References 2000 - today

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

589. Pervushin, K., Fernàndez, C., Riek, R., Ono, A. Kainosho, M. and Wüthrich, K. (2000) J. Biomol. NMR 16, 39–46.
Determination of ^h2J_NN and ^h1J_HN coupling constants across Watson–Crick base pairs in the Antennapedia homeodomain–DNA complex using TROSY.

590. Lòpez Garcia, F., Szyperski, T., Dyer, J.H., Choinowski, T., Seedorf, U., Hauser, H. and Wüthrich, K. (2000) J. Mol. Biol. 295, 595–603.
NMR structure of the sterol carrier protein-2: implications for the biological role.

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

592. Wüthrich, K. (2000) Nature Struct. Biol. 7, 188–189.
Protein recognition by NMR.

593. Damberger, F., Nikonova, L., Horst, R., Peng, G., Leal, W. S. and Wüthrich, K. (2000) Protein Sci. 9, 1038–1041.
NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori.

594. Hochuli, M., Szyperski, T. and Wüthrich, K. (2000) J. Biomol. NMR 17, 33–42.
Deuterium isotope effects on the central carbon metabolism of Escherichia coli cells grown on a D₂O-containing minimal medium.

595. Wüthrich, K. (1999) in Kyoto Prizes & Inamori Grants 1998, pp. 104–141, The Inamori Foundation, Kyoto, Japan.
From Nature to Natural Science.

596. Lopez Garcia, F., Zahn, R., Riek, R. and Wüthrich, K. (2000) Proc. Natl. Acad. Sci. USA 97, 8334–8399.
NMR structure of the bovine prion protein.

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

598. Pervushin, K., Braun, D., Fernàndez C. and Wüthrich, K. (2000) J. Biomol. NMR 17, 195– 202.
[¹⁵N,¹H]/[¹³C,¹H]-TROSY for simultaneous detection of backbone ¹⁵N–¹H, aromatic ¹³C– ¹H and side-chain ¹⁵N–¹H₂ correlations in large proteins.

599. Salzmann, M., Pervushin, K., Wider, G., Senn, H. and Wüthrich, K. (2000) J. Am. Chem. Soc. 122, 7543–7548.
NMR assignment and secondary structure determination of an octameric 110 kDa protein using TROSY in triple resonance experiments.

600. Riek, R., Pervushin, K. and Wüthrich. K. (2000) Trends Biochem. Sci. 25, 462– 468.
TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution.

601. Güntert, P., Salzmann, M., Braun, D. and Wüthrich, K. (2000) J. Biomol. NMR 18, 129 – 137.
Sequence-specific NMR assignment of proteins by global fragment mapping with the program MAPPER.

602. Billeter, M. and Wüthrich, K. (2000) Arch. Virol. (Suppl.) 16, 251 – 263.
The prion protein globular domain and disease-related mutants studied by molecular dynamics simulations.

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

604. Liu, A., Luginbühl, P., Zerbe, O., Ortenzi, C., Luporini, P. and Wüthrich, K. (2001) J. Biomol. NMR 19, 75 – 78.
NMR structure of the pheromone Er-22 from Euplotes raikovi.

605. Horst, R., Damberger, F., Peng, G., Nikonova, L., Leal, W.S. and Wüthrich, K. (2001) J. Biomol. NMR 19, 79 – 80.
NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.

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

607. Frey, A.D., Fiaux, J., Szypersky, T., Wüthrich, K., Bailey, J.E. and Kallio, P.T. (2001) Appl. Environm. Microbiol. 67, 680 – 687.
Dissection of central carbon metabolism of hemoglobin-expressing Escherichia coli by ¹³C nuclear magnetic resonance flux distribution analysis in microaerobic bioprocesses.

608. Fernandéz, C., Adeishvili, K. and Wüthrich, K. (2001) Proc. Natl. Acad. Sci. USA 98, 2358– 2363.
Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles.

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

610. Wüthrich, K. (2001) in Prionen und Prionenkrankheiten (B. Hörnlimann, D. Riesner und H. Kretschmar, Hrsg.) pp. 69–-73, de Gruyter, Berlin.
Die Bestimmung der dreidimensionalen Struktur des zellulären Prion-Proteins PrP^C.

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

612. Wüthrich, K. (2001) in International Tables for Crystallography, Vol. F: Crystallography of Biological Macromolecules (M.G. Rossmann and E. Arnold, eds.) pp. 464–467, Kluwer, Dordrecht, The Netherlands.
Nuclear magnetic resonance (NMR) spectroscopy.

613. Güntert, P. and Wüthrich, K. (2001) Comp. Phys. Commun. 138, 155–169.
Sampling of conformation space in torsion angle dynamics calculations.

614. Fernández, C., Hilty, C., Bonjour, S., Adeishvili, K., Pervushin, K. and Wüthrich, K. (2001) FEBS Lett. 504, 173–178.
Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli.

