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Year Citation  Score
2015 Henrich E, Ma Y, Engels I, Münch D, Otten C, Schneider T, Henrichfreise B, Sahl HG, Dötsch V, Bernhard F. Lipid Requirements for the Enzymatic Activity of MraY Translocases and in vitro Reconstitution of Lipid II Synthesis Pathway. The Journal of Biological Chemistry. PMID 26620564 DOI: 10.1074/jbc.M115.664292  0.96
2015 Klingler FM, Moser D, Büttner D, Wichelhaus TA, Löhr F, Dötsch V, Proschak E. Probing metallo-β-lactamases with molecular fragments identified by consensus docking. Bioorganic & Medicinal Chemistry Letters. 25: 5243-6. PMID 26463134 DOI: 10.1016/j.bmcl.2015.09.056  0.96
2015 Stadel D, Millarte V, Tillmann KD, Huber J, Tamin-Yecheskel BC, Akutsu M, Demishtein A, Ben-Zeev B, Anikster Y, Perez F, Dötsch V, Elazar Z, Rogov V, Farhan H, Behrends C. TECPR2 Cooperates with LC3C to Regulate COPII-Dependent ER Export. Molecular Cell. 60: 89-104. PMID 26431026 DOI: 10.1016/j.molcel.2015.09.010  0.96
2015 Mehler M, Eckert CE, Busche A, Kulhei J, Michaelis J, Becker-Baldus J, Wachtveitl J, Dötsch V, Glaubitz C. Assembling a correctly folded and functional heptahelical membrane protein by protein trans-splicing. The Journal of Biological Chemistry. PMID 26405032 DOI: 10.1074/jbc.M115.681205  0.96
2015 Merk H, Rues RB, Gless C, Beyer K, Dong F, Dötsch V, Gerrits M, Bernhard F. Biosynthesis of membrane dependent proteins in insect cell lysates: identification of limiting parameters for folding and processing. Biological Chemistry. PMID 25999328 DOI: 10.1515/hsz-2015-0105  0.96
2015 Chatterjee D, Kudlinzki D, Linhard V, Saxena K, Schieborr U, Gande SL, Wurm JP, Wöhnert J, Abele R, Rogov VV, Dötsch V, Osiewacz HD, Sreeramulu S, Schwalbe H. Structure and Biophysical Characterization of the S-Adenosylmethionine-dependent O-Methyltransferase PaMTH1, a Putative Enzyme Accumulating during Senescence of Podospora anserina. The Journal of Biological Chemistry. 290: 16415-30. PMID 25979334 DOI: 10.1074/jbc.M115.660829  0.96
2015 Löhr F, Tumulka F, Bock C, Abele R, Dötsch V. An extended combinatorial (15)N, (13)C (α), and [Formula: see text] labeling approach to protein backbone resonance assignment. Journal of Biomolecular Nmr. PMID 25953311 DOI: 10.1007/s10858-015-9941-8  0.96
2015 Henrich E, Hein C, Dötsch V, Bernhard F. Membrane protein production in Escherichia coli cell-free lysates. Febs Letters. PMID 25937121 DOI: 10.1016/j.febslet.2015.04.045  0.96
2015 Henrich E, Dötsch V, Bernhard F. Screening for lipid requirements of membrane proteins by combining cell-free expression with nanodiscs. Methods in Enzymology. 556: 351-69. PMID 25857790 DOI: 10.1016/bs.mie.2014.12.016  0.96
2015 Schwamb B, Pick R, Fernández SB, Völp K, Heering J, Dötsch V, Bösser S, Jung J, Beinoraviciute-Kellner R, Wesely J, Zörnig I, Hammerschmidt M, Nowak M, Penzel R, Zatloukal K, et al. FAM96A is a novel pro-apoptotic tumor suppressor in gastrointestinal stromal tumors. International Journal of Cancer. Journal International Du Cancer. 137: 1318-1329. PMID 25716227 DOI: 10.1002/ijc.29498  0.96
2015 Genau HM, Huber J, Baschieri F, Akutsu M, Dötsch V, Farhan H, Rogov V, Behrends C. CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP proteins to spatially restrict TIAM1-RAC1 signaling. Molecular Cell. 57: 995-1010. PMID 25684205 DOI: 10.1016/j.molcel.2014.12.040  0.96
