@unpublished{AcharyaActisAghajanietal.2013,
  author    = {Acharya, B. S. and Actis, M. and Aghajani, T. and Agnetta, G. and Aguilar, J. and Aharonian, Felix A. and Ajello, M. and Akhperjanian, A. G. and Alcubierre, M. and Aleksic, J. and Alfaro, R. and Aliu, E. and Allafort, A. J. and Allan, D. and Allekotte, I. and Amato, E. and Anderson, J. and Ang{\"u}ner, Ekrem Oǧuzhan and Antonelli, L. A. and Antoranz, P. and Aravantinos, A. and Arlen, T. and Armstrong, T. and Arnaldi, H. and Arrabito, L. and Asano, K. and Ashton, T. and Asorey, H. G. and Awane, Y. and Baba, H. and Babic, A. and Baby, N. and Baehr, J. and Bais, A. and Baixeras, C. and Bajtlik, S. and Balbo, M. and Balis, D. and Balkowski, C. and Bamba, A. and Bandiera, R. and Barber, A. and Barbier, C. and Barcelo, M. and Barnacka, Anna and Barnstedt, J{\"u}rgen and Barres de Almeida, U. and Barrio, J. A. and Basili, A. and Basso, S. and Bastieri, D. and Bauer, C. and Baushev, Anton N. and Becerra Gonzalez, J. and Becherini, Yvonne and Bechtol, K. C. and Tjus, J. Becker and Beckmann, Volker and Bednarek, W. and Behera, B. and Belluso, M. and Benbow, W. and Berdugo, J. and Berger, K. and Bernard, F. and Bernardino, T. and Bernl{\"o}hr, K. and Bhat, N. and Bhattacharyya, S. and Bigongiari, C. and Biland, A. and Billotta, S. and Bird, T. and Birsin, E. and Bissaldi, E. and Biteau, Jonathan and Bitossi, M. and Blake, S. and Blanch Bigas, O. and Blasi, P. and Bobkov, A. A. and Boccone, V. and Boettcher, Markus and Bogacz, L. and Bogart, J. and Bogdan, M. and Boisson, Catherine and Boix Gargallo, J. and Bolmont, J. and Bonanno, G. and Bonardi, A. and Bonev, T. and Bonifacio, P. and Bonnoli, G. and Bordas, Pol and Borgland, A. W. and Borkowski, Janett and Bose, R. and Botner, O. and Bottani, A. and Bouchet, L. and Bourgeat, M. and Boutonnet, C. and Bouvier, A. and Brau-Nogue, S. and Braun, I. and Bretz, T. and Briggs, M. S. and Bringmann, T. and Brook, P. and Brun, Pierre and Brunetti, L. and Buanes, T. and Buckley, J. H. and Buehler, R. and Bugaev, V. and Bulgarelli, A. and Bulik, Tomasz and Busetto, G. and Buson, S. and Byrum, K. and Cailles, M. and Cameron, R. A. and Camprecios, J. and Canestrari, R. and Cantu, S. and Capalbi, M. and Caraveo, P. A. and Carmona, E. and Carosi, A. and Carr, John and Carton, P. H. and Casanova, Sabrina and Casiraghi, M. and Catalano, O. and Cavazzani, S. and Cazaux, S. and Cerruti, M. and Chabanne, E. and Chadwick, Paula M. and Champion, C. and Chen, Andrew and Chiang, J. and Chiappetti, L. and Chikawa, M. and Chitnis, V. R. and Chollet, F. and Chudoba, J. and Cieslar, M. and Cillis, A. N. and Cohen-Tanugi, J. and Colafrancesco, Sergio and Colin, P. and Calome, J. and Colonges, S. and Compin, M. and Conconi, P. and Conforti, V. and Connaughton, V. and Conrad, Jan and Contreras, J. L. and Coppi, P. and Corona, P. and Corti, D. and Cortina, J. and Cossio, L. and Costantini, H. and Cotter, G. and Courty, B. and Couturier, S. and Covino, S. and Crimi, G. and Criswell, S. J. and Croston, J. and Cusumano, G. and Dafonseca, M. and Dale, O. and Daniel, M. and Darling, J. and Davids, I. and Dazzi, F. and De Angelis, A. and De Caprio, V. and De Frondat, F. and de Gouveia Dal Pino, E. M. and de la Calle, I. and De La Vega, G. A. and Lopez, R. de los Reyes and De Lotto, B. and De Luca, A. and de Mello Neto, J. R. T. and de Naurois, M. and de Oliveira, Y. and de Ona Wilhelmi, E. and de Souza, V. and Decerprit, G. and Decock, G. and Deil, C. and Delagnes, E. and Deleglise, G. and Delgado, C. and Della Volpe, D. and Demange, P. and Depaola, G. and Dettlaff, A. and Di Paola, A. and Di Pierro, F. and Diaz, C. and Dick, J. and Dickherber, R. and Dickinson, H. and Diez-Blanco, V. and Digel, S. and Dimitrov, D. and Disset, G. and Djannati-Ata{\"i}, A. and Doert, M. and Dohmke, M. and Domainko, W. and Prester, Dijana Dominis and Donat, A. and Dorner, D. and Doro, M. and Dournaux, J-L. and