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The Wüthrich Laboratory

Publications on Research at TSRI

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.

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

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

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

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.

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.

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.

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

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

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.

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.

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 microcoil NMR.

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.

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.

Serrano, P., Almeida, M.S., Johnson, M.A. and Wüthrich, K. (2006) J. Biomol. NMR 36, 45.
NMR assignment of the protein nsp3a from SARS-CoV.

Almeida, M.S., Johnson, M.A. and Wüthrich, K. (2006) J. Biomol. NMR 36, 46.
NMR assignment of the SARS-CoV protein nsp1.

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.

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.

Placzek, W.J., Almeida, M.A. and Wüthrich, K. (2006) J. Biomol. NMR 36, 59.
NMR assignment of a human cancer-related nucleoside triphosphatase.

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.

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.

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. 

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

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.

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.

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.

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.

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.

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.

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 protein 3.

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

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.

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.

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.

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.

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.

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.

Johnson, M.A., Jaudzems, K. and Wüthrich, K. (2010) J. Mol. Biol. 402, 619–628.
NMR structure of the SARS-CoV nonstructural protein 7 in solution at pH 6.5.

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.

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.

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

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.

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.

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.

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.

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.

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.

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.

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.

Liu, J.J., Horst, R., Katritch, V., Stevens, R.C. and Wüthrich, K. (2012) Science 335, 1106-1110.
Biased signaling pathways in β2-adrenergic receptor characterized by 19F-NMR.

Horst, R., Stanczak, P., Serrano, P. and Wüthrich, K. (2012) J. Phys. Chem. B 116, 6775–6780.
Translational diffusion measurements by microcoil NMR in aqueous solutions of the Fos-10 detergent-solublized membrane protein OmpX.

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.

Stanczak, P., Zhang, Q., Horst, R., Serrano, P. and Wüthrich, K. (2012) J. Biomol. NMR 54, 129–133.
Micro-coil NMR to monitor optimization of the reconstitution conditions for the integral membrane protein OmpW in detergent micelles.

Horst, R., Stanczak, P., Stevens, R.C. and Wüthrich, K. (2012)  Angew. Chem. DOI: 10.1002/anie.20120547433.
β2-adrenergic receptor solutions for structural biology analyzed with micro-scale NMR diffusion measurements.

Geralt, M., Alimenti, C., Vallesi, A., Luporini, P. and Wüthrich, K. (2013) Biology 2, 142–150.
Thermodynamic stability of psychrophilic and mesophilic pheromones of the protozoan ciliate Europlotes.

Serrano, P., Geralt, M., Mohanty, B. and Wüthrich, K. (2013) Protein Science 22, 1000–1007. 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.

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.Corrigendum to “The ζ subunit of the α-proteobacterial F1FO-ATP synthase in Paracoccus denitrificans: A novel control mechanism of the central rotor” [Biochim. Biophys. Acta 1817S (2012) S27–S28].

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.

Pedrini, B., Serrano, P., Mohanty, B., Geralt, M. and Wüthrich, K. (2013) Biopolymers 99, 825–831.NMR-profiles of protein solutions.

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.

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.

Horst, R., Stanczak, P. and Wüthrich, K. (2014) Structure 22, 1–6. NMR polypeptide backbone conformation of the E. coli outer membrane protein W.

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.

Mohanty, B., Serrano, P., Geralt, M. and Wüthrich, K. (2014) J. Biomol. NMR 61, 83–87. NMR structure determination of the protein NP_344798.1 as the first representative of Pfam PF06042.

Jaudzems, K., Pedrini, B., Geralt, M., Serrano, P. and Wüthrich, K. (2014) J. Biomol. NMR 61, 65–72. J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumonia TIGR4.

Dutta, S.K., Serrano, P., Proudfoot, A., Geralt, M., Pedrini, B., Herrmann, T. and Wüthrich, K. (2014) J. Biomol. NMR 61, 47–53. APSY-NMR for protein backbone assignment in high-throughput structural biology.

Horst. R. and Wüthrich, K. (2015) Bio-protocol 5 (14) http://www.bio-protocol.org/e1539. Micro-scale NMR experiments for monitoring the optimization of membrane protein solutions for structural biology.

Didenko, T., Proudfoot, A., Dutta, S.M., Serrano, P. and Wüthrich, K. (2015) Chem. Eur. J. 21, 1236–1239. Non-uniform sampling and J-UNIO Automation for efficient protein NMR structure determination.

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.

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.

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.

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.

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.

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.

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.

Liu, D. and Wüthrich, K. (2016) J. Biomol. NMR 65, 1–5. Ring current shifts in 19F-NMR of membrane proteins.

Proudfoot, A., Geralt, M., Elsliger, M.A., Wilson, I.A., Wüthrich, K. and Serrano, P. (2016) Structure 24, 1372–1379. Dynamic local polymorphisms in the Gbx1 homeodomain induced by DNA binding.

Serrano, P., Dutta, S.K., Proudfoot, A., Mohanty, B., Susac, L., Martin, B., Geralt, M., Jaroszewski, L., Godzik, A., Elsliger, M., Wilson, I.A. and Wüthrich, K. (2016) FEBS J. 283, 3870–3881. NMR in structural genomics to increase structural coverage of the protein universe.

Beuck, C., Williamson, J.R., Wüthrich, K. and Serrano, P. (2016) Protein Sci. 25, 1545–1550.The acidic domain is a unique structural feature of the splicing factor SYNCRIP.

Landreh, M., Sawaya, M.R., Hipp, M.S., Eisenberg, D.S., Wüthrich, K. and Hartl, F.U. (2016) J. Intern. Med. 280, 164–176. The formation, function and regulation of amyloids: insights from structural biology. 

Eddy, M.T., Didenko, T., Stevens, R.C. and Wüthrich, K. (2016) Structure 24, 2190–2197. β2-adrenergic receptor conformational response to fusion protein in the third intracellular loop.

Serrano, P., Aubol, B.E., Keshwani, M.M., Flori, S., Ma, C.T., Dutta, S.K., Geralt, M., Wüthrich, K. and Adams J.A. (2016) J. Mol.Biol. 428, 2430–2445.         Directional phosphorylation and nuclear transport of the splicing factor SRSF1 is regulated by an RNA recognition motif.

Leske, H., Hornemann, S., Herrmann, U.S., Zhu, C., Dametto, P., Li, B., Laferriere, F., Polymenidou, M., Pelczar, P., Reimann, R.R., Schwarz, P., Rushing, E.J., Wüthrich, K. and Aguzzi, A. (2017) PLOS ONE doi:10.137/journal.pone.0170503. Protease resistance of infectious prions is suppressed by removal of a single atom in the cellular prion protein.

Hou, Y., Hu, W., Li, X., Skinner, J.J., Liu, D. and Wüthrich, K. (2017) J. Biomol. NMR 68, 1–6. Solvent-accessibility of discrete residue positions in the polypeptide hormone glucagon by 19F-NMR observation of 4-fluorphenylalanine.