2015 Orbán E, Proverbio D, Haberstock S, Dötsch V, Bernhard F. Cell-free expression of G-protein-coupled receptors. Methods in Molecular Biology (Clifton, N.J.). 1261: 171-95. PMID 25502200 DOI: 10.1007/978-1-4939-2230-7_10  0.96
2015 Kai L, Orbán E, Henrich E, Proverbio D, Dötsch V, Bernhard F. Co-translational stabilization of insoluble proteins in cell-free expression systems. Methods in Molecular Biology (Clifton, N.J.). 1258: 125-43. PMID 25447862 DOI: 10.1007/978-1-4939-2205-5_7  0.96
2015 LaGuerre A, Löhr F, Bernhard F, Dötsch V. Labeling of Membrane Proteins by Cell-Free Expression Methods in Enzymology. DOI: 10.1016/bs.mie.2015.06.001  0.96
2014 Löhr F, Laguerre A, Bock C, Reckel S, Connolly PJ, Abdul-Manan N, Tumulka F, Abele R, Moore JM, Dötsch V. Time-shared experiments for efficient assignment of triple-selectively labeled proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 248: 81-95. PMID 25442777 DOI: 10.1016/j.jmr.2014.09.014  0.96
2014 Stindt MH, Muller PA, Ludwig RL, Kehrloesser S, Dötsch V, Vousden KH. Functional interplay between MDM2, p63/p73 and mutant p53. Oncogene. PMID 25417702 DOI: 10.1038/onc.2014.359  0.96
2014 Rues RB, Orbán E, Dötsch V, Bernhard F. Cell-free expression of G-protein coupled receptors: new pipelines for challenging targets. Biological Chemistry. 395: 1425-34. PMID 25178907 DOI: 10.1515/hsz-2014-0217  0.96
2014 Schröder M, Häfner AK, Hofmann B, Rådmark O, Tumulka F, Abele R, Dötsch V, Steinhilber D. Stabilisation and characterisation of the isolated regulatory domain of human 5-lipoxygenase. Biochimica Et Biophysica Acta. 1842: 1538-47. PMID 25107828 DOI: 10.1016/j.bbalip.2014.07.022  0.96
2014 Hänsel R, Luh LM, Corbeski I, Trantirek L, Dötsch V. In-cell NMR and EPR spectroscopy of biomacromolecules. Angewandte Chemie (International Ed. in English). 53: 10300-14. PMID 25070284 DOI: 10.1002/anie.201311320  0.96
2014 Boland C, Li D, Shah ST, Haberstock S, Dötsch V, Bernhard F, Caffrey M. Cell-free expression and in meso crystallisation of an integral membrane kinase for structure determination. Cellular and Molecular Life Sciences : Cmls. 71: 4895-910. PMID 25012698 DOI: 10.1007/s00018-014-1655-7  0.96
2014 Tufar P, Rahighi S, Kraas FI, Kirchner DK, Löhr F, Henrich E, Köpke J, Dikic I, Güntert P, Marahiel MA, Dötsch V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification. Chemistry & Biology. 21: 552-62. PMID 24704508 DOI: 10.1016/j.chembiol.2014.02.014  0.96
2014 Tikole S, Jaravine V, Rogov V, Dötsch V, Güntert P. Peak picking NMR spectral data using non-negative matrix factorization. Bmc Bioinformatics. 15: 46. PMID 24511909 DOI: 10.1186/1471-2105-15-46  0.96
2014 Rogov V, Dötsch V, Johansen T, Kirkin V. Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy. Molecular Cell. 53: 167-78. PMID 24462201 DOI: 10.1016/j.molcel.2013.12.014  0.96
2014 Roos C, Kai L, Haberstock S, Proverbio D, Ghoshdastider U, Ma Y, Filipek S, Wang X, Dötsch V, Bernhard F. High-level cell-free production of membrane proteins with nanodiscs. Methods in Molecular Biology (Clifton, N.J.). 1118: 109-30. PMID 24395412 DOI: 10.1007/978-1-62703-782-2_7  0.96
2014 Proverbio D, Henrich E, Orbán E, Dötsch V, Bernhard F. Membrane protein quality control in cell-free expression systems: Tools, strategies and case studies Membrane Proteins Production For Structural Analysis. 45-70. DOI: 10.1007/978-1-4939-0662-8_2  0.96
