@article{PostemaHoogmanAmbrosinoetal.2021,
  author    = {Postema, Merel C. and Hoogman, Martine and Ambrosino, Sara and Asherson, Philip and Banaschewski, Tobias and Bandeira, Cibele E. and Baranov, Alexandr and Bau, Claiton H.D. and Baumeister, Sarah and Baur-Streubel, Ramona and Bellgrove, Mark A. and Biederman, Joseph and Bralten, Janita and Brandeis, Daniel and Brem, Silvia and Buitelaar, Jan K. and Busatto, Geraldo F. and Castellanos, Francisco X. and Cercignani, Mara and Chaim-Avancini, Tiffany M. and Chantiluke, Kaylita C. and Christakou, Anastasia and Coghill, David and Conzelmann, Annette and Cubillo, Ana I. and Cupertino, Renata B. and de Zeeuw, Patrick and Doyle, Alysa E. and Durston, Sarah and Earl, Eric A. and Epstein, Jeffery N. and Ethofer, Thomas and Fair, Damien A. and Fallgatter, Andreas J. and Faraone, Stephen V. and Frodl, Thomas and Gabel, Matt C. and Gogberashvili, Tinatin and Grevet, Eugenio H. and Haavik, Jan and Harrison, Neil A. and Hartman, Catharina A. and Heslenfeld, Dirk J. and Hoekstra, Pieter J. and Hohmann, Sarah and H{\o}vik, Marie F. and Jernigan, Terry L. and Kardatzki, Bernd and Karkashadze, Georgii and Kelly, Clare and Kohls, Gregor and Konrad, Kerstin and Kuntsi, Jonna and Lazaro, Luisa and Lera-Miguel, Sara and Lesch, Klaus-Peter and Louza, Mario R. and Lundervold, Astri J. and Malpas, Charles B and Mattos, Paulo and McCarthy, Hazel and Namazova-Baranova, Leyla and Nicolau, Rosa and Nigg, Joel T. and Novotny, Stephanie E. and Oberwelland Weiss, Eileen and O'Gorman Tuura, Ruth L. and Oosterlaan, Jaap and Oranje, Bob and Paloyelis, Yannis and Pauli, Paul and Picon, Felipe A. and Plessen, Kerstin J. and Ramos-Quiroga, J. Antoni and Reif, Andreas and Reneman, Liesbeth and Rosa, Pedro G.P. and Rubia, Katya and Schrantee, Anouk and Schweren, Lizanne J.S. and Seitz, Jochen and Shaw, Philip and Silk, Tim J. and Skokauskas, Norbert and Soliva Vila, Juan C. and Stevens, Michael C. and Sudre, Gustavo and Tamm, Leanne and Tovar-Moll, Fernanda and van Erp, Theo G.M. and Vance, Alasdair and Vilarroya, Oscar and Vives-Gilabert, Yolanda and von Polier, Georg G. and Walitza, Susanne and Yoncheva, Yuliya N. and Zanetti, Marcus V. and Ziegler, Georg C. and Glahn, David C. and Jahanshad, Neda and Medland, Sarah E. and Thompson, Paul M. and Fisher, Simon E. and Franke, Barbara and Francks, Clyde},
  title     = {Analysis of structural brain asymmetries in attention-deficit/hyperactivity disorder in 39 datasets},
  series = {Journal of Child Psychology and Psychiatry},
  volume    = {62},
  journal   = {Journal of Child Psychology and Psychiatry},
  number    = {10},
  doi       = {10.1111/jcpp.13396},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-239968},
  pages     = {1202 -- 1219},
  year      = {2021},
  abstract  = {Objective Some studies have suggested alterations of structural brain asymmetry in attention-deficit/hyperactivity disorder (ADHD), but findings have been contradictory and based on small samples. Here, we performed the largest ever analysis of brain left-right asymmetry in ADHD, using 39 datasets of the ENIGMA consortium. Methods We analyzed asymmetry of subcortical and cerebral cortical structures in up to 1,933 people with ADHD and 1,829 unaffected controls. Asymmetry Indexes (AIs) were calculated per participant for each bilaterally paired measure, and linear mixed effects modeling was applied separately in children, adolescents, adults, and the total sample, to test exhaustively for potential associations of ADHD with structural brain asymmetries. Results There was no evidence for altered caudate nucleus asymmetry in ADHD, in contrast to prior literature. In children, there was less rightward asymmetry of the total hemispheric surface area compared to controls (t = 2.1, p = .04). Lower rightward asymmetry of medial orbitofrontal cortex surface area in ADHD (t = 2.7, p = .01) was similar to a recent finding for autism spectrum disorder. There were also some differences in cortical thickness asymmetry across age groups. In adults with ADHD, globus pallidus asymmetry was altered compared to those without ADHD. However, all effects were small (Cohen's d from -0.18 to 0.18) and would not survive study-wide correction for multiple testing. Conclusion Prior studies of altered structural brain asymmetry in ADHD were likely underpowered to detect the small effects reported here. Altered structural asymmetry is unlikely to provide a useful biomarker for ADHD, but may provide neurobiological insights into the trait.},
