the maintenance of cartilage and bone. We have studied a large inbred Pakistani family with a distinct form of recessively inherited spondyloepimetaphyseal dysplasia (SEMD) and mapped a gene associated with this dwarfing condition to chromosome 10q23–24, a region syntenic with the locus for the brachymorphic mutation on mouse chromosome 19. We identified two orthologous genes, ATPSK2 and Atpsk2, encoding novel ATP sulfurylase/APS kinase orthologues in the respective regions of the human and mouse genomes. We characterized a nonsense mutation in ATPSK2 in the SEMD family and a missense mutation in the region of Atpsk2 encoding the APS kinase activity in the brachymorphic mouse. ATP sulfurylase/APS kinase catalyses the metabolic activation of inorganic sulfate to PAPS, the universal donor for post-translational protein sulfation in all cell types. The cartilage-specificity of the human and mouse phenotypes provides further evidence of the critical role of sulfate activation in the maturation of cartilage extracellular matrix molecules and the effect of defects in this process on the architecture of cartilage and skeletogenesis.