Publications

2)
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.
Abstract
 Article

3)
Glockshuber, R., Hornemann, S., Riek, R., Billeter, M., Wider, G. and Wüthrich, K. (1996).
Drei-dimensionale Struktur einer Domäne des zellulären Prion-Proteins aufgeklärt.
Spektrum der Wissenschaften9, 16­18.

4)
Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. and Wider, G. (1996).
NMR studies of the hydration of biological macromolecules.
Faraday Discuss. 103, 245-253.

5)
Glockshuber, R., Hornemann, S., Riek, R., Wider, G., Billeter, M. and Wüthrich, K. (1997).
Autonomous folding and three-dimensional structure of the carboxy-terminal domain of the mouse prion protein, PrP(121-231).
Proceedings NATO advanced research workshop, in press.

6)
Billeter, M., Riek, R., Wider, G., Hornemann, S., Glockshuber, R. and Wüthrich, K. (1997).
Prion protein NMR structure and species barrier for prion diseases.
Proc. Natl. Acad. Sci. USA 94, 7281-7285.
Abstract
Article

7)
Glockshuber, R., Hornemann, S., Riek, R., Wider, G., Billeter, M. and Wüthrich, K. (1997).
Three-dimensional NMR structure of a self-folding domain of the prion protein, PrP(121-231).
Trends Biochem Sci. 22, 241-242.
 Article

8)
Hornemann, S., Korth, C., Oesch, B., Riek, R., Wider, M., Wüthrich, K. and Glockshuber, R. (1997).
Recombinant full-length murine prion protein, mPrP(23­231): Purification and spectroscopic characterization.
FEBS Letters 413, 277-281.
Abstract
Article

9)
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.
Abstract

10)
Korth, C., Stierli, B., Streit, Moser, M., Schaller, O., Fischer, R., Schulz-Schaefer, W., Kretzschmar, H., Raeber, A., Braun, U., Ehrensperger, F., Hornemann, S., Glockshuber, R., Riek, R., Billeter, M., Wüthrich, K. and Oesch, B. (1997).
Prion (PrPSc)-specific epitope defined by a monoclonal antibody.
Nature 390 , 74-77.
Abstract

11)
Pervushin, K., Riek, R., Wider, G. and Wüthrich, K. (1997).
Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution.
Proc. Natl. Acad. Sci. USA  94, 12366-12371.
Abstract
Article

12)
Glockshuber, R., Hornemann, S., Billeter, M., Riek, R., Wider, G., Wüthrich, K. (1998).
Prion protein structural features indicate possible relations to signal peptidases.
FEBS Letters 426, 291-296.
Abstract
Article

13)
Pervushin K., Riek, R., Wider, G., Wüthrich, K. (1998). Transverse Relaxation-Optimized Spectroscopy (TROSY) for NMR studies of aromatic spin systems in 13C-labeled proteins.
J. Am. Chem. Soc.  120, 6394-6400.
Article

14)
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. USA95, 11667-11672.
Abstract
Article

15)
Glockshuber, R., Hornemann, S., Riek, R., Billeter, M., Wider, G., Liemann, S., Zahn, R. and Wüthrich, K. (1998).
Folding and Three-Dimensional NMR Structure of the Recombinant Cellular Prion Protein from the Mouse.
In PRIONS - Molecular and Cellular Biology (D. A. Harris, ed.), Horizon Scientific Press, pp. 1-25.

16)
Riek,R., Wider, G., Pervushin, K.  and Wüthrich, K. (1999).
Polarization transfer by cross-correlated relaxation in  solution NMR with very large  molecules.
Proc. Natl. Acad. Sci. USA  96, 4918-4923.
Abstract
Article

17)
Wüthrich, K. Billeter, M., Riek, R., Wider, G., Hornemann, S. and Glockshuber, R. (1999). Prion protein structure and pathology of transmissible spongiform encephalopathies in: Peptide Science - Present and Future  (Y. Shimonishi, ed.), Kluwer, Dordrecht, pp. 330-334.
 Article

18)
Pervushin, K., Wider, G., Riek, R. and Wüthrich, K. (1999).
The 3D NOESY-[1H,15N,1H]-ZQ-TROSY NMR experiment with diagonal peak suppression.
Proc. Natl. Acad. Sci. USA  96, 9607-9612.
Abstract
Article

19)
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.
Abstract

20)
Riek, R.,  Precheur, B., Wang, Y., Mackay, E.A., Wider, G., Guntert, P., Liu., A., Kagi, J.H.R.  and Wüthrich, K. (1999).
NMR structure of the sea urchin (Strongylocentrotus purpuratus) metallothionein MTA.
J. Mol. Biol.  291, 417-428.
Abstract
Article

21)
Wüthrich, K. , Riek, R.,  Wider, G.,  Garcia, F.L., Liu.,  A., Zahn, R., Hornemann, S.  and Glockshuber, R. (1999).
Structural biology of prion proteins.
Transfusion clinique et biologique  6, 31.

