University of Oviedo

About: University of Oviedo is a education organization based out in Oviedo, Spain. It is known for research contribution in the topics: Population & Large Hadron Collider. The organization has 13423 authors who have published 31649 publications receiving 844799 citations. The organization is also known as: Universidá d'Uviéu & Universidad de Oviedo.

Search for top-squark pair production in the single-lepton final state in pp collisions at √s=8 TeV

Abstract: This paper presents a search for the pair production of top squarks in events with a single isolated electron or muon, jets, large missing transverse momentum, and large transverse mass. The data sample corresponds to an integrated luminosity of 19.5 inverse femtobarns of pp collisions collected in 2012 by the CMS experiment at the LHC at a center-of-mass energy of sqrt(s) = 8 TeV. No significant excess in data is observed above the expectation from standard model processes. The results are interpreted in the context of supersymmetric models with pair production of top squarks that decay either to a top quark and a neutralino or to a bottom quark and a chargino. For small mass values of the lightest supersymmetric particle, top-squark mass values up to around 650 GeV are excluded.

The Determinants of Individuals' Attitudes Towards Preventing Environmental Damage

Abstract: This paper investigates empirically the determinants of individuals' attitudes towards preventing environmental damage in Spain using data from the World Values Survey and European Values Survey for the periods 1990, 1995 and 1999/2000 Compared to many previous studies, we present a richer set of independent variables and found that strongly neglected variables such as political interest and social capital have a strong impact on individuals' preferences to prevent environmental damage An interesting aspect in our study is the ability to investigate environmental preferences over time The results show strong differences over time Finally, using disaggregated data for Spanish regions, we also find significant regional differences

Collagenase 3 is a target of Cbfa1, a transcription factor of the runt gene family involved in bone formation.

Abstract: The human matrix metalloproteinases (MMPs) or matrixins are a family of structurally related neutral proteinases that are collectively capable of degrading essentially all extracellular matrix components (9). These enzymes play a major role in normal tissue-remodeling processes such as embryonic development, ovulation, and wound healing (44, 81). In addition, abnormal expression of these proteases may contribute to a variety of pathological conditions characterized by matrix destruction, including rheumatoid arthritis (52), atherosclerosis (25), and cancer invasion and metastasis (43, 72). Recently, and based on the hypothesis that samples of human tumor specimens could be an appropriate material to identify novel proteinases potentially involved in the spread of cancer, we have cloned from a breast carcinoma cDNA library a new member of the MMP family of enzymes that has been called collagenase 3 (MMP-13) (21, 55). Biochemical characterization of this enzyme has revealed that it degrades very efficiently the native helix of fibrillar collagens, with preferential activity on type II collagen. In addition, collagenase 3 may also act as a potent gelatinase, thus contributing to further degrade the initial cleavage products of collagenolysis to small fragments suitable for subsequent metabolism (33). Furthermore, recent studies have shown that collagenase 3 is also able to degrade the large cartilage proteoglycan aggrecan and other components of the extracellular matrix and basement membranes, including type IV collagen (19, 33, 35). Analysis of the expression of collagenase 3 in human tissues has revealed that in addition to its presence in diverse malignant tumors including breast carcinomas (21, 26), chondrosarcomas (77), basal cell carcinomas of the skin (1), and head and neck carcinomas (13, 29), this enzyme is produced during fetal ossification (30, 70) and in destructive joint diseases such as osteoarthritis and rheumatoid arthritis (41, 49, 59). Recent studies have provided information on the mechanisms controlling human collagenase 3 expression in pathological conditions. Thus, we have reported that this gene is predominantly expressed in fibroblasts adjacent to invasive breast cancer cells, in response to diffusible factors released from the epithelial tumor cells (76). A search of molecular factors with ability to induce collagenase 3 expression in human fibroblasts has shown that interleukin-1 (IL-1), tetradecanoyl phorbol acetate (TPA), and transforming growth factor β (TGF-β) are able to up-regulate the expression of this gene (76, 78). Functional analysis of the collagenase 3 gene promoter region has revealed that the inductive effects of all of these factors on the expression of collagenase 3 are mediated in part by an AP-1 site present in the 5′-flanking region of this gene (56, 78). Similar studies using human chondrosarcoma cells have indicated that basic fibroblast growth factor (bFGF) may be a major in vivo modulator of collagenase 3 expression in these malignant tumors (77). Furthermore, different groups have reported that IL-1β and tumor necrosis factor alpha (TNF-α) may induce collagenase 3 expression in osteoarthritic cartilage (11, 59). However, in marked contrast to these data on human collagenase 3 expression in pathological conditions, very little information is available on the mechanisms mediating its expression in normal conditions and, more specifically, in the process of bone formation, in which high levels of collagenase 3 have been detected. Recent structural analysis of the 5′-flanking region of the human collagenase 3 gene (56) has shown that it contains a sequence motif located at positions −133 to −139 that exhibits striking similarity to a sequence motif called nuclear matrix protein 2 (NMP-2) binding site (8, 47) or osteoblast-specific element 2 (OSE2) (15, 17). This sequence, originally described as a structural element essential for the osteoblastic expression of osteocalcin, is recognized by a transcription factor of the runt domain gene family, called Cbfa1 or Osf2 (7, 15, 17, 69, 83), that plays a major role in the expression of different osteoblast-specific genes (6, 7, 17, 37, 53). In this work we have evaluated the possibility that Cbfa1 is involved in the expression of collagenase 3 during bone formation. It was recently reported that parathyroid hormone (PTH) regulates the rat collagenase 3 promoter in osteoblastic cells through the cooperative interaction of an AP-1 site and a runt domain binding sequence recognized by runt domain proteins including Cbfa1 (67). Here, we provide in vitro and in vivo evidence that collagenase 3 is a target of Cbfa1 in osteoblastic and chondrocytic cells. In addition, on the basis of these transcriptional regulation studies, together with the potent proteolytic activity of collagenase 3 on bone and cartilage collagens, we propose that this enzyme may play a key role during fetal ossification.

