@article{HoppeSchairerSebald1980,
  author    = {Hoppe, J. and Schairer, H. U. and Sebald, Walter},
  title     = {The proteolipid of a mutant ATPase from Escherichia coli defective in H\(^+\)-conduction contains a glycine instead of the carbodiimide-reactive aspartyl residue},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62769},
  year      = {1980},
  abstract  = {No abstract available},
  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{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{HoppeSebald1986,
  author    = {Hoppe, J. and Sebald, Walter},
  title     = {Topological studies suggest that the pathway of the protons through F\(_0\) is provided by amino acid residues accessible from the lipid phase},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62602},
  year      = {1986},
  abstract  = {The structure of the F0 part of ATP synthases from E. coli and Neurospora crassa was analyzed by hydrophobic surface labeling with [125I]TID. In the E. co/i F0 all three subunits were freely accessible to the reagent, suggesting that these subunits are independently integrated in the membrane. Labeted amino acid residues were identified by Edman degradation of the dicyclohexylcarbodiimide binding (DCCD) proteins from E. coli and Neurospora crassa. The very similar patterns obtained with the two homologaus proteins suggested the existence of tightly packed cx-helices. The oligomeric structure of the DCCD binding protein appeared to be very rigid since little, if any, change in the labeling patternwas observed upon addition of oligomycin or DCCD to membranes from Neurospora crassa. When membrancs were pretrcated with DCCD prior to the reaction with [125I]TID an additionally labeled amino acid appeared at the position of Glu·65 which binds DCCD covalently, indicating the Jocation of this inhibitor on the outside of the oligomer. It is suggested that proton conduction occurs at the surface of the oligomer of the DCCD binding protein. Possibly this oligomer rotates against the subunit a or b and thus enables proton translocation. Conserved residues in subunit a, probably located in the Iipid bilayer, might participate in the pro· ton translocation mechanism.},
  subject      = {Biochemie},
  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{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{KonigJakubiczkaWieackeretal.1993,
  author    = {Konig, Anja and Jakubiczka, Sybille and Wieacker, Peter and Schl{\"o}sser, Hans W. and Gessler, Manfred},
  title     = {Further evidence that imbalance of WT1 isoforms may be involved in Denys-Drash syndrome},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59167},
  year      = {1993},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@phdthesis{Kraich2008,
  author    = {Kraich, Michael},
  title     = {Strukturelle und funktionelle Untersuchungen der Interaktion zwischen Ligand und Rezeptor im Interleukin-4- und Interleukin-13-System},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-27655},
  school      = {Universit{\"a}t W{\"u}rzburg},
  year      = {2008},
  abstract  = {Interleukin-4 (IL-4) und Interleukin-13 (IL-13) sind bedeutende Regulatorproteine des Immunsystems. Sie spielen eine entscheidende Rolle bei der Entstehung und dem Verlauf von allergischen Erkrankungen, wie z.B. Asthma. Um ihre Signale in die Zielzelle zu transduzieren, kann von beiden Zytokinen der gleiche Zelloberfl{\"a}chenrezeptor verwendet werden, wodurch sich die {\"u}berlappenden, biologischen Funktionen erkl{\"a}ren lassen. Dieser gemeinsam genutzte Rezeptor ist aus den beiden Untereinheiten IL-4Ralpha; und IL-13Ralpha1 aufgebaut. Da IL-4 und IL-13 auf Aminos{\"a}ureebene nur etwa 25\% Sequenzidentit{\"a}t besitzen und stark unterschiedliche Affinit{\"a}ten zu den beiden Rezeptorketten besitzen, stellt sich die Frage, durch welchen molekularen Erkennungsmechanismus, die Affinit{\"a}t und die Spezifit{\"a}t der Ligand-Rezeptor-Interaktion unabh{\"a}ngig voneinander reguliert werden kann. In dieser Arbeit gelang es, rekombinante Expressions- und Aufreinigungsstrategien f{\"u}r IL-13 und die extrazellul{\"a}ren Dom{\"a}nen der Rezeptorketten IL-13Ralpha1 und IL-13Ralpha2 zu entwickeln. Dadurch war es m{\"o}gliche, eine breite Mutations-/Interaktionsanalyse der IL-13Ralpha1-Kette durchzuf{\"u}hren.Es konnte gezeigt werden, dass die N-terminale FnIII-{\"a}hnliche Dom{\"a}ne von IL-13Ralpha1 sowohl an der Bindung von IL-13 als auch an der Interaktion mit IL-4 beteiligt ist. Im funktionellen Bindeepitop der IL-13Ralpha1-Kette wurden die Aminos{\"a}urereste Arg84, Phe253 und Tyr321 als Hauptbindungsdeterminanten f{\"u}r die Interaktion mit IL-13 identifiziert. Durch die Interaktionsstudien der IL-13Ralpha1-Varianten mit IL-4 wurde gezeigt, dass diese Hauptbindungsdeterminanten auch f{\"u}r die niederaffine Bindung von IL-4 von gr{\"o}ßter Bedeutung sind. Die funktionellen Bindeepitope