22)
Zahn, R., Liu, A., Luehrs, T., Riek, R., von Schroetter, C., Garcia, F.L., Billeter, M., Calzolai, L., Wider, G. and Wüthrich, K. (2000).
NMR solution structure of the human prion protein.
Proc. Natl. Acad. Sci. USA 97, 145-150.
Abstract
Article

23)
Pervushin, K., Fernandez, C., Riek, R., Ono, A., Kainosho, M. and Wüthrich, K. (2000).
Determination of (h2)J(NN) and (h1)J(HN) coupling constants across Watson-Crick base pairs in the Antennapedia homeodomain-DNA complex using TROSY.
J. Biomol. NMR 16, 39-46.
Abstract
Article

24)
Liu, A., Riek, R.,  Wider, G., von Schroetter C., Zahn, R. and Wüthrich, K. (2000).
NMR experiments for resonance assignments of C-13, N-15 doubly-labeled flexible polypeptides: Application to the human prion protein hPrP(23-230).
J. Biomol. NMR 16, 127-138.
Abstract
Article

25)
Lopez-Garcia, F., Zahn, R., Riek, R. and Wüthrich, K. (2000).
NMR  structure of the bovine prion protein.
Proc. Natl. Acad. Sci. USA 97, 8334-8339.
Abstract
Article

26)
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.
Abstract
Article

27)
Riek, R., Pervushin, K.  and Wüthrich, K. (2000).
TROSY and CRINEPT:NMR with large molecular and supramolecular structures in solution.
TiBS 25, 462-468.
Abstract
Article

28)
Riek, R., Pervushin, K., Fernandez, C., Kainosho, M.  and Wüthrich, K. (2001).
[13C,13C]- and [13C,1H]-TROSY in a triple resonance experiment for ribose-base and intrabase correlations in nucleic acids.
J. of Am. Chem. Soc.  123, 658-664.
Abstract
Article
 

29)
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.
Abstract
Article

30)
Riek, R. (2001).
Characterization of Hydrogen Bond Lengths in Watson-Crick Base pairs by Cross-correlated Relaxation
J. of Magn. Reson.  149, 149-153.
Abstract
Article

31)
Wüthrich, K. and Riek, R. (2001).
Three-dimensional structures of prion proteins
Adv. in Prot. Chem.  57, 55-82.

32)
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.
Abstract
Article

33)
Riek, R. (2001)
Enhancement of the steady-state magnetization in TROSY experiments
J. Biomol. NMR 21, 99-105.
Article

34)
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.
Abstract
Article

35)
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 calretiuclin P-domain.
Proc. Natl. Acad. Sci. USA 99, 19544-1959.
Abstract
Article

36)
Riek, R., Fiaux, J., Bertlesen, E.B., Horwich, A.L. and Wuthrich, K. (2002)
Solution NMR techniques for large molecular and supramolecular structures.
J. Am. Chem. Soc. 124, 12144-12153.
Abstract
Article

37)
Riek, R. (2002)
TROSY: Transverse Relaxation-Optimized Spectroscopy
in BioNMR in Drug Research (ed. Oliver Zerbe)
Methods and Principles in Medicinal Chemistry 16, 227-241, Wiley-VCH, Weinheim (Germany).
Article

38)
Luhrs, T., Riek, R., Guntert,  P. and Wuthrich, K. (2003)
NMR structure of the Human Doppel Protein.
J. Mol. Biol. 326, 1549-1557.
Abstract
Article

39)
Kwiatkowski, W. and Riek, R. (2003)
Chemical shift-dependent apparent scalar couplings: An alternative concept of chemical shift monitoring in multi-dimensional NMR experiments.
J. Biomol. NMR 25, 281-290.
Abstract
Article

40)
Riek, R. and Luhrs,  T. (2003)
Three-dimensional structures of the prion protein and its doppel
Clin. Lab. Med. 23, 209-225.
Abstract
Article

41)
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.
Abstract
Article

42)
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. 18, 5606-5618.
Article

43)
Grace, C.R.R. and Riek, R. (2003)
Pseudomultidimensional NMR by Spin-state Selective Off-Resonance Decoupling
J. Am. Chem. Soc. 125, 16104-16113.
Article

44)
Pegan, S., Kwiatkowski, W., Choe, S and Riek, R. (2003)
High-throughput backbone resonance assignment of small 13C,15N-labeled proteins by a triple-resonance experiment with four sequential connectivity pathways using chemical shift-dependent, apparent 1J(1H,13C): HNCACBcodedHAHB
J. Magn. Reson. 165, 315-319.
Article

