References 2010 - today
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Molecular insights into mammalian end-binding protein heterodimerization.
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Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein.
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NMR structure of the SARA-CoV nonstructural protein 7 in solution at pH 6.5.
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Dynamic conformational equilibria in the physiological function of the Bombyx mori pheromone-binding protein.
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NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554.
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Nuclear Magnetic Resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.
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Translational diffusion of macromolecular assemblies measured using transverse-relaxation-optimized pulsed field gradient NMR.
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Spongiform encephalopathy in transgenic mice expressing a point mutation in the β2-α2 loop of the prion protein.
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Biased signaling pathways in β2-adrenergic receptor characterized by 19F-NMR.
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Translational diffusion measurements by microcoil NMR in aqueous solutions of the Fos-10 detergent-solublized membrane protein OmpX.
753. Vallesi, A., Alimenti, C., Pedrini, B., Di Giuseppe, G., Dini, F., Wüthrich, K. and Luporini, P. (2012) Marine Genomics 8, 9–13.
Coding genes and molecular structures of the diffusible signaling proteins (pheromones) of the polar ciliate, Euplotes nobilii.
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High-yield Escherichia coli-based cell-free expression of human proteins.
755. Serrano, P., Pedrini, B., Mohanty, B., Geralt, M., Herrmann, T. and Wüthrich K. (2012) J. Biomol. NMR 53, 341–354.
The J-UNIO protocol for automated protein structure determination by NMR in solution.
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Cell-free expression of disulfide-containing eukaryotic proteins for structural biology.
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Micro-coil NMR to monitor optimization of the reconstitution conditions for the integral membrane protein OmpW in detergent micelles.
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Prion protein mPrP[F175A]: Structure and stability in solution.
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β2-adrenergic receptor solutions for structural biology analyzed with micro-scale NMR diffusion measurements.
760. Stevens, R., Cherezov, V., Katritch, V., Abagyan, R., Kuhn, P., Rosen, H. and Wüthrich, K. (2013) Nature Rev. Drug Discovery 12, 1–10.
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Amino acid-selective segmental isotope labeling of multidomain proteins for structural biology.
763. Christen, B., Damberger, F.F., Pérez, D.R., Hornemann, S. and Wüthrich, K. (2013) Proc. Natl. Acad. Sci. USA 110, 8549–8554.
Structural plasticity of the cellular prion protein and implications in health and disease.
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Structural representative of the protein family PF14466 has a new fold and establishes links with the C2 and PLAT domains from the widely distant Pfams PF00168 and PF01477.
765. Zarco-Zavala, M., Morales-Ríos, E., Serrano-Navarro, P., Wüthrich, K., Mendoza-Hernández, G., Ramírez-Silva L. and García-Trejo, J.J. (2013) Biochim. Biophys. Acta 1827, 60.
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766. Didenko, T., Liu, J.J., Horst, R., Stevens, R.C. and Wüthrich, K. (2013) Curr. Opin. Struct. Biol. 23, 1–8.
Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs.
767. Pedrini, B., Serrano, P., Mohanty, B., Geralt, M. and Wüthrich, K. (2013) Biopolymers 99, 825–831.
NMR-profiles of protein solutions.
768. Horst, R., Liu, J.J., Stevens, R.C. and Wüthrich, K. (2013) Angew. Chem. Int. Ed. 52, 331–335.
β2-adrenergic receptor activation by agonists studied with 19F-NMR Spectroscopy.
769. Damberger, F.F., Michel, E., Ishida, Y., Leal, W.S. and Wüthrich, K. (2013) Proc. Natl. Acad. Sci. USA 110, 18680–18685.
Pheromone discrimination by a pH-tuned polymorphism of the Bombyx mori pheromone-binding protein.
770. Kurt, T.D., Bett, C., Fernández-Borges, N., Johi-Barr, S., Hornemann, S., Rülicke, T., Castilla, J., Wüthrich, K., Aguzzi, A. and Sigurdson, C.J. (2014) J. Neurosci. 34, 1022–1027.
Prion transmission prevented by modifying the β2-α2 loop structure of host PrPC.
771. Sušac, L., Horst, R. and Wüthrich, K. (2014) ChemBioChem 15, 995–1000.
Solution-NMR characterization of outer-membrane protein A from E. coli in lipid bilayer nanodiscs and detergent micelles.
772. Horst, R., Stanczak, P. and Wüthrich, K. (2014) Structure 22, 1–6.
NMR polypeptide backbone conformation of the E. coli outer membrane protein W.
