@article{MerzFliednerLehrnbecheretal.1990,
  author    = {Merz, H. and Fliedner, A. and Lehrnbecher, T. and Sebald, Walter and M{\"u}ller-Hermelink, H. K. and Feller, A. C.},
  title     = {Cytokine expression in B-cell non-Hodgkin lymphomas},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62539},
  year      = {1990},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{MerzFliednerOrschescheketal.1991,
  author    = {Merz, H. and Fliedner, A. and Orscheschek, K. and Binder, T. and Sebald, Walter and M{\"u}ller-Hermelink, H. K. and Feller, A. C.},
  title     = {Cytokine expression in T-cell lymphomas and Hodgkin's disease. Its possible implication in autocrine or paracrine production as a potential basis for neoplastic growth},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62483},
  year      = {1991},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{MichelWachterSebald1979,
  author    = {Michel, R. and Wachter, E. and Sebald, Walter},
  title     = {Synthesis of a larger precursor for the proteolipid subunit of the mitochondrial ATPase complex of Neurospora crassa in a cell-free wheat germ system},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62789},
  year      = {1979},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{MuellerFiebigWeidaueretal.2013,
  author    = {Mueller, Thomas D. and Fiebig, Juliane E. and Weidauer, Stella E. and Qiu, Li-Yan and Bauer, Markus and Schmieder, Peter and Beerbaum, Monika and Zhang, Jin-Li and Oschkinat, Hartmut and Sebald, Walter},
  title     = {The Clip-Segment of the von Willebrand Domain 1 of the BMP Modulator Protein Crossveinless 2 Is Preformed},
  series = {Molecules},
  journal   = {Molecules},
  doi       = {10.3390/molecules181011658},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-97196},
  year      = {2013},
  abstract  = {Bone Morphogenetic Proteins (BMPs) are secreted protein hormones that act as morphogens and exert essential roles during embryonic development of tissues and organs. Signaling by BMPs occurs via hetero-oligomerization of two types of serine/threonine kinase transmembrane receptors. Due to the small number of available receptors for a large number of BMP ligands ligand-receptor promiscuity presents an evident problem requiring additional regulatory mechanisms for ligand-specific signaling. Such additional regulation is achieved through a plethora of extracellular antagonists, among them members of the Chordin superfamily, that modulate BMP signaling activity by binding. The key-element in Chordin-related antagonists for interacting with BMPs is the von Willebrand type C (VWC) module, which is a small domain of about 50 to 60 residues occurring in many different proteins. Although a structure of the VWC domain of the Chordin-member Crossveinless 2 (CV2) bound to BMP-2 has been determined by X-ray crystallography, the molecular mechanism by which the VWC domain binds BMPs has remained unclear. Here we present the NMR structure of the Danio rerio CV2 VWC1 domain in its unbound state showing that the key features for high affinity binding to BMP-2 is a pre-oriented peptide loop.},
  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{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{NeupertSebaldSchwabetal.1969,
  author    = {Neupert, W. and Sebald, Walter and Schwab, A. J. and Massinger, P. and B{\"u}cher, T.},
  title     = {Incorporation in vivo of \(^{14}\)C-labelled amino acids into the proteins of mitochondrial ribosomes from Neurospora crassa sensitive to cycloheximide and insensitive to Chloramphenicol},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62884},
  year      = {1969},
  abstract  = {Radioactive amino acids were incorporated in vivo into N eurospora crassa cells, and the mitochondrial ribosomes were isolated. The incorporation of radioactivity into the proteins of these ribosomes was inhibited by cycloheximide, but not by chloramphenicol. It is therefore concluded that these proteins are synthesized on the cycloheximide sensitive and chloramphenicol insensitive cytoplasmic ribosomes.},
  subject      = {Biochemie},
  language  = {en}
}
@article{NeupertSebaldSchwabetal.1969,
  author    = {Neupert, W. and Sebald, Walter and Schwab, A. J. and Pfaller, A. and B{\"u}cher, T.},
  title     = {Puromycin sensitivity of ribosomal label after incorporation of \(^{14}\)C-labelled amino acids into isolated mitochondria from Neurospora crassa},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62899},
  year      = {1969},
