Publications

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2013

  • Luh LM, Kehrloesser S, Deutsch GB, Gebel J, Coutandin D, Schäfer B, Agostini M, Melino G, Dötsch V. Analysis of the oligomeric state and transactivation potential of TAp73α Cell Death Differ (2013)
  • Kai L, Dötsch V, Kaldenhoff R, Bernhard F. Artificial environments for the co-translational stabilization of cell-free expressed proteins.

PLoS One 8(2):e56637 (2013)


2012

  • Schneidman-Duhovny D, Rossi A, Avila-Sakar A, Kim SJ, Velázquez-Muriel J, Strop P, Liang H, Krukenberg KA, Liao M, Kim HM, Sobhanifar S, Dötsch V, Rajpal A, Pons J, Agard DA, Cheng Y, Sali A. A method for integrative structure determination of protein-protein complexes. Bioinformatics 28:3282-9 (2012)
  • Ma Y, Ghoshdastider U, Wang J, Ye W, Dötsch V, Filipek S, Bernhard F, Wang X. Cell-free expression of human glucosamine 6-phosphate N-acetyltransferase (HsGNA1) for inhibitor screening. Protein Expr Purif. 86:120-6 (2012)
  • Roos C, Zocher M, Müller D, Münch D, Schneider T, Sahl HG, Scholz F, Wachtveitl J, Ma Y, Proverbio D, Henrich E, Dötsch V, Bernhard F. Characterization of co-translationally formed nanodisc complexes with small multidrug transporters, proteorhodopsin and with the E. coli MraY translocase. Biochim Biophys Acta 1818:3098-106 (2012)
  • Tucci P, Agostini M, Grespi F, Markert EK, Terrinoni A, Vousden KH, Muller PA, Dötsch V, Kehrloesser S, Sayan BS, Giaccone G, Lowe SW, Takahashi N, Vandenabeele P, Knight RA, Levine AJ, Melino G. Loss of p63 and its microRNA-205 target results in enhanced cell migration and metastasis in prostate cancer. Proc Natl Acad Sci U S A. 109:15312-7 (2012)
  • Hänsel R, Foldynová-Trantírková S, Dötsch V, Trantírek L. Investigation of Quadruplex Structure Under Physiological Conditions Using In-Cell NMR. Top Curr Chem. (2012)
  • Roos C, Kai L, Proverbio D, Ghoshdastider U, Filipek S, Dötsch V, Bernhard F. Co-translational association of cell-free expressed membrane proteins with supplied lipid bilayers. Mol Membr Biol. (2012)
  • Gottstein D, Reckel S, Dötsch V, Güntert P. Requirements on paramagnetic relaxation enhancement data for membrane protein structure determination by NMR. Structure 20:1019-27 (2012)
  • Imre G, Heering J, Takeda AN, Husmann M, Thiede B, zu Heringdorf DM, Green DR, van der Goot FG, Sinha B, Dötsch V, Rajalingam K. Caspase-2 is an initiator caspase responsible for pore-forming toxin-mediated apoptosis. The EMBO Journal 31:2615 - 2628 (2012)
  • Tikole S, Jaravine V, Rogov VV, Rozenknop A, Schmöe K, Löhr F, Dötsch V, Güntert P. Fast automated NMR spectroscopy of short-lived biological samples. Chembiochem. 13:964-7 (2012)
  • Rogov VV, Rozenknop A, Rogova NY, Löhr F, Tikole S, Jaravine V, Güntert P, Dikic I, Dötsch V. A universal expression tag for structural and functional studies of proteins.Chembiochem. 13:964-7 (2012)
  • Haberstock S, Roos C, Hoevels Y, Dötsch V, Schnapp G, Pautsch A, Bernhard F. A systematic approach to increase the efficiency of membrane protein production in cell-free expression systems. Protein Expr Purif. 82:308-16 (2012)
  • Reckel S, Lopez JJ, Löhr F, Glaubitz C, Dötsch V. In-cell solid-state NMR as a tool to study proteins in large complexes. Chembiochem. 13:534-7 (2012)
  • Löhr F, Reckel S, Karbyshev M, Connolly PJ, Abdul-Manan N, Bernhard F, Moore JM, Dötsch V. Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment. J Biomol NMR. 52:197-210 (2012)
  • Zocher M, Roos C, Wegmann S, Bosshart PD, Dötsch V, Bernhard F, Müller DJ. Single-molecule force spectroscopy from nanodiscs: an assay to quantify folding, stability, and interactions of native membrane proteins. ACS Nano. 6:961-71. (2012)
  • Busche A.E., Gottstein D., Hein C., Ripin N., Pader I., Tufar P., Eisman E.B., Gu L., Walsh C.T., Loehr F., Sherman D.H., Güntert P., Dötsch V. Characterization of molecular interactions between ACP and halogenase domains in the curacin A polyketide synthase. ACS Chem Biol. 7:378-86 (2012)
  • Reckel S, Gottstein D, Stehle J, Löhr F,Verhoefen MK, Takeda M, Silvers R, Kainosho M, Glaubitz C, Wachtveitl J, Bernhard F, Schwalbe H, Güntert P, Dötsch V. Solution NMR structure of Proteorhodopsin. Angew Chem INt Ed Engl. 50:11942-6 (2012)


