@article{SebaldMachleidtWachter1980,
  author    = {Sebald, Walter and Machleidt, Werner and Wachter, Elmar},
  title     = {N,N'-dicyclohexylcarbodiimide binds specifically to a single glutamyl residue of the proteolipid subunit of the mitochondrial adenosinetriphosphatases from Neurospora crassa and Saccharomyces cerevisiae},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-47394},
  year      = {1980},
  abstract  = {T~e N,N'-dicrclohexylcarbodiimide-binding proteolipid subumt of the mitochondrial adenosinetriphosphatases (ATP phosphohydrolase, EC 3.6.1.3) of Neurosporacrassa and Saccharomyces cerevisiae were purified from mitochondria incubated with the radioactively labeled inhibitor. The specifically labeled subunit was cleaved with cyanogen bromide and N-bromosuccinimide, and the resultant fragments were separated by gel chromatography in the presence of 80\% (vol/vol) formic acid. The N,N'-dicyclohexylcarbodiimide label was recovered in each organism exclusively in a 17-residue fragment. Further analysis by automated solid-phase Edman degrada.ti.on revealed tha~ the bound label was present at only one positIOn, correspondmg to a glutamyl residue. The NN'~ icyc~ohexyl~a~bodiiJ?1~de-'!l0dified glutamyl residue is the ~nly Id~ntIcal aCidic posItIon m both proteins and occurs in the middle of a hydrophobic sequence of about 25 residues.},
  subject      = {Dicyclohexylcarbodiimid},
  language  = {en}
}
@article{WeigelMeyerSebald1989,
  author    = {Weigel, U. and Meyer, M. and Sebald, Walter},
  title     = {Mutant proteins of human interleukin 2. Renaturation yield, proliferative activity and receptor binding},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62543},
  year      = {1989},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{ViebrockPerzSebald1983,
  author    = {Viebrock, A and Perz, A and Sebald, Walter},
  title     = {Molecular cloning of middle-abundant mRNAs from Neurospora crassa},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-82033},
  year      = {1983},
  abstract  = {no abstract available},
  subject      = {Neurospora crassa},
  language  = {en}
}
@article{KleenePfannerPfalleretal.1987,
  author    = {Kleene, R. and Pfanner, N. and Pfaller, R. and Link, T. A. and Sebald, Walter and Neupert, W. and Tropschug, M.},
  title     = {Mitochondrial porin of Neurospora crassa: cDNA cloning, in vitro expression and import into mitochondria},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62566},
  year      = {1987},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{TzagoloffMacinoSebald1979,
  author    = {Tzagoloff, A. and Macino, G. and Sebald, Walter},
  title     = {Mitochondrial genes and translation products},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-47408},
  year      = {1979},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{SebaldWild1979,
  author    = {Sebald, Walter and Wild, G.},
  title     = {Mitochondrial ATPase complex from Neurospora crassa},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-82065},
  year      = {1979},
  abstract  = {The A TPase eomplex has been isolated from mitoehondria of N eurospora crassa by immunologieal teehniques. The protein ean be obtained rapidly and qua ntitatively in high purity by miero- or large-seale immunopreeipitation. Immunopreeipitation has been applied to labeled and doubly labeled mitoehondrial proteins in order to investigate the number and moleeular weights of subunit polypeptides , the site of synthesis of subunit polypeptides, and the dieycIohexyIcarbodiimide-binding protein . The A TPase complex obtained by large-seale immunopreeipitation has been used as starting ma terial for the isolation of hydrophobie polypeptides.},
  subject      = {Biochemie},
  language  = {en}
}
@article{HoppeGattiWeberetal.1986,
  author    = {Hoppe, J. and Gatti, D. and Weber, H. and Sebald, Walter},
  title     = {Labeling of individual amino acid residues in the membrane-embedded F\(_0\) part of the F\(_1\) F\(_0\) ATP synthase from Neurospora crassa. Influence of oligomycin and dicyclohexylcarbodiimide},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62598},
  year      = {1986},
