TY - JOUR A1 - Abdalla, Hassan E. A1 - Adam, R. A1 - Aharonian, Felix A. A1 - Benkhali, F. Ait A1 - Angüner, Ekrem Oǧuzhan A1 - Arakawa, M. A1 - Arcaro, C. A1 - Armand, C. A1 - Ashkar, H. A1 - Backes, M. A1 - Martins, V. Barbosa A1 - Barnard, M. A1 - Becherini, Y. A1 - Berge, D. A1 - Bernloehr, K. A1 - Bissaldi, E. A1 - Blackwell, R. A1 - Boettcher, M. A1 - Boisson, C. A1 - Bolmont, J. A1 - Bonnefoy, S. A1 - Bregeon, J. A1 - Breuhaus, M. A1 - Brun, F. A1 - Brun, P. A1 - Bryan, M. A1 - Buechele, M. A1 - Bulik, T. A1 - Bylund, T. A1 - Capasso, M. A1 - Caroff, S. A1 - Carosi, A. A1 - Casanova, Sabrina A1 - Cerruti, M. A1 - Chand, T. A1 - Chandra, S. A1 - Chen, A. A1 - Colafrancesco, S. A1 - Curylo, M. A1 - Davids, I. D. A1 - Deil, C. A1 - Devin, J. A1 - deWilt, P. A1 - Dirson, L. A1 - Djannati-Atai, A. A1 - Dmytriiev, A. A1 - Donath, A. A1 - Doroshenko, V A1 - Dyks, J. A1 - Egberts, Kathrin A1 - Emery, G. A1 - Ernenwein, J-P A1 - Eschbach, S. A1 - Feijen, K. A1 - Fegan, S. A1 - Fiasson, A. A1 - Fontaine, G. A1 - Funk, S. A1 - Fussling, Matthias A1 - Gabici, S. A1 - Gallant, Y. A. A1 - Gate, F. A1 - Giavitto, G. A1 - Giunti, L. A1 - Glawion, D. A1 - Glicenstein, J. F. A1 - Gottschall, D. A1 - Grondin, M-H A1 - Hahn, J. A1 - Haupt, M. A1 - Heinzelmann, G. A1 - Henri, G. A1 - Hermann, G. A1 - Hinton, J. A. A1 - Hofmann, W. A1 - Hoischen, Clemens A1 - Holch, T. L. A1 - Holler, M. A1 - Horns, D. A1 - Huber, D. A1 - Iwasaki, H. A1 - Jamrozy, M. A1 - Jankowsky, D. A1 - Jankowsky, F. A1 - Jardin-Blicq, A. A1 - Jung-Richardt, I A1 - Kastendieck, M. A. A1 - Katarzynski, K. A1 - Katsuragawa, M. A1 - Katz, U. A1 - Khangulyan, D. A1 - Khelifi, B. A1 - King, J. A1 - Klepser, S. A1 - Kluzniak, W. A1 - Komin, Nu A1 - Kosack, K. A1 - Kostunin, D. A1 - Kreter, M. A1 - Lamanna, G. A1 - Lemiere, A. A1 - Lemoine-Goumard, M. A1 - Lenain, J-P A1 - Leser, Eva A1 - Levy, C. A1 - Lohse, T. A1 - Lypova, I A1 - Mackey, J. A1 - Majumdar, J. A1 - Malyshev, D. A1 - Marandon, V A1 - Marcowith, Alexandre A1 - Mares, A. A1 - Mariaud, C. A1 - Marti-Devesa, G. A1 - Marx, R. A1 - Maurin, G. A1 - Meintjes, P. J. A1 - Mitchell, A. M. W. A1 - Moderski, R. A1 - Mohamed, M. A1 - Mohrmann, L. A1 - Moore, C. A1 - Moulin, Emmanuel A1 - Muller, J. A1 - Murach, T. A1 - Nakashima, S. A1 - de Naurois, M. A1 - Ndiyavala, H. A1 - Niederwanger, F. A1 - Niemiec, J. A1 - Oakes, L. A1 - Odaka, H. A1 - Ohm, S. A1 - Wilhelmi, E. de Ona A1 - Ostrowski, M. A1 - Oya, I A1 - Panter, M. A1 - Parsons, R. D. A1 - Perennes, C. A1 - Petrucci, P-O A1 - Peyaud, B. A1 - Piel, Q. A1 - Pita, S. A1 - Poireau, V A1 - Noel, A. Priyana A1 - Prokhorov, D. A. A1 - Prokoph, H. A1 - Puehlhofer, G. A1 - Punch, M. A1 - Quirrenbach, A. A1 - Raab, S. A1 - Rauth, R. A1 - Reimer, A. A1 - Reimer, O. A1 - Remy, Q. A1 - Renaud, M. A1 - Rieger, F. A1 - Rinchiuso, L. A1 - Romoli, C. A1 - Rowell, G. A1 - Rudak, B. A1 - Ruiz-Velasco, E. A1 - Sahakian, V A1 - Sailer, S. A1 - Saito, S. A1 - Sanchez, D. A. A1 - Santangelo, Andrea A1 - Sasaki, M. A1 - Schlickeiser, R. A1 - Schussler, F. A1 - Schulz, A. A1 - Schutte, H. M. A1 - Schwanke, U. A1 - Schwemmer, S. A1 - Seglar-Arroyo, M. A1 - Senniappan, M. A1 - Seyffert, A. S. A1 - Shafi, N. A1 - Shiningayamwe, K. A1 - Simoni, R. A1 - Sinha, A. A1 - Sol, H. A1 - Specovius, A. A1 - Spir-Jacob, M. A1 - Stawarz, L. A1 - Steenkamp, R. A1 - Stegmann, Christian A1 - Steppa, Constantin Beverly A1 - Takahashi, T. A1 - Tavernier, T. A1 - Taylor, A. M. A1 - Terrier, R. A1 - Tiziani, D. A1 - Tluczykont, M. A1 - Trichard, C. A1 - Tsirou, M. A1 - Tsuji, N. A1 - Tuffs, R. A1 - Uchiyama, Y. A1 - van der Walt, D. J. A1 - van Eldik, C. A1 - van Rensburg, C. A1 - van Soelen, B. A1 - Vasileiadis, G. A1 - Veh, J. A1 - Venter, C. A1 - Vincent, P. A1 - Vink, J. A1 - Voelk, H. J. A1 - Vuillaume, T. A1 - Wadiasingh, Z. A1 - Wagner, S. J. A1 - White, R. A1 - Wierzcholska, A. A1 - Yang, R. A1 - Yoneda, H. A1 - Zacharias, M. A1 - Zanin, R. A1 - Zdziarski, A. A. A1 - Zech, Alraune A1 - Ziegler, A. A1 - Zorn, J. A1 - Zywucka, N. A1 - de Palma, F. A1 - Axelsson, M. A1 - Roberts, O. J. T1 - A very-high-energy component deep in the gamma-ray burst afterglow JF - Nature : the international weekly journal of science N2 - Gamma-ray bursts (GRBs) are brief flashes of gamma-rays and are considered to be the most energetic explosive phenomena in the Universe(1). The emission from GRBs comprises a short (typically tens of seconds) and bright prompt emission, followed by a much longer afterglow phase. During the afterglow phase, the shocked outflow-produced by the interaction between the ejected matter and the circumburst medium-slows down, and a gradual decrease in brightness is observed(2). GRBs typically emit most of their energy via.-rays with energies in the kiloelectronvolt-to-megaelectronvolt range, but a few photons with energies of tens of gigaelectronvolts have been detected by space-based instruments(3). However, the origins of such high-energy (above one gigaelectronvolt) photons and the presence of very-high-energy (more than 100 gigaelectronvolts) emission have remained elusive(4). Here we report observations of very-high-energy emission in the bright GRB 180720B deep in the GRB afterglow-ten hours after the end of the prompt emission phase, when the X-ray flux had already decayed by four orders of magnitude. Two possible explanations exist for the observed radiation: inverse Compton emission and synchrotron emission of ultrarelativistic electrons. Our observations show that the energy fluxes in the X-ray and gamma-ray range and their photon indices remain comparable to each other throughout the afterglow. This discovery places distinct constraints on the GRB environment for both emission mechanisms, with the inverse Compton explanation alleviating the particle energy requirements for the emission observed at late times. The late timing of this detection has consequences for the future observations of GRBs at the highest energies. Y1 - 2019 U6 - https://doi.org/10.1038/s41586-019-1743-9 SN - 0028-0836 SN - 1476-4687 VL - 575 IS - 7783 SP - 464 EP - + PB - Nature Publ. Group CY - London ER - TY - GEN A1 - Best, Robert B. A1 - Zheng, Wenwei A1 - Borgia, Alessandro A1 - Buholzer, Karin A1 - Borgia, Madeleine B. A1 - Hofmann, Hagen A1 - Soranno, Andrea A1 - Nettels, Daniel A1 - Gast, Klaus A1 - Grishaev, Alexander A1 - Schuler, Benjamin T1 - Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water" T2 - Science N2 - Riback et al. (Reports, 13 October 2017, p. 238) used small-angle x-ray scattering (SAXS) experiments to infer a degree of compaction for unfolded proteins in water versus chemical denaturant that is highly consistent with the results from Forster resonance energy transfer (FRET) experiments. There is thus no "contradiction" between the two methods, nor evidence to support their claim that commonly used FRET fluorophores cause protein compaction. Y1 - 2018 U6 - https://doi.org/10.1126/science.aar7101 SN - 0036-8075 SN - 1095-9203 VL - 361 IS - 6405 PB - American Assoc. for the Advancement of Science CY - Washington ER - TY - JOUR A1 - Borgia, Alessandro A1 - Zheng, Wenwei A1 - Buholzer, Karin A1 - Borgia, Madeleine B. A1 - Schüler, Anja A1 - Hofmann, Hagen A1 - Soranno, Andrea A1 - Nettels, Daniel A1 - Gast, Klaus A1 - Grishaev, Alexander A1 - Best, Robert B. A1 - Schuler, Benjamin T1 - Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods JF - Journal of the American Chemical Society N2 - There has been a long-standing controversy regarding the effect of chemical denaturants on the dimensions of unfolded and intrinsically disordered proteins: A wide range of experimental techniques suggest that polypeptide chains expand with increasing denaturant concentration, but several studies using small-angle X-ray scattering (SAXS) have reported no: such increase of the radius of gyration (R-g). This inconsistency challenges our current understanding of the mechanism of chemical denaturants, which are widely employed to investigate protein folding and stability. Here, we use a combination Of single-molecule Forster resonance energy transfer (FRET), SAXS, dynamic light scattering (DLS), and two-focus fluorescence correlation spectroscopy (2f-FCS) to characterize the denaturant dependence of the unfolded state of the spectrin domain R17 and the intrinsically disordered protein ACTR in two different denaturants. Standard analysis of the primary data clearly indicates an expansion of the unfolded state with increasing denaturant concentration irrespective of the protein, denaturant, or experimental method used. This is the first case in which SAXS and FRET have yielded even qualitatively consistent results regarding expansion in denaturant when applied to the same proteins. To more directly illustrate this self-consistency, we used both SAXS and FRET data in a Bayesian procedure to refine structural ensembles representative of the observed unfolded state. This analysis demonstrates that both of these experimental probes are compatible with a common ensemble of protein configurations for each denaturant concentration. Furthermore, the resulting ensembles reproduce the trend of increasing hydrodynamic radius, with denaturant concentration obtained by 2f-FCS,and DLS. We were thus able to reconcile the results from all four experimental techniques quantitatively, to obtain a comprehensive structural picture of denaturant;induced unfolded state expansion, and to identify the Most likely sources of earlier discrepancies. Y1 - 2016 U6 - https://doi.org/10.1021/jacs.6b05917 SN - 0002-7863 VL - 138 SP - 11714 EP - 11726 PB - American Chemical Society CY - Washington ER - TY - BOOK A1 - Finkelmann, B. A1 - Hofmann, H. A1 - Koch, Uwe A1 - Telschow, Stephan T1 - 10 Jahre Projekt "Sport mit Aussiedlern" BT - Zehn Jahre Projekt "Sport mit Aussiedlern" Y1 - 1998 PB - Deutscher Sportbund CY - Frankfurt am Main ER - TY - JOUR A1 - Nettels, Daniel A1 - Müller-Späth, Sonja A1 - Küster, Frank A1 - Hofmann, Hagen A1 - Haenni, Domminik A1 - Rüegger, Stefan A1 - Reymond, Luc A1 - Hoffmann, Armin S. A1 - Kubelka, Jan A1 - Heinz, Benjamin A1 - Gast, Klaus A1 - Best, Robert B. A1 - Schuler, Benjamin T1 - Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins N2 - We used single-molecule FRET in combination with other biophysical methods and molecular simulations to investigate the effect of temperature on the dimensions of unfolded proteins. With singlemolecule FRET, this question can be addressed even under nearnative conditions, where most molecules are folded, allowing us to probe a wide range of denaturant concentrations and temperatures. We find a compaction of the unfolded state of a small cold shock protein with increasing temperature in both the presence and the absence of denaturant, with good agreement between the results from single-molecule FRET and dynamic light scattering. Although dissociation of denaturant from the polypeptide chain with increasing temperature accounts for part of the compaction, the results indicate an important role for additional temperaturedependent