773. Serrano, P., Geralt, M., Mohanty, B. and Wüthrich, K. (2014) J. Mol. Biol. 426, 2547–2553.
NMR structures of α-proteobacterial ATPase-regulating ζ-subunits.
774. Wüthrich, K., Wilson I.A., Hilvert, D., Wolan, D. and De Wit, A., eds. (2014) New Chemistry and New Opportunities from the Expanding Protein Universe. Proceedings of the 23rd Solvay Conference on Chemistry, World Scientific, Singapore.
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Studies of GPCR conformations in non-crystalline milieus.
777. Jaudzems, K., Pedrini, B., Geralt, M., Serrano, P. and Wüthrich, K. (2004) J. Biomol. NMR; DOI:10.1007/s10858-014-9886-3.
J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumonia TIGR4.
778. Dutta, S.K., Serrano, P., Proudfoot, A., Geralt, M., Pedrini, B., Herrmann, T. and Wüthrich, K. (2004) J. Biomol. NMR; DOI: 10.1007/s10858-014-9881-8.
APSY-NMR for protein backbone assignment in high-throughput structural biology.
779. Horst. R. and Wüthrich, K. (2015) Bio-protocol. 5 (14) http://www.bio-protocol.org/e1539.
NMR-profiles of protein solutions.
780. Didenko, T., Proudfoot, A., Dutta, S.M., Serrano, P. and Wüthrich, K. (2015) Chem. Eur. J. DOI:10.1002/chem.201502554.
Non-uniform sampling and J-UNIO Automation for efficient protein NMR structure determination.
781. Dutta, S.K., Serrano, P., Geralt, M., Axelrod, H.L., Xu, Q., Lesley, S.A., Godzik, A., Deacon, A.M., Elsliger, M.A., Wilson, I.A. and Wüthrich, K. (2015) Protein Sci. DOI: 10.1002/pro.2743.
Cofactor-induced reversible folding of flavodoxin-4 from Lactobacillus acidophilus.
782. O’Connor, C., White, K.L., Doncescu, N., Didenko, T., Roth, B.L., Czaplicki, G., Stevens, R.C., Wüthrich, K. and Milon, A. (2015) Proc. Natl. Acad. Sci. USA 112, 11852–11857.
NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opiod receptor.
783. Lamichhane, R., Liu, J.J., Pljevaljcic, G., White, K.L., van der Schans, E., Katritch, V., Stevens, R.C., Wüthrich, K. and Millar, D.P. (2015) Proc. Natl. Acad. Sci. USA 112, 14254–14259.
Single-molecule view of basal activity and activation mechanisms of the G protein-coupled receptor β2AR.
784. Wüthrich, K. (2015). JOSHA – J. Science, Humanities and Arts. DOI: 10.17160/josha.2.7.84.
The NMR view of proteins.
785. Sušac, L., O’Connor, C.O., Stevens, R.C. and Wüthrich, K. (2015) Angew. Chem. Int. Ed. 54, 15246–15249.
In-membrane chemical modification (IMCM) for site-specific chromophore labeling of GPCRs.
786. Martin, B.T., Serrano, P., Geralt, M. and Wüthrich K. (2016) Structure 24, 1–7.
Nuclear magnetic resonance structure of a novel globular domain in RBM10 containing OCRE, the octamer repeat sequence motif.
787. Stepanyuk, G.A., Serrano, P., Peralta, E., Farr, C.L., Axelrod, H.L., Geralt, M., Das, D., Chiu, H.J., Jaroszewski, L., Deacon, A.M., Lesley, S.A., Elsliger, M.A., Godzik, A., Wilson, I.A., Wüthrich, K., Salomon, D.R. and Williamson, J.R. (2016) Acta Cryst D. 72, 497–511.
UHM–ULM interactions in the RBM39–U2AF65 splicing-factor complex.
788. Proudfoot, A., Axelrod, H.L., Geralt, M., Fletterick, R.J., Yumoto, F., Deacon, A.M., Elsliger, M.A., Wilson, I.A., Wüthrich, K. and Serrano, P. (2016) J. Mol.Biol. 428, 1130–1141.
Dlx5 homeodomain: DNA complex: structure, binding and effect of mutations related to split hand and food malformation syndrome.
789. Mohanty, B., Geralt, M., Wüthrich, K. and Serrano, P. (2016) Protein Sci. 25, 917–925.
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
790. Dongsheng Liu, Kurt Wüthrich (2016) J Biomol NMR 65,1–5.
Ring current shifts in 19F-NMR of membrane proteins.