  abstract  = {Three F0 subunits and the F\(_1\) subunit P of the ATP synthase from Neurospora crassa were labeled with the lipophilic photoactivatable reagent 3-(trifluoromethyl)-3-(m-[\(^{125}\)I]iodophenyl)diazirine ([\(^{125}\)I]TID). In the proteolipid subunit which was the most heavily labeled polypeptide labeling was confmed to five residues at the NH2-terminus and five residues at the C-terminus ofthe protein. Labeling occurred at similar positions compared with the homologaus protein (subunit c) in the ATP synthase from Escherichia coli, indicating a similar structure of the proteolipid subunits in their respective organisms. The inhibitors oligomycin and dicyclohexylcarbodiimide did not change the pattern of accessible surface residues in the proteolipid, suggesting that neither inhibitor induces gross conformational changes. However, in the presence of oligomycin, the extent oflabeling in some residues was reduced. Apparently, these residues provide part of the binding site for the inhibitor. After reaction with dicyclohexylcarbodiimide an additional labeled amino acid was found at position 65 corresponding to the invariant carbod{\"u}mide-binding glutamic acid. These results and previous observations indicate that the carboxyl side chain of Glu-65 is located at the protein-lipid interphase. The idea is discussed that proton translocation occurs at the interphase between different types if F\(_0\) subunits. Dicyclohexylcarbodiimide or oligomycin might disturb this essential interaction between the F\(_0\) subunits.},
  subject      = {Biochemie},
  language  = {en}
}
@article{LindenmaierDittmarHauseretal.1985,
  author    = {Lindenmaier, W. and Dittmar, K. E. and Hauser, H. and Necker, A. and Sebald, Walter},
  title     = {Isolation of a functional human interleukin 2 gene from a cosmid library by recombination in vivo},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62662},
  year      = {1985},
  abstract  = {A method has been developed that allows the isolation of genomic clones from a cosmid library by homologaus recombination in vivo. This method was used to isolate a human genomic interleukin 2 (IL2) gene. The genomic cosmid library was packaged in vivo into A. phage particles. A recombination-proficient host strain carrying IL2 cDNA sequences in a non-homologaus plasmid vector was infected by the packaged cosmid library. After in vivo packaging and reinfection, recombinants carrying the antibiotic resistance genes of both vectors were selected. From a recombinant cosmid clone the chromosomal IL2 genewas restored. After DNA mediated gene transfer into mouse Ltk- cells human IL2 was expressed constitutively.},
  subject      = {Biochemie},
  language  = {en}
}
@article{SebaldArendsMcCarthy1984,
  author    = {Sebald, Walter and Arends, Hermann and McCarthy, John E. G.},
  title     = {Isolation and manipulation of genes coding for energy-transducing enzymes from Neurospora crassa and Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-86768},
  year      = {1984},
  abstract  = {No abstract available.},
  subject      = {Escherichia coli},
  language  = {en}
}
@article{SebaldNeupertBirkmayer1970,
  author    = {Sebald, Walter and Neupert, W. and Birkmayer, G. D.},
  title     = {Internal and external contributions to the biogenesis of mitochondrial proteins},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62876},
  year      = {1970},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{LehrnbecherPootOrschescheketal.1994,
  author    = {Lehrnbecher, T. and Poot, M. and Orscheschek, K. and Sebald, Walter and Feller, A. C. and Merz, H.},
  title     = {Interleukin 7 as interleukin 9 drives phytohemagglutinin-activated T cells through several cell cycles; no synergism between interleukin 7, interleukin 9 and interleukin 4},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62438},
  year      = {1994},
  abstract  = {The effects of the interlenkins IL-7 and IL-9 on cell cycle progression were investigated by conventional [3H]thymidine incorporation and by the bivariate BrdU/Hoechst technique. 8oth IL· 7 and IL-9 drive phytohemagglutinin-activated T cells through more than one cell cycle, but IL-7 wasmorepotent on cell cycle progression than IL-9. Neither synergistic nor inhibitory effects were seen between various combinations of the lymphokines IL-7, IL-9 and IL-4 compared to each lymphokine alone. When T cells are activated with phytohemagglutinin for 3 days, all or most IL-4 responsive cells respond to IL-7 as weil, whereas only a part of IL-7 responders are IL-4 responders. In contrast, when T cells are activated with phytohemagglutinin for 7 days, the quantitative data of the cell cycle distribution soggest that the population of IL-7 responders is at least an overlapping, if not a real subset of the population of the IL-4 responders.},
