Analyzing double degrees in Spain: A proposal

[EN] This article reviews the situation of single and double degrees in both public and private Spanish universities. To do so, this study analyzes information from the Registry of Universities, Centers, and Qualifications (RUCT) and Universia Spain. After analyzing the programs currently available to students, we present a proposal to establish a double degree in Administration and Business Management/Industrial Management Engineering. The proposal specifies the degree’s main objectives, specific nature, and fundamental aims and benefits in terms of technical, corporate, innovative, and entrepreneurial competencies.Roig-Tierno, N.; Mas Tur, A.; Ribeiro Navarrete, B. (2015). Analyzing double degrees in Spain: A proposal. En 1ST INTERNATIONAL CONFERENCE ON HIGHER EDUCATION ADVANCES (HEAD' 15). Editorial Universitat Politècnica de València. 334-339. https://doi.org/10.4995/HEAD15.2015.487OCS33433

A bibliometric overview of the Journal of Business Research

Abstract de la ponencia[EN] The Journal of Business Research is a leading international journal in business research dating back to 1973. This study analyzes all the publications in the journal since its creation by using a bibliometric approach. The objective is to provide a complete overview of the main factors that affect the journal. This analysis includes key issues such as the publication and citation structure of the journal, the most cited articles, and the leading authors, institutions, and countries in the journal. Unsurprisingly, the USA is the leading region in the journal although a considerable dispersion exists, especially during the last years when European and Asian universities are taking a more significant position.Merigó, J.; Mas-Tur, A.; Roig-Tierno, N.; Ribeiro-Soriano, D. (2016). A bibliometric overview of the Journal of Business Research. En CARMA 2016: 1st International Conference on Advanced Research Methods in Analytics. Editorial Universitat Politècnica de València. 148-148. https://doi.org/10.4995/CARMA2016.2015.423814814

A bibliometric overview of the Journal of Business Research

Abstract de la ponencia[EN] The Journal of Business Research is a leading international journal in business research dating back to 1973. This study analyzes all the publications in the journal since its creation by using a bibliometric approach. The objective is to provide a complete overview of the main factors that affect the journal. This analysis includes key issues such as the publication and citation structure of the journal, the most cited articles, and the leading authors, institutions, and countries in the journal. Unsurprisingly, the USA is the leading region in the journal although a considerable dispersion exists, especially during the last years when European and Asian universities are taking a more significant position.Merigó, J.; Mas-Tur, A.; Roig-Tierno, N.; Ribeiro-Soriano, D. (2016). A bibliometric overview of the Journal of Business Research. En CARMA 2016: 1st International Conference on Advanced Research Methods in Analytics. Editorial Universitat Politècnica de València. 148-148. https://doi.org/10.4995/CARMA2016.2015.423814814

Marshall University Music Department Presents a Chamber Choir Invitational, Music 2015

https://mds.marshall.edu/music_perf/1684/thumbnail.jp

Diagnosis of mycobacteria in bovine milk: an overview

Tuberculosis remains as the world’s biggest threat. In 2014, human tuberculosis ranked as a major infectious disease by the first time, overcoming HIV death rates. Bovine tuberculosis is a chronic disease of global distribution that affects animals and can be transmitted to humans by the consumption of raw milk, representing a serious public health concern. Despite the efforts of different countries to control and eradicate bovine tuberculosis, the high negative economic impact on meat and milk production chains remains, given the decreased production efficiency (approximately 25%), the high number of condemned carcasses, and increased animal culling rates. This scenario has motivated the establishment of official programs based on regulations and diagnostic procedures. Although Mycobacterium tuberculosis and Mycobacterium bovis are the major pathogenic species to humans and bovines, respectively, nontuberculous mycobacteria within the Mycobacterium genus have become increasingly important in recent decades due to human infections, including the ones that occur in immunocompetent people. Diagnosis of mycobacteria can be performed by microbiological culture from tissue samples (lymph nodes, lungs) and secretions (sputum, milk). In general, these pathogens demand special nutrient requirements for isolation/growth, and the use of selective and rich culture media. Indeed, within these genera, mycobacteria are classified as either fast- or slow-growth microorganisms. Regarding the latter ones, incubation times can vary from 45 to 90 days. Although microbiological culture is still considered the gold standard method for diagnosis, molecular approaches have been increasingly used. We describe here an overview of the diagnosis of Mycobacterium species in bovine milk

Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase

Cyclic ADP-ribose (cADPR) metabolism in mammals is catalyzed by NAD glycohydrolases (NADases) that, besides forming ADP-ribose, form and hydrolyze the N(1)-glycosidic linkage of cADPR. Thus far, no cADPR phosphohydrolase was known. We tested rat ADP-ribose/CDP-alcohol pyrophosphatase (ADPRibase-Mn) and found that cADPR is an ADPRibase-Mn ligand and substrate. ADPRibase-Mn activity on cADPR was 65-fold less efficient than on ADP-ribose, the best substrate. This is similar to the ADP-ribose/cADPR formation ratio by NADases. The product of cADPR phosphohydrolysis by ADPRibase-Mn was N(1)-(5-phosphoribosyl)-AMP, suggesting a novel route for cADPR turnover.info:eu-repo/semantics/publishedVersio

Contribution of protein domains to the activities of the human enzyme and molecular dynamics simulation of domain movements

Mammalian triokinase, which phosphorylates exogenous dihydroxyacetone and fructose-derived glyceraldehyde, is neither molecularly identified nor firmly associated to an encoding gene. Human FMN cyclase, which splits FAD and other ribonucleoside diphosphate-X compounds to ribonucleoside monophosphate and cyclic X-phosphodiester, is identical to a DAK-encoded dihydroxyacetone kinase. This bifunctional protein was identified as triokinase. It was modeled as a homodimer of two-domain (K and L) subunits. Active centers lie between K1 and L2 or K2 and L1: dihydroxyacetone binds K and ATP binds L in different subunits too distant (≈ 14 Å) for phosphoryl transfer. FAD docked to the ATP site with ribityl 4'-OH in a possible near-attack conformation for cyclase activity. Reciprocal inhibition between kinase and cyclase reactants confirmed substrate site locations. The differential roles of protein domains were supported by their individual expression: K was inactive, and L displayed cyclase but not kinase activity. The importance of domain mobility for the kinase activity of dimeric triokinase was highlighted by molecular dynamics simulations: ATP approached dihydroxyacetone at distances below 5 Å in near-attack conformation. Based upon structure, docking, and molecular dynamics simulations, relevant residues were mutated to alanine, and kcat and Km were assayed whenever kinase and/or cyclase activity was conserved. The results supported the roles of Thr(112) (hydrogen bonding of ATP adenine to K in the closed active center), His(221) (covalent anchoring of dihydroxyacetone to K), Asp(401) and Asp(403) (metal coordination to L), and Asp(556) (hydrogen bonding of ATP or FAD ribose to L domain). Interestingly, the His(221) point mutant acted specifically as a cyclase without kinase activity.info:eu-repo/semantics/publishedVersio

Molecular Bases of Catalysis and ADP-Ribose Preference of Human Mn2+-Dependent ADP-Ribose/CDP-Alcohol Diphosphatase and Conversion by Mutagenesis to a Preferential Cyclic ADP-Ribose Phosphohydrolase

Among metallo-dependent phosphatases, ADP-ribose/CDP-alcohol diphosphatases form a protein family (ADPRibase-Mn-like) mainly restricted, in eukaryotes, to vertebrates and plants, with preferential expression, at least in rodents, in immune cells. Rat and zebrafish ADPRibase-Mn, the only biochemically studied, are phosphohydrolases of ADP-ribose and, somewhat less efficiently, of CDP-alcohols and 2´,3´-cAMP. Furthermore, the rat but not the zebrafish enzyme displays a unique phosphohydrolytic activity on cyclic ADP-ribose. The molecular basis of such specificity is unknown. Human ADPRibase-Mn showed similar activities, including cyclic ADP-ribose phosphohydrolase, which seems thus common to mammalian ADPRibase-Mn. Substrate docking on a homology model of human ADPRibase-Mn suggested possible interactions of ADP-ribose with seven residues located, with one exception (Cys253), either within the metallo-dependent phosphatases signature (Gln27, Asn110, His111), or in unique structural regions of the ADPRibase-Mn family: s2s3 (Phe37 and Arg43) and h7h8 (Phe210), around the active site entrance. Mutants were constructed, and kinetic parameters for ADP-ribose, CDP-choline, 2´,3´-cAMP and cyclic ADP-ribose were determined. Phe37 was needed for ADP-ribose preference without catalytic effect, as indicated by the increased ADP-ribose Km and unchanged kcat of F37A-ADPRibase-Mn, while the Km values for the other substrates were little affected. Arg43 was essential for catalysis as indicated by the drastic efficiency loss shown by R43A-ADPRibase-Mn. Unexpectedly, Cys253 was hindering for cADPR phosphohydrolase, as indicated by the specific tenfold gain of efficiency of C253A-ADPRibase-Mn with cyclic ADP-ribose. This allowed the design of a triple mutant (F37A+L196F+C253A) for which cyclic ADP-ribose was the best substrate, with a catalytic efficiency of 3.5´104 M-1s-1 versus 4´103 M-1s-1 of the wild type.info:eu-repo/semantics/publishedVersio