2011

  • Ma Y., Münch D., Schneider T., Sahl H.G., Bouhss A., Ghoshdastider U., Wang J., Dötsch V., Wang X., Bernhard F. Preparative Scale Cell-free Production and Quality Optimization of MraY Homologues in Different Expression Modes. J Biol Chem 413:593-603(2011)
  • Matthies D., Haberstock S., Joos F., Dötsch V., Vonck J., Bernhard F., Meier T. Cell-free expression and assembly of ATP synthase. J Mol Biol 413:593-603 (2011)
  • Keller T., Egenberger B., Gorboulev V., Bernhard F., Uzelac Z., Gorbunov D., Wirth C., Koppatz S., Dötsch V., Hunte C., Sitte H.H., Koepsell H. The large extracellular loop of organic cation transporter 1 influences substrate affinity and is pivotal for oligomerization. J Biol Chem 286:37874-86(2011)
  • Rath P., Demange P., Saurel O., Tropis M., Daffé M., Dötsch V., Ghazi A., Bernhard F., Milon A. Functional expression of the PorAH channel from Corynebacterium glutamicum in cell-free expression systems: implications for the role of the naturally occurring mycolic acid modification. J Biol Chem 286:32525-32 (2011)
  • Stefer S., Reitz S., Wang F., Wild K., Pang Y.Y., Schwarz D., Bomke J., Hein C., Löhr F., Bernhard F., Denic V., Dötsch V., Sinning I. Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex. Science 333:758-62 (2011)
  • Löhr F., Reckel S., Stefer S., Dötsch V., Schmidt J.M. Improved accuracy in measuring one-bond and two-bond (15)N, (13)C (α) coupling constants in proteins by double-inphase/antiphase (DIPAP) spectroscopy. J Biomol NMR 50:167-90 (2011)
  • Rozenknop A., Rogov V.V., Rogova N.Y., Löhr F., Güntert P., Dikic I., Dötsch V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1. J Mol Biol. 410:477-87 (2011)
  • Kantaputra P.N., Malaivijitnond S., Vieira A.R., Heering J., Dötsch V., Khankasikum T., Sripathomsawat W. Mutation in SAM domain of TP63 is associated with nonsyndromic cleft lip and palate and cleft palate. Am J Med Genet A. 155A:1432-6 (2011)
  • Wild, P., Farhan, H., McEwan, D.G., Wagner, S., Rogov, V.V., Brady, N.R., Richter, B., Korac, J., Waidmann, O., Choudhary, C., Dötsch, V., Bumann, D., Dikic, I. Phosphorylation of the Autophagy Receptor Optineurin Restricts Salmonella Growth. Science. 2011 May 26. [Epub ahead of print]
  • Rogov, V.V., Rogova, N.Y., Bernhard, F., Loehr, F., Doetsch, V. A disulphide bridge network within the soluble periplasmic domain determines structure and function of the outer membrane protein RcsF. J Biol Chem. 286(21):18775-83 (2011)
  • Kodama, Y., Reese, M.L., Shimba, N., Ono, K., Kanamori, E., Dötsch, V., Noguchi, S., Fukunishi, Y., Suzuki, E.I., Shimada, I., Takahashi, H. Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements. J Struct Biol. 174, 434-442 (2011)
  • Schmöe, K., Rogov, V.V., Rogova, N.Y., Löhr, F., Güntert, P., Bernhard, F., Dötsch, V. Structural Insights into Rcs Phosphotransfer: The Newly Identified RcsD-ABL Domain Enhances Interaction with the Response Regulator RcsB. Structure. 19(4):577-87 (2011)
  • Hänsel, R., Löhr, F., Foldynová-Trantírková, S., Bamberg, E., Trantírek, L., Dötsch, V. The parallel G-quadruplex structure of vertebrate telomeric repeat sequences is not the preferred folding topology under physiological conditions. Nucleic Acids Res. Epub ahead of print
  • Deutsch, G., Zielonka, E.M., Coutandin, D., Weber, T.A., Schäfer, B., Hannewald, J., Luh, L.M., Durst, F.G., Ibrahim, M., Hoffmann, J., Niesen, F.H., Sentürk, A., Kunkel, H., Brutschy, B., Schleiff, E., Knapp, S., Acker-Palmer, A., Grez, M., McKeon, F., Dötsch, V. DNA Damage in Oocytes Induces a Switch of the Quality Control Factor TAp63α from Dimer to Tetramer. Cell 144(4) 566-567 (2011)
  • Sripathomsawat, W., Tanpaiboon, P., Heering, J., Dötsch, V., Hennekam, R.C., Kantaputra, P. Phenotypic analysis of Arg227 mutations of TP63 with emphasis on dental phenotype and micturition difficulties in EEC syndrome. J Med Genet A: 155A(1):228-32 (2011)
  • Hefke, F., Bagaria, A., Reckel, S., Ullrich, S.J., Dötsch, V., Glaubitz, C., Güntert, P. Optimization of amino acid type-specific 13C and 15N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm. J Biomol NMR. 49(2):75-84 (2011)