Drake, G. and Dravins, D. and Drury, L. and Dubois, F. and Dubois, R. and Dubus, G. and Dufour, C. and Dumas, D. and Dumm, J. and Durand, D. and Dyks, J. and Dyrda, M. and Ebr, J. and Edy, E. and Egberts, Kathrin and Eger, P. and Einecke, S. and Eleftheriadis, C. and Elles, S. and Emmanoulopoulos, D. and Engelhaupt, D. and Enomoto, R. and Ernenwein, J-P and Errando, M. and Etchegoyen, A. and Evans, P. and Falcone, A. and Fantinel, D. and Farakos, K. and Farnier, C. and Fasola, G. and Favill, B. and Fede, E. and Federici, S. and Fegan, S. and Feinstein, F. and Ferenc, D. and Ferrando, P. and Fesquet, M. and Fiasson, A. and Fillin-Martino, E. and Fink, D. and Finley, C. and Finley, J. P. and Fiorini, M. and Firpo Curcoll, R. and Flores, H. and Florin, D. and Focke, W. and Foehr, C. and Fokitis, E. and Font, L. and Fontaine, G. and Fornasa, M. and Foerster, A. and Fortson, L. and Fouque, N. and Franckowiak, A. and Fransson, C. and Fraser, G. and Frei, R. and Albuquerque, I. F. M. and Fresnillo, L. and Fruck, C. and Fujita, Y. and Fukazawa, Y. and Fukui, Y. and Funk, S. and Gaebele, W. and Gabici, S. and Gabriele, R. and Gadola, A. and Galante, N. and Gall, D. and Gallant, Y. and Gamez-Garcia, J. and Garcia, B. and Garcia Lopez, R. and Gardiol, D. and Garrido, D. and Garrido, L. and Gascon, D. and Gaug, M. and Gaweda, J. and Gebremedhin, L. and Geffroy, N. and Gerard, L. and Ghedina, A. and Ghigo, M. and Giannakaki, E. and Gianotti, F. and Giarrusso, S. and Giavitto, G. and Giebels, B. and Gika, V. and Giommi, P. and Girard, N. and Giro, E. and Giuliani, A. and Glanzman, T. and Glicenstein, J. -F. and Godinovic, N. and Golev, V. and Gomez Berisso, M. and Gomez-Ortega, J. and Gonzalez, M. M. and Gonzalez, A. and Gonzalez, F. and Gonzalez Munoz, A. and Gothe, K. 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  title     = {Introducing the CTA concept},
  series = {Astroparticle physics},
  volume    = {43},
  journal   = {Astroparticle physics},
  number    = {2},
  publisher = {Elsevier},
  address   = {Amsterdam},
  organization    = {CTA Consortium},
  issn      = {0927-6505},
  doi       = {10.1016/j.astropartphys.2013.01.007},
  pages     = {3 -- 18},
  year      = {2013},
  abstract  = {The Cherenkov Telescope Array (CTA) is a new observatory for very high-energy (VHE) gamma rays. CTA has ambitions science goals, for which it is necessary to achieve full-sky coverage, to improve the sensitivity by about an order of magnitude, to span about four decades of energy, from a few tens of GeV to above 100 TeV with enhanced angular and energy resolutions over existing VHE gamma-ray observatories. An international collaboration has formed with more than 1000 members from 27 countries in Europe, Asia, Africa and North and South America. In 2010 the CTA Consortium completed a Design Study and started a three-year Preparatory Phase which leads to production readiness of CTA in 2014. In this paper we introduce the science goals and the concept of CTA, and provide an overview of the project.},
  language  = {en}
}
@misc{SchernthanerGroopCooperetal.2016,
  author    = {Schernthaner, G. and Groop, P. and Cooper, M. and Perkovic, V and Hocher, Berthold and Kanasaki, K. and Sharma, K. and Stanton, R. and Toto, R. and Cescutti, Jessica and Gordat, M. and Meinicke, T. and Koitka-Weber, A. and Woerle, H. and Eynatten, M.},
  title     = {EFFECTS OF LINAGLIPTIN ON GLYCAEMIC CONTROL AND ALBUMINURIA IN TYPE 2 DIABETES - THE MARLINA-T2D (TM) TRIAL},
  series = {Nephrology},
  volume    = {21},
  journal   = {Nephrology},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {1320-5358},
  doi       = {10.1111/nep.12887},
  pages     = {60 -- 60},
  year      = {2016},
  language  = {en}
}
@article{MuellerWindhofMaximovetal.2013,
  author    = {M{\"u}ller, Sara and Windhof, Indra M. and Maximov, Vladimir and Jurkowski, Tomasz and Jeltsch, Albert and F{\"o}rstner, Konrad U. and Sharma, Cynthia M. and Gr{\"a}f, Ralph and Nellen, Wolfgang},