615. Wüthrich, K. (2001) in Encyclopedia of Life Sciences, online at www.els.net..
Nuclear magnetic resonance (NMR) spectroscopy of proteins.

616. Wüthrich, K. (2001) Nature Struct. Biol. 8, 923–925.
The way to NMR structures of proteins.

617. Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. and Wüthrich, K. (2001) Proc. Natl. Acad. Sci. USA 98, 14374–14379.
NMR structure reveals intramolecular regulation mechanism for pheromone binding and release.

618. Riek, R., Güntert, P., Döbeli, H., Wipf, B. and Wüthrich, K. (2001) Eur. J. Biochem. 268, 5930–5936.
NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, A^ox and A^ox.

619. Zahn, R., Damberger, F., Ortenzi, C., Luporini, P. and Wüthrich, K. (2001) J. Mol. Biol. 313, 923–931.
NMR structure of the Euplotes raikovi pheromone Er-23 and identification of its five disulfide bonds.

620. Di Giuseppe, G., Miceli, C., Zahn, R., Damberger, F., Wüthrich, K. and Luporini, P. (2002) J. Eukaryot. Microbiol. 49, 86–92.
A structurally deviant member of the Euplotes raikovi pheromone family: Er-23.

621. Emmerling, M., Dauner, M., Ponti, A., Fiaux, J., Hochuli, M., Szyperski, T., Wüthrich, K., Bailey, J.E. and Sauer, U. (2002) J. Bacteriol. 184, 152–164.
Metabolic flux responses to pyruvate kinase knockout in Escherichia coli.

622. Pellecchia, M., Sem, D. S. and Wüthrich, K. (2002) Nature Rev. Drug Disc. 1, 211–219.
NMR in drug discovery.

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

624. Dauner, M., Sonderegger, M., Hochuli, M., Szyperski, T., Wüthrich, K., Hohmann, H.P., Sauer, U. and Bailey, J.E. (2002) Appl. Env. Microbiol. 68,1760–1771.
Intracellular carbon fluxes in riboflavin-producing Bacillus subtilis during growth on two-carbon substrate mixtures.

625. Luginbühl, P. and Wüthrich, K. (2002) Progr. Nucl. Magn. Reson. Spect. 40, 199–247.
Semi-classical nuclear spin relaxation theory revisited for use with biological macromolecules.

626. Herrmann, T., Güntert, P. and Wüthrich, K. (2002) J. Mol. Biol. 319, 209–227.
Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.

627. Etezady-Esfarjani, T., Hilty, C., Wüthrich, K., Rueping, M., Schreiber, J. and Seebach, D. (2002) Helv. Chim. Acta. 85, 1197–1209.
NMR-structural investigations of a β3-dodecapeptide with proteinogenic side chains in methanol and in aqueous solutions.

628. Fiaux, J., Bertelsen, E., Horwich, A. and Wüthrich, K. (2002) Nature 418, 207–211.
NMR analysis of a 900K GroEL–GroES complex.

629. Wüthrich, K. and Wider, G. (2002) in Encyclopedia of Nuclear Magnetic Resonance (D.M. Grant and R.K. Harris, eds.), Vol. 9, pp. 468–477, Wiley, New York.
Transverse relaxation-optimized NMR spectroscopy with biomacromolecular structures in solution.

630. Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. and Wüthrich, K. (2002) J. Mol. Biol. 322, 773–784.
NMR structures of 36- and 73-residue fragments of the calreticulin P-domain.

631. Hilty, C., Fernández, C., Wider, G. and Wüthrich, K. (2002) J. Biomol. NMR 23, 289–301.
Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles.

632. Riek, R., Fiaux, J., Bertelsen, E., Horwich, A. and Wüthrich, K. (2002) J. Am. Chem. Soc. 124, 12144–12153.
Solution NMR techniques for large molecular and supramolecular structures.

633. Fernández, C., Hilty, C., Wider, G. and Wüthrich, K. (2002) Proc. Natl. Acad. Sci. USA 99, 13533–13537.
Lipid–protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy.

634. Lee, D., Damberger, F., Guihong, P., Horst, R., Güntert, P., Nikonova, L., Leal, W. and Wüthrich, K. (2002) FEBS Lett. 531, 314–318.
NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH.

635. Herrmann, T., Güntert, P. and Wüthrich, K. (2002) J. Biomol. NMR 24, 171–189.
Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS.

636. Fiaux, J., Cakar, Z.P., Sonderegger, M., Wüthrich, K., Szyperski, T. and Sauer, U. (2003) Eukaryotic Cell 2, 170–180.
Metabolic-flux profiling of the yeasts Saccharomyces cerevisiae and Pichia stipitis.

637. Etezady-Esfarjani, T., Peti, W. and Wüthrich, K. (2003) J. Biomol. NMR 25, 167–168.
NMR assignment of the conserved hypothetical protein TM1290 of Thermotoga maritima.

