Helmholtz-Zentrum für Infektionsforschung

Helmholtz-Zentrum für Infektionsforschung

Publikationen der Arbeitsgruppe

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Wasmer,C.; Zimmer,A.; Sabate,R.; Soragni,A.; Saupe,S.J.; Ritter,Christiane*; Meier,B.H.; (2010). Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity. Journal of Molecular Biology: 402 2, 311-325

Greenwald,J.; Buhtz,C.; Ritter,Christiane*; Kwiatkowski,W.; Choe,S.; Maddelein,M.L.; Ness,F.; Cescau,S.; Soragni,A.; Leitz,D.; Saupe,S.J.; Riek,R.; (2010). The mechanism of prion inhibition by HET-S. Molecules and Cells: 38 6, 889-899

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Weitere Publikationen

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Siemer, A.B., Ritter, C., Steinmetz, M.O., Ernst, M., Riek, R., Meier, B.H.; (2006). 13C, 15N resonance assignment of parts of the HET-s prion protein in its amyloid form. J Biomol NMR: 34, 75-87 PubMed

Siemer, A.B., Arnold, A.A., Ritter, C., Westfeld, T., Ernst, M., Riek, R., Meier B.H.; (2006). Observation of highly flexible residues in amyloid fibrils of the HET-s prion. J Am Chem Soc: 128(40), 13224-13228 PubMed

Liu, Y., Ritter, C., Riek, R., Schubert, D.; (2006). The formation of bioactive amyloid Species by prion proteins in vitro and in cells. Neurosci Lett.: 406(3), 200-204

Luhrs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Dobeli, H., Schubert, D., Riek, R. ; (2005). 3D structure of Alzheimer's amyloid-beta(1-42) fibrils. Proc Natl Acad Sci USA: 102(48), 17342-17347 PubMed

Ritter, C., Maddelein, M.L., Siemer, A.B., Luhrs, T., Ernst, M., Meier, B.H., Saupe, S., Riek, R. ; (2005). Correlation of structural elements and infectivity of the HET-s prion. Nature: Correlation of structural elements and Infectivity of the HET-s prion, 844-848 PubMed

Siemer, A.B., Ritter, C., Ernst, M., Riek, R., Meier B.H; (2005). High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation. Angewandte Chemie International: 44, 2441-2444 PubMed

Ritter, C., Quirin, K., Kowarik, M., Helenius, A. ; (2005). Minor folding defects trigger local modification of glycoproteins by the ER folding sensor GT. EMBO J.: 24(9), 1730-1738 PubMed

Ritter, C., Luhrs, T., Kwiatkowski, W., Riek, R. ; (2004). 3D TROSY-HNCA(coded)CB and TROSY-HNCA(coded)CO experiments: triple resonance NMR experiments with two sequential connectivity pathways and high sensitivity. J Biomol NMR: 28, 289-294 PubMed

Balguerie, A., Dos Reis, S., Ritter, C., Chaignepain, S., Coulary-Salin, B., Forge, V., Bathany, K., Lascu, I., Schmitter, J.M., Riek, R., Saupe, S.J.; (2003). Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. EMBO J.: 22, 2071-2081 PubMed

Ritter, C., Helenius, A.; (2000). Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase. Nat Struct Biol.: 7, 278-280 PubMed

Pervushin, K., Gallius, V., Ritter, C.; Improved TROSY-HNCA experiment with suppression of conformational exchange induced relaxation. J Biomol NMR: 21, 161-166 PubMed

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17.05.2012