@article{ArendsSebald1984,
  author    = {Arends, H. and Sebald, Walter},
  title     = {Nucleotide sequence of the cloned mRNA and gene of the ADP/ATP carrier from Neurospora crassa},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62684},
  year      = {1984},
  abstract  = {A cDNA complementary to the mRNA of the ADPIATP carrier from Neurospora crassa was identified among ordered cDNA clones by hybridizing total polyadenylated RNA to pools of 96 cDNA recombinant plasmids and subsequent cellfree translation of hybridization-selected mRNA. Further carrier cDNAs were found by colony fdter hybridization at a frequency of 0.2-0.3\%. The gene of the carrier was cloned and isolated on a 4.6-kbp EcoRl fragment of total Neurospora DNA, and the start of the mRNA was determined by Sl nuclease mapping. From the nucleotide sequence of the cDNA and the genomic DNA, the primary structure of the gene, of the mRNA and of the ADP I ATP carrier protein could be deduced. The gene occurs in a single copy in the genome and related genes are absent. It contains two short introns, and a pyrimidine-rieb promoter region. The mRNA has a 46-bp 5 1 end and a 219-bp 3 1 end. There is an open reading frame coding for the 313 amino acid residues of the Neurospora carrier protein. The amino acid sequence is homologous in 148 positions with the established primary structure of the beef heart carrier.},
  subject      = {Biochemie},
  language  = {en}
}
@article{DemchukMuellerOschkinatetal.1994,
  author    = {Demchuk, E. and Mueller, T. and Oschkinat, H. and Sebald, Walter and Wade, R. C.},
  title     = {Receptor binding properties of four-helix-bundle growth factors deduced from electrostatic analysis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62424},
  year      = {1994},
  abstract  = {Hormones of the hematopoietin class mediate signal transduction by binding to specific transmembrane receptors. Structural data show that the human growth hormone (hGH) forms a complex with a homodimeric receptor and that hGH is a member of a class of hematopoietins possessing an antiparallel 4-a-helix bundle fold. Mutagenesis experiments suggest that electrostatic interactions may have an important influence on hormonereceptor recognition. In order to examine the specificity of hormone-receptor complexation, an analysis was made of the electrostatic potentials of hGH, interleukin-2 (IL-2), interleukin-4 (IL-4), granulocyte colony-stimulating factor (G-CSF), granulocyte-macrophage colony-stimulating factor (GM-CSF), and the hGH and IL-4 receptors. The binding surfaces of hGH and its receptor, and of IL-4 and its receptor, show complementary electrostatic potentials. The potentials of the hGH and its receptor display approximately 2-fold rotational symmetry because the receptor subunits are identical. In contrast, the potentials of GM-CSF and IL-2 Iack such symmetry, consistent with their known high affinity for hetero-oligomeric receptors. Analysis of the electrostatic potentials supports a recently proposed hetero-oligomeric model for a high-affinity IL-4 receptor and suggests a possible new receptor binding mode for G-CSF; it also provides valuable information for guiding structural and mutagenesis studies of signal-transducing proteins and their receptors.},
  subject      = {Biochemie},
  language  = {en}
}
@article{DummerPosseckertNestleetal.1992,
  author    = {Dummer, R. and Posseckert, G. and Nestle, F. and Witzgall, R. and Burger, M. and Becker, J. C. and Sch{\"a}fer, E. and Wiede, J. and Sebald, Walter and Burg, G.},
  title     = {Soluble interleukin-2 receptors inhibit interleukin 2-dependent proliferation and cytotoxicity: explanation for diminished natural killer cell activity in cutaneous T-cell lymphomas in vivo?},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62473},
  year      = {1992},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{DuschlJahnBertlingetal.1992,
  author    = {Duschl, Albert and Jahn, Ute and Bertling, Claudia and Sebald, Walter},
  title     = {A comparison of assays for the response of primary human T-cells upon stimulation with interleukin-2, interleukin-4 and interleukin-7},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-86750},
  year      = {1992},
