Protein Folding

Ou, H.D., Kwiatkowski, W., Deerinck, T., Noske, A., Blain, K.Y., Land, H., Soria, C., Powers, C.J., Shu, X., Tsien, R., Fitzpatrick, J.A.J., Long, J.A., Ellisman, M.H., Choe,S., O'Shea, C.C. (2012) Structure of E4-ORF3 reveals a viral supramolecular assembly that inactivates multiple tumor suppressors. Cell, 151, 304-19 [Cover].

Greenwald, J., Buhtz, C., Ritter, C., 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. Mol. Cell, 38, 889-99.

Kefala, G., Ahn, C., Krupa, M., Esquivies, L., Maslennikov, I., Kwiatkowski, W., Choe, S. (2010) Structures of the OmpF porin crystallized in the presence of foscholine-12. Protein Sci. 19(5), 1117-25.

Wang, L., Maji, S.K., Sawaya, M.R., Eisenberg, D., Riek, R. (2008) Bacterial Inclusion Bodies Contain Amyloid-Like Structure. PLoS Biol. 6, e195.

Rodgers, L., Gamez, A., Riek, R., Ghosh, P. (2008) The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE. J Biol Chem.283, 20857-63.

Vilar, M., Chou, H.T., Luhrs, T., Maji, S.K., Riek-Loher, D., Verel, R., Manning, G., Stahlberg, H., Riek, R. (2008) The fold of alpha-synuclein fibrils. Proc Natl Acad Sci U S A. 105,8637-42.

Maji, S.K., Schubert, D., Rivier, C., Lee, S., Rivier, J.E., Riek, R. (2008) Amyloid as a depot for the formulation of long-acting drugs. PLoS Biol., 6,e17.

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, 200-4.

T. Roosild, S. Castronovo, S. Choe (2006) ) Structure of anti-FLAG M2 Fab domain and its use in the stabilization of engineered membrane proteins. Acta Cryst. F 62, 835-839.

Roosild TP, Vega M, Castronovo S, Choe S. (2006) Characterization of the family of Mistic homologues. BMC Struct Biol. 6,10

Luhrs, T., Ritter, C., Adrianm 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, 17342-7.

Christiane Ritter, Marie-Lise Maddelein, Ansgar Siemer, Thorsten Luhrs, Matthias Ernst, Beat Meier, Sven Saupe, Roland Riek (2005) Correlation of structural elements and infectivity of the HET-s prion. Nature 435, 844-848.

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.

Tarmo P. Roosild & Senyon Choe (2005) Redesigning an integral membrane K+ channel into a soluble protein Protein Engineering, 18, 79-84.

Tarmo P. Roosild, Jason Greenwald, Mark Vega, Samantha Castronovo, Roland Riek, and Senyon Choe (2005) NMR Structure of Mistic, a Membrane-Integrating Protein for Membrane Protein Expression Science 307,1317-21.

Grace, C.R.R., Koerber, S. C., Erchegyi, J., Reubi, J.C., Rivier, J. and Riek, R. (2003) Novel sst4-selective Somatostatin (SRIF) Agonists. 4. Three-Dimensional Consensus structure by NMR. J. Med. Chem. online, 1-13.

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

Riek, R. and Luhrs, T. (2003) Three-dimensional structures of the prion protein and its doppel Clin. Lab. Med. 23, 209-225.

Luhrs, T., Riek, R., Guntert, P. and Wuthrich, K. (2003) NMR structure of the Human Doppel Protein. J. Mol. Biol. 326, 1549-1557.

Frickel, E.M.,Riek, R., Jelesarov, I. Helenius, A., Wutrhich, K. and Ellgaard, L. (2002) TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc. Natl. Acad. Sci. USA, 99, 1954-1959.

Ellgaard, L., Riek, R., Braun, D., Herrmann, T., Helenius, A., and Wüthrich, K. (2001). Three-dimensional structure topology of the calretiuclin P-domain based on NMR assignment. FEBS Lett. 488, 69-73.

Wuthrich, K. and Riek, R. (2001). Three-dimensional structures of prion proteins. Adv. in Prot. Chem. 57, 55-82.

Ellgaard, L., Riek, R., Guentert, P, Herrmann, T., Helenius, A., and Wüthrich, K. (2001). NMR structure of the calreticulin P-domain. Proc. Natl. Acad. Sci. USA 98, 3133-3138.

Riek, R., Guntert, P., Dobeli, H., Wipf, B., and Wutrhich, K. (2001) NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Abeta(1-40)ox and Abeta(1-42)ox. Eur. J. Biochem 268, 5930-5936.

Calzolai, L., Lysek, D. A., Guentert, P., von Schroetter, C., Riek, R., Zahn, R. and Wüthrich, K. (2000). NMR structures of three single-residue variants of the human prion protein. Proc. Natl. Acad. Sci. USA 97, 8340-8345.

Liu, A., Riek, R., Zahn, R., Hornemann, S., Glockshuber, R. and Wüthrich, K. (1999). Peptides and proteins in neurodegenerative disease: helix propensitiy of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy. Biopolymers 51, 145-152.

Riek, R., Wider, Billeter, M., Hornemann, S., G., Glockshuber, R. and Wüthrich, K. (1998). Prion protein NMR structure and familial human spongiform encephalopathies. Proc. Natl. Acad. Sci. USA 95, 11667-11672

Riek, R., Hornemann, S., Wider, G., Glockshuber, R. and Wüthrich, K. (1997). NMR characterization of the full-length recombinant murine prion protein, mPrP(23­231). FEBS Letters 413, 282-288.

Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R. and Wüthrich, K. (1996). NMR structure of the mouse prion protein domain PrP(121­231). Nature 382, 180­182.