@article{LondershausenTurbergBieseleretal.1996,
  author    = {Londershausen, M. and Turberg, Andreas and Bieseler, Barbara and Lennarz, M. and Peter, Martin G.},
  title     = {Characterization and Inhibitor Studies of Chitinases from Parasitic Blowfly (Lucilia cuprina), Tick (Boophilus micoplus), Intestinale Nematode (Haemonchus contortus), and a Bean (Phaseolus vulgaris)},
  year      = {1996},
  language  = {en}
}
@article{LondershausenTurbergSpindlerBarthetal.1996,
  author    = {Londershausen, M. and Turberg, Andreas and Spindler-Barth, Margarethe and Peter, Martin G.},
  title     = {Screening Test for Insecticides Interfering with Cuticular Sclerotization},
  year      = {1996},
  language  = {en}
}
@article{Peter1995,
  author    = {Peter, Martin G.},
  title     = {Applications and environmental aspects of chitin and chitosan},
  issn      = {0022-233X},
  year      = {1995},
  language  = {en}
}
@article{SchumacherWanderslebPeter1995,
  author    = {Schumacher-Wandersleb, Michael H. M. G. and Peter, Martin G.},
  title     = {Synthesis of chitobiosyl pyrrolidines},
  year      = {1995},
  language  = {en}
}
@article{AbegazPeter1995,
  author    = {Abegaz, Berhanu M. and Peter, Martin G.},
  title     = {Emodine and emodinanthrone rhamnoside acetates from fruits of rhamnus prinoides},
  issn      = {0031-9422},
  year      = {1995},
  language  = {en}
}
@article{Peter1995,
  author    = {Peter, Martin G.},
  title     = {The Bio-organic chemistry of melanogenesis},
  year      = {1995},
  language  = {en}
}
@article{Peter1995,
  author    = {Peter, Martin G.},
  title     = {Chemie i Biochemia Zewnetrznego Szkieletu Owadow : (Chemistry and biochemistry of the insect exoskeleton)},
  year      = {1995},
  language  = {en}
}
@article{Peter1995,
  author    = {Peter, Martin G.},
  title     = {Chemistry and biochemistry of the insect exoskeleton},
  year      = {1995},
  language  = {en}
}
@article{Peter1995,
  author    = {Peter, Martin G.},
  title     = {Chitin in den Startl{\"o}chern},
  issn      = {0009-2959},
  year      = {1995},
  language  = {de}
}
@article{PeterMerz1995,
  author    = {Peter, Martin G. and Merz, A.},
  title     = {Stereoselective benzylic deprotonation in the enzymatic rearrangement of N-acetyldopamine derived o-Quinone to the p-Quinone methide},
  issn      = {0957-4166},
  year      = {1995},
  language  = {en}
}
@article{LeyPeter1994,
  author    = {Ley, J. P. and Peter, Martin G.},
  title     = {Synthesis of N-(2-Acetamido-2-deoxy-ß-D-glucopyranosyl)- and of N-(N,N-Diacetylchitobiosyl)-amide of lhistidine},
  issn      = {0039-7881},
  year      = {1994},
  language  = {en}
}
@article{PeterAndersen1994,
  author    = {Peter, Martin G. and Andersen, S. O.},
  title     = {The molecular architecture of the insect exoskeleton},
  year      = {1994},
  language  = {en}
}
@article{SchumacherWanderslebPetersenPeter1994,
  author    = {Schumacher-Wandersleb, Michael H. M. G. and Petersen, Stefan and Peter, Martin G.},
  title     = {Preparation of the N-Acetylglucosaminidase inhibitor 1-Acetamido-1,2,5-tride oxy-2,5-imino-D-glucitol from methyl a-D-Mannopyranoside},
  year      = {1994},
  language  = {en}
}
@article{PeterLeyPetersenetal.1994,
  author    = {Peter, Martin G. and Ley, J. P. and Petersen, Stefan and Londershausen, M. and Schumacher-Wandersleb, Michael H. M. G. and Spindler, Klaus-Dieter and Spindler-Barth, Margarethe and Turberg, Andreas},
  title     = {Synthesis of chitinase inhibitors},
  year      = {1994},
  language  = {en}
}
@article{KroescheCrescenziHoffbaueretal.1994,