638. Zahn, R., Güntert, P., von Schroetter, C. and Wüthrich, K. (2003) J. Mol. Biol. 326, 225–234.
NMR structure of a variant human prion protein with two disulfide bridges.

639. Lührs, T., Riek, R., Güntert, P. and Wüthrich, K. (2003) J. Mol. Biol. 326, 1549–1557.
NMR structure of the human doppel protein.

640. Wüthrich, K. (2003) Angew.Chem. Int. Ed. 42, 3340−3363.
NMR studies of structure and function of biological macromolecules (Nobel Lecture).

641. Wüthrich, K. (2003) Angew.Chem. 115, 3462−3486.
NMR–Untersuchungen von Struktur und Funktion biologischer Makromoleküle (Nobel-Vortrag).

642. Wüthrich, K. (2003) J. Biomol. NMR 27, 1–12.
Kurt Wüthrich: Biographical note.

643. Wüthrich, K. (2003) J. Biomol. NMR 27, 13–39.
NMR studies of structure and function of biological macromolecules (Nobel Lecture).

644. Wüthrich, K. (2003) in Les Prix Nobel 2002 (T. Frängsmyr and B. Lundeberg, eds. Almquist and Wiksell International, Stockholm, Sweden, pp. 219–234.

645. Wüthrich, K. (2003) in Les Prix Nobel 2002 (T. Frängsmyr and B. Lundeberg, eds.) Almquist and Wiksell International, Stockholm, Sweden, pp. 235–267.
NMR studies of structure and function of biological macromolecules (Nobel Lecture).

646. Hochuli, M., Wüthrich, K. and Steinmann, B. (2003) NMR Biomed. 16, 224–236.
Two-dimensional NMR spectroscopy of urinary glycosaminoglycans from patients with different mucopolysaccharidoses.

647. Hiller, S., Kohl, A., Fiorito, F., Herrmann, T., Wider, G., Tschopp, J., Grütter, M. and Wüthrich, K. (2003) Structure 11, 1198–1205.
NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain.

648. Braun, D., Wüthrich, K. and Wider, G. (2003) J. Magn. Reson. 165, 89–94.
Dissection of heteronuclear NMR experiments for studies of magnetization transfer efficiencies.

649. Hilty, C., Wider, G., Fernández, C. and Wüthrich, K. (2003) J. Biomol. NMR 27, 377–382.
Stereospecific assignments of the isopropyl methyl groups of the membrane protein OmpX in DHPC micelles.

650. Fernández, C. and Wüthrich, K. (2003) FEBS Lett. 555, 144–150.
NMR solution structure determination of membrane proteins reconstituted in detergent micelles.

651. Wüthrich, K. (2003) Biosci. Reports 23, 119−168.
NMR studies of structure and function of biological macromolecules (Nobel Lecture).

652. Wüthrich, K. and Wider, G. (2003) Magn. Reson. Chem. 41, 580-588.
Transverse relaxation-optimized NMR spectroscopy with biomacromolecular structures in solution.

653. Etezady-Esfarjani, T. and Wüthrich, K. (2004) J. Biomol. NMR 29, 99–100.
Letter to the Editor: NMR assignment of TM1442, a putative anti-σ factor antagonist from Thermotoga maritima.

654. Fernández, C., Hilty, C., Wider, G., Güntert, P. and Wüthrich, K. (2004) J. Mol. Biol. 336, 1211–1221.
NMR structure of the integral membrane protein OmpX.

655. Tafer, H., Hiller, S., Hilty, H., Fernández, C. and Wüthrich, K. (2004) Biochemistry 43, 860–869.
Nonrandom structure in the urea-unfolded Escherichia coli outer membrane protein X (OmpX).

656. Hilty, C., Wider, G., Fernández, C. and Wüthrich, K. (2004) Chem BioChem 5, 467–473.
Membrane protein – lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents.

657. Fiaux, J., Bertelsen, E.B., Horwich, A.L. and Wüthrich, K. (2004) J. Biomol. NMR 29, 280–297.
Uniform and residue-specific ¹⁵N-labeling of proteins on a highly deuterated background.

658. Iwai, H., Wider, G and Wüthrich, K. (2004) J. Biomol. NMR 29, 395–398.
Letter to the Editor: NMR structure of a variant 434 repressor DNA-binding domain devoid of hydroxyl groups

659. Etezady-Esfarjani, T., Herrmann, T., Peti, W., Klock, H.E., Lesley, S.A. and Wüthrich, K. (2004) J. Biomol. NMR 29, 403–406.
Letter to the Editor: NMR structure determination of the hypothetical protein TM1290 from Thermotoga maritima using automated NOESY analysis.

