@misc{PeterFoerster1989,
  author    = {Peter, Martin G. and F{\"o}rster, Hans},
  title     = {Zur Struktur von Eumelaninen : Identifizierung von Konstitutionsmustern durch Festk{\"o}rper-NMR-Spektroskopie},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-17038},
  year      = {1989},
  abstract  = {Aus dem Inhalt: Melanine sind komplexe polyphenolische Polymere. In der Natur entstehen sie durch meist enzymkatalysierte oxidative Polymerisation von o-Diphenolen. Man unterscheidet die aus Dopa 1 oder Dopamin 3 hervorgehenden, tiefschwarzen Eumelanine von den aus Dopa in Gegenwart von Cystein entstehenden, gelben bis braunen Phaomelaninen. [...]},
  language  = {de}
}
@misc{FerenzPeter1987,
  author    = {Ferenz, Hans-J{\"o}rg and Peter, Martin G.},
  title     = {The inhibitory effect of sinefungin on juvenile hormone biosynthesis and development in locusts},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-16811},
  year      = {1987},
  abstract  = {The antibiotic fungal metabolite sinefungin is a potent inhibitor of S-adenosylmethionine-acceptor methyltransferases. Its effect on insect metabolism and especially on corpora allata farnesoic acid methyltransferase, which catalyzes the penultimate step of juvenile hormone biosynthesis, was investigated in Locusta migratoria. Injection of sinefungin results in a delay of imaginal molt and in suppression of ovary development. Isolated corpora allata are unable to synthesize juvenile hormone III in the presence of more than 1.0 mM sinefungin. In a cell-free system containing the S-adenosylmethionine-dependent farnesoic acid methyltransferase from corpora allata sinefungin is a competitive inhibitor of the synthesis of methylfarnesoate with Ki of 1 μM.},
  language  = {en}
}
@misc{FerenzPeterBerg1983,
  author    = {Ferenz, Hans-J{\"u}rgen and Peter, Martin G. and Berg, Dieter},
  title     = {Inhibition of farnesoic acid methyltransferase by sinefungin},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-17016},
  year      = {1983},
  abstract  = {Sinefungin inhibited the S-adenosylmethionine-dependent farnesoic acid methyltransferase in a cell-free system containing a homogenate of corpora allata from female locusts, Locusta migratoria. The enzyme catalyzed the penultimate step of juvenile hormone biosynthesis in the insects. Culturing corpora allata in the presence of sinefungin greatly suppressed juvenile hormone production. The following in vivo effects were visible after injection of the inhibitor: increase in mortality and reduction of total haemolymph protein liter and ovary fresh weight, as well as length of terminal oocytes. Attempts to reverse these effects by topical application of the juvenile hormone analog ZR-515 (methoprene) were only partly successful. Therefore, the in vivo effects may be due to a general inhibition of methyltransferase enzymes in the insect. Sinefungin appeared to be of potential interest as the first representative of a new class of insect growth regulators.},
  language  = {en}
}
@misc{KortPeterKoopmanschap1983,
  author    = {Kort, C. A. D. de and Peter, Martin G. and Koopmanschap, A. B.},
  title     = {Binding and degradation of juvenile hormone III by haemolymph proteins of the Colorado potato beetle: a re-examination},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-16777},
  year      = {1983},
  abstract  = {The haemolymph of the adult Colorado potato beetle, Lepinotarsa decemlineata Say, contains a high molecular weight (MW > 200,000) JH-III specific binding protein. The Kd value of the protein for racemic JH-III is 1.3 ± 0.2 × 10-7 M. It has a lower affinity for racemic JH-I and it does not bind JH-III-diol or JH-III-acid. The binding protein does discriminate between the enantiomers of synthetic, racemic JH-III as was determined by stereochemical anaysis of the bound and the free JH-III. Incubation of racemic JH-III with crude haemolymph results in preferential formation of (10S)-JH-III-acid, the unnatural configuration. The JH-esterase present in L. decemlineata haemolymph is not enantioselective. It is concluded that the most important function of the binding protein is that of a specific carrier, protecting the natural hormone against degradation by esterases. The carrier does not protect JH-I as efficiently as the lower homologue.},
  language  = {en}
}
@misc{PeterStuppLentes1983,
  author    = {Peter, Martin G. and Stupp, Hans-Peter and Lentes, Klaus-Ulrich},
  title     = {Umkehr der Enantioselektivit{\"a}t bei der enzymatischen Hydrolyse von Juvenilhormon als Ergebnis einer Proteinfraktionierung},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-17001},
  year      = {1983},
  abstract  = {Aus dem Inhalt: Die Juvenilhormone 1a-c werden im Blut von Insekten enzymatisch zu den biologisch inaktiven Sluren hydrolysiert. Bei der Hydrolyse von racemischem 1c im Blut der Wanderheuschrecke Locusta migratoria wird ein Umsatz von 40-60\% erreicht. Das unumgesetzte Edukt enth{\"a}llt einen {\"U}berschuß an nat{\"u}rlich konfiguriertem (10R)-1c (e.e. 47.2\%). Wir konnten zeigen, daß das in der H{\"a}molymphe vorhandene Hormon-Bindungsprotein bevorzugt mit (10R)- 1c assoziiert.},
  language  = {de}
}
@misc{Peter1980,
  author    = {Peter, Martin G.},
  title     = {Products of in vitro oxidation of N-acetyldopamine as possible components in the sclerotization of insect cuticle},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-16759},
  year      = {1980},
  abstract  = {[1-14C]-N-Acetyldopamine (NADA) was oxidized in the presence of methyl [3-3H]-β-alanate with mushroom tyrosinase. The complex mixture of reaction products was partly resolved by chromatographic procedures and analyzed by spectroscopic methods. Methyl-β-alanate is incorporated to only a small extent into oxidation products of NADA which inter alia are presumed to be oligomeric hydroxyquinones. After oxidation of [1-14C, 2-3H]-NADA with preparations from tanning Manduca sexta pupal cuticle, N-acetylnoradrenalin was identified as one of the products. Binding of radioactivity to melanin-like material was also observed. These results suggest that oxidation products different from those formulated usually for the crosslinkages between protein amino groups and N-acetyldopaquinone are deposited in darkly brown coloured insect cuticles during sclerotization.},
  language  = {en}
}