  author    = {Kr{\"o}sche, Christian and Crescenzi, Orlando and Hoffbauer, Wilfried and Jansen, Martin and Napolitano, Alessandra and Prota, Guiseppe and Peter, Martin G.},
  title     = {Synthesis of dopamines labelled with 13C in the alpha- or beta-side chain positions, and their application for structure studies on melanins by solid state NMR spectroscopy},
  year      = {1994},
  language  = {en}
}
@misc{PeterAndersenHartmannetal.1992,
  author    = {Peter, Martin G. and Andersen, Svend Olav and Hartmann, Rudolf and Miessner, Merle and Roepstorff, Peter},
  title     = {Catecholamine-protein conjugates : isolation of 4-phenylphenoxazin-2-ones from oxidative coupling of N-acetyldopamine with alipathic amino acids},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-17571},
  year      = {1992},
  abstract  = {4-Phenylphenoxazinones were isolated after biomimetic oxidation, using diphenoloxidases of insect cuticle, mushroom tyrosinase, or after autoxidation of N-acetyldopamine (Image ) in the presence of β-alanine, β-alanine methyl ester or N-acetyl-L-lysine. They are formed presumably by addition of 2-aminoalkyl-5-alkylphenols to the o-quinone of biphenyltetrol which, in turn, arises from oxidative coupling of. The structures of present the first examples for the assembly of reasonably stable intermediates in the rather complex process of chemical modifications of aliphatic amino acid residues by o-quinones.},
  language  = {en}
}
@misc{AndersenPerterRoepstorff1992,
  author    = {Andersen, Svend Olav and Perter, Martin G. and Roepstorff, Peter},
  title     = {Cuticle-catalyzed coupling between N-acetylhistidine and N-acetyldopamine},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-16762},
  year      = {1992},
  abstract  = {Several types of insect cuticle contain enzymes catalyzing the formation ofof adducts between N-acetyldopamine (NADA) and N-acetylhistidine (NAH). Two such adducts, NAH-NADA-I and NAH NADA-II, have been isolated and their structures determined. In one of the adducts the link connecting the two residues occurs between the I-position (ß-position) in the NADA side chain and the 1-N atom (τ-N) in the imidazole ring of histidine. Diphenoloxidase activity alone is not sufficient for formation of this adduct, whereas extracts containing both diphenoloxidase and o-quinone-p-quinone methide isomerase activities catalyze the coupling reaction. The adduct consists of a mixture of two diastereomers and they are presumably formed by spontaneous reaction between enzymatically produced NADA-p-quinone methide and N-acetylhistidine. The other adduct has been identified as a ring addition product of N-acetylhistidine and NADA. In contrast to the former adduct it can be formed by incubation of the two substrates with mushroom tyrosinase alone. An adduct between N-acetylhistidine and the benzodioxan-type NADA-dimer is produced in vitro, when the N-acetylhistidine-NADA adduct is incubated with NADA and locust cuticle containing a 1,2-dehydro-NADA generating enzyme system. Trimeric NADA-polymerization products of the substituted benzodioxan-type have been obtained from in vivo sclerotized locust cuticle, confirming the ability of cuticle to produce NADA-oligomers. The results indicate that some insect cuticles contain enzymes promoting linkage of oxidized NADA to histidine residues. It is suggested that histidine residues in the cuticular proteins can serve as acceptors for oxidized NADA and that further addition of NADA-residues to the phenolic groups of bound NADA can occur, resulting in formation of protein-linked NADA-oligomers. The coupling reactions identified may be an important step in natural cuticular sclerotization.},
  language  = {en}
}