45)
Ritter, C., Luhrs, T., Kwiatkwoski W. and Riek, R. (2004)
3D TROSY-HNCAcodedCB and TROSY-HNCAcodedCO experiments: Triple resonance experiments with two sequential connectivity pathways and high sensitivity.
J. Biomol NMR. 28, 289-294.
Article
 
 46)
Grace, C.R., Perrin, M.H., DiGruccio, M.R. Miller, C.L., Rivier, J.E. Vale, W.W., Riek, R. (2004)
NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor. Proc. Natl. Acad. Sci. USA, 101, 12836-12841.
Article

47)
Grace, C.R., Durrer, L., Koerber, S.C., Erchegyi, J., Reubi, J.C., Rivier, J., Riek, R. (2005) , Somatostatin Receptor 1 Selective Analogs: 4. Three-Dimensional Consensus Structure by NMR. J. Med. Chem. 48, 523-533.
Article

48)
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.
Article

49)
Roosild, T.P., Greenwald, J. Vega, M. Castronovo, S., Riek R., Choe, S. (2005) NMR structure of Mistic, a membrane integrating protein for membrane protein expression. Science, 307, 1317-1321.
Article
Supplementary Material 

57)
Perrin, M.H, Grace, C.R., Riek, R., Vale, W.W. (2006) The three-dimensional structure of the N-terminal domain of a corticotropin releasing factor receptor: sushi domains and the B1 family of G protein-coupled receptors. Ann N.Y. Acad. Sci. 1070:105-119.
Article

58)
Liu, Y., Ritter, C., Riek, R. Schubert, D. (2006) The formation of bioactive amyloid speceis by prion proteins in vitro and in cells.  Neurosci. Lett., 406, 200-204.
Article

 59)
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, 13224-13228.
Article

Talks

• Riek, R., Wider, G., Billeter, M., Liemann, S., Hornemann, S., Glockshuber, R. and Wüthrich, K.(1997). Prion Protein NMR structure and Familial Spongiform Encephalopathies INSERM: Molecular Mechanisms of Infection and Pathology in Prion Diseases, Aix-Les Bains, France, 16th-20. November, (1997).
• Riek, R., Wider, G., Hornemann, S. and Glockshuber, R. (1998).Prion protein structure and pathology of transmissible spongiform encephalopathies (TSE). Proceedings First International Peptide Symposium, Kyoto. (1998).
• Riek, R. (1998). Das Prion Protein. Zentralschweizerische Internisten Vereinigung, Luzern, Switzerland. 8th April 1998.
• Riek, R. (1998). Physik, Eiweisse & Rinderwahnsinn. Volkshochschule, Schwyz, Switzerland. 30th October, (1998).
• Riek, R. (1999). Solution structure of the Mouse Prion Protein. Reunion de suivi des recherches engagees sur les ESST et les Prions, Bougival, France, 25th-26. January, (1999).
• Riek, R. (1999). NMR, a Tool for Structural Studies of Small, Highly Flexible or Large Macromolecules. Strucutral Characterization of Proteins by NMR, X-ray Diffraction and Computational Methods. Verona, Italy, 17th-20. February, (1999).
• Riek, R. (1999). TROSY and CRINEPT, Tokyo Metropolitan University,Tokyo, Japan, 20th August, (1999).
• Riek, R., (1999). NMR structure of the mouse prion protein: Implications to the species barrier and familial diseases. The 4th Keihanna International Conference on Molecular Biophysics- Structural Biology of Proteins and Nucleic Acids: Molecular Basis of Noncanonical Structures, Kyoto, Japan, 23rd-25th August, (1999).
• Riek, R., (2000). NMR with very large molecules. Institute of physical chemistry, ETH Zuerich,  Switzerland.
• Riek, R., (2000). Transverse Relaxation-Optimized Spectroscopy and the three dimensional structure of the prion protein. Contribution of NMR to Structural Biology, Biozentrum, Basel.
• Riek, R. (2000). Structural Studies on the N-terminal "flexible tail" of PrP. International Symposium on Prion Diseases and Related Processes, Annecy, France.
• Riek, R. (2000). Prion Protein und BSE. Erwachsenenbildung Liestal, Liestal, Switzerland.
• Riek, R. (2001). Transverse Relaxation-Optimized Spectroscopy and the three dimensional structure of the prion protein. The Salk Institute, San Diego, U.S.A.
• Riek, R. (2001) NMR with very large molecules ICMRBS, Toronto
• Riek, R. (2003). Spin-state selective off-resonance decoupling. EPFL, Lausanne, Switzerland.
• Riek, R. (2003). Protein NMR, Pfizer , San Diego, U.S.A.
• Riek, R. (2004). Conformational switches of amyloid proteins, ETH Zurich, Switzerland.
• Riek, R. (2004). Membrane protein structures by solution NMR, ETH Zurich, Switzerland.
• Riek, R. (2004). Membrane protein structures by solution NMR, University of Zuerich, Switzerland.
• Riek, R. (2004). Mad cow disease. Art&Science Forum, San Diego.
• Riek, R. (2005). Structure of Alzheimer Abeta(1-42) fibrils, Adler symposium, San Diego.
• Riek, R. (2005). Structure of Alzheimer Abeta(1-42) fibrils, The Scripps Research Institute, San Diego.
• Riek, R. (2005). Structure of amyloid fibrils, The American Peptide Symposium, San Diego .
• Riek, R. (2005). 4 talks: TROSY; Structure determination of membrane proteins by NMR; 3D structures of amyloid fibrils, Correlated motion in proteins. RRR workshop, Yokohama, Japan.
• Riek, R. (2005). 3D structures of amyloid fibrils, Osaka University, Osaka, Japan.
• Riek, R. (2005). 3D structures of amyloid fibrils, Neuroscience Seminar, Princeton. November 3.
  