interactions within the unfolded chain. The observation of a collapse of a similar extent in the extremely hydrophilic, intrinsically disordered protein prothymosin suggests that the hydrophobic effect is not the sole source of the underlying interactions. Circular dichroism spectroscopy and replica exchange molecular dynamics simulations in explicit water show changes in secondary structure content with increasing temperature and suggest a contribution of intramolecular hydrogen bonding to unfolded state collapse. Y1 - 2009 UR - http://www.pnas.org/content/106/49/20740.full.pdf+html SN - 0027-8424 ER - TY - CHAP A1 - Bilitewski, Ursula A1 - Kaba, H. A1 - Heilmann, Katja A1 - Mayer, Yvonne A1 - Hofmann, B. A1 - Mueller, P. A1 - van den Heuvel, J. T1 - Monoclonal antibodies against specific peptides derived from the 1,3-beta-glucosyltransferase Bgl2p allow detection of Candida albicans cells T2 - Mycoses : diagnosis, therapy and prophylaxis of fungal diseases Y1 - 2013 SN - 0933-7407 VL - 56 IS - 1 SP - 27 EP - 27 PB - Wiley-Blackwell CY - Hoboken ER - TY - JOUR A1 - Föllmi, Karl B. A1 - Hofmann, Helene A1 - Chiaradia, Massimo A1 - de Kaenel, Eric A1 - Frijia, Gianluca A1 - Parente, Mariano T1 - Miocene phosphate-rich sediments in Salento (southern Italy) JF - Sedimentary geology : international journal of applied and regional sedimentology N2 - The upper Middle to lower Upper Miocene (Serravallian to Tortonian) sedimentary succession in Salento (southern Italy) includes glauconite- and phosphate-rich deposits, which are associated with pelagic micrite. In Baia del Ciolo and Marittima (southern Salento), the succession is composed of shallow-water platform carbonates of Late Oligocene age (Chattian; Porto Badisco Formation), which are overlain by a 20- to 30-cm-thick level of glauconite-rich micrite with abundant reworked particles and fossils of the underlying Porto Badisco Formation. This interval is in turn covered by an up to 15 cm thick phosphatic crust ("Livello ad Aturia"), which itself is overlain either by a hemipelagic chalk-like carbonate of Middle to Late Miocene age ("Pietra Leccese"; Marittima) or directly by a micrite of Late Miocene age (Messinian; Novaglie Formation; Baia del Ciolo), which shallows upwards into a shallow-water platform carbonate. A large hiatus is present in this succession, which likely includes the Lower and lower Middle Miocene. In the region of Lecce, two discrete levels enriched in glauconite and phosphate-each associated with a major discontinuity-occur within the Pietra Leccese. The strontium-isotope ages derived on phosphate nodules and phosphatized and non-phosphatized fossils and calcareous nannofossil ages indicate a time interval of phosphogenesis between 13.5 and 7.5 Ma, with two clusters at 12 and 10.5 Ma. The glauconite and phosphate-rich sediments resulted from a current-dominated regime, which was characterized by low overall sedimentation rates, erosion and sediment reworking, and authigenesis. This regime was likely related to a generally westward-directed bottom current, which was forced to upwell once it arrived at the western border of the eastern Mediterranean basin. The timing of the principal phosphogenic phases can only partly be correlated to those of other occurrences in this part of the Mediterranean (Malta, Gozo, southern Sicily, Matese, Latium-Abruzzi platform). The partial diachrony in phosphogenesis may express the effect of lateral switching in and/or focusing of upwelling zones. (C) 2015 Elsevier B.V. All rights reserved. KW - Miocene KW - Salento KW - Italy KW - Phosphogenesis KW - Paleoceanography Y1 - 2015 U6 - https://doi.org/10.1016/j.sedgeo.2015.07.009 SN - 