2014 Hein C, Henrich E, Orbán E, Dötsch V, Bernhard F. Hydrophobic supplements in cell-free systems: Designing artificial environments for membrane proteins Engineering in Life Sciences. 14: 365-379. DOI: 10.1002/elsc.201300050  0.96
2013 Zettler J, Eppmann S, Busche A, Dikovskaya D, Dötsch V, Mootz HD, Sonntag T. SPLICEFINDER - a fast and easy screening method for active protein trans-splicing positions. Plos One. 8: e72925. PMID 24023792 DOI: 10.1371/journal.pone.0072925  0.96
2013 Tumulka F, Roos C, Löhr F, Bock C, Bernhard F, Dötsch V, Abele R. Conformational stabilization of the membrane embedded targeting domain of the lysosomal peptide transporter TAPL for solution NMR. Journal of Biomolecular Nmr. 57: 141-54. PMID 24013930 DOI: 10.1007/s10858-013-9774-2  0.96
2013 Luh LM, Hänsel R, Löhr F, Kirchner DK, Krauskopf K, Pitzius S, Schäfer B, Tufar P, Corbeski I, Güntert P, Dötsch V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition. Journal of the American Chemical Society. 135: 13796-803. PMID 23968199 DOI: 10.1021/ja405244v  0.96
2013 Hein C, Wittinghofer A, Dötsch V. How to switch a master switch. Elife. 2: e01159. PMID 23908771 DOI: 10.7554/eLife.01159  0.96
2013 Denic V, Dötsch V, Sinning I. Endoplasmic reticulum targeting and insertion of tail-anchored membrane proteins by the GET pathway. Cold Spring Harbor Perspectives in Biology. 5: a013334. PMID 23906715 DOI: 10.1101/cshperspect.a013334  0.96
2013 Rogov VV, Suzuki H, Fiskin E, Wild P, Kniss A, Rozenknop A, Kato R, Kawasaki M, McEwan DG, Löhr F, Güntert P, Dikic I, Wakatsuki S, Dötsch V. Structural basis for phosphorylation-triggered autophagic clearance of Salmonella. The Biochemical Journal. 454: 459-66. PMID 23805866 DOI: 10.1042/BJ20121907  0.96
2013 Proverbio D, Roos C, Beyermann M, Orbán E, Dötsch V, Bernhard F. Functional properties of cell-free expressed human endothelin A and endothelin B receptors in artificial membrane environments. Biochimica Et Biophysica Acta. 1828: 2182-92. PMID 23747296 DOI: 10.1016/j.bbamem.2013.05.031  0.96
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 and Differentiation. 20: 1008-16. PMID 23538419 DOI: 10.1038/cdd.2013.23  0.96
2013 Kai L, Dötsch V, Kaldenhoff R, Bernhard F. Artificial environments for the co-translational stabilization of cell-free expressed proteins. Plos One. 8: e56637. PMID 23451062 DOI: 10.1371/journal.pone.0056637  0.96
2013 Hänsel R, Löhr F, Trantirek L, Dötsch V. High-resolution insight into G-overhang architecture. Journal of the American Chemical Society. 135: 2816-24. PMID 23339582 DOI: 10.1021/ja312403b  0.96
2013 Mörs K, Roos C, Scholz F, Wachtveitl J, Dötsch V, Bernhard F, Glaubitz C. Modified lipid and protein dynamics in nanodiscs. Biochimica Et Biophysica Acta. 1828: 1222-9. PMID 23276833 DOI: 10.1016/j.bbamem.2012.12.011  0.96
2013 Hänsel R, Foldynová-Trantírková S, Dötsch V, Trantírek L. Investigation of quadruplex structure under physiological conditions using in-cell NMR. Topics in Current Chemistry. 330: 47-65. PMID 22760824 DOI: 10.1007/128_2012_332  0.96
2013 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. Molecular Membrane Biology. 30: 75-89. PMID 22716775 DOI: 10.3109/09687688.2012.693212  0.96