  abstract  = {The most commonly used assay to quantitate the response of peripheral T~cells upon stimulation with growth factors is determination of incorporated (JH]TdR. We compared thls test to three other methods: 1. direct countlog of cells with a Coulter type counter as reference assay, 2. a colorimetric assay using the tetrazolium dye 3-[ 4,S-dimethylthiazol-l-yl]-2,5diphenyl tetrazolium (MTT), which is a cheap and increasingly popular non-radioactive method and 3. incorporation of the thymidine analog 5-bromo-2'-deoxyuridine detection with a monoclonal antibody on cytospins. Primary human PHA-blasts from >30 healthy individuals were stimulated with IL-2, IL-4 aod IL-7 and assayed with up to four different methods. We discuss the advantages and disadvantages of the assays used and tbe effects of differences between cell preparations. We observed no significant variations between individuals for the dose dependence, but the relative emctency of IL4 compared to IL-2 and IL-7 was variable. This was probably due to the slower response observed upon stimulation with this factor.},
  subject      = {T-Lymphozyt},
  language  = {en}
}
@article{FlueggeFischerGrossetal.1989,
  author    = {Fl{\"u}gge, U. I. and Fischer, K. and Gross, A. and Sebald, Walter and Lottspeich, F. and Eckerskorn, C.},
  title     = {The triose phosphate-3-phosphoglycerate-phosphate translocator from spinach chloroplasts: nucleotide sequence of a full-length cDNA clone and import of the in vitro synthesized precursor protein into chloroplasts},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62559},
  year      = {1989},
  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{GabelliniSebald1986,
  author    = {Gabellini, N. and Sebald, Walter},
  title     = {Nucleotide sequence and transcription of the fbc operon from Rhodopseudomonas sphaeroides. Evaluation of the deduced amino acid sequences of the FeS protein, cytochrome b and cytochrome c\(_1\)},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62615},
  year      = {1986},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{GrafSebald1978,
  author    = {Graf, T. and Sebald, Walter},
  title     = {The dicyclohexylcarbodiimide-binding protein of the mitochondrial ATPase complex from beef heart. Isolation and amino acid composition},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62806},
  year      = {1978},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{HarnischWeissSebald1985,
  author    = {Harnisch, U. and Weiss, H. and Sebald, Walter},
  title     = {The primary structure of the iron-sulfur subunit of ubiquinol-cytochrome c reductase from Neurospora, determined by cDNA and gene sequencing},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62631},
  year      = {1985},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{HarthKotzschHuetal.2010,
  author    = {Harth, Stefan and Kotzsch, Alexander and Hu, Junli and Sebald, Walter and Mueller, Thomas D.},
  title     = {A Selection Fit Mechanism in BMP Receptor IA as a Possible Source for BMP Ligand-Receptor Promiscuity},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-68497},
  year      = {2010},
  abstract  = {Background: Members of the TGF-b superfamily are characterized by a highly promiscuous ligand-receptor interaction as is readily apparent from the numeral discrepancy of only seven type I and five type II receptors available for more than 40 ligands. Structural and functional studies have been used to address the question of how specific signals can be deduced from a limited number of receptor combinations and to unravel the molecular mechanisms underlying the protein-protein recognition that allow such limited specificity. Principal Findings: In this study we have investigated how an antigen binding antibody fragment (Fab) raised against the extracellular domain of the BMP receptor type IA (BMPR-IA) recognizes the receptor's BMP-2 binding epitope and thereby neutralizes BMP-2 receptor activation. The crystal structure of the complex of the BMPR-IA ectodomain bound to the Fab AbD1556 revealed that the contact surface of BMPR-IA overlaps extensively with the contact surface for BMP-2 interaction. Although the structural epitopes of BMPR-IA to both binding partners coincides, the structures of BMPR-IA in the two complexes differ significantly. In contrast to the structural differences, alanine-scanning mutagenesis of BMPR-IA showed that the functional determinants for binding to the antibody and BMP-2 are almost identical. Conclusions: Comparing the structures of BMPR-IA bound to BMP-2 or bound to the Fab AbD1556 with the structure of unbound BMPR-IA shows that binding of BMPR-IA to its interaction partners follows a selection fit mechanism, possibly indicating that the ligand promiscuity of BMPR-IA is inherently encoded by structural adaptability. The functional and structural analysis of the BMPR-IA binding antibody AbD1556 mimicking the BMP-2 binding epitope may thus pave the way for the design of low-molecular weight synthetic receptor binders/inhibitors.},
  subject      = {Physiologische Chemie},
  language  = {en}
}