  title     = {Target recognition, RNA methylation activity and transcriptional regulation of the dictyostelium discoideum Dnmt2-homologue (DnmA)},
  series = {Nucleic acids research},
  volume    = {41},
  journal   = {Nucleic acids research},
  number    = {18},
  publisher = {Oxford Univ. Press},
  address   = {Oxford},
  issn      = {0305-1048},
  doi       = {10.1093/nar/gkt634},
  pages     = {8615 -- 8627},
  year      = {2013},
  abstract  = {Although the DNA methyltransferase 2 family is highly conserved during evolution and recent reports suggested a dual specificity with stronger activity on transfer RNA (tRNA) than DNA substrates, the biological function is still obscure. We show that the Dictyostelium discoideum Dnmt2-homologue DnmA is an active tRNA methyltransferase that modifies C38 in tRNA(Asp(GUC)) in vitro and in vivo. By an ultraviolet-crosslinking and immunoprecipitation approach, we identified further DnmA targets. This revealed specific tRNA fragments bound by the enzyme and identified tRNA(Glu(CUC/UUC)) and tRNA(Gly(GCC)) as new but weaker substrates for both human Dnmt2 and DnmA in vitro but apparently not in vivo. Dnmt2 enzymes form transient covalent complexes with their substrates. The dynamics of complex formation and complex resolution reflect methylation efficiency in vitro. Quantitative PCR analyses revealed alterations in dnmA expression during development, cell cycle and in response to temperature stress. However, dnmA expression only partially correlated with tRNA methylation in vivo. Strikingly, dnmA expression in the laboratory strain AX2 was significantly lower than in the NC4 parent strain. As expression levels and binding of DnmA to a target in vivo are apparently not necessarily accompanied by methylation, we propose an additional biological function of DnmA apart from methylation.},
  language  = {en}
}
@article{SinghDaniSharmaetal.2006,
  author    = {Singh, Jasbir and Dani, Harinder M. and Sharma, Reeta and Steinberg, Pablo},
  title     = {Inhibition of the biosynthesis of SRP polypeptides and secretory proteins by aflatoxin B-1 can disrupt protein targeting},
  series = {Cell biochemistry and function},
  volume    = {24},
  journal   = {Cell biochemistry and function},
  publisher = {Wiley},
  address   = {Chichester},
  issn      = {0263-6484},
  doi       = {10.1027/cbf.1285},
  pages     = {507 -- 510},
  year      = {2006},
  abstract  = {Cell culture and western blotting studies revealed that aflatoxin B-1 (AFB(1)) inhibits the biosynthesis of two of the constituent polypeptides of signal recognition particle (SRP) (SRP54 and 72). SRP escorts polyribosomes carrying signal peptides from free form in the cytosol to the bound form on endoplasmic reticulum (ER) membrane during protein targeting. These effects of AFB(1) on SRP biosynthesis may inhibit the formation of functional SRP Our experiments have further shown that AFB(1) also inhibits the biosynthesis/translocation of a secretory protein, preprolactin, which fails to appear in the lumen of ER consequent to the treatment with this hepatocarcinogen. The results of the experiments presented in this article therefore enable us to infer for the first time that aflatoxin B-1 may inhibit the functioning of SRP as an escort and deplete the ER of polyribosomes for secretory protein synthesis. As these secretory proteins are important components of the plasma membrane, gap junctions and intercellular matrix, their absence from these locations could disturb cell to cell communication leading to tumorigenesis.},
  language  = {en}
}
@article{SinghSinghDanietal.2005,
  author    = {Singh, Jasbir and Singh, S. and Dani, H. M. and Sharma, Reeta and Steinberg, Pablo},
  title     = {Interactions of aflatoxin B-1 with SRP components can disrupt protein targeting},