  language  = {en}
}
@article{McCarthySebaldGrossetal.1986,
  author    = {McCarthy, J. E. and Sebald, Walter and Gross, G. and Lammers, R.},
  title     = {Enhancement of translational efficiency by the Escherichia coli atpE translational initiation region: its fusion with two human genes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62626},
  year      = {1986},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{GabelliniHarnischMcCarthyetal.1985,
  author    = {Gabellini, N. and Harnisch, U. and McCarthy, J. E. and Hauska, G. and Sebald, Walter},
  title     = {Cloning and expression of the fbc operon encoding the FeS protein, cytochrome b and cytochrome c\(_1\) from the Rhodopseudomonas sphaeroides b/c\(_1\) complex},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62642},
  year      = {1985},
  abstract  = {The gene for the FeS protein of the Rhodopseudomonas sphaeroides b/c1 complex was identified by means of crosshybridization with a segment of the gene encoding the corresponding FeS protein of Neurospora crassa. Plasmids (pRSF1-14) containing the cross-hybridizing region, covering in total 13.5 kb of chromosomal DNA, were expressed in vitro in a homologous system. One RSF plasmid directed the synthesis of all three main polypeptides of the R. sphaeroides blc1 complex: the FeS protein, cytochrome b and cytochrome c1• The FeS protein and cytochrome c1 were apparently synthesized as precursor fonns. None of the pRSF plasmids directed the synthesis of the 10-kd polypeptide found in b/c1 complex preparations. Partial sequencing of the cloned region was performed. Several sites of strong homology between R. sphaeroides and eukaryotic polypeptides of the b/c1 complex were identified. The genes encode the three b/c1 polypeptides in the order: (5') FeS protein, cytochrome b, cytochrome c1• The three genes are transcribed to give a polycistronic mRNA of 2.9 kb. This transcriptional unit has been designated the jbc operon; its coding capacity corresponds to the size of the polycistronic mRNA assuming that only the genes for the FeS protein (jbcF), cytochrome b (jbcß) and cytochrome c1 (jbcC) are present. This could indicate that these three subunits constitute the minimal catalytic unit of the b/c1 complex from photosynthetic membranes.},
  subject      = {Biochemie},
  language  = {en}
}
@article{McCarthySchairerSebald1985,
  author    = {McCarthy, J. E. and Schairer, H. U. and Sebald, Walter},
  title     = {Translational initiation frequency of atp genes from Escherichia coli: identification of an intercistronic sequence that enhances translation},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62657},
  year      = {1985},
  abstract  = {The c, b and {\"o} subunit genes of the Escherichia coli atp operon were cloned individually in an expression vector between the tac fusion promoter and the galK gene. The relative rates of subunit synthesis directed by the cloned genes were similar in vitro andin vivo and compared favourably with the subunit stoichiometry of the assembled proton-translocating A TP synthase of E. coli in vivo. The rate of synthesis of subunit c was at least six times that of subunit b and 18 times that of subunit {\"o}. Progressive shortening of the long intercistronic sequence lying upstream of the subunit c gene showed that maximal expression of this gene is dependent upon the presence of a sequence stretching > 20 bp upstream of the Shine-Dalgarno site. This sequence thus acts to enhance the rate of translational initiation. The possibility that similar sequences might perform the same function in other operons of E. coli and bacteriophage A is also discussed. Translation of the subunit b cistron is partially coupled to translation of the preceding subunit c cistron. In conclusion, the expression of all the atp operon genes could be adjusted to accommodate the subunit requirements of A TP synthase assembly primarily by means of mechanisms which control the efficiency of translational initiation and re-initiation at the respective cistron start codons.},
  subject      = {Biochemie},
  language  = {en}
}