  subject      = {Biochemie},
  language  = {en}
}
@article{LehrnbecherMerzSebaldetal.1991,
  author    = {Lehrnbecher, T. and Merz, H. and Sebald, Walter and Poot, M.},
  title     = {Interleukin 4 drives phytohemagglutinin-activated T cells through several cell cycles: no synergism between interleukin 2 and interleukin 4},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62491},
  year      = {1991},
  abstract  = {Cell kinetic studies of T cells stimulated with the interleukin 2 (11-2), D-4, or both lymphokines were performed with conventional [3H] thymidine incorporation and with the bivariate BrdU/Hoechst technique. 11-2 and 11-4 are able to drive phytohemagglutininactivated T cells through more than one cell cycle. Neither synergistic nor inhibitory efl'ect on T -cell proliferationwas seen for the stimulation with both 11-2 and 11-4 as compared with the effect ofll-2 alone. The quantitative data ofthe cell cycle distribution ofphytohemagglutininactivated T cells suggestthat the population ofll-4-responsive cells is at least an overlapping population, if not a real subset of the ·population of the 11-2-responsive cells.},
  subject      = {Biochemie},
  language  = {en}
}
@article{SebaldWeissJackl1972,
  author    = {Sebald, Walter and Weiss, H. and Jackl, G.},
  title     = {Inhibition of the assembly of cytochrome oxidase in Neurospora crassa by chloramphenicol},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62852},
  year      = {1972},
  abstract  = {Cytochrome oxidasewas prepared from Neurospora crassa by chromatography on oleyl polymethacrylic acid resin and separated into seven polypeptides by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate. Incorporation oflabelled amino acids into the single polypeptideswas investigated after a pulse labelling in the absence and presence of chloramphenicol, and afterwashing out the inhibitor. Chloramphenicol (4 mg/ml) inhibited amino acid incorporation into all polypeptides 90-95\%• while labeHing of the whole membrane protein was inhibited only 30\%• Mter washing out the inhibitor and further growth of the cells. the four smaller polypeptides were highly labelled, whereas the other polypeptides showed only a. small increase in radioactivity. It is concluded that the four small-sized polypeptides of cytochrome oxidase are synthesized but not integrated into the functional enzyme under the action of chloramphenicol.},
  subject      = {Biochemie},
  language  = {en}
}
@article{SebaldHofstoetterHackeretal.1969,
  author    = {Sebald, Walter and Hofst{\"o}tter, T. and Hacker, D. and B{\"u}cher, T.},
  title     = {Incorporation of amino acids into mitochondrial protein of the flight muscle of Locusta migratoria in vitro and in vivo in the presence of cycloheximide},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62919},
  year      = {1969},
  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{KueblerReutherKirchneretal.1994,
  author    = {K{\"u}bler, N. and Reuther, J. and Kirchner, T. and Pfaff, M. and M{\"u}ller-Hermelink, H. K. and Albert, R. and Sebald, Walter},
  title     = {IgG monoclonal antibodies that inhibit osteoinductivity of human bone matrix-derived proteins (hBMP/NCP)},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62388},
  year      = {1994},
  abstract  = {Monoclonal hBMP/NCP (human bone morphogenetic protein anrl associaterl noncollagenous proteins) antiborlies of the lgG class were prorlucerl. In vitro, 12 of 19 hBMP/NCP antiborlies showerl functional inhibition of hBMP/ NCP-induced chondroneogenesis in a neonatal muscle tissue assay. Inducing factors were characterized by their inhibiting antibodies with immunoblotting. Several peptide factors seem to be involved in the cascade of inducerl chondro- and osteogenesis.},
  subject      = {Biochemie},
  language  = {en}
}