2012 Stehle J, Scholz F, Löhr F, Reckel S, Roos C, Blum M, Braun M, Glaubitz C, Dötsch V, Wachtveitl J, Schwalbe H. Characterization of the ground state dynamics of proteorhodopsin by NMR and optical spectroscopies. Journal of Biomolecular Nmr. 54: 401-13. PMID 23160927 DOI: 10.1007/s10858-012-9684-8  0.96
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, et al. A method for integrative structure determination of protein-protein complexes. Bioinformatics (Oxford, England). 28: 3282-9. PMID 23093611 DOI: 10.1093/bioinformatics/bts628  0.96
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 Expression and Purification. 86: 120-6. PMID 23036358 DOI: 10.1016/j.pep.2012.09.011  0.96
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. Biochimica Et Biophysica Acta. 1818: 3098-106. PMID 22960287 DOI: 10.1016/j.bbamem.2012.08.007  0.96
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, et al. Loss of p63 and its microRNA-205 target results in enhanced cell migration and metastasis in prostate cancer. Proceedings of the National Academy of Sciences of the United States of America. 109: 15312-7. PMID 22949650 DOI: 10.1073/pnas.1110977109  0.96
2012 Gottstein D, Reckel S, Dötsch V, Güntert P. Requirements on paramagnetic relaxation enhancement data for membrane protein structure determination by NMR. Structure (London, England : 1993). 20: 1019-27. PMID 22560730 DOI: 10.1016/j.str.2012.03.010  0.96
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: 2615-28. PMID 22531785 DOI: 10.1038/emboj.2012.93  0.96
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 : a European Journal of Chemical Biology. 13: 964-7. PMID 22492650 DOI: 10.1002/cbic.201200044  0.96
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 : a European Journal of Chemical Biology. 13: 959-63. PMID 22434781 DOI: 10.1002/cbic.201200045  0.96
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 Expression and Purification. 82: 308-16. PMID 22342679 DOI: 10.1016/j.pep.2012.01.018  0.96
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 : a European Journal of Chemical Biology. 13: 534-7. PMID 22298299 DOI: 10.1002/cbic.201100721  0.96
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. Journal of Biomolecular Nmr. 52: 197-210. PMID 22252484 DOI: 10.1007/s10858-012-9601-1  0.96
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. PMID 22196235 DOI: 10.1021/nn204624p  0.96
2012 Busche A, Gottstein D, Hein C, Ripin N, Pader I, Tufar P, Eisman EB, Gu L, Walsh CT, Sherman DH, Löhr F, Güntert P, Dötsch V. Characterization of molecular interactions between ACP and halogenase domains in the Curacin A polyketide synthase. Acs Chemical Biology. 7: 378-86. PMID 22103656 DOI: 10.1021/cb200352q  0.96
2012 Kai L, Roos C, Haberstock S, Proverbio D, Ma Y, Junge F, Karbyshev M, Dötsch V, Bernhard F. Systems for the cell-free synthesis of proteins. Methods in Molecular Biology (Clifton, N.J.). 800: 201-25. PMID 21964791 DOI: 10.1007/978-1-61779-349-3_14  0.96
2012 Sobhanifar S, Reckel S, Löhr F, Bernhard F, Dötsch V. Structural Investigation of Cell-Free Expressed Membrane Proteins Nmr of Biomolecules: Towards Mechanistic Systems Biology. 496-508. DOI: 10.1002/9783527644506.ch30  0.96
2011 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. Angewandte Chemie (International Ed. in English). 50: 11942-6. PMID 22034093 DOI: 10.1002/anie.201105648  0.96