791. Proudfoot, A., Geralt, M., Elsliger, M-A., Wilson, I. A., Wüthrich, K., Serrano P. (2016) Structure 24, 1372–1379.
Dynamic Local Polymorphisms in the Gbx1 Homeodomain Induced by DNA Binding.
792. Pedro Serrano, Samit K. Dutta, Andrew Proudfoot, Biswaranjan Mohanty, Lukas Susac, Bryan Martin, Michael Geralt, Lukasz Jaroszewski, Adam Godzik,Marc Elsliger, Ian A. Wilson1, and Kurt Wüthrich (2016) The FEBS Journal.
NMR in structural genomics to increase structural coverage of the protein universe.
793. Christine Beuck, James R. Williamson, Kurt Wüthrich and Pedro Serrano (2016) PROTEIN SCIENCE 25, 1545—1550.
The acidic domain is a unique structural feature of the splicing factor SYNCRIP.
794. M. Landreh, M. R. Sawaya, M. S. Hipp, D. S. Eisenberg, K. Wüthrich & F. U. Hartl (2016) Journal of Internal Medicine, 280, 164–176.
The formation, function and regulation of amyloids: insights from structural biology.
795. M. T. Eddy, T. Didenko, R. C. Stevens, K. Wüthrich (2016) Structure 24, 2190-2197.
ß2-Adrenergic Receptor Conformational Response to Fusion Protein in the Third Intracellular Loop.
796. Pedro Serrano, Brandon E. Aubol, Malik M. Keshwani, Stefano Forli, Chen-Ting Ma, Samit K. Dutta, Michael Geralt, Kurt Wüthrich and Joseph A. Adams (2016) J Mol Biol., 428, 2430–2445.
Directional Phosphorylation and Nuclear Transport of the Splicing Factor SRSF1 Is Regulated by an RNA Recognition Motif.
798. Yaguang Hou, Wanhui Hu, Xiaona Li, John J. Skinner, Dongsheng Liu1, Kurt Wüthrich (2017) J Biomol NMR 68:1-6
Solvent-accessibility of discrete residue positions in the polypeptide hormone glucagon by 19F-NMR observation of 4-fluorophenylalanine.
799. Enrico Caldarulo, Alessandro Barduccic, Kurt Wüthrich, and Michele Parrinelloa (2017) PNAS 114, 36, 9617–9622.
Prion protein ß2–a2 loop conformational landscape.
800. Eddy et al., (2018), Cell 172, 68–80.
Allosteric Coupling of Drug Binding and Intracellular Signaling in the A2A Adenosine Receptor.
801. Pedro Serrano, John A. Hammond, Michael Geralt, and Kurt Wüthrich, (2018) Biochemistry, 57, 1563−1567.
Splicing Site Recognition by Synergy of Three Domains in Splicing Factor RBM10.
802. Matthew T. Eddy, Zhan-Guo Gao, Philip Mannes, Nilkanth Patel, Kenneth A. Jacobson, Vsevolod Katritch, Raymond C. Stevens, and Kurt Wüthrich, (2018) J. Am. Chem. Soc. 140, 8228−8235.
Extrinsic Tryptophans as NMR Probes of Allosteric Coupling in Membrane Proteins: Application to the A2A Adenosine Receptor.
803. Wüthrich, K., Grubbs, R.H., Visart de Bocarmé, T. and De Wit, A., eds. (2018) Catalysis in Chemistry and Biology. Proceedings of the 24th Solvay Conference on Chemistry, World Scientific, Singapore.
804. Wüthrich, K. (2018) in ‘Il cibo: salute, cultura, piacere e tormento’, Atti del Meeting “Le Due Culture”, IX edizione, O. Zecchino, G. Capasso, M. De Felice, G. Marino, C. Pisano, eds., Fondazione Biogem, Ariano Irpino, Italy.
Basic Scientific Research and Daily Human Life.
805. Sušac, L., Eddy, M.T., Didenko, T., Stevens, R.C. and Wüthrich, K. (2018) Proc. Natl. Acad. Sci. USA 115, 12733–12738.
A2A adenosine receptor functional states characterized by 19F-NMR.
806. Aubol, B.E., Serrano, P., Fattet, L., Wüthrich, K. and Adams, J.A. (2018) J. Biol. Chem. 293, 16751–16760.
Molecular interactions connecting the function of the serine-arginine-rich protein SRSF1 to protein phosphatase 1.