  issn      = {0263-6484},
  year      = {2005},
  abstract  = {Spectrofluorimetric studies have revealed that aflatoxin B-1 (AFB(1)) interacts with signal recognition particle (SRP), which acts as an escort for polyribosomes with signal peptides to be transported and bound to the cytoplasmic face of the endoplasmic reticulum (ER). We further report that the binding of AFB(1) to SRP is selective as it only binds to two (SRP9 and 14) out of its three constituent polypeptides studied. Binding of AFB(1) to proteins is known to alter their conformations. Interactions of AFB(1) with SRP polypeptides may generate structural and functional alterations in this particle and hinder secretory protein synthesis. Copyright (C) 2004 John Wiley Sons, Ltd},
  language  = {en}
}
@article{BrajpuriyaTripathiSharmaetal.2007,
  author    = {Brajpuriya, Ranjeet and Tripathi, Sumit and Sharma, Abhishek and Chaudhari, S.M. and Phase, D.M. and Gupta, Ajay and Shripathi, Thoudinja and Leitenberger, Wolfram and Pietsch, Ullrich and Laxmi, N.},
  title     = {Temperature dependent energy-dispersive X-ray diffraction and magnetic study of Fe/Al interface},
  issn      = {0169-4332},
  doi       = {10.1016/j.apsusc.2007.04.069},
  year      = {2007},
  abstract  = {In situ temperature dependent energy-dispersive structural and magnetic study of electron beam evaporated Fe/Al multilayer sample (MLS) has been investigated. The structural studies show the formation of an intermixed FeAl transition layer of a few nanometers thick at the interface during deposition, which on annealing at 300 degrees C transforms to B2FeAl intermetallic phase. Magnetization decreases with increase in temperature and drops to minimum above 300 degrees C due to increase in anti-ferromagnetic interlayer coupling and formation of nonmagnetic FeAl phase at the interface. The Curie temperature (T-c) is found to be 288 degrees C and is much less than that of bulk bcc Fe.},
  language  = {en}
}
@article{KalliesKunzKlausetal.2000,
  author    = {Kallies, Bernd and Kunz, Iris and Klaus, Susanne and Schorr, Ulrike and Sharma, Arya M.},
  title     = {Kinetic analysis of the thermic effect of food and its relationship to body composition in humans},
  year      = {2000},
  abstract  = {The course of energy expenditure after a meal can vary widely with regard to the slope of onset, amplitude, and duration of the thermic effect. The aim of the present study was to explore the relationship between the thermic effect of food (TEF), as characterized by kinetic analysis of postprandial energy expenditure, body composition, and variables related to the metabolic syndrome including central obesity, hypertension, and glucose tolerance. A total of 181 men and women (body mass index [BMI] range, 19.4 to 52.2 kg/m2) were characterized for body composition, blood pressure, oral glucose tolerance, and energy expenditure after a test meal. Energy expenditure, as measured by indirect calorimetry, was analyzed over a 6-hour period by 3-parameter curve fitting using equations derived from kinetics describing a biphasic reaction involving 2 consecutive first-order reactions (A->B->C). Apart from total thermic effect of food (TEFk), the curve also provided an estimate of time of peak (Tp) and amplitude of peak (Ap) for each subject. Multiple stepwise regression analysis with TEFk, Ap, and Tp as dependent variables showed significant effects of sex, age, body weight, body fat, -blockade, and body composition on TEF curve parameters. Cluster analysis based on Tp shown 2 distinct clusters with significant differences in age and body fat mass. This study shows that kinetic analysis of postprandial energy expenditure can be used to examine the determinants of the time course of the thermic effect of food in man.},
  language  = {en}
}
@misc{HixsonSharmaKainzetal.2015,
  author    = {Hixson, Stefanie M. and Sharma, Bhanu and Kainz, Martin J. and Wacker, Alexander and Arts, Michael T.},
