@article{DamaschunDamaschunGastetal.1993,
  author    = {Damaschun, Gregor and Damaschun, Hilde and Gast, Klaus and Misselwitz, Rolf and M{\"u}ller, J{\"u}rgen J. and Pfeil, Wolfgang and Zirwer, Dietrich},
  title     = {Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast},
  year      = {1993},
  language  = {en}
}
@article{GastDamaschunDesmadriletal.1995,
  author    = {Gast, Klaus and Damaschun, Gregor and Desmadril, Michel and Minard, Philippe and M{\"u}ller-Frohne, Marlies and Pfeil, Wolfgang and Zirwer, Dietrich},
  title     = {Cold denaturation of yeast phosphoglycerate kinase : which domain is more stable?},
  year      = {1995},
  language  = {en}
}
@article{HerbstGastSeckler1998,
  author    = {Herbst, R. and Gast, Klaus and Seckler, Robert},
  title     = {Folding of firefly (Photinus pyralis) luciferase : aggregation and reactivation of unfolding intermediates},
  year      = {1998},
  language  = {en}
}
@article{HanischvanRossumGastetal.2004,
  author    = {Hanisch, Uwe-Karsten and van Rossum, D. and Gast, Klaus and Misselwitz, Rolf and Goldstein, Gundars and Koistinaho, Jari and M{\"o}ller, Thomas},
  title     = {The microglia-activating potential of thrombin : is the protease able to induce cyto- and chemokines?},
  year      = {2004},
  language  = {en}
}
@article{PiontekWinklerBaletal.2004,
  author    = {Piontek, J. and Winkler, Lars and Bal, M. S. and Lassowski, Birgit and Mueller, Sandra L. and Gast, Klaus and Blasig, Ingolf E.},
  title     = {Investigating of homophilic interactions of the tight junction proteins occludin and claudin-5},
  year      = {2004},
  language  = {en}
}
@article{ModlerFabianSokolowskietal.2004,
  author    = {Modler, Andreas Johannes and Fabian, H. and Sokolowski, F. and Lutsch, G. and Gast, Klaus and Damaschun, Gregor},
  title     = {Polymerization of proteins into amyloid protofibrils shares common critical oligomeric states but differs in the mechanisms of their formation},
  year      = {2004},
  abstract  = {Amyloid protofibril formation of phosphoglycerate kinase (PGK) and Syrian hamster prion protein (SHaPrP(90- 232)) were investigated by static and dynamic light scattering, size exclusion chromatography and electron microscopy. Changes in secondary structure were monitored by Fourier transform infrared spectroscopy and by circular dichroism. Protofibril formation of the two proteins is found to be a two-stage process. At the beginning, an ensemble of critical oligomers is built lip. These critical oligomeric states possess a predominant beta-sheet structure and do not interact considerably with monomers. Initial oligomerization and transition to beta-sheet structure are coupled events differing in their details for both proteins. Intermediate oligomeric states (dimers, trimers, etc.) are populated in case of PGK, whereas SHaPrP(90-232) behaves according to oil apparent two-state reaction between monomers and octamers rich in beta- structure with a reaction order varying between 2 and 4. All oligomers coalesce to PGK protofibrils in the second stage, while SHaPrP(90-232) protofibrils are only formed by a subpopulation. The rates of both growth stages can be tuned in case of PGK by different salts preserving the underlying generalized diffusion-collision mechanism. The different kinetics of the early misfolding and oligomerization events of the two proteins argue against a common mechanism of protofibril formation. A classification scheme for misassembly, mechanisms of proteins based on energy landscapes is presented. It includes scenarios of downhill polymerization to which protofibril formation of PGK and SHaPrP(90-232) belong},
  language  = {en}
}
@article{HanischVanRossumXieetal.2004,
  author    = {Hanisch, Uwe-Karsten and Van Rossum, Denise and Xie, Yiheng and Misselwitz, Rolf and Auriola, Seppo and Goldstein, Gundars and Koistinaho, Jari and Kettemann, Helmut and M{\"o}ller, Thomas and Gast, Klaus},
