ALBERT

Description: The energy problem, one the most important on a global scale, greatly affects the environment. Much of the current energy consumption occurs in existing buildings, including heritage buildings with varying protected status. Energy intervention and heritage conservation conflict to some extent, as research focuses more on the search for improved energy efficiency solutions for materials and systems than on their application to heritage buildings. This study describes experimental research on environmental conditioning techniques in spaces of worship in a temperate climate in southern Spain. Buildings were monitored and assessed in the implementation of different environmental techniques—active and combined (passive and active)—with the aim of improving the thermal comfort conditions of the faithful while preserving the cultural heritage of these buildings. The need for a control system of RH and the air system was concluded, as well as radiant floors and radiators, which, in the considered case studies, would barely affect the artworks. 24- and 12-h operation are better suited to heritage preservation than occasional use. All operation schedules are valid for thermal comfort.

Description: Nuclear collisions recreate conditions in the universe microseconds after the Big Bang. Only a very small fraction of the emitted fragments are light nuclei, but these states are of fundamental interest. We report the observation of antihypertritons--comprising an antiproton, an antineutron, and an antilambda hyperon--produced by colliding gold nuclei at high energy. Our analysis yields 70 +/- 17 antihypertritons ((Lambda)(3)-H) and 157 +/- 30 hypertritons (Lambda3H). The measured yields of Lambda3H ((Lambda)(3)-H) and 3He (3He) are similar, suggesting an equilibrium in coordinate and momentum space populations of up, down, and strange quarks and antiquarks, unlike the pattern observed at lower collision energies. The production and properties of antinuclei, and of nuclei containing strange quarks, have implications spanning nuclear and particle physics, astrophysics, and cosmology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉STAR Collaboration -- Abelev, B I -- Aggarwal, M M -- Ahammed, Z -- Alakhverdyants, A V -- Alekseev, I -- Anderson, B D -- Arkhipkin, D -- Averichev, G S -- Balewski, J -- Barnby, L S -- Baumgart, S -- Beavis, D R -- Bellwied, R -- Betancourt, M J -- Betts, R R -- Bhasin, A -- Bhati, A K -- Bichsel, H -- Bielcik, J -- Bielcikova, J -- Biritz, B -- Bland, L C -- Bonner, B E -- Bouchet, J -- Braidot, E -- Brandin, A V -- Bridgeman, A -- Bruna, E -- Bueltmann, S -- Bunzarov, I -- Burton, T P -- Cai, X Z -- Caines, H -- Calderon, M -- Catu, O -- Cebra, D -- Cendejas, R -- Cervantes, M C -- Chajecki, Z -- Chaloupka, P -- Chattopadhyay, S -- Chen, H F -- Chen, J H -- Chen, J Y -- Cheng, J -- Cherney, M -- Chikanian, A -- Choi, K E -- Christie, W -- Chung, P -- Clarke, R F -- Codrington, M J M -- Corliss, R -- Cramer, J G -- Crawford, H J -- Das, D -- Dash, S -- Davila Leyva, A -- De Silva, L C -- Debbe, R R -- Dedovich, T G -- DePhillips, M -- Derevschikov, A A -- Derradi de Souza, R -- Didenko, L -- Djawotho, P -- Dogra, S M -- Dong, X -- Drachenberg, J L -- Draper, J E -- Dunlop, J C -- Dutta Mazumdar, M R -- Efimov, L G -- Elhalhuli, E -- Elnimr, M -- Engelage, J -- Eppley, G -- Erazmus, B -- Estienne, M -- Eun, L -- Evdokimov, O -- Fachini, P -- Fatemi, R -- Fedorisin, J -- Fersch, R G -- Filip, P -- Finch, E -- Fine, V -- Fisyak, Y -- Gagliardi, C A -- Gangadharan, D R -- Ganti, M S -- Garcia-Solis, E J -- Geromitsos, A -- Geurts, F -- Ghazikhanian, V -- Ghosh, P -- Gorbunov, Y N -- Gordon, A -- Grebenyuk, O -- Grosnick, D -- Grube, B -- Guertin, S M -- Gupta, A -- Gupta, N -- Guryn, W -- Haag, B -- Hamed, A -- Han, L-X -- Harris, J W -- Hays-Wehle, J P -- Heinz, M -- Heppelmann, S -- Hirsch, A -- Hjort, E -- Hoffman, A M -- Hoffmann, G W -- Hofman, D J -- Hollis, R