660. Almeida, M.S., Peti, W. and Wüthrich, K. (2004) J. Biomol. NMR 29, 453–454.
Letter to the Editor: ¹H-, ¹³C- and ¹⁵N-NMR assignment of the conserved hypothetical protein TM0487 from Thermotoga maritima.

661. Peti, W., Etezady-Esfarjani, T., Herrmann, T., Klock, H.E., Lesley, S.A. and Wüthrich, K. (2004) J. Struct. Funct. Genom. 5, 205–215.
NMR for structural proteomics of Thermotoga maritima: screening and structure determination.

662. Lysek, D.A. and Wüthrich, K. (2004) Biochemistry 43, 10393–10399.
Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.

663. Lysek, D.A., Nivon, L.G. and Wüthrich, K. (2004) Gene 341, 249–253.
Amino acid sequence of the Felis catus prion protein.

664. Hornemann, S., Schorn, C. and Wüthrich, K. (2004) EMBO Reports 5, 1159–1164.
NMR structure of the bovine prion protein isolated from healthy calf brains.

665. Kelker, M.S., Foss, T.R., Peti, W., Teyton, L., Kelly, J.W., Wüthrich, K. and Wilson, I.A. (2004) J. Mol. Biol. 342, 1237–1248.
Crystal structure of human triggering receptor expressed on myeloid cells 1 (TREM-1) at 1.47 Ǻ.

666. Pervushin, K., Wider, G., Iwai, H. and Wüthrich, K. (2004) Biochemistry 43, 13937–13943.
NMR structures of salt-refolded forms of the 434-repressor DNA-binding domain in 6 M urea.

667. Lysek, D.A., Schorn, C., Nivon, L.G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. and Wüthrich, K. (2005) Proc. Natl. Acad. Sci. USA 102, 640–645.
Prion protein NMR structures of cats, dogs, pigs and sheep.

668. Gossert, A.D., Bonjour, S., Lysek, D.A., Fiorito, F. and Wüthrich, K. (2005) Proc. Natl. Acad. Sci. USA 102, 646–650.
Prion protein NMR structures of elk and mouse/elk hybrids.

669. Calzolai, L., Lysek, D.A., Pérez, D.R., Güntert, P. and Wüthrich, K. (2005) Proc. Natl. Acad. Sci. USA 102, 651–655.
Prion protein NMR structures of chickens, turtles, and frogs.

670. Page, R., Peti, W., Wilson, I.A., Stevens, R.C. and Wüthrich, K. (2005) Proc. Natl. Acad. Sci. USA 102, 1901–1905.
NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline.

671. Michel, E., Damberger, F.F., Chen, A.M., Ishida, Y., Leal, W.S. and Wüthrich, K. (2005) J. Biomol. NMR 31, 65.
Assignments for the Bombyx mori pheromone-binding protein fragment BmPBP (1 – 128) at pH 6.5.

672. Pérez, D.R. and Wüthrich, K. (2005) J. Biomol. NMR 31, 260.
NMR assignment of the Xenopus laevis prion protein fragment xlPrP(98-226).

673. Nishiyama, M., Horst, R., Eidam, O., Herrmann, T., Ignatov, O., Vetsch, M., Bettendorf, P., Jelesarov, I., Grütter, M.G., Wüthrich, K., Glockshuber, R. and Capitani, G. (2005) EMBO J. 24, 2075–2086.
Structural basis of chaperone–subunit complex recognition by the type 1 pilus assembly platform FimD.

674. Peti, W., Herrmann, T., Zagnitko, O., Grzechnik, S.K. and Wüthrich, K. (2005) Proteins: Struct. Funct. Bioinform. 59, 387–390.
NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima.

675. Columbus, L., Peti, W., Etezady-Esfarjani, T., Herrmann, T. and Wüthrich, K. (2005) Proteins: Struct. Funct. Bioinform. 60, 552–557.
NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima.

676. Hiller, S., Fiorito, F., Wüthrich, K. and Wider, G. (2005) Proc. Natl. Acad. Sci. USA 102, 10876–10881.
Automated projection spectroscopy (APSY).

677. Hiller, S., Wider, G., Etezady-Esfarjani, T., Horst, R. and Wüthrich, K. (2005) J. Biomol. NMR. 32, 61–70.
Managing the solvent water polarization to obtain improved NMR spectra of large molecular structures.

678. Horst, R., Bertelsen, E.B., Fiaux, J., Wider, G., Horwich, A.L. and Wüthrich, K. (2005) Proc. Natl. Acad. Sci. USA 102, 12748–12753.
Direct NMR observation of a substrate protein bound to the chaperonin GroEL.

679. Peti, W., Johnson, M.A., Herrmann, T., Neuman, B.W., Buchmeier, M.J., Nelson, M., Joseph, J., Page, R., Stevens, R.C., Kuhn, P. and Wüthrich, K. (2005) J. Virol. 79, 12905– 12913.
Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7.