2011 Ma Y, Münch D, Schneider T, Sahl HG, 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. The Journal of Biological Chemistry. 286: 38844-53. PMID 21937437 DOI: 10.1074/jbc.M111.301085  0.96
2011 Matthies D, Haberstock S, Joos F, Dötsch V, Vonck J, Bernhard F, Meier T. Cell-free expression and assembly of ATP synthase. Journal of Molecular Biology. 413: 593-603. PMID 21925509 DOI: 10.1016/j.jmb.2011.08.055  0.96
2011 Keller T, Egenberger B, Gorboulev V, Bernhard F, Uzelac Z, Gorbunov D, Wirth C, Koppatz S, Dötsch V, Hunte C, Sitte HH, Koepsell H. The large extracellular loop of organic cation transporter 1 influences substrate affinity and is pivotal for oligomerization. The Journal of Biological Chemistry. 286: 37874-86. PMID 21896487 DOI: 10.1074/jbc.M111.289330  0.96
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. The Journal of Biological Chemistry. 286: 32525-32. PMID 21799011 DOI: 10.1074/jbc.M111.276956  0.96
2011 Stefer S, Reitz S, Wang F, Wild K, Pang YY, 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 (New York, N.Y.). 333: 758-62. PMID 21719644 DOI: 10.1126/science.1207125  0.96
2011 Browne G, Cipollone R, Lena AM, Serra V, Zhou H, van Bokhoven H, Dötsch V, Merico D, Mantovani R, Terrinoni A, Knight RA, Candi E, Melino G. Differential altered stability and transcriptional activity of ΔNp63 mutants in distinct ectodermal dysplasias. Journal of Cell Science. 124: 2200-7. PMID 21652629 DOI: 10.1242/jcs.079327  0.96
2011 Löhr F, Reckel S, Stefer S, Dötsch V, Schmidt JM. Improved accuracy in measuring one-bond and two-bond (15)N, (13)C (α) coupling constants in proteins by double-inphase/antiphase (DIPAP) spectroscopy. Journal of Biomolecular Nmr. 50: 167-90. PMID 21647741 DOI: 10.1007/s10858-011-9507-3  0.96
2011 Rozenknop A, Rogov VV, Rogova NY, Löhr F, Güntert P, Dikic I, Dötsch V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1. Journal of Molecular Biology. 410: 477-87. PMID 21620860 DOI: 10.1016/j.jmb.2011.05.003  0.96
2011 Wild P, Farhan H, McEwan DG, Wagner S, Rogov VV, Brady NR, Richter B, Korac J, Waidmann O, Choudhary C, Dötsch V, Bumann D, Dikic I. Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. Science (New York, N.Y.). 333: 228-33. PMID 21617041 DOI: 10.1126/science.1205405  0.96
2011 Kantaputra PN, Malaivijitnond S, Vieira AR, 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. American Journal of Medical Genetics. Part A. 155: 1432-6. PMID 21567929 DOI: 10.1002/ajmg.a.34011  0.96
2011 Dötsch V. How to create a specific recognition for an unspecific interaction. Structure (London, England : 1993). 19: 601-2. PMID 21565694 DOI: 10.1016/j.str.2011.04.003  0.96
2011 Deutsch GB, Zielonka EM, Coutandin D, Dötsch V. Quality control in oocytes: domain-domain interactions regulate the activity of p63. Cell Cycle (Georgetown, Tex.). 10: 1884-5. PMID 21555912 DOI: 10.4161/cc.10.12.15590  0.96
2011 Krsti? I, Hänsel R, Romainczyk O, Engels JW, Dötsch V, Prisner TF. Long-range distance measurements on nucleic acids in cells by pulsed EPR spectroscopy. Angewandte Chemie (International Ed. in English). 50: 5070-4. PMID 21506223 DOI: 10.1002/anie.201100886  0.96
2011 Kodama Y, Reese ML, Shimba N, Ono K, Kanamori E, Dötsch V, Noguchi S, Fukunishi Y, Suzuki E, 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. Journal of Structural Biology. 174: 434-42. PMID 21501688 DOI: 10.1016/j.jsb.2011.04.001  0.96
