Publications before 2003 incl. 2000

Main content

2002

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).

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.

Frickel, E.M., Riek, R., Jelesarov, I. Helenius, A., Wuthrich, 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.

2001

Riek, R., Guntert, P., Dobeli, H., Wipf,  B., and Wuthrich, 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.

Riek, R. (2001)
Enhancement of the steady-state magnetization in TROSY experiments

J. Biomol. NMR 21, 99-105.

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.

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

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

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.

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.

2000

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

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.

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.

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.

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.

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.

1999

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.

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.

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.

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.

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.

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.

1998

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. (PDF, 2.1 MB)
In PRIONS - Molecular and Cellular Biology (D. A. Harris, ed.), Horizon Scientific Press, pp. 1-25.

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.

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.

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.

1997

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.

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.

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

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

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.

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.

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.

1996

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.

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 Wissenschaften 9, 16-18.

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

Wider, G., Riek, R. and Wüthrich, K. (1996).
Diffusion filters for separation of solvent-protein and protein-protein nuclear overhauser effects (HYDRA).
J. Am. Chem. Soc. 118, 11629-11634.

 
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