680. Fadel, W., Bettendorff, P., Herrmann, T., de Zevedo Jr, W.F., Oliveira, E.B., Yamane, T. and Wüthrich, K. (2005) Toxicon, 46, 759–767.
Automated NMR structure determination and disulfide bond identification of the myotoxin crotamine from Crotalus durissus terrificus.

681. Almeida, M.S., Herrman, T., Peti, W., Wilson, I.A. and Wüthrich, K. (2005) Protein Sci. 14, 2880 – 2886.
NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: Implications for 216 homologous DUF59 proteins.

682. Lee, D., Hilty, C., Wider, G. and Wüthrich, K. (2006) J. Magn. Reson. 178, 72–76.
Effective rotational correlation times of proteins from NMR relaxation interference.

683. Baker, K.A., Hilty, C., Peti, W., Prince, A., Pfaffinger, P.J., Wider, G., Wüthrich, K. and Choe, S. (2006) Biochemistry 45, 1663–1672.
NMR-derived dynamic aspects of N-type inactivation of a Kv channel suggest a transient interaction with the T1 domain.

684. Lührs, T., Zhan, R. and Wüthrich, K., (2006) J. Mol Biol. 357, 833–841.
Amyloid formation by recombinant lull-length prion proteins in phospholipid bicelle solutions.

685. Peti, W., Page, R., Moy, K., O’Neil-Johnson, M., Wilson, I.A., Stevens, R.C. and Wüthrich, K. (2005) J. Struct. Funct. Genom.6, 259–267.
Towards miniaturization of a structural genomics pipeline using micro-expression and microlcoil NMR.

686. Etezady-Esfarjani, T., Herrmann, T., Horst, R. and Wüthrich, K. (2006) J. Biomol. NMR. 34, 3–11.
Automated protein NMR structure determination in crude cell-extract.

687. Johnson, M., Peti, W., Herrmann, T., Wilson, I. and Wüthrich, K. (2006) Protein Sci. 15, 1030–1041.
Solution structure of As11650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence.

688. Almeida, M. S., Johnson, M.A. and Wüthrich, K. (2006) J. Biomol. NMR, DOI 10.1007/s10858-006-9018-9.
NMR assignment of the SARS-CoV protein nsp1.

689. Serrano, P., Almedia, M.S., Johnson, M.A. and Wüthrich, K. (2006) J. Biomol. NMR, DOI 10.1007/s10858-006-9017-x.
NMR assignment of the protein nsp3a from SARS-CoV.

690. Fiorito, F., Hiller, S., Wider, G. and Wüthrich, K. (2006) J. Biomol. NMR. 35, 27–37.
Automated resonance assignment of proteins: 6D APSY-NMR.

691. Etezady-Esfarjani, T., Placzek, W.J., Herrmann, T. and Wüthrich, K. (2006) Magn. Reson. Chem. 44, S61–S70.
Solution structures of the putative anti-σ-factor antagonist TM1442 from Thermotoga maritima in the free and phosphorylated states.

692. Horst, R., Wider, G., Fiaux, J., Bertelsen, E.B., Horwich, A.L. and Wüthrich, K. (2006) Proc. Natl. Acad. Sci. USA 103, 15445–15450.
Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures.

693. Placzek, W.J., Almeida, M.A. and Wüthrich, K. (2006) J. Biomol. NMR, DOI 10.1007/s10858-006-9042-9.
NMR assignment of a human cancer-related nucleoside triphosphatase.

694. Banci, L., Bertini, I., Cantini, F., DellaMalva, N., Herrmann, T., Rosato, A. and Wüthrich, K. (2006) J Biol. Chem. 281, 29141–29147.
Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease protein.

695. Placzek, W.J., Almeida, M.S. and Wüthrich, K. (2007) J. Mol. Biol. 367, 788–801.
NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase.

696. Almeida, M.S., Johnson, M.A., Herrmann, T., Geralt, M. and Wüthrich, K. (2007) J.Virol. 81, 3151–3161.
Novel β-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.

697. Gossert, A.D., Hiller, S., Fiorito, F. and Wüthrich K. (2007) J. Biolmol. NMR 38, 195.
NMR assignment of the E. coli type 1 pilus protein FimF.

698. Johnson, M.A., Southworth, M.W., Perler, F.B. and Wüthrich K. (2007) Biomol. NMR Assign. 1, 19–21.
NMR assignment of a KlbA intein precursor from Methanococcus jannaschii.

699. Placzek, W.J., Etezady-Esfarjani, T., Herrmann, T., Pedrini, B., Peti, W., Alimenti, C., Luporini, P. and Wüthrich, K. (2007) IUBMB Life 59, 578–585.
Cold-adapted signal proteins: NMR structures of pheromones from the antarctic ciliate Euplotes nobilii.