  title     = {The microglia-activating potential of thrombin : the protease is not involved in the induction of proinflammatory cytokines and chemokines},
  year      = {2004},
  abstract  = {The serine protease thrombin is known as a blood coagulation factor. Through limited cleavage of proteinase- activated receptors it can also control growth and functions in various cell types, including neurons, astrocytes, and microglia ( brain macrophages). A number of previous studies indicated that thrombin induces the release of proinflammatory cytokines and chemokines from microglial cells, suggesting another important role for the protease beyond hemostasis. In the present report, we provide evidence that this effect is not mediated by any proteolytic or non- proteolytic mechanism involving thrombin proper. Inhibition of the enzymatic thrombin activity did not affect the microglial release response. Instead the cyto-/chemokine-inducing activity solely resided in a high molecular weight protein fraction that could be isolated in trace amounts even from apparently homogenous alpha- and gamma-thrombin preparations. High molecular weight material contained thrombin-derived peptides as revealed by mass spectrometry but was devoid of thrombin-like enzymatic activity. Separated from the high molecular weight fraction by fast protein liquid chromatography, enzymatically intact alpha- and gamma-thrombin failed to trigger any release. Our findings may force a revision of the notion that thrombin itself is a direct proinflammatory release signal for microglia. In addition, they could be relevant for the study of other cellular activities and their assignment to this protease},
  language  = {en}
}
@article{KellerSauerStraussetal.2005,
  author    = {Keller, S. and Sauer, I. and Strauss, H. and Gast, Klaus and Dathe, M. and Bienert, Michael C.},
  title     = {Membrane-mimetic nanocarriers formed by a dipalmitoylated cell-penetrating peptide},
  year      = {2005},
  language  = {en}
}
@article{FabianGastFilimonovetal.2005,
  author    = {Fabian, H. and Gast, Klaus and Filimonov, Vladimir V. and Zamyatkin, D. F. and Rogov, V. V.},
  title     = {Thermal unfolding of two designed monomeric lambda Cro repressor variants},
  issn      = {0924-2031},
  year      = {2005},
  abstract  = {The thermal unfolding of the wild-type lambda Cro repressor and of two designed variants, Cro K56-[DGEVK] and Cro K56-[DGEVK] Q16L, was studied by Fourier transform infrared spectroscopy and dynamic light scattering. The engineered Cro K56-[DGEVK] monomer has five additional amino acids inserted after position 56 of the wild-type sequence, while the K56-[DGEVK] Q16L variant differs only in one position (Gln-16 to Leu substitution) from the Cro K56-[DGEVK] sequence. The temperature dependence of selected protein backbone infrared `marker' bands revealed that Cro K56- [DGEVK] is slightly more stable than the wild-type protein, while the replacement of Gln-16 by Leu increases the thermal transition temperature by similar to 20 degrees C. Moreover, thermal unfolding of the two Cro variants was found to proceed through equilibrium unfolding intermediates and to involve the formation of oligomers. The first thermal transition of Cro K56-[DGEVK] involves the melting of major parts of its native secondary structure and is accompanied by the formation of dinners and non-native beta-sheet structures. These structures unfold during a second transition at higher temperatures, accompanied by the dissociation of the dimers. In contrast to the Cro K56-[DGEVK] protein, the intermediate state of the Cro K56-[DGEVK] Q16L variant is less well defined, and involves the formation of oligomers of different size. (c) 2005 Elsevier B.V. All rights reserved},
  language  = {en}
}
@article{GastModler2005,
  author    = {Gast, Klaus and Modler, Andreas Johannes},
  title     = {Studying protein folding and aggregation by LASER light scattering},
  isbn      = {3-527-30784-2},
  year      = {2005},
  language  = {en}
}