S -- Huang, B -- Huang, H Z -- Humanic, T J -- Huo, L -- Igo, G -- Iordanova, A -- Jacobs, P -- Jacobs, W W -- Jakl, P -- Jena, C -- Jin, F -- Jones, C L -- Jones, P G -- Joseph, J -- Judd, E G -- Kabana, S -- Kajimoto, K -- Kang, K -- Kapitan, J -- Kauder, K -- Keane, D -- Kechechyan, A -- Kettler, D -- Kikola, D P -- Kiryluk, J -- Kisiel, A -- Klein, S R -- Knospe, A G -- Kocoloski, A -- Koetke, D D -- Kollegger, T -- Konzer, J -- Kopytine, M -- Koralt, I -- Koroleva, L -- Korsch, W -- Kotchenda, L -- Kouchpil, V -- Kravtsov, P -- Krueger, K -- Krus, M -- Kumar, L -- Kurnadi, P -- Lamont, M A C -- Landgraf, J M -- LaPointe, S -- Lauret, J -- Lebedev, A -- Lednicky, R -- Lee, C-H -- Lee, J H -- Leight, W -- Levine, M J -- Li, C -- Li, L -- Li, N -- Li, W -- Li, X -- Li, Y -- Li, Z -- Lin, G -- Lindenbaum, S J -- Lisa, M A -- Liu, F -- Liu, H -- Liu, J -- Ljubicic, T -- Llope, W J -- Longacre, R S -- Love, W A -- Lu, Y -- Luo, X -- Ma, G L -- Ma, Y G -- Mahapatra, D P -- Majka, R -- Mal, O I -- Mangotra, L K -- Manweiler, R -- Margetis, S -- Markert, C -- Masui, H -- Matis, H S -- Matulenko, Yu A -- McDonald, D -- McShane, T S -- Meschanin, A -- Milner, R -- Minaev, N G -- Mioduszewski, S -- Mischke, A -- Mitrovski, M K -- Mohanty, B -- Mondal, M M -- Morozov, B -- Morozov, D A -- Munhoz, M G -- Nandi, B K -- Nattrass, C -- Nayak, T K -- Nelson, J M -- Netrakanti, P K -- Ng, M J -- Nogach, L V -- Nurushev, S B -- Odyniec, G -- Ogawa, A -- Okada, H -- Okorokov, V -- Olson, D -- Pachr, M -- Page, B S -- Pal, S K -- Pandit, Y -- Panebratsev, Y -- Pawlak, T -- Peitzmann, T -- Perevoztchikov, V -- Perkins, C -- Peryt, W -- Phatak, S C -- Pile, P -- Planinic, M -- Ploskon, M A -- Pluta, J -- Plyku, D -- Poljak, N -- Poskanzer, A M -- Potukuchi, B V K S -- Powell, C B -- Prindle, D -- Pruneau, C -- Pruthi, N K -- Pujahari, P R -- Putschke, J -- Qiu, H -- Raniwala, R -- Raniwala, S -- Ray, R L -- Redwine, R -- Reed, R -- Ritter, H G -- Roberts, J B -- Rogachevskiy, O V -- Romero, J L -- Rose, A -- Roy, C -- Ruan, L -- Sahoo, R -- Sakai, S -- Sakrejda, I -- Sakuma, T -- Salur, S -- Sandweiss, J -- Sangaline, E -- Schambach, J -- Scharenberg, R P -- Schmitz, N -- Schuster, T R -- Seele, J -- Seger, J -- Selyuzhenkov, I -- Seyboth, P -- Shahaliev, E -- Shao, M -- Sharma, M -- Shi, S S -- Sichtermann, E P -- Simon, F -- Singaraju, R N -- Skoby, M J -- Smirnov, N -- Sorensen, P -- Sowinski, J -- Spinka, H M -- Srivastava, B -- Stanislaus, T D S -- Staszak, D -- Stevens, J R -- Stock, R -- Strikhanov, M -- Stringfellow, B -- Suaide, A A P -- Suarez, M C -- Subba, N L -- Sumbera, M -- Sun, X M -- Sun, Y -- Sun, Z -- Surrow, B -- Svirida, D N -- Symons, T J M -- Szanto de Toledo, A -- Takahashi, J -- Tang, A H -- Tang, Z -- Tarini, L H -- Tarnowsky, T -- Thein, D -- Thomas, J H -- Tian, J -- Timmins, A R -- Timoshenko, S -- Tlusty, D -- Tokarev, M -- Trainor, T A -- Tram, V N -- Trentalange, S -- Tribble, R E -- Tsai, O D -- Ulery, J -- Ullrich, T -- Underwood, D G -- Van Buren, G -- van Leeuwen, M -- van Nieuwenhuizen, G -- Vanfossen, J A Jr -- Varma, R -- Vasconcelos, G M S -- Vasiliev, A N -- Videbaek, F -- Viyogi, Y P -- Vokal, S -- Voloshin, S A -- Wada, M -- Walker, M -- Wang, F -- Wang, G -- Wang, H -- Wang, J S -- Wang, Q -- Wang, X L -- Wang, Y -- Webb, G -- Webb, J C -- Westfall, G D -- Whitten, C Jr -- Wieman, H -- Wingfield, E -- Wissink, S W -- Witt, R -- Wu, Y -- Xie, W -- Xu, H -- Xu, N -- Xu, Q H -- Xu, W -- Xu, Y -- Xu, Z -- Xue, L -- Yang, Y -- Yepes, P -- Yip, K -- Yoo, I-K -- Yue, Q -- Zawisza, M -- Zbroszczyk, H -- Zhan, W -- Zhang, J -- Zhang, S -- Zhang, W M -- Zhang, X P -- Zhang, Y -- Zhang, Z P -- Zhao, J -- Zhong, C -- Zhou, J -- Zhou, W -- Zhu, X -- Zhu, Y H -- Zoulkarneev, R -- Zoulkarneeva, Y -- New York, N.Y. -- Science. 2010 Apr 2;328(5974):58-62. doi: 10.1126/science.1183980. Epub 2010 Mar 4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20203011" target="_blank"〉PubMed〈/a〉

Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bolukbasi, Burcu -- Berente, Nicholas -- Cutcher-Gershenfeld, Joel -- Dechurch, Leslie -- Flint, Courtney -- Haberman, Michael -- King, John Leslie -- Knight, Eric -- Lawrence, Barbara -- Masella, Ethan -- McElroy, Charles -- Mittleman, Barbara -- Nolan, Mark -- Radik, Melanie -- Shin, Namchul -- Thompson, Cheryl A -- Winter, Susan -- Zaslavsky, Ilya -- Allison, M Lee -- Arctur, David -- Arrigo, Jennifer -- Aufdenkampe, Anthony K -- Bass, Jay -- Crowell, Jim -- Daniels, Mike -- Diggs, Stephen -- Duffy, Christopher -- Gil, Yolanda -- Gomez, Basil -- Graves, Sara -- Hazen, Robert -- Hsu, Leslie -- Kinkade, Danie -- Lehnert, Kerstin -- Marone, Chris -- Middleton, Don -- Noren, Anders -- Pearthree, Genevieve -- Ramamurthy, Mohan -- Robinson, Erin -- Percivall, George -- Richard, Stephen -- Suarez, Celina -- Walker, Doug -- New York, N.Y. -- Science. 2013 Nov 29;342(6162):1041-2. doi: 10.1126/science.342.6162.1041-b.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Labor and Employment Relations, University of Illinois at Urbana-Champaign, Champaign, IL 61820, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24288316" target="_blank"〉PubMed〈/a〉