f{\"u}r IL-4 und IL-13 auf der IL-13Ralpha1-Kette sind nahezu identisch und {\"u}berlappen in einem großen Bereich. Aufgrund der Ergebnisse aus der Mutagenesestudie war es m{\"o}glich, ein Strukturmodell der extrazellul{\"a}ren Dom{\"a}ne der IL-13Ralpha1-Kette zu erstellen. Darin wird eine neuartige Orientierung der N-terminalen FnIII-Dom{\"a}ne und deren Beteiligung an der Ligandeninteraktion dargestellt. Mit Hilfe des Strukturmodells gelang es, neue Aminos{\"a}urerest auf der Oberfl{\"a}che von IL-13 zu identifizieren, die an der Bindung zu IL-13Ralpha1 beteiligt sind, was die Relevanz des Strukturmodells weiter unterstreicht. In einem weiteren Teil dieser Arbeit wurde versucht, den molekularen Mechanismus aufzukl{\"a}ren, durch den es den superagonistischen IL-4-Varianten T13D und F82D gelingt, mit dreifach h{\"o}herer Affinit{\"a}t an die IL-4Ralpha-Kette zu binden, als wildtypischer Ligand. Durch strukturelle und funktionelle Untersuchungen wurde gezeigt, dass der Affinit{\"a}tssteigerung ein indirekter Mechanismus zugrunde liegt, bei dem eine Konformations{\"a}nderung und die Fixierung der Arg85-Seitenkette von IL-4 zur Ausbildung von zus{\"a}tzlichen Ligand-Rezeptor-Interaktionen f{\"u}hrt. Das Bindeepitop zwischen IL-4 und der IL-4Ralpha-Kette besitzt eine modulare Architektur aus drei unabh{\"a}ngig voneinander agierenden Interaktionsclustern. Bei der Interaktion von wildtypischem IL-4 mit IL-4Ralpha tragen nur zwei dieser Cluster in signifikanter Weise zur freien Bindeenergie bei. Im Falle der superagonistischen IL-4-Varianten ist jedoch auch das dritte Cluster an der Generierung von zus{\"a}tzlicher, freier Bindeenergie beteiligt, wodurch die Affinit{\"a}t zwischen Ligand und Rezeptor erh{\"o}ht wird. Damit stellt der modulare Aufbau der Interaktionsfl{\"a}che zwischen IL-4 und der IL-4Ralpha-Kette m{\"o}glicherweise einen Mechanismus dar, {\"u}ber den Proteine die Affinit{\"a}t von Wechselwirkungen {\"u}ber einen großen Bereicht variieren k{\"o}nnen, ohne dabei Spezifit{\"a}t einzub{\"u}ssen. Da IL-4 und IL-13 als interessante Zielmolek{\"u}le f{\"u}r die Therapie von allergischen und asthmatischen Erkrankungen erkannt worden sind, k{\"o}nnen die in der vorliegenden Arbeit gewonnenen Informationen {\"u}ber den Bindemechanismus und die Einblicke in den molekularen Charakter der Interaktion zwischen den beiden Zytokinen und ihren spezifischen Rezeptorketten dabei helfen, neuartige und hoch spezifische, inhibitorische Molek{\"u}le zu entwickeln.},
  subject      = {Renaturierung <Biochemie>},
  language  = {de}
}
@article{KruseLehrnbecherSebald1991,
  author    = {Kruse, N. and Lehrnbecher, T. and Sebald, Walter},
  title     = {Site-directed mutagenesis reveals the importance of disulfide bridges and aromatic residues for structure and proliferative activity of human interleukin-4},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62505},
  year      = {1991},
  abstract  = {Mutant proteins (muteins) of human lnterleukin-4 (llA) were constructed by means of in vitro mutagenesis. The muteins were expressed in E. co/1, submitted to a renaturation and purification protocol and analysed for biological activity. Exchange of the cysteines at either position 46 or 99 which form one of the three disulfide bridges resulted. in a nearly co•mplete loss · of biological actiyity and an unstable protein. The exchange of tyrosine 124 also inactivated the protein, while a mutation of tyrosine 56 left some residual activity. Exchange of the other four cysteines or of · the single tryptophane had smaller etTects.},
  subject      = {Biochemie},
  language  = {en}
}
@article{KruseShenArnoldetal.1993,
  author    = {Kruse, N. and Shen, B. J. and Arnold, S. and Tony, H. P. and M{\"u}ller, T. and Sebald, Walter},
  title     = {Two distinct functional sites of human interleukin 4 are identified by variants impaired in either receptor binding or receptor activation},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62451},
  year      = {1993},
  abstract  = {Interleukin 4 (IL-4) exerts a decisive role in the coord.ination of proteelive immune responses against parasites, particularly helminths. A disregulation of ll.r4 function is possibly involved in the genesis of allergic disease states. The search for important amino acid residues in human ll.r4 by mutational analysis of charged invariant amino acid positions identified two distinct functional sites in the 4-helix-bundle protein. Site 1 was marked by amino acid substitutions of the glutamic acid at position 9 in helix A and arginine at position 88 in helix C. Exchanges at both positions led to IL-4 variants deficient in binding to the extracellular domain of the ll.r4 receptor (IL-4ReJ. In parallel, up to 1000-fold increased concentrations of this type of variant were required to induce T -cell proliferation and B-eeil CD23 expression. Site 2 was marked by amino acid exchanges in helix D at positions 121, 124 and 125 (arginine, tyrosine and serine respectively in the wild-type).