0037-0738 SN - 1879-0968 VL - 327 SP - 55 EP - 71 PB - Elsevier CY - Amsterdam ER - TY - GEN A1 - Moser, Othmar A1 - Mueller, Alexander A1 - Tschakert, Gerhard A1 - Koehler, Gerd A1 - Lawrence, Jimmy B. A1 - Groeschl, Werner A1 - Pieber, Thomas R. A1 - Bracken, Richard M. A1 - Hofmann, Peter T1 - Exercise Prescription in Type 1 Diabetes: Should We Use Percentages of Maximum Heart Rate? T2 - Medicine and science in sports and exercise : official journal of the American College of Sports Medicine Y1 - 2017 U6 - https://doi.org/10.1249/01.mss.0000519798.35679.cf SN - 0195-9131 SN - 1530-0315 VL - 49 SP - 1020 EP - 1020 PB - Lippincott Williams & Wilkins CY - Philadelphia ER - TY - JOUR A1 - Briesemeister, Benny B. A1 - Hofmann, Markus J. A1 - Kuchinke, Lars A1 - Jacobs, Arthur M. T1 - The BAWL databases in research on emotional word processing JF - Potsdam cognitive science series N2 - Inhalt: Introduction A two-dimensional affective space: Valence and arousal effects in word processing Higher dimensional affective space: a role of discrete emotions in word processing? A direct comparison of the affective space models References Y1 - 2012 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-62377 SN - 2190-4545 SN - 2190-4553 IS - 3 SP - 61 EP - 66 PB - Universitätsverlag Potsdam CY - Potsdam ER - TY - BOOK A1 - Baayen, Rolf Harald A1 - Kresse, Lara A1 - Kirschner, Stefan A1 - Dipper, Stefanie A1 - Belke, Eva A1 - Keuleers, Emmanuel A1 - Brysbaert, Marc A1 - New, Boris A1 - Heister, Julian A1 - Kliegl, Reinhold A1 - Zinsmeister, Heike A1 - Smolka, Eva A1 - Briesemeister, Benny B. A1 - Hofmann, Markus J. A1 - Kuchinke, Lars A1 - Jacobs, Arthur M. ED - Würzner, Kay-Michael ED - Pohl, Edmund T1 - Lexical resources in psycholinguistic research N2 - Experimental and quantitative research in the field of human language processing and production strongly depends on the quality of the underlying language material: beside its size, representativeness, variety and balance have been discussed as important factors which influence design, analysis and interpretation of experiments and their results. This volume brings together creators and users of both general purpose and specialized lexical resources which are used in psychology, psycholinguistics, neurolinguistics and cognitive research. It aims to be a forum to report experiences and results, review problems and discuss perspectives of any linguistic data used in the field. N2 - Experimentelle und quantitative Forschung im Bereich der menschlichen Sprachverarbeitung und -produktion hängt wesentlich von der Qualität des zugrundeliegenden Sprachmaterials ab: Neben dessen Umfang wurden auch Repräsentativität, Vielfalt und Ausgewogenheit als wichtige Einflüsse auf Design, Analyse und Interpretation entsprechender Experimente und deren Ergebnisse diskutiert. Der vorliegende Band enthält Arbeiten von Entwicklern und Anwendern sowohl allgemeiner als auch spezialisierter lexikalischer Ressourcen aus den Bereichen Psychologie, Psycho-, Neurolinguistik und Kongitionswissenschaften. Ziel ist es anhand der dargestellten Ergebnisse Probleme und Perspektiven bei der Arbeit mit linguistischen Daten aufzuzeigen. T3 - Potsdam Cognitive Science Series - 3 KW - Psychologie KW - Psycholinguistik KW - Kognitionswissenschaften KW - lexikalische Datenbanken KW - menschliche Sprachverarbeitung KW - Worterkennung KW - Psychology KW - psycholinguistics KW - cognitive sciences KW - lexical databases KW - human language processing KW - word recognition Y1 - 2012 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-59100 SN - 978-3-86956-178-3 SN - 2190-4545 SN - 2190-4553 PB - Universitätsverlag Potsdam CY - Potsdam ER -