The characterization of Escherichia coli CpdB as a recombinantpProtein reveals that, besides having the expected 3´-nucleotidase and 2´,3´-cyclic mononucleotide phosphodiesterase activities, it is also active as cyclic dinucleotide phosphodiesterase

Endogenous cyclic diadenylate phosphodiesterase activity was accidentally detected in lysates of Escherichia coli BL21. Since this kind of activity is uncommon in Gram-negative bacteria, its identification was undertaken. After partial purification and analysis by denaturing gel electrophoresis, renatured activity correlated with a protein identified by fingerprinting as CpdB (cpdB gene product), which is annotated as 3´-nucleotidase / 2´,3´- cyclicmononucleotide phosphodiesterase, and it is synthesized as a precursor protein with a signal sequence removable upon export to the periplasm. It has never been studied as a recombinant protein. The coding sequence of mature CpdB was cloned and expressed as a GST fusion protein. The study of the purified recombinant protein, separated from GST, confirmed CpdB annotation. The assay of catalytic efficiencies (kcat/Km) for a large substrate set revealed novel CpdB features, including very high efficiencies for 3´-AMP and 2´,3´- cyclic mononucleotides, and previously unknown activities on cyclic and linear dinucleotides. The catalytic efficiencies of the latter activities, though low in relative terms when compared to the major ones, are far from negligible. Actually, they are perfectly comparable to those of the ‘average’ enzyme and the known, bona fide cyclic dinucleotide phosphodiesterases. On the other hand, CpdB differs from these enzymes in its extracytoplasmic location and in the absence of EAL, HD and DHH domains. Instead, it contains the domains of the 5´-nucleotidase family pertaining to the metallophosphoesterase superfamily, although CpdB lacks 5´-nucleotidase activity. The possibility that the extracytoplasmic activity of CpdB on cyclic dinucleotides could have physiological meaning is discussed.Trabajo financiado por: Junta de Extremadura y Fondos FEDER. Ayudas GR10133 y GR15143 Donación privada para María Jesús Costas Vázquez. Contrato 2015/00481/001peerReviewe

Nitrate removal in saline water by photo-reduction using natural FeTiO as catalyst

As climate change progresses, there is an increasing interest on the use of non-conventional water sources such as brackish or saline waters. Nowadays, the main threat in Europe detected in these waterbodies is nitrate contamination. Within the multiple available methods studied for nitrate reduction, photocatalysis presents promising results, but this technology has not yet been tested in saline water. This work tackles the elimination of nitrate ([NO3−] =50 mg/L) in brackish and saline water ([sea salt] = 5–33 g/L) using ilmenite as photocatalyst and oxalic acid as an environmental-friendly reducing agent. The main challenge when working in saline water is to overcome oxalic acid scavenging by Ca2+ present in the water matrix. This can be solved either working at over stoichiometric concentrations of oxalic acid (≈300% stoich. dose) or acidifying the reaction media. The addition of hydrochloric acid ensures the protonation of oxalic acid, reducing drastically its precipitation as CaC2O4. Working at [C2O42−] = 180 mg/L, [FeTiO3] = 450 mg/L and [HCl 37%] = 13 mM, 73% total nitrogen (TN) elimination was reached after 420 min. Reaction temperature was also evaluated in the range of 20–80 °C, which allowed to calculate the Ea=9.8 kJ/mol. Finally, the effect of dissolved O2 on the TN reduction was assessed. Overall, photocatalytic nitrate reduction presents itself as a feasible technology regardless of the water salinit