@article{AndersenPeterRoepstorff1996,
  author    = {Andersen, S. O. and Peter, Martin G. and Roepstorff, Peter},
  title     = {Cuticular sclerotization in insects},
  year      = {1996},
  language  = {en}
}
@article{AsgeirssonHaebelThorsteinssonetal.1998,
  author    = {Asgeirsson, Bjarni and Haebel, Sophie and Thorsteinsson, Leifur and Helgason, Erlendur and Gudmundsson, Kristbj{\"o}rn O. and Gudmundsson, Gunnar and Roepstorff, Peter},
  title     = {Hereditary cystatin C amyloid angiopathy: monitoring the presence of the Leu-68 -> Gln cystatin C variant in cerebrospinal fluids and monocyte cultures by MS},
  year      = {1998},
  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}
}