• Riek, R. (2005). 3D structures of amyloid fibrils, Structural biology Seminar, University of California Berkley. October 17
• Riek, R. (2006). Membrane protein structure determination by NMR, University Southwestern, Dallas, March 23.
• Riek, R. (2006). 3D structure of membrane proteins by solution NMR, The Burnham Institute, January 28. /font>
• Riek, R. (2006). 3D structures of amyloid fibrils, The Adler foundation, San Diego, Feb 6-8.
• Riek, R. (2006). 3D structure of the binding domain of corticotropin releasing factor receptor, Gordon conference, Ventura, Feb. 19-20.
  
• Riek, R. (2006). Structure of amyloid fibrils, Keystone Conference, Feb. 21-26. Colorado .
• Riek, R. (2006). Structure of amyloid fibrils, FASEB Conference, June. 10-15. Colorado
• Riek, R. (2006). Structure of amyloid fibrils and membrane proteins studied by NMR, University Frankfurt, Fankfurt. June, 5.
• Riek, R. (2006). Structure of amyloid fibrils and membrane proteins studied by NMR, ETH Zurich, June 18.
• Riek, R. (2006). Structural investigations of membrane proteins by NMR, NMR workshop, Utrecht, June 18-19.
• Riek, R. (2006). Structure of Alzheimer Abeta(1-42) fibrils, American Protein Society, San Diego. August 5-9.
• 
  
Riek, R. (2006). Structure of Alzheimer Abeta(1-42) fibrils, FASEB conference, July 2-6, Saxtons River, Vermont.
• Riek, R. (2006). Structural investigations of KcsA potassium channel, ICMRBS, Goettingen, August 20-25. /font>
• Riek, R. (2007). Structural investigations of amyloid fibrils, Annual Meeting of the American society of Biochemistry and Molecular Biology, April 28-May 2, Washington DC.
  
•  Riek, R. (2007). Structural investigations of amyloid fibrils,. 11th Annual Structural Biology Symposium, May 18-19, Galveston.
  
• Riek, R. (2007). Structural Studies of Aggregates, 11th Chianti Workshop, Vallombrosa, June 3-8. 2007
  
• Riek, R. (2007). Structural investigations of amyloid fibrils, Gordon Research Conference, Plymouth, June 17-22.
Riek, R. (2007). Structural investigations of protein aggregates, Aguzzi retreat, Valens Switzerland, August 16-19, 2007.
i>Riek, R. (2007). Structural investigations of protein aggregates, Swiss NMR symposium Switzerland, September 4, 2007.

• Riek, R. (2007). Structural investigations of amyloid fibrils, Murnau, Germany, September 5-8, 2007.
  
• Riek, R. (2007). Structural investigations of amyloid fibrils, Frankfurt, Germany,November 16-17, 2007.
  
• Riek, R. (2008). Structural investigations of amyloid fibrils, UCLA, January 31, 2008.
• Riek, R. (2008). Structural and dynamical investigations of KcsA potassium channel, Biophysical Society Annual Meeting, Long Beach, February 2-6, 2008.
  >Riek,R. (2008). Structural investigations of membrane proteins, ENC, Asilomar, March 9-14, 2008.
• l,Helvetica"> Riek,R. (2008). Structural investigations of protein aggregates, ICMRBS San Diego, August 24-29, 2008.
• l,Helvetica"> Riek,R. (2008). Structural investigations of protein aggregates, Cologne, September 14-16, 2008.
• Riek,R. (2008). Structural investigations of protein aggregates, Regensburg, September 22-25, 2008.
• < Riek,R. (2008). Structural investigations of protein aggregates, Murnau, Murnau, October 16-18.
• Riek,R. (2009). Structural investigations of protein aggregates, Halle, February 8-11, 2009 ="Arial,Helvetica"> Riek,R. (2008). Structural investigations of protein aggregates, Regensburg, September 22-25, 2008.
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