2011 Schmöe K, Rogov VV, Rogova NY, 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 (London, England : 1993). 19: 577-87. PMID 21481780 DOI: 10.1016/j.str.2011.01.012  0.96
2011 Rogov VV, Rogova NY, Bernhard F, Löhr F, Dötsch V. A disulfide bridge network within the soluble periplasmic domain determines structure and function of the outer membrane protein RCSF. The Journal of Biological Chemistry. 286: 18775-83. PMID 21471196 DOI: 10.1074/jbc.M111.230185  0.96
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 Research. 39: 5768-75. PMID 21450807 DOI: 10.1093/nar/gkr174  0.96
2011 Deutsch GB, Zielonka EM, Coutandin D, Weber TA, Schäfer B, Hannewald J, Luh LM, Durst FG, Ibrahim M, Hoffmann J, Niesen FH, Sentürk A, Kunkel H, Brutschy B, Schleiff E, et al. DNA damage in oocytes induces a switch of the quality control factor TAp63α from dimer to tetramer. Cell. 144: 566-76. PMID 21335238 DOI: 10.1016/j.cell.2011.01.013  0.96
2011 Sripathomsawat W, Tanpaiboon P, Heering J, Dötsch V, Hennekam RC, Kantaputra P. Phenotypic analysis of Arg227 mutations of TP63 with emphasis on dental phenotype and micturition difficulties in EEC syndrome. American Journal of Medical Genetics. Part A. 155: 228-32. PMID 21204238 DOI: 10.1002/ajmg.a.33768  0.96
2011 Hefke F, Bagaria A, Reckel S, Ullrich SJ, 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. Journal of Biomolecular Nmr. 49: 75-84. PMID 21170670 DOI: 10.1007/s10858-010-9462-4  0.96
2011 Junge F, Haberstock S, Roos C, Stefer S, Proverbio D, Dötsch V, Bernhard F. Advances in cell-free protein synthesis for the functional and structural analysis of membrane proteins. New Biotechnology. 28: 262-71. PMID 20637904 DOI: 10.1016/j.nbt.2010.07.002  0.96
2010 Straub WE, Weber TA, Schäfer B, Candi E, Durst F, Ou HD, Rajalingam K, Melino G, Dötsch V. The C-terminus of p63 contains multiple regulatory elements with different functions. Cell Death & Disease. 1: e5. PMID 21364624 DOI: 10.1038/cddis.2009.1  0.96
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. 5: e12972. PMID 20885983 DOI: 10.1371/journal.pone.0012972  0.96
2010 Ledwidge R, Hong B, Dötsch V, Miller SM. NmerA of Tn501 mercuric ion reductase: structural modulation of the pKa values of the metal binding cysteine thiols. Biochemistry. 49: 8988-98. PMID 20828160 DOI: 10.1021/bi100537f  0.96
2010 Coutandin D, Ou HD, Löhr F, Dötsch V. Tracing the protectors path from the germ line to the genome. Proceedings of the National Academy of Sciences of the United States of America. 107: 15318-25. PMID 20696896 DOI: 10.1073/pnas.1001069107  0.96
2010 Dötsch V, Bernassola F, Coutandin D, Candi E, Melino G. p63 and p73, the ancestors of p53. Cold Spring Harbor Perspectives in Biology. 2: a004887. PMID 20484388 DOI: 10.1101/cshperspect.a004887  0.96
2010 Junge F, Luh LM, 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. Journal of Structural Biology. 172: 94-106. PMID 20460156 DOI: 10.1016/j.jsb.2010.05.004  0.96
2010 Sobhanifar S, Schneider B, Löhr F, Gottstein D, Ikeya T, Mlynarczyk K, Pulawski W, Ghoshdastider U, Kolinski M, Filipek S, Güntert P, Bernhard F, Dötsch V. Structural investigation of the C-terminal catalytic fragment of presenilin 1. Proceedings of the National Academy of Sciences of the United States of America. 107: 9644-9. PMID 20445084 DOI: 10.1073/pnas.1000778107  0.96