2010

  • Kai, L., Kaldenhoff, R., Lian, J., Zhu, X., Dötsch, V., Bernhard, F., Cen, P. & Xu, Z. Preparative scale production of functional mouse aquaporin 4 using different cell-free expression modes. PLoS One in process
  • Junge F., Haberstock S., Roos C., Stefer S., Proverbio D., Dötsch V., Bernhard F. Advances in cell-free synthesis for the functional and structural analysis of membrane proteins. N Biotechnology epub ahead of print
  • Junge, F., Luh, L. M., Proverbio, D., Schäfer, B., Abele, R., Beyermann, M., Dötsch, V. & Bernhard, F. Modulation of G-protein coupled receptor sample quality by modified cell-free expression protocols: A case study of the human endothelin A receptor.J. Struct. Biol. 172, 94-106 (2010)
  • Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. & Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)
  • Reckel. S., Sobhanifar, S., Durst, F., Löhr, F., Shirokov, V. A., Dötsch, V. & Bernhard, F. Strategies for the cell-free expression of membrane proteins. Methods Mol. Biol. 607, 187-212 (2010)
  • Koeberle, A., Rossi, A., Zettl, H.,Pergola, C.,Dehm, F., Bauer, J., Greiner, C., Reckel, S.,Hoernig, C., Northoff, H., Bernhard, F., Dötsch, V.,Sautebin, L., Schubert-Zsilavecz, M. & Werz, O. The molecular pharmacology and in vivo activity of 2-(4-Chloro-6-(2,3-dimethylphenylamino)pyrimidin-2-ylthio)octanoic acid (YS121), a dual inhibitor of microsomal prostaglandin E-2 Synthase-1 and 5-Lipoxygenase. J. Pharmacol. Exp. Ther. 332, 840-848 (2010)
  • Novak, I., Kirkin V., McEwan, D. G., Zhang, J., Wild, P., Rozenknop, A., Rogov, V., Löhr, F., Popovic, D., Occhipinti, A., Reichert, A.S., Terzic, J., Dötsch, V., Ney P.A. & Dikic, I. Nix is a selective autophagy receptor for mitochondrial clearance. EMBO Reports 11, 45-51 (2010)
  • Schwarz, D., Daley, D., Beckhaus, T., Dötsch, V. & Bernhard, F. Cell-free expression profiling of E. coli inner membrane proteins. Proteomics 10, 1762-1779 (2010)
  • Sobhanifar, S., Reckel, S., Junge, F., Schwarz, D., Kai, L., Karbyshev, M., Löhr, F., Bernhard, F. & Dötsch, V. Cell-free expression and stable isotope labelling strategies for membrane proteins. J. Biomol. NMR 46, 33-43 (2010)
  • Straub, W.E., Weber, T.A., Schäfer, B., Candi, E., Durst, F., Ou, H.D., Rajalingam, K., Melino, G. & Dötsch, V. The C-terminus of p63 contains multiple regulatory elements with different functions. Cell Death & Disease 1, e5 (2010)