@misc{PeterBoldtNiedersteinetal.1990,
  author    = {Peter, Martin G. and Boldt, Peter C. and Niederstein, Yvonne and Peter-Katalinić, Jasna},
  title     = {Synthesen von Galactose-Cluster-haltigen Steroid-Derivaten},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-16783},
  year      = {1990},
  abstract  = {The synthesis of galactose clusters that are linked to a steroid moiety by a peptide-like spacer unit is described. The galactose cluster is obtained by Koenigs-Knorr glycosylation of TRIS-Gly-Fmoc (2b) under Helferich conditions. Peptide and ester bonds are formed after activation of carboxylic acids as diphenylthiophene dioxide (TDO) esters. 6a is synthesized in a convergent way by coupling of (Ac4Gal)3-TRIS-Gly (3e) with cholesteryl TDO succinate (5b). Coupling of (Ac4Gal)3-TRIS-Gly hydrogen succinate (3f) with Gly-O-Chol (5d) by means of EEDQ yields 6d. Reaction of (Ac4Gal)3-TRIS-Gly-SUCC-O-TDO (3g) with 25-hydroxycholesterol leads in a linear sequence to the oxysterol derivative 6f. Selective cleavage of the acetyl groups from galactose units yields the known compound 6b and the new derivatives 6e and 6g.},
  language  = {de}
}
@misc{PeterFoerster1989,
  author    = {Peter, Martin G. and F{\"o}rster, Hans},
  title     = {On the structure of Eumelanins : identification of constitutional patterns by solid-state NMR spectroscopy},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-17027},
  year      = {1989},
  abstract  = {Aus dem Inhalt: Melanins are complex polyphenolic polymers. They are usually formed in nature by enzyme-catalyzed oxidative polymerization of o-diphenols. The deep black eumelanins, derived from Dopa 1 or dopamine 3, are distinguished from the yellow to brown phaeomelanins obtained from Dopa in the presence of cysteine. Characteristic of eumelanins are the indole units, which are formed from catecholamines by intramolecular addition of the amino groups to the oxidatively generated o-quinones. [...]},
  language  = {en}
}
@misc{Peter1989,
  author    = {Peter, Martin G.},
  title     = {Chemische Modifikation von Biopolymeren durch Chinone und Chinonmethide},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-16802},
  year      = {1989},
  abstract  = {Chinone und Vorstufen, die oxidativ in Chinone und/oder Chinonmethide umgewandelt werden k{\"o}nnen, sind in der Natur weit verbreitet. Als sekund{\"a}re Naturstoffe wirken sie h{\"a}ufig antibiotisch, cytotoxisch, aber auch pathogen, und eine Reihe von Pflanzen und Tieren benutzt chinoide Substanzen als Abwehrstoffe, oft mit spektakul{\"a}rem Erfolg. Auf makromolekularer Ebene spielen Chinonmethide im Pflanzenreich eine Schl{\"u}sselrolle bei der Biosynthese von Lignin, w{\"a}hrend die Bildung von Melanoproteinen ein Beispiel f{\"u}r Reaktionen von o-Chinonen im Tierreich ist. Bei den Insekten dienen Chinone und Chinonmethide zur Bildung des lebensnotwendigen Exoskeletts. Die Reaktivit{\"a}t von Chinonen in biologischen Systemen hat auch f{\"u}r den Menschen unmittelbare Bedeutung in pharmazeutischer, toxikologischer und technologischer Hinsicht. Den Beispielen in diesem Aufsatz liegt ein gemeinsames Prinzip zugrunde, n{\"a}mlich die chemische Modifikation von Biopolymeren durch Chinone und Chinonmethide. Wie sich besonders bei einer detaillierteren Betrachtung der Reaktionen zeigt, die zur Sklerotisierung der Insektencuticula f{\"u}hren, sind in den letzten Jahren wichtige neue Erkenntnisse hinzugekommen, die vor allem durch die modernen Methoden der Stofftrennung und der Festk{\"o}rper-NMR-Spektroskopie erm{\"o}glicht worden sind.},
  language  = {de}
}
@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}
}