Description: The actin cross-linking domain (ACD) is an actin-specific toxin produced by several pathogens, including life-threatening spp. of Vibrio cholerae, Vibrio vulnificus, and Aeromonas hydrophila. Actin cross-linking by ACD is thought to lead to slow cytoskeleton failure owing to a gradual sequestration of actin in the form of nonfunctional oligomers. Here, we found that ACD converted cytoplasmic actin into highly toxic oligomers that potently "poisoned" the ability of major actin assembly proteins, formins, to sustain actin polymerization. Thus, ACD can target the most abundant cellular protein by using actin oligomers as secondary toxins to efficiently subvert cellular functions of actin while functioning at very low doses.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4648357/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4648357/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heisler, David B -- Kudryashova, Elena -- Grinevich, Dmitry O -- Suarez, Cristian -- Winkelman, Jonathan D -- Birukov, Konstantin G -- Kotha, Sainath R -- Parinandi, Narasimham L -- Vavylonis, Dimitrios -- Kovar, David R -- Kudryashov, Dmitri S -- R01 GM079265/GM/NIGMS NIH HHS/ -- R01 GM098430/GM/NIGMS NIH HHS/ -- R01 GM114666/GM/NIGMS NIH HHS/ -- R01 HL076259/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2015 Jul 31;349(6247):535-9. doi: 10.1126/science.aab4090.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA. The Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA. ; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA. kudryashov.1@osu.edu kudryashova.1@osu.edu. ; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA. ; Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USA. ; Section of Pulmonary and Critical Care and Lung Injury Center, Department of Medicine, The University of Chicago, Chicago, IL 60637, USA. ; Lipid Signaling and Lipidomics Laboratory, Division of Pulmonary, Allergy, Critical Care and Sleep Medicine, Department of Medicine, Dorothy M. Davis Heart and Lung Research Institute, College of Medicine, The Ohio State University, Columbus, OH 43210, USA. ; Department of Physics, Lehigh University, Bethlehem, PA 18015, USA. ; Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USA. Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA. ; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA. The Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA. kudryashov.1@osu.edu kudryashova.1@osu.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26228148" target="_blank"〉PubMed〈/a〉

Description: Chemical Reviews DOI: 10.1021/cr400204z

Description: Biochemistry DOI: 10.1021/bi301139d

Description: Environmental Science & Technology DOI: 10.1021/es4015629

Description: In order to help unravel the thermal history of middle Paleozoic sedimentary rocks in West Virginia, a rock magnetic study was conducted with a focus on the Marcellus Shale. Vitrinite reflectance, fluid inclusions microthermometry and conodont alteration index data yield contradictory burial temperature within the range 150–250°C (302–482°F). The characterization of magnetite and pyrrhotite may be used as an index to track burial temperature around 200°C (392°F). Low-temperature and room-temperature magnetic measurements were performed in order to determine the magnetic assemblage. Three magnetic assemblages were identified that were stratigraphically distributed. The goethite and nanosized magnetite (A1) assemblage is mainly found in the Clinton Group–Oriskany Sandstone stratigraphic interval (Silurian–Lower Devonian). Nanosized fraction of magnetite and probably pyrrhotite (A3) assemblage essentially constitutes the Marcellus Shale–Chemung Formation sequence (Devonian). Microsized pyrrhotite is the typical mineral for A2 that is only identified near the Alleghenian structural front. Overall, the rare occurrence of micron pyrrhotite in our samples suggests that the study area has not experienced burial temperatures higher than 200°C (392°F).

Description: The control of antibody specificity plays pivotal roles in key technological fields such as diagnostics and therapeutics. During the development of immunoassays (IAs) for the biosensing of pathogens in food matrices, we have found a way to rationalize and control the specificity of polyclonal antibodies (sera) for a complex analytical target (the Salmonella genus), in terms of number of analytes (Salmonella species) and potential cross-reactivity with similar analytes (other bacteria strains). Indeed, the biosensing of Salmonella required the development of sera and serum mixtures displaying homogeneous specificity for a large set of strains showing broad biochemical variety (54 Salmonella serovars tested in this study), which partially overlaps with the molecular features of other class of bacteria (like specific serogroups of E. coli). To achieve a trade-off between specificity harmonisation and maximization, we have developed a strategy based on the conversion of the specificity profiles of individual sera in to numerical descriptors, which allow predicting the capacity of serum mixtures to detect multiple bacteria strains. This approach does not imply laborious purification steps and results advantageous for process scaling-up, and may help in the customization of the specificity profiles of antibodies needed for diagnostic and therapeutic applications such as multi-analyte detection and recombinant antibody engineering, respectively.