Performance of the CMS muon detector and muon reconstruction with proton-proton collisions at s=13 TeV

Abstract: The CMS muon detector system, muon reconstruction software, and high-level trigger underwent significant changes in 2013–2014 in preparation for running at higher LHC collision energy and instantaneous luminosity. The performance of the modified system is studied using proton-proton collision data at center-of-mass energy √s=13 TeV, collected at the LHC in 2015 and 2016. The measured performance parameters, including spatial resolution, efficiency, and timing, are found to meet all design specifications and are well reproduced by simulation. Despite the more challenging running conditions, the modified muon system is found to perform as well as, and in many aspects better than, previously. We dedicate this paper to the memory of Prof. Alberto Benvenuti, whose work was fundamental for the CMS muon detector.

Neanderthal medics? Evidence for food, cooking, and medicinal plants entrapped in dental calculus

Abstract: Neanderthals disappeared sometime between 30,000 and 24,000 years ago. Until recently, Neanderthals were understood to have been predominantly meat-eaters; however, a growing body of evidence suggests their diet also included plants. We present the results of a study, in which sequential thermal desorption-gas chromatography-mass spectrometry (TD-GC-MS) and pyrolysis-gas chromatography-mass spectrometry (Py-GC-MS) were combined with morphological analysis of plant microfossils, to identify material entrapped in dental calculus from five Neanderthal individuals from the north Spanish site of El Sidron. Our results provide the first molecular evidence for inhalation of wood-fire smoke and bitumen or oil shale and ingestion of a range of cooked plant foods. We also offer the first evidence for the use of medicinal plants by a Neanderthal individual. The varied use of plants that we have identified suggests that the Neanderthal occupants of El Sidron had a sophisticated knowledge of their natural surroundings which included the ability to select and use certain plants.