2009

  • Pedò, M., Löhr, F., D'Onofrio, M., Assfalg, M., Dötsch, V. & Molinari, H. NMR studies reveal the role of biomembranes in modulating ligand binding and release by intracellular bile acid binding proteins. J. Mol. Biol. 394, 852-863 (2009)
  • Hänsel, R., Foldynová-Trantírková, S., Löhr, F., Buck, J., Bongartz, E., Bamberg, E., Schwalbe, H., Dötsch, V. & Trantírek, L. Evaluation of parameters critical for observing nucleic acids inside living Xenopus laevis oocytes by in-cell NMR spectroscopy. Am. Chem. Soc. 131, 15761-15768 (2009)
  • Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. & Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain. Cell Death Diff. 16, 1582–1589 (2009)
  • Busche, A.E., Aranko, A.S., Talebzadeh-Farooji, M., Bernhard, F., Dötsch, V. & Iwai, H. (2009). Segmental isotopic labeling of a central domain in a multidomain protein by protein trans-splicing using only one robust DnaE intein. Angew. Chem. Int. Ed. 48, 6128-6131 (2009)
  • Foldynova-Trantirkova, S., Matulova, J., Dötsch, V., Löhr, F., Cirstea, I., Alexandov, K., Breitling, R., Lukes, J. & Trantirek, L. A cost-effective amino-acid-type selective isotope labeling of proteins expressed in Leishmania tarentolae. J. Biomol. Struct. Dyn. 26, 755-762 (2009)


2008

  • Wagner, S., Carpentier, I., Rogov, V., Kreike, M., Ikeda, F., Löhr, F., Wu, C.J., Ashwell, J.D., Dötsch, V., Dikic, I. & Beyaert, R. Ubiquitin binding mediates the NF-kappa B inhibitory potential of ABIN proteins. Oncogene 27, 3739-3745 (2008)
  • Keller, T., Schwarz, D., Bernhard, F., Dötsch, V., Hunte, C., Gorboulev, V. & Koepsell, H. Cell free expression and functional reconstitution of eukaryotic drug transporters. Biochemistry 47, 4552-4564 (2008)
  • Reckel, S., Sobhanifar, S., Schneider, B., Junge, F., Schwarz, D., Durst, F., Löhr, F., Güntert, P., Bernhard, F. & Dötsch, V. Transmembrane segment enhanced labeling as a tool for the backbone assignment of α-helical membrane proteins. Proc. Natl. Acad. Sci. USA 105, 8262–8267 (2008)
  • Koglin, A., Löhr, F., Bernhard, F., Rogov, V.R., Frueh, D.P., Strieter, E.R., Mofid, M.R., Güntert, P., Wagner, G., Walsh, C.T., Marahiel, M.A. & Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase. Nature 454, 907–911 (2008)


