@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} }