@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{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}
}
@article{VeloursEsparzaHoppeetal.1984,
  author    = {Velours, J. and Esparza, M. and Hoppe, J. and Sebald, Walter and Guerin, B.},
  title     = {Amino acid sequence of a new mitochondrially synthesized proteolipid of the ATP synthase of Saccharomyces cerevisiae},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62695},
  year      = {1984},
  abstract  = {The purification and the amino acid sequence of a proteolipid translated on ribosomes in yeast mitochondria is reported. This protein, which is a subunit of the A TP synthase, was purified by extraction with chloroform/methanol (2/1) and subsequent chromatography on phosphocellulose and reverse phase h.p.l.c. A mol. wt. of 5500 was estimated by chromatography on Bio-Gel P-30 in 8011/o fonnie acid. The complete amino acid sequence of this protein was determined by automated solid phase Edman degradation of the whole protein and of fragments obtained after cleavage with cyanogen bromide. The sequence analysis indicates a length of 48 amino acid residues. The calculated mol. wt. of 5870 corresponds to the value found by gel chromatography. This polypeptide contains three basic residues and no negatively charged side chain. The three basic residues are clustered at the C terminus. The primary structure of this protein is in full agreement with the predicted amino acid sequence of the putative polypeptide encoded by the mitochondrial aap1 gene recently discovered in Saccharomyces cerevisiae. Moreover, this protein shows 5011/o homology with the amino acid sequence of a putative polypeptide encoded by an unidentified reading frame also discovered near the mitochondrial ATPase subunit 6 genein Aspergillus nidulans.},
  subject      = {Biochemie},
  language  = {en}
}
@article{HoppeSebald1980,
  author    = {Hoppe, J. and Sebald, Walter},
  title     = {Amino acid sequence of the proteolipid subunit of the proton-translocating ATPase complex from the thermophilic bacterium PS-3},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62754},
  year      = {1980},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{MuellerSebaldOschkinat1994,
  author    = {M{\"u}ller, T. and Sebald, Walter and Oschkinat, H.},
  title     = {Antagonist design through forced electrostatic mismatch},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62408},
  year      = {1994},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{MuellerDieckmannSebaldetal.1994,
  author    = {M{\"u}ller, T. and Dieckmann, T. and Sebald, Walter and Oschkinat, H.},
  title     = {Aspects of receptor binding and signalling of interleukin-4 investigated by site-directed mutagenesis and NMR spectroscopy},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62444},
  year      = {1994},
  abstract  = {Cytokines are hormones that carry information from ceJI to ceH. This information is read from their surface upon binding to transmembrane receptors and by the subsequent initiation of receptor oligomerization. An inftuence on this process through mutagenesis on the hormone surface is highly desirab)e for medical reasons. However, an understanding of hormone-receptor interactions requires insight into the structural changes introduced by the mutations. In this line structural studies on human TL-4 and the medically important IL-4 antagonists YI24D and Y124G are presented. The site a.round YI24 is an important epitope responsible for the a.bility of 11-4 t.o ca.use a signal in the target cells. It is shown that the local main-chain structure around residue 124 in the variants remains unchanged. A strategy is presented here which allows the study of these types of proteins and their variants by NMR which does not require carbon Iabeiied sa.mples.},
  subject      = {Biochemie},
  language  = {en}
}
@article{vonJagowSebald1980,
  author    = {von Jagow, Gerhard and Sebald, Walter},
  title     = {b-Type cytochromes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-47383},
  year      = {1980},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{Sebald1977,
  author    = {Sebald, Walter},
  title     = {Biogenesis of mitochondrial ATPase},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-47362},
  year      = {1977},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{SebaldWernerWeiss1979,
  author    = {Sebald, Walter and Werner, S and Weiss, H},
  title     = {Biogenesis of mitochondrial membrane proteins in Neurospora crassa},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-82055},
  year      = {1979},
  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}
}