  title     = {Production, distribution, and abundance of long-chain omega-3 polyunsaturated fatty acids: a fundamental dichotomy between freshwater and terrestrial ecosystems},
  series = {Environmental reviews = Dossiers environnement},
  volume    = {23},
  journal   = {Environmental reviews = Dossiers environnement},
  number    = {4},
  publisher = {NRC Research Press},
  address   = {Ottawa},
  issn      = {1208-6053},
  doi       = {10.1139/er-2015-0029},
  pages     = {414 -- 424},
  year      = {2015},
  abstract  = {Long-chain polyunsaturated fatty acids (LC-PUFA) are critical for the health of aquatic and terrestrial organisms; therefore, understanding the production, distribution, and abundance of these compounds is imperative. Although the dynamics of LC-PUFA production and distribution in aquatic environments has been well documented, a systematic and comprehensive comparison to LC-PUFA in terrestrial environments has not been rigorously investigated. Here we use a data synthesis approach to compare and contrast fatty acid profiles of 369 aquatic and terrestrial organisms. Habitat and trophic level were interacting factors that determined the proportion of individual omega-3 (n-3) or omega-6 (n-6) PUFA in aquatic and terrestrial organisms. Higher total n-3 content compared with n-6 PUFA and a strong prevalence of the n-3 PUFA eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) characterized aquatic versus terrestrial organisms. Conversely, terrestrial organisms had higher linoleic acid (LNA) and alpha-linolenic acid (ALA) contents than aquatic organisms; however, the ratio of ALA: LNA was higher in aquatic organisms. The EPA + DHA content was higher in aquatic animals than terrestrial organisms, and increased from algae to invertebrates to vertebrates in the aquatic environment. An analysis of covariance (ANCOVA) revealed that fatty acid composition was highly dependent on the interaction between habitat and trophic level. We conclude that freshwater ecosystems provide an essential service through the production of n-3 LC-PUFA that are required to maintain the health of terrestrial organisms including humans.},
  language  = {en}
}
@article{ReifarthBekirBapolisietal.2022,
  author    = {Reifarth, Martin and Bekir, Marek and Bapolisi, Alain M. and Titov, Evgenii and Nusshardt, Fabian and Nowaczyk, Julius and Grigoriev, Dmitry and Sharma, Anjali and Saalfrank, Peter and Santer, Svetlana and Hartlieb, Matthias and B{\"o}ker, Alexander},
  title     = {A dual pH- and light-responsive spiropyrane-based surfactant},
  series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  volume    = {61},
  journal   = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  number    = {21},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1433-7851},
  doi       = {10.1002/anie.202114687},
  pages     = {10},
  year      = {2022},
  abstract  = {A cationic surfactant containing a spiropyrane unit is prepared exhibiting a dual-responsive adjustability of its surface-active characteristics. The switching mechanism of the system relies on the reversible conversion of the non-ionic spiropyrane (SP) to a zwitterionic merocyanine (MC) and can be controlled by adjusting the pH value and via light, resulting in a pH-dependent photoactivity: While the compound possesses a pronounced difference in surface activity between both forms under acidic conditions, this behavior is suppressed at a neutral pH level. The underlying switching processes are investigated in detail, and a thermodynamic explanation based on a combination of theoretical and experimental results is provided. This complex stimuli-responsive behavior enables remote-control of colloidal systems. To demonstrate its applicability, the surfactant is utilized for the pH-dependent manipulation of oil-in-water emulsions.},
  language  = {en}
}