@article{JacklSebald1974,
  author    = {Jackl, G. and Sebald, Walter},
  title     = {Identification of two products of mitochondrial protein synthesis associated with oligomycin-sensitive ATPase from Neurospora crassa},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-82093},
  year      = {1974},
  abstract  = {no abstract available},
  subject      = {Physiologische Chemie},
  language  = {en}
}
@article{JacklSebald1975,
  author    = {Jackl, G. and Sebald, Walter},
  title     = {Identification of two products of mitochondrial protein synthesis associated with mitochondrial adenosine triphosphatase from Neurospora crassa},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62812},
  year      = {1975},
  abstract  = {Soluble mitochondrial ATPase (F1) isolated from Neurospora crassa is resolved by dodecylsulfate- gel electrophoresis into five polypeptide bands with apparent molecular weights of 59000, 55000, 36000, 15000 and 12000. At least nine further polypeptides remain associated with ATPase after disintegration of mitochondria with Triton X-100 as shown by the analysis of an immunoprecipitate obtained with antiserum to F 1 A TPase. Two of the associated polypeptides with apparent molecular weights of 19000 and 11000 are translated on mitochondrial ribosomes, as demonstrated by incorporation in vivo of radioactive leueine in the presence of specific inhibitors of mitochondrial (chloramphenicol) and extramitochondrial ( cycloheximide) protein synthesis. The appearance of mitochondrial translation products in the immunoprecipitated A TPase complex is inhibited by' cycloheximide. The same applies for some of the extramitochondrial translation products in the presence of chloramphenicol. This suggests that both types of polypeptides are necessary for the assembly of the A TPase complex.},
  subject      = {Biochemie},
  language  = {en}
}
@article{HoppeSchairerSebald1980,
  author    = {Hoppe, J. and Schairer, HU and Sebald, Walter},
  title     = {Identification of amino-acid substitutions in the proteolipid subunit of the ATP synthase from dicyclohexylcarbodiimide-resistant mutants of Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-47374},
  year      = {1980},
  abstract  = {The amino acid sequence of the proteolipid subunit of the A TP synthase was analyzed in six mutant strains from Escherichia coli K 12, selected for their increased resistance towards the inhibitor N,N'-dicyclohexylcarbodiimide. All six inhibitor-resistant mutants were found to be altered at the same position of the proteolipid, namely at the isoleucine at residue 28. Two substitutions could be identified. In type I this residue was substituted by a valine resulting in a moderate decrease in sensitivity to dicyclohexylcarbodiimide. Type II contained a threonine residue at this position. Here a strong resistance was observed. These two amino acid substitutions did not influence functional properties of the ATPase complex. ATPase as well as A TP-dependent proton-translocating activities of mutant membranes were indistinguishable from the wild type. At elevated concentrations, dicyclohexylcarbodiimide still bound specifically to the aspartic acid at residue 61 of the mutant proteolipid as in the wild type, and thereby inhibited the activity of the ATPase complex. It is suggested that the residue 28 substituted in the resistant mutants interacts with dicyclohexylcarbodiimide during the reactions leading to the covalent attachment of the inhibitor to the aspartic acid at residue 61. This could indicate that these two residues are in close vicinity and would thus provide a first hint on the functional conformation of the proteolipid. Its polypeptide chain would have to fold back to bring together these two residues separated by a segment of 32 residues.},
  subject      = {Biochemie},
  language  = {en}
}
@article{SebaldWachterTzagoloff1979,
  author    = {Sebald, Walter and Wachter, E. and Tzagoloff, A.},
  title     = {Identification of amino acid substitutions in the dicyclohexylcarbodiimide-binding subunit of the mitochondrial ATPase complex from oligomycin-resistant mutants of Saccharomyces cerevisiae},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62770},
  year      = {1979},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}