700. Johnson, M.A., Southworth, M.W., Herrmann, T., Brace, L., Perler, F.B. and Wüthrich, K. (2007) Protein Sci. 16, 1316–1328.
NMR structure of a Klba intein precursor from Methanococcus jannaschii.

701. Damberger, F.F., Ishida, Y., Leal, W.S. and Wüthrich, K. (2007) J. Mol. Biol. 373, 811–819.
Structural basis of ligand binding and release in insect pheromone-binding proteins: NMR structure of Antheraea polyphemus PBP1 at pH 4.5.

702. Serrano, P., Johnson, M.A., Almeida, M.S., Horst, R., Herrmann, T., Joseph, J.S., Neuman, B.W., Subramanian V., Saikatendu, K.S., Buchmeier, M.J., Stevens, R.C., Kuhn, P. and Wüthrich, K. (2007) J.Virol. 81, 12049–12060.
Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.

703. Chatterjee, A., Johnson, M.A., Serrano, P., Pedrini, B. and Wüthrich, K. (2007) Biomol. NMR Assign. 1, 191–194.
NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3.

704. Etezady-Esfarjani, T., Hiller, S., Villalba, C. and Wüthrich, K. (2007) J. Biomol. NMR 39, 229–238.
Cell-free protein synthesis of perdeuterated proteins for NMR studies.

705. Hiller, S., Wasmer, C., Wider, G. and Wüthrich, K. (2007) J. Am. Chem. Soc. 129, 10823–10828.
Sequence-specific resonance assignment of soluble nonglobular proteins by 7D APSY-NMR spectroscopy.

706. Sigurdson, C.J., Nilsson, K.P.R., Hornemann, S., Manco, G., Polymenidou, M., Schwarz, P., Leclerc, M., Hammarström, P., Wüthrich, K. and Aguzzi, A. (2007) Nature Methods 12, 1023–1030.
Prion strain discrimination using luminescent conjugated polymers.

707. Horst, R., Fenton, W.A., Englander, W.S., Wüthrich, K. and Horwich A.L. (2007) Proc. Natl. Acad. Sci. USA 104, 20788–20792.
Folding trajectories of human dihydrofolate reductase inside the GroEL-GroES chaperonin cavity and free in solution.

708. Pedrini, B., Placzek, W.J., Koculi, E., Alimenti, C., LaTerza, A., Luporini, P. and Wüthrich, K. (2007) J. Mol. Biol. 372, 277–286.
Cold-adaptation in sea-water-borne signal proteins: sequence and NMR structure of the pheromone En-6 from the antarctic ciliate Euplotes nobilii.

709. Gossert, A.D., Bettendorff, P., Puorger, C., Vetsch, M., Herrmann, T., Glockshuber, R. and Wüthrich, K. (2008) J. Mol. Biol. 375, 752–763.
NMR structure of the Escherichia coli type 1 pilus subunit FimF and its interactions with other pilus subunits.

710. Christen, B., Wüthrich, K. and Hornemann, S. (2008) FEBS J. 275, 263–270.
Putative prion protein from Fugu (Takifugu rubripes).

711. Hiller, S., Wider, G., Imbach, L.L. and Wüthrich, K. (2008) Angew. Chem. Int. Ed (2007) 47, 977–981.
Interactions with hydrophobic clusters in the urea-unfolded membrane protein OmpX.

712. Zhang, Q., Horst, R., Geralt, M., Ma, X., Hong, W., Finn, M.G. Stevens, R. and Wüthrich, K. (2008) J. Am. Chem. Soc. 130, 7357–7363.
Microscale NMR screening of new detergents for membrane protein structural biology.

713. Neuman, B.W., Joseph, J.S., Saikatendu, K.S., Serrano, P., Chatterjee, A., Johnson, M.A., Liao, L., Klaus, J.P., Yates, J.R., Wüthrich, K., Stevens, R., Buchmeier, M.J. and Kuhn, P. (2008) J.Virol. 82, 5279–5294.
Proteomics analysis unravels the functional repertoire of Coronavirus nonstructural proten 3.

714. Volk, J., Herrmann, T. and Wüthrich, K. (2008) J. Biomol. NMR 41, 127–138.
Automated sequence-specific protein NMR assignment using the memetic algorithm MATCH.

715. Christen, B., Pérez, D.R., Hornemann, S. and Wüthrich, K. (2008) J. Mol. Biol. 383, 306–312.
NMR structure of the bank vole prion protein at 20 ◦C contains a structured loop of residues 165–171.

716. Billeter, M., Wagner, G. and Wüthrich K. (2008) J. Biomol. NMR 42, 155–158.
Solution NMR structure determination of proteins revisited.

717. Fiorito, F., Herrmann, T., Damberger, F.F. and Wüthrich K. (2008) J. Biomol. NMR 42, 23–33.
Automated amino acid side-chain NMR assignment of proteins using 13C- and 15N-resolved 3D [1H,1H]-NOESY.