  abstract  = {Radioactive amino acids were incorporated into isolated mitochondria from Neurospora crassa. Then the mitochondrial ribosomes were isolated and submitted to density gradient centrifugation. A preferential labelling of polysomes was observed. However, when the mitochondrial suspension was treated with puromycin after amino acid incorporation, no radioactivity could be detected in either the monosomes or the polysomes. The conclusion is drawn that isolated mitochondria under these conditions do not incorporate significant amounts of amino acids into proteins of their ribosomes.},
  subject      = {Biochemie},
  language  = {en}
}
@article{OnoSonoyamaNemaetal.2014,
  author    = {Ono, Mitsuaki and Sonoyama, Wataru and Nema, Kazuki and Hara, Emilio Satoshi and Oida, Yasutaka and Pham, Hai Thanh and Yamamoto, Katushi and Hirota, Kazuo and Sugama, Kazushige and Sebald, Walter and Kuboki, Takuo},
  title     = {Regeneration of calvarial defects with Escherichia coli-derived rhBMP-2 adsorbed in PLGA membrane},
  series = {Cells Tissues Organs},
  volume    = {198},
  journal   = {Cells Tissues Organs},
  number    = {5},
  issn      = {1422-6405},
  doi       = {10.1159/000356947},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-196680},
  pages     = {367 -- 376},
  year      = {2014},
  abstract  = {Objective: Escherichia coli-derived recombinant human bone morphogenetic protein-2 (E-BMP-2) has been shown to be as effective as mammalian cell-derived BMP-2. However, several in vitro and in vivo experiments are still necessary to validate the effectiveness of E-BMP-2 due to the difference in synthesis process, mainly related to protein nonglycosylation. The objective of this study was to investigate whether biodegradable polylactide-co-glycolide (PLGA) membrane is a suitable carrier for E-BMP-2 delivery for bone regeneration of critical-sized defects in rat calvaria. Materials and Methods: First, the osteoinductive effect of E-BMP-2 was confirmed in vitro in mouse bone marrow stromal cells by analysis of osteocalcin mRNA levels, and calcium deposition was detected by alizarin red staining. Before in vivo experiments, the release profile of E-BMP-2 from PLGA membranes was determined by ELISA. E-BMP-2 (0, 1, 5 and 10 μg/μl) was applied for ectopic and orthotopic bone formation and was analyzed by X-ray, micro-CT and histology. Results: Release-profile testing showed that PLGA membrane could retain 94\% of the initially applied E-BMP-2. Ectopic bone formation assay revealed that combination of E-BMP-2/PLGA membrane strongly induced bone formation. Stronger osteoinductivity with complete repair of critical-sized defects was observed only with PLGA membranes adsorbed with 5 and 10 μg/μl of E-BMP-2, whereas no bone formation was observed in the groups that received no membrane or 0-μg/μl dose of E-BMP-2. Conclusion: PLGA membrane was shown to be a suitable carrier for sustained release of E-BMP-2, and the E-BMP-2/PLGA membrane combination was demonstrated to be efficient in bone regeneration in a model of critical-sized defects.},
  language  = {en}
}
@article{ReuschArnoldHeusseretal.1994,
  author    = {Reusch, P. and Arnold, S. and Heusser, C. and Wagner, K. and Weston, B. and Sebald, Walter},
  title     = {Neutralizing monoclonal antibodies define two different functional sites in human interleukin-4},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62418},
  year      = {1994},
  abstract  = {Human interleukin-4 (IL-4) is a small four-helix-bundle protein which is essential for organizing defense reactions against macroparasites, in particular helminths. Human IL-4 also appears to exert a pathophysiological role during various IgE-mediated allergic diseases. Seven different monoclonal antibodies neutralizing the activity of human IL-4 were studied in order to identify functionally important epitopes. A collection of 41 purified IL-4 variants was used to analyse how defined amino acid replacements affect binding affinity for each individual mAb. Specific amino acid positions could be assigned to four different epitopes. mAbs recognizing epitopes on helix A and/or C interfered with IL-4 receptor binding and thus inhibited IL-4 function. However, other mAbs also inhibiting IL-4 function recognized an epitope on helix D of IL-4 and did not inhibit IL-4 binding to the receptor protein. One mAb, recognizing N-terminal and C-terminal residues, partially competed for binding to the receptor. The results of these mAb epitope analyses confirm and extend previous data on the functional consequences of the amino acid replacements which showed that amino acid residues in helices A and C of IL-4 provide a binding site for the cloned IL-4 receptor and that a signalling site in helix D interacts with a further receptor protein.},
  subject      = {Biochemie},
  language  = {en}
}