@article{NaithaniKlostermeyerLangeetal.1971,
  author    = {Naithani, V. K and Klostermeyer, Henning and Lange, H. R. and [u.a.], and Berndt, Heinz and [u.a.],},
  title     = {Preparation of peptide derivatives for porcine proinsulin-synthesis},
  series = {Biological Chemistry},
  volume    = {352},
  journal   = {Biological Chemistry},
  number    = {1},
  publisher = {De Gruyter},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1971.352.1.1},
  pages     = {2 -- 3},
  year      = {1971},
  language  = {en}
}
@article{MatoniBerndt1980,
  author    = {Matoni, Georg and Berndt, Heinz},
  title     = {Thermal synthesis of the optical pure pentapeptide derivative Z-(L)-Ala-(L)-Phe-Gly-(L)-Phe-Gly-OMe},
  series = {Tetrahedron letters},
  volume    = {21},
  journal   = {Tetrahedron letters},
  number    = {1},
  issn      = {0040-4039},
  doi       = {10.1016/S0040-4039(00)93618-9},
  pages     = {37 -- 40},
  year      = {1980},
  language  = {en}
}
@article{NokiharaBerndt1978,
  author    = {Nokihara, Kiyoshi and Berndt, Heinz},
  title     = {Studies on sulfur-containing peptides : tert-butyloxycarbonylsulfenyl and benzyloxycarbonylsulfenyl derivatives as protecting groups for cysteine},
  series = {The journal of organic chemistry},
  volume    = {43},
  journal   = {The journal of organic chemistry},
  number    = {25},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {0022-3263},
  doi       = {10.1021/jo00419a046},
  pages     = {4893 -- 4895},
  year      = {1978},
  language  = {en}
}
@article{DanhoNaithaniSasakietal.1980,
  author    = {Danho, Waleed and Naithani, Vinod K. and Sasaki, Andr{\´e} N. and F{\"o}hles, Joseph and Berndt, Heinz and [u.a.],},
  title     = {Human proinsulin, VII : synthesis of two protected peptides corresponding to the sequences 1—45 and 46—86 of the prohormone},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {361},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {1},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1980.361.1.857},
  pages     = {857 -- 863},
  year      = {1980},
  language  = {en}
}
@inproceedings{KalbeKuropkaMeyerStorketal.1988,
  author    = {Kalbe, Jochen and Kuropka, Rolf and Meyer-Stork, L. Sebastian and Lauter, S. L. and H{\"o}cker, Hartwig and Berndt, Heinz},
  title     = {Identification of fine animal hair via DNA analysis},
  series = {Proceedings of the 1st International Symposium on Specialty Animal Fibers : Aachen, October 26 - 27, 1987 ; [scientific, technological and economical aspects] . - (Schriftenreihe des Deutschen Wollforschungsinstitutes an der Technischen Hochschule Aachen e.V. ; 103)},
  booktitle = {Proceedings of the 1st International Symposium on Specialty Animal Fibers : Aachen, October 26 - 27, 1987 ; [scientific, technological and economical aspects] . - (Schriftenreihe des Deutschen Wollforschungsinstitutes an der Technischen Hochschule Aachen e.V. ; 103)},
  editor    = {K{\"o}rner, Andrea},
  publisher = {Dt. Wollforschungsinst.},
  address   = {Aachen},
  issn      = {0930-3723},
  pages     = {221 -- 227},
  year      = {1988},
  language  = {en}
}
@article{BerndtKrueger1985,
  author    = {Berndt, Heinz and Kr{\"u}ger, G{\"o}tz},
  title     = {Resolution of enantiomeric amino acid derivatives by high-performance liquid chromatography on chiral stationary phases},
  series = {Journal of chromatography A},
  volume    = {1985},
  journal   = {Journal of chromatography A},
  number    = {348},
  issn      = {0021-9673},
  doi       = {10.1016/S0021-9673(01)92461-6},
  pages     = {275 -- 279},
  year      = {1985},
  language  = {en}
}
@misc{BerndtHoeckerKuropkaetal.1991,
  author    = {Berndt, Heinz and H{\"o}cker, Hartwig and Kuropka, Rolf and Kinkel, Joachim},
  title     = {Silane coated inorganic materials for chromatography : United States Patent},
  publisher = {[The United States Patent and Trademark Office]},
  address   = {[Alexandria, VA u.a.]},
  pages     = {9 S. : graph. Darst.},
  year      = {1991},
  language  = {en}
}
@article{WangDruckenmuellerElbersetal.2014,
  author    = {Wang, Ren-Qi and Druckenm{\"u}ller, Katharina and Elbers, Gereon and Guenther, Klaus and Crou{\´e}, Jean-Philippe},
  title     = {Analysis of aquatic-phase natural organic matter by optimized LDI-MS method},
  series = {Journal of mass spectrometry},
  volume    = {49},
  journal   = {Journal of mass spectrometry},
  number    = {2},
  publisher = {Wiley},
  address   = {Bognor Regis},
  issn      = {1096-9888},
  doi       = {10.1002/jms.3321},
  pages     = {154 -- 160},
  year      = {2014},