718. Serrano, P., Johnson, M.A., Chatterjee, A., Pedrini, B. and Wüthrich, K. (2008) Biomol. NMR Assign. 2, 135–138.
NMR assignment of the nonstructural protein nsp3(1066–1181) from SARS-CoV.

719. Hiller, S., Wider, G. and Wüthrich, K. (2008) J. Biomol. NMR. 42, 179–195.
APSY-NMR with proteins: practical aspects and backbone assignment.

720. Polymenidou, M., Moos, R., Scott, M., Sigurdson, C., Shi, Y.-Z, Yajima, B., Hafner-Bratkovic, I., Jerala, R., Hornemann, S., Wüthrich, K., Bellon, A., Vey, M., Garen, G., James, M.N.G., Kav, N. and Aguzzi, A. (2008) PLoS ONE 3, e3872, 1–17.
The POM monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes.

721. Sigurdson, C.J., Nilsson, K.P., Hornemann, S., Heikenwalder, M., Manco, G., Schwarz, P., Ott, D., Rülicke, T., Liberski, P.P., Julius, C., Falsig, J., Stitz, L., Wüthrich, K. and Aguzzi, A. (2009) Proc. Natl. Acad. Sci. USA 106, 304–309.
De novo generation of transmissible spongiform encephalopathy by mouse transgenesis.

722. Chatterjee, A., Johnson, M.A., Serrano, P., Pedrini, B., Joseph, J.J., Neuman, B.W., Saikatendu, K., Buchmeier, M.J., Kuhn, P. and Wüthrich, K. (2009) J. Virol. 83, 1823–1836.
NMR structure shows that the SARS-unique domain contains a macrodomain fold.

723. Hornemann, S., Christen, B., von Schroetter, C., Pérez, D.R. and Wüthrich, K. (2009) FEBS Journal 276, 2359–2367.
Prion protein library of recombinant constructs for structural biology.

724. Christen, B., Hornemann, S., Damberger, F.F. and Wüthrich, K. (2009) J. Mol. Biol. 389, 833–845.
Prion protein NMR structure from Tammar Wallaby (Macropus eugenii) shows that the β2–α2 loop is modulated by long-range sequence effects.

725. Alimenti,C., Vallesi, A., Pedrini, B., Wüthrich, K. and Luporini, P. (2009) IUBMB Life 61, 838–845.
Molecular cold-adaptation: Comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes.

726. Honnappa, S., Montenegro Gouveia, S., Weisbrich, A., Damberger, F.F., Bhavesh, N.S., Jawhari, H., Grigoriev, I., van Rijssel, F.J.A., Buey, R.M., Lawera, A., Jelesarov, I., Winkler, F.K., Wüthrich, K, Akhmanova, A. and Steinmetz, M.O (2009) Cell 138, 366–376.
An EB1-binding motif acts as a microtubule tip localization signal.

727. Hornemann, S., von Schroetter, C., Damberger, F.F. and Wüthrich, K. (2009) J. Biol. Chem. 284, 22713–22721.
Prion protein–detergent micelle interactions studied by NMR in solution.

728. Serrano, P., Johnson, M.A., Chatterjee, A., Neuman, B.W., Joseph, J.S., Buchmeier, M.J., Kuhn, P. and Wüthrich, K. (2009) J. Virol. 83, 12998–13008.
Nuclear magnetic resonance structure of the nucleic acid-binding domain of severe acute respiratory syndrome coronavirus nonstructural protein 3.

729. Stanczak, P., Horst, R., Serrano, P. and Wüthrich, K. (2009) J. Am. Chem. Soc. 131, 18450–18456
NMR characterization of membrane protein–detergent micelle solutions by use of microcoil equipment.

730. De Groot, C.O., Jelesarov, I., Damberger, F.F., Bjelić, S., Schärer, M.A., Bhavesh, N.S., Grigoriev, I., Buey, R.M., Wüthrich, K., Capitani, G., Akhmanova, A. and Steinmetz, M.O. (2010) J. Biol. Chem. 285, 5802–5814.
Molecular insights into mammalian end-binding protein heterodimerization.

731. Pérez, D.R., Damberger, F.F. and Wüthrich, K. (2010) J. Mol. Biol. 400, 121–128.
Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein.

732. Sigurdson, C.J., Nilsson, K.P.R., Hornemann, S., Manco, G., Fernández-Borges, Schwarz, P., Wüthrich, K. and Aguzzi, A. (2010) J. Clin. Invest. 120, 2590–2599.
A molecular switch controls interspecies prion disease transmission in mice.

733. Johnson, M.A., Chatterjee, A., Neuman, B.W. and Wüthrich, K. (2010) J. Mol. Biol. 400, 724–742.
SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding.