2007

  • Klammt, C., Schwarz, D., Eifler, N., Engel, A., Piehler, J., Haase, W., Hahn, S., Dötsch, V. & Bernhard, F. Cell-free production of G protein-coupled receptors for functional and structural studies. J. Struct. Biol. 158, 482-493 (2007)
  • Der Ou, H., Löhr, F., Vogel, V., Mantele, W. & Dötsch, V. Structural evolution of C-terminal domains in the p53 family. EMBO J. 26, 3463-3473 (2007)
  • Hoeller, D., Hecker, C.M., Wagner, S., Rogov, V., Dötsch, V. & Dikic, I. E3-independent monoubiquitination of ubiquitin-binding proteins. Mol. Cell 26, 891-898 (2007)
  • Ikeda, F., Hecker, C.M., Rozenknop, A., Nordmeier, R.D., Rogov, V., Hofmann, K., Akira, S., Dötsch, V. & Dikic, I. Involvement of the ubiquitin-like domain of TBK1/IKK-i kinases in regulation of IFN-inducible genes. EMBO J. 26, 3451-3462 (2007)
  • Klammt, C., Srivastava, A., Eifler, N., Junge, F., Beyermann, M., Schwarz, D., Michel, H., Doetsch, V. & Bernhard, F. Functional analysis of cell-free-produced human endothelin B receptor reveals transmembrane segment 1 as an essential area for ET-1 binding and homodimer formation. FEBS J. 274, 3257-69 (2007)
  • Klammt, C., Schwarz, D., Dötsch, V. & Bernhard, F. Cell-free production of integral membrane proteins on a preparative scale. Methods Mol Biol. 375, 57-78 (2007)
  • Schwarz, D., Junge, F., Durst, F., Frölich, N., Schneider, B., Reckel, S., Sobhanifar, S., Dötsch, V. & Bernhard, F. Preparative scale expression of membrane proteins in Escherichia coli-based continuous exchange cell-free systems. Nature Protocols 2, 2945-2957 (2007)
  • Löhr, F., Hänsel, R., Rogov, V.V. & Dötsch, V. Improved pulse sequences for sequence specific assignment of aromatic proton resonances in proteins. J. Biomol. NMR 37, 205-224 (2007)


2006

  • Kelly, A.E., Kranitz, H., Dötsch, V. & Mullins, R.D. Actin binding to the C domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex. J. Biol. Chem. 281, 10589-10597 (2006)
  • Nomura, A.M., Marnett, A.B., Shimba, N., Dötsch, V. & Craik, C.S. One functional switch mediates reversible and irreversible inactivation of a herpesvirus protease. Biochemistry 45, 3572-3579 (2006)
  • Koglin, A., Klammt, C., Trbovic, N., Schwarz, D., Schneider, B., Schäfer, B. Löhr, F., Bernhard, F. & Dötsch, V. Combination of cell-free expression and NMR spectroscopy as a new approach for structural investigation of membrane proteins. Magn. Reson. Chem. 44, 17-23 (2006)
  • Koglin, A., Mofid, M.R., Löhr, F., Schäfer, B., Rogov, V.V., Blum, M.M., Mittag, T., Marahiel, M.A., Bernhard, F. & Dötsch, V. Conformational switches modulate protein interactions in peptide antibiotic synthetases. Science 312, 273-276 (2006)
  • Rogov, V.V., Rogova, N.Y., Bernhard, F., Koglin, A., Löhr, F. & Dötsch, V. A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains. J. Mol. Biol. 364, 68-79 (2006)
  • Klammt, C., Schwarz, D, Löhr, F., Schneider, B., Dötsch, V. & Bernhard, F. Preparative scale cell-free expression systems: New tools for the large scale preparation of integral membrane proteins for functional and structural studies. FEBS J. 273, 4141-4153 (2006)
  • Schwarz, D., Klammt, C., Koglin, A., Löhr, F., Schneider, B., Dötsch, V. & Bernhard, F. Preparative scale cell-free expression systems: New tools for the large scale preparation of integral membrane proteins for functional and structural studies. Methods 41, 355-369 (2006)
  • Ab, E., Atkinson, A.R., Banci, L., Bertini, I., Ciofi-Baffoni, S., Brunner, K., Diercks, T., Dötsch, V., Engelke, F., Folkers, G.E., Griesinger, C., Gronwald, W., Günther, U., Habeck, M., de Jong, R.N., Kalbitzer, H.R., Kieffer, B., Leeflang, B.R., Loss, S., Luchinat, C., Marquardsen, T., Moskau, D., Neidig, K.P., Nilges, M., Piccioli, M., Pierattelli, R., Rieping, W., Schippmann, T., Schwalbe, H., Trave, G., Trenner, J., Wöhnert, J., Zweckstetter, M. & Kaptein, R. NMR in the SPINE structural proteomics project. Acta Crystallogr. D., Biol. Crystallogr. 62, 1150-1161 (2006)
  • Serber, Z., Selenko, P., Hänsel, R., Reckel, S., Löhr, F., Ferrell, J., Wagner, G. & Dötsch, V. Investigating macromolecules inside cultured and injected cells by in-cell NMR spectroscopy. Nat. Prot. 1, 2701-2709 (2006)