  abstract  = {The composition and physiochemical properties of aquatic-phase natural organic matter (NOM) are most important problems for both environmental studies and water industry. Laser desorption/ionization (LDI) mass spectrometry facilitated successful examinations of NOM, as humic and fulvic acids in NOM are readily ionized by the nitrogen laser. In this study, hydrophobic NOMs (HPO NOMs) from river, reservoir and waste water were characterized by this technique. The effect of analytical variables like concentration, solvent composition and laser energy was investigated. The exact masses of small molecular NOM moieties in the range of 200-1200 m/z were determined in reflectron mode. In addition, spectra of post-source-decay experiments in this range showed that some compounds from different natural NOMs had the same fragmental ions. In the large mass range of 1200-15 000 Da, macromolecules and their aggregates were found in HPO NOMs from natural waters. Highly humic HPO exhibited mass peaks larger than 8000 Da. On the other hand, the waste water and reservoir water mainly had relatively smaller molecules of about 2000 Da. The LDI-MS measurements indicated that highly humic river waters were able to form large aggregates and membrane foulants, while the HPO NOMs from waste water and reservoir water were unlikely to form large aggregates. Copyright © 2014 John Wiley \& Sons, Ltd.},
  language  = {en}
}
@article{HeineHerrmannSelmeretal.2014,
  author    = {Heine, A. and Herrmann, G. and Selmer, Thorsten and Terwesten, F. and Buckel, W. and Reuter, K.},
  title     = {High resolution crystal structure of clostridium propionicum β-Alanyl-CoA:Ammonia Lyase, a new member of the "Hot Dog Fold" protein superfamily},
  series = {Proteins},
  volume    = {82},
  journal   = {Proteins},
  number    = {9},
  publisher = {Wiley-Liss},
  address   = {New York},
  issn      = {1097-0134 (E-Journal); 0887-3585 (Print)},
  doi       = {10.1002/prot.24557},
  pages     = {2041 -- 2053},
  year      = {2014},
  abstract  = {Clostridium propionicum is the only organism known to ferment β-alanine, a constituent of coenzyme A (CoA) and the phosphopantetheinyl prosthetic group of holo-acyl carrier protein. The first step in the fermentation is a CoA-transfer to β-alanine. Subsequently, the resulting β-alanyl-CoA is deaminated by the enzyme β-alanyl-CoA:ammonia lyase (Acl) to reversibly form ammonia and acrylyl-CoA. We have determined the crystal structure of Acl in its apo-form at a resolution of 0.97 {\AA} as well as in complex with CoA at a resolution of 1.59 {\AA}. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called "hot dog fold" which is characterized by a five-stranded antiparallel β-sheet with a long α-helix packed against it. The functional unit of all "hot dog fold" proteins is a homodimer containing two equivalent substrate binding sites which are established by the dimer interface. In the case of Acl, three functional dimers combine to a homohexamer strongly resembling the homohexamer formed by YciA-like acyl-CoA thioesterases. Here, we propose an enzymatic mechanism based on the crystal structure of the Acl·CoA complex and molecular docking. Proteins 2014; 82:2041-2053. © 2014 Wiley Periodicals, Inc.},
  language  = {en}
}
@article{TakenagaBiselliSchnitzleretal.2014,
  author    = {Takenaga, Shoko and Biselli, Manfred and Schnitzler, Thomas and {\"O}hlschl{\"a}ger, Peter and Wagner, Torsten and Sch{\"o}ning, Michael Josef},
  title     = {Toward multi-analyte bioarray sensors: LAPS-based on-chip determination of a Michaelis-Menten-like kinetics for cell culturing},
  series = {Physica status solidi A : Applications and materials science},
  volume    = {211},
  journal   = {Physica status solidi A : Applications and materials science},
  number    = {6},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1521-396X (E); 1862-6319 (E-Journal); 0031-8965 (Print); 1862-6300 (Print)},
  doi       = {10.1002/pssa.201330464},
  pages     = {1410 -- 1415},
  year      = {2014},
  abstract  = {The metabolic activity of Chinese hamster ovary (CHO) cells was observed using a light-addressable potentiometric sensor (LAPS). The dependency toward different glucose concentrations (17-200 mM) follows a Michaelis-Menten kinetics trajectory with Kₘ = 32.8 mM, and the obtained Kₘ value in this experiment was compared with that found in literature. In addition, the pH shift induced by glucose metabolism of tumor cells transfected with the HPV-16 genome (C3 cells) was successfully observed. These results indicate the possibility to determine the tumor cells metabolism with a LAPS-based measurement device.},
  language  = {en}
}