734. Vallesi, A., Alimenti, C., Di Giuseppe, G., Dini, F., Pedrini, B., Wüthrich, K. and Luporini, P. (2010) Polar Science 4, 237–244.
The water-born protein pheromones of the polar protozoan ciliate, Euplotes nobilii: Coding genes and molecular structures.

735. Johnson, M.A., Jaudzems, K. and Wüthrich, K. (2010) J. Mol. Biol. doi: 10.1016/jmb.2010.07.043,=.
NMR structure of the SARA-CoV nonstructural protein 7 in solution at pH 6.5.

736. Vila, J.A., Serrano, P., Wüthrich, K. and Scheraga, H.A. (2010) J. Biomol. NMR 48, 23–30.
Sequential nearest-neighbor effects on computed 13Cα chemical shifts.

737. Elsliger, M-A., Deacon, A.M., Godzik, A., Lesley, S.A., Wooley, J., Wüthrich, K. and Wilson, I.A. (2010) Acta Cryst. F.66, 1137–1142.
The JCSG high-throughput structural biology pipeline.

738. Wüthrich, K. (2010) Acta Cryst. F.66, 1365–1366.
NMR in a crystallography-based high-throughput protein structure-determination environment.

739. Jaudzems, K., Geralt, M., Serrano, P., Mohanty, B., Horst, R., Pedrini, B., Elsliger, M-A., Wilson, I.A. and Wüthrich, K. (2010) Acta Cryst. F. 66, 1367–1380.
NMR structure of the protein NP_247299.1: comparison with the crystal structure.

740. Mohanty, B., Serrano, P., Pedrini, B., Jaudzems, K., Geralt, M., Horst, R., Herrmann, T., Elsliger, M-A., Wilson, I.A. and Wüthrich, K. (2010) Acta Cryst. F. 66, 1381–1392.
Comparison of NMR and crystal structures for the proteins TM1112 and TM1367.

741. Serrano, P., Pedrini, B., Geralt, M., Jaudzems, K., Mohanty, B., Horst, R., Herrmann, T., Elsliger, M-A., Wilson, I.A. and Wüthrich, K. (2010) Acta Cryst. F. 66, 1393–1405.
Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites.

742. Choutko, A., Glättli, A., Fernández, C., Hilty, C., Wüthrich, K. and van Gunsteren, W.F. (2010) Eur Biophys. J. 40,39–58.
Membrane protein dynamics in different environments: simulation study of the outer membrane protein X in a lipid bilayer and in a micelle.

743. Orcajo-Rincón, A.L., Ortega-Gutiérrez, S., Serrano, P., Torrecillas, I.R., Wüthrich, K., Campillo, M., Pardo, L.,Viso, A., Benhamú, B. and López-Rodriguez, M.L. (2011) J. Med. Chem. 54, 1096–1100.
Development of non-peptide ligands of growth factor receptor-bound protein 2-Src homology 2 domain using molecular modeling and NMR spectroscopy.

744. Di Giuseppe, G., Erra, F., Dini, F., Alimenti, C., Vallesi, A., Pedrini, B., Wüthrich, K. and Luporini, P. (2011) Proc. Natl. Acad. Sci. USA. 108, 3181–3186.
Antarctic and Arctic populations of the ciliate Euplotes nobilii show common pheromone-mediated cell-cell signaling and cross-mating.

745. Michel, E., Damberger, F.F., Ishida, Y., Fiorito, F., Lee, D.H., Leal, W.S. and Wüthrich, K. (2011) J. Mol. Biol. 408, 922–931.
Dynamic conformational equilibria in the physiological function of the Bombyx mori pheromone-binding protein.

746. Wahab, A.T., Serrano, P., Geralt, M. and Wüthrich, K. (2011) Protein Science 20, 1137–1144.
NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554.

747. Koculi, Eda, Horst, R., Horwich, A.L. and Wüthrich, K. (2011) Protein Science 20, 1380–1386.
Nuclear Magnetic Resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.

748. Horst, R., Horwich, A.L. and Wüthrich, K. (2011) J. Am. Chem. Soc. 20, 16354–16357.
Translational diffusion of macromolecular assemblies measured using transverse-relaxation-optimized pulsed field gradient NMR.

749. Damberger, F.F., Christen, B., Pérez, D.R., Hornemann, S. and Wüthrich, K. (2011) Proc. Natl. Acad. Sci. USA 108, 17308–17313.
Cellular prion protein conformation and function.

750. Sigurdson, C.J., Joshi-Barr, S., Bett, C., Winson, O., Manco, G., Schwarz, P., Rülicke, T., Nilsson, K.P.R., Margalith, I., Raeber, A., Peretz, D., Hornemann, S., Wüthrich, K. and Aguzzi, A. (2011) J. Neurosci. 31, 13840–13847.
Spongiform encephalopathy in transgenic mice expressing a point mutation in the β2-α2 loop of the prion protein.