ß.A variants affected at site 2 exhibited partial agonist activity during T -cell proliferation; however, they still bound with high affinity to IL-4Rex. [The generation of an IL-4 antagonist by replacing tyrosine 124 with aspartic acid has been described before by Kruse et al. (1992) (EMBO }., 11, 3237-3244)]. These findings indicate that IL-4 functions by bind.ing IL-4Rex via site 1 which is constituted by residues on helices A and C. They further suggest that the association of a second, still undetined receptor protein with site 2 in helix D activates the receptor system and generates a transmembrane signal.},
  subject      = {Biochemie},
  language  = {en}
}
@article{KruseTonySebald1992,
  author    = {Kruse, N. and Tony, H. P. and Sebald, Walter},
  title     = {Conversion of human interleukin-4 into a high affinity antagonist by a single amino acid replacement},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62469},
  year      = {1992},
  abstract  = {lnterleukin-4 (IL-4) represents a prototypic lymphokine (for a recent review see Paul, 1991). It promotes differentiation of B-cells and the proliferation of T- and B-cell, and other cell types of the lymphoid system. An antagonist of human IL-4 was discovered during the studies presented here after Tyr124 of the recombinant proteinbad been substituted by an aspartic acid residue. This IL-4 variant, Y124D, bound with high affinity to the IL-4 receptor (K\(_D\) = 310 pM), but retained no detectable proliferative activity for T -<:ells and inhibited IL-4-dependent T -cell proliferation competitively (K\(_i\) = 620 pM). The loss of efficacy in variant Y124D was estimated to be > 100-fold on the basis of a weak partial agonist activity for the very sensitive induction of CD23 positive B-cells. The subsitution of Tyr124 by either phenylalanine, histidine, asparagine, Iysine or glycine resulted in partial agonist variants with unaltered receptor binding atTmity and relatively small deficiencies in efficacy. These results demoostrate that high affinity binding and signal generation can be uncoupled efticiently in a Iigand of a receptor betonging to the recently identified hematopoietin receptor family. In addition we show for the first time, that a powerful antagonist acting on the IL-4 receptor system can be derived from the IL-4 protein.},
  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{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{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{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{McCarthySchairerSebald1985,
  author    = {McCarthy, J. E. and Schairer, H. U. and Sebald, Walter},
  title     = {Translational initiation frequency of atp genes from Escherichia coli: identification of an intercistronic sequence that enhances translation},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62657},
  year      = {1985},
  abstract  = {The c, b and {\"o} subunit genes of the Escherichia coli atp operon were cloned individually in an expression vector between the tac fusion promoter and the galK gene. The relative rates of subunit synthesis directed by the cloned genes were similar in vitro andin vivo and compared favourably with the subunit stoichiometry of the assembled proton-translocating A TP synthase of E. coli in vivo. The rate of synthesis of subunit c was at least six times that of subunit b and 18 times that of subunit {\"o}. Progressive shortening of the long intercistronic sequence lying upstream of the subunit c gene showed that maximal expression of this gene is dependent upon the presence of a sequence stretching > 20 bp upstream of the Shine-Dalgarno site. This sequence thus acts to enhance the rate of translational initiation. The possibility that similar sequences might perform the same function in other operons of E. coli and bacteriophage A is also discussed. Translation of the subunit b cistron is partially coupled to translation of the preceding subunit c cistron. In conclusion, the expression of all the atp operon genes could be adjusted to accommodate the subunit requirements of A TP synthase assembly primarily by means of mechanisms which control the efficiency of translational initiation and re-initiation at the respective cistron start codons.},
  subject      = {Biochemie},
  language  = {en}
}
@article{McCarthySebaldGrossetal.1986,
  author    = {McCarthy, J. E. and Sebald, Walter and Gross, G. and Lammers, R.},
  title     = {Enhancement of translational efficiency by the Escherichia coli atpE translational initiation region: its fusion with two human genes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62626},
  year      = {1986},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@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}
}