2005

  • He, C., Hus, J.C., Sun, L.J., Zhou, P., Norman, D.P.G., Dötsch, V., Wei, H., Gross, J.D., Lane, W.S., Wagner, G. & Verdine, G.L. A methylation-dependent electrostatic switch controls DNA repair and transcriptional activation by E. coli ada. Mol. Cell 20, 117-129 (2005)
  • Löhr, F., Rogov, V.V., Shi, M., Bernhard, F. & Dötsch, V. Triple-resonance methods for complete resonance assignment or aromatic protons and directly bound heteronuclei in histidine and tryptophane residues. J. Biomol. NMR 32, 309-328 (2005)
  • Petrosky, K.Y., Ou, H.D., Löhr, F., Dötsch, V. & Lim, W.A. A general model for preferential hetero-oligomerization of L27 domains: Mechanism underlying directed assembly of superamolecular signaling complexes. J. Biol. Chem. 280, 38528-38536 (2005)
  • Klammt, C., Schwarz, D., Fendler, K., Haase, W., Dötsch, V. & Bernhard, F. Evaluation of detergents fort he soluble expression of α-helical and β-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system. FEBS J. 272, 6024-6038 (2005)


2004

  • Klammt, C., Löhr, F., Schäfer, B., Haase, W., Dötsch, V., Rüterjans, H., Glaubitz, C. & Bernhard, F. High level cell-free expression and specific labeling of integral membrane proteins. Eur. J. Biochem. 271, 568-580 (2004)
  • Serber, Z., Straub, W., Corsini, L., Nomura, A.M., Shimba, N., Craik, C.S. Ortiz de Montellano, P. & Dötsch, V. Methyl groups as probes for proteins and complexes in In-Cell NMR experiments. J. Am. Chem. Soc. 126, 7119-7125 (2004)
  • Shimba, N., Kovacs, H., Stern, A.S., Nomura, A.M., Shimada, I., Hoch, J.C., Craik, C.S. & Dötsch, V. Optimization of 13C direct detection NMR methods. J. Biomol. NMR 30, 175-179 (2004)
  • Rogov, V.V., Bernhard, F., Löhr, F. & Dötsch, V. Letter to the editor: Assignment of 1H, 13C and 15N resonances of the Escherichia coli YojN histidine-phosphotransferase (HPt) domain. J. Biomol. NMR 30, 103-104 (2004)
  • Rogov, V.V., Bernhard, F., Löhr, F. & Dötsch, V. Solution structure of the Escherichia coli YojN histidine phosphotransferase domain and its interaction with cognate phosphoryl receiver domains. J. Mol. Biol. 343, 1035-1048 (2004)