807. Shimada, I., Ueda, T., Kofuku, Y., Eddy, M.T. and Wüthrich, K. (2019) Nat. Rev. Drug Disc. 18, 59–82.
GPCR drug discovery: integrating solution NMR data with crystal and cryo-EM structures.
808. Chen, S., Lu, M., Liu, D., Yang, L., Yi, C., Ma, L., Zhang, H., Liu, Q., Frimurer T.M., Wang, M.W., Schwartz, T.W., Stevens, R.C., Wu, B., Wüthrich, K. and Zhao, Q. (2019) Nat. Commun. 10, 638–646.
Human substance P receptor binding mode of the antagonist drug aprepitant by NMR and crystallography.
809. Xue, D., Xu, T., Wang, H., Wu, M., Yuan, Y., Wang, W., Tan, Q., Zhao, F., Zhou, F., Hu, T., Jiang, Z., Liu, Z.-J., Zhao, S., Liu, D., Wüthrich, K. and Tao, H. (2019) Chemistry Eur. J. 25, DOI 10.1002/chem.201903190.
Disulfide-containing detergents (DCDs) for the structural biology of membrane proteins.
810. Rajan Lamichhane, Jeffrey J. Liu, Kate L. White, Vsevolod Katritch, Raymond C. Stevens, Kurt Wuthrich, David P. Millar (2020) Structure 28, 371–377,
Biased Signaling of the G-Protein-Coupled Receptor b2AR Is Governed by Conformational Exchange Kinetics
811. Jinfeng Zhang, Wenzhong Yan, Wenwen Duan, Kurt Wüthrich and Jianjun Cheng Pharmaceuticals 2020, 13, 237; doi:10.3390/ph13090237
Tumor Immunotherapy Using A2A Adenosine Receptor Antagonists
812. Bryan T. Martin, Robert D. Malmstrom, Rommie E. Amaro, and Kurt Wüthrich ChemBioChem 2020, 21, 1 –7
OCRE Domains of Splicing Factors RBM5 and RBM10: Tyrosine Ring-Flip Frequencies Determined by Integrated Use of 1H NMR Spectroscopy and Molecular Dynamics Simulations
813. Matthew T. Eddy, Bryan T. Martin, Kurt Wuthrich Structure 29, 170–176, February 4, 2021
A2A Adenosine Receptor Partial Agonism Related to Structural Rearrangements in an Activation Microswitch
814. Huixia Wang, Wanhui Hu, Dongsheng Liu and Kurt Wuthrich The FEBS Journal (2021)
Design and preparation of the class B G protein-coupled receptors GLP-1R and GCGR for 19F-NMR studies in solution
815. Wüthrich, K.. Weckhuysen, B., Rongy, L. and De Wit, A., eds. (2021) Computational Modeling: from Chemistry to Materials to Biology, Proceedings of the 25th Solvay Conference on Chemistry. World Scientific, Singapore.
816. Wüthrich, K. (2021) J. Magn. Reson. doi: 10.1016/jmr.2021.107031.
Brownian motion, spin diffusion and protein structure determination in solution.
817. Wüthrich, K. (2021) Nature 595, 645.
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818. Wüthrich, K. (2021) NMR with Biological Macromolecules in Solution. World Scientific, Singapore.
819. Wüthrich, K. (2021) J. Magn. Reson. 331, doi: 10.1016/j.jmr.2021.107047
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820. Pan, B., Liu, D., Yang, L. and Wüthrich, K. (2022) Proc. Natl. Acad. Sci. USA 119,
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GPCR large-amplitude dynamics by 19F-NMR of aprepitant bound to the neurokinin 1 receptor.
821. Zhang, J., Luo, Z. Duan, W. Yang, K., Ling, L., Yan, W. Liu, R. Wüthrich, K., Jiang, H., Xie, C. and Cheng J. (2022) Eur. J. Med. Chem., doi:10.1016/j.ejmech.2022.114326.
Dual-acting antitumor agents targeting the A2A adenosine receptor and histone deacetylases: Design and synthesis of 4-(furan-2-yl)-2-1H-pyrazolo[3,4-d]pyrimidin-6-amine derivatives.
822. Ge, H., Wang, H., Pan, B., Feng, D., Guo, C. Yang, L., Liu, D. and Wüthrich, K. (2022) Molecules doi: 10.3390/molecules27092658.
G protein-coupled receptor (GPCR) reconstitution and labeling for solution nuclear magnetic resonance (NMR) studies of the structural basis of transmembrane signaling.