2003 & earlier

  • Shimba, N., Stern, A.S., Craik, C.S., Hoch, J.C. & Dötsch, V. Elimination of 13Ca splitting in protein NMR spectra by deconvolution with maximum entropy reconstruction. J. Am. Chem. Soc. 125, 2382-2383 (2003)
  • Shimba, N., Serber, Z., Ledwidge, R., Miller, S.M., Craik, C. & Dötsch, V. Quantitative identification of the protonation state of histidines in vitro & in vivo. Biochemistry 42, 9227-9234 (2003)
  • Duijf, P.H.G., Vanmolkot, K.R.J., Propping, P., Friedl, W., Krieger, E., McKeon, F., Dötsch, V., Brunner, H.G. & van Bokhoven, H. Gain-of-function mutation in ADULT syndrome reveals the presence of a second transactivation domain in p63. Hum. Mol. Genet. 11, 799-804 (2002)
  • Serber, Z., Lai, H.C., Yang, A., Yang, A., Ou, H.D., Sigal, M., Kelly, A.E., Darimont, B.D., Duijf, P.H.G., van Bokhoven, H., McKeon, F. & Dötsch, V. A C-terminal inhibitory domain controls the activity of p63 by an intramolecular mechanism. Molecular Cellular Biology 22, 8601-8611 (2002)
  • McGrath, J.A., Duijf, P., Kelly, A., Dötsch, V., Irvine, A.D., de Waal, R., Vanmolkot, K., Wessagowit, V., Atherton, D.J., Griffiths, W.A.D., Orlow, S.J., Yang, A., McKeon, F., Bamshad, M.A., Brunner, H.G., Hamel, B.C.J. & van Bokhoven, H. Hay-Wells syndrome is caused by heterozygous missense mutations in the SAM domain of p63. Human Molecular Genetics 10, 221-229 (2001)
  • Serber, Z., Keatinge-Clay, A.T., Ledwidge, R., Kelly, A.E., Miller, S.M. & Dötsch, V. High–resolution macromolecular NMR spectroscopy inside living cells. J. Am. Chem. Soc. 123, 2446-2447 (2001)
  • Serber, Z., Richter, C. & Dötsch, V. Carbon-detected NMR experiments to investigate structure and dynamics of biological macromolecules. ChemBioChem, 2, 247-251(2001)
  • Serber, Z., Ledwidge, R., Miller, S.M. & Dötsch, V. Evaluation of parameters critical to observing proteins inside living Escherrichia coli by in-cell NMR spectroscopy. J. Am. Chem. Soc. 123, 8895-8901 (2001)
  • Ou, H.D., Lai, H.C., Serber, Z. & Dötsch, V. Efficient identification of amino acid types for fast protein backbone assignments. J. Biomol. NMR 21, 269-273 (2001)
  • Serber, Z., Boehlen, J.M., Gerfin, T., Marek, D., Häberli, M., Baselgia, L., Laukien, F., Stern, A., Hoch, J.C. & Dötsch, V. New carbon-detected protein NMR experiments using CryoProbes. J. Am. Chem. Soc. 122, 3554-3555 (2000)
  • Sun, Z.Y.J., Dötsch, V., Kim, M., Li, J., Reinherz, E.L. & Wagner, G. Functional glycan-free adhesion domain of human cell surface receptor CD58: Design, production and NMR studies. Article EMBO J. 18, 2941-2949 (1999)
  • Zhou, P., Sun, L.J., Dötsch, V., Wagner, G. & Verdine, G.L. Solution ｓtructure of the ｃore NFATC1/DNA ｃomplex. Cell 92, 687-696　(1998)
  • Zhu, J., Shibasaki, F., Price, R., Guillemot, J.C., Yano, T., Dötsch, V., Wagner, G., Ferrara, P. & McKeon, F. Intramolecular masking of nuclear import signal on NF-AT4 by casein kinase I and MEKK1. Cell 93, 851-862 (1998)
  • Yang, A., Kaghad, M., Wang, Y., Gillett, E., Fleming, M.D., Dötsch, V., Andrews, N.C., Caput, D. & McKeon, F. p63, a p53 homolog at 3q27-29, encodes multiple products with transactivating, death-inducing, and dominant-negative activities. Molecular Cell 2, 305-316 (1998)
  • Wolfe, S.A., Zhou, P., Dötsch, V., Chen, L., You, A., Ho, S.N., Crabtree, G.R., Wagner, G. & Verdine, G.L. Unusual Rel-like architecture in the DNA-binding domain of the transcription factor NFATc. Letter Nature 385, 172-176 (1997)
  • Feltham, J.L., Dötsch, V., Raza, S., Manor, D., Cerione, R.A., Sutcliffe, M.J., Wagner, G. & Oswald, R.E. Definition of the switch surface in the solution structure of Cdc42Hs. Biochemistry 36, 8755-8766 (1997)
  • Jicheng Y., Griffin O.M., Wang H.T., Meadows G.A., Ibrahim M.M., Ibrahim M.S., Legarreta L., Uliana M.A. & Dötsch, V. Characterization of protein-solvent interactions with NMR-spectroscopy: The role of urea in the unfolding of proteins. Pharmaceutica Acta Helvetiae 71, 87-96 (1996)
  • Dötsch, V., Wider, G., Siegal, G. & Wüthrich, K. Interaction of urea with an unfolded protein. The DNA-binding domain of the 434-repressor. FEBS Letters 366, 6-10 (1995)
  • Schiffer, C.A., Dötsch, V., Wüthrich, K. & van Gunsteren, W.F. Exploring the role of the solvent in the denaturation of a protein: A molecular dynamics study of the DNA binding domain of the 434 repressor. Biochemistry 34, 15057-15067 (1995).
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