2010 Reckel S, Sobhanifar S, Durst F, Löhr F, Shirokov VA, Dötsch V, Bernhard F. Strategies for the cell-free expression of membrane proteins. Methods in Molecular Biology (Clifton, N.J.). 607: 187-212. PMID 20204858 DOI: 10.1007/978-1-60327-331-2_16  0.96
2010 Schwarz D, Daley D, Beckhaus T, Dötsch V, Bernhard F. Cell-free expression profiling of E. coli inner membrane proteins. Proteomics. 10: 1762-79. PMID 20198639 DOI: 10.1002/pmic.200900485  0.96
2010 Schneider B, Junge F, Shirokov VA, Durst F, Schwarz D, Dötsch V, Bernhard F. Membrane protein expression in cell-free systems. Methods in Molecular Biology (Clifton, N.J.). 601: 165-86. PMID 20099146 DOI: 10.1007/978-1-60761-344-2_11  0.96
2010 Novak I, Kirkin V, McEwan DG, Zhang J, Wild P, Rozenknop A, Rogov V, Löhr F, Popovic D, Occhipinti A, Reichert AS, Terzic J, Dötsch V, Ney PA, Dikic I. Nix is a selective autophagy receptor for mitochondrial clearance. Embo Reports. 11: 45-51. PMID 20010802 DOI: 10.1038/embor.2009.256  0.96
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 E2 synthase-1 and 5-lipoxygenase. The Journal of Pharmacology and Experimental Therapeutics. 332: 840-8. PMID 19934399 DOI: 10.1124/jpet.109.160663  0.96
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. Journal of Biomolecular Nmr. 46: 33-43. PMID 19680602 DOI: 10.1007/s10858-009-9364-5  0.96
2009 Dikic I, Dötsch V. Ubiquitin linkages make a difference. Nature Structural & Molecular Biology. 16: 1209-10. PMID 19956206 DOI: 10.1038/nsmb1209-1209  0.96
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. Journal of Molecular Biology. 394: 852-63. PMID 19836400 DOI: 10.1016/j.jmb.2009.10.014  0.96
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. Journal of the American Chemical Society. 131: 15761-8. PMID 19824671 DOI: 10.1021/ja9052027  0.96
2009 Coutandin D, Löhr F, Niesen FH, Ikeya T, Weber TA, Schäfer B, Zielonka EM, Bullock AN, Yang A, Güntert P, Knapp S, McKeon F, Ou HD, Dötsch V. Conformational stability and activity of p73 require a second helix in the tetramerization domain. Cell Death and Differentiation. 16: 1582-9. PMID 19763140 DOI: 10.1038/cdd.2009.139  0.96
2009 Dötsch V. The jugglery of a mythophilic animal Embo Reports. 10: 937. PMID 19721458 DOI: 10.1038/embor.2009.194  0.96
2009 Dötsch V. On track to tenure-track. Embo Reports. 10: 936-7. PMID 19721457 DOI: 10.1038/embor.2009.190  0.32
2009 Busche AE, Aranko AS, Talebzadeh-Farooji M, Bernhard F, Dötsch V, Iwaï H. Segmental isotopic labeling of a central domain in a multidomain protein by protein trans-splicing using only one robust DnaE intein. Angewandte Chemie (International Ed. in English). 48: 6128-31. PMID 19591176 DOI: 10.1002/anie.200901488  0.96
2009 Foldynová-Trantirková S, Matulová J, Dötsch V, Löhr F, Cirstea I, Alexandov K, Breitling R, Lukes J, Trantírek L. A cost-effective amino-acid-type selective isotope labeling of proteins expressed in Leishmania tarentolae. Journal of Biomolecular Structure & Dynamics. 26: 755-61. PMID 19385703 DOI: 10.1080/07391102.2009.10507287  0.96
2008 Dötsch V. Investigation of proteins in living bacteria with in-cell NMR experiments. Topics in Current Chemistry. 273: 203-14. PMID 23605464 DOI: 10.1007/128_2007_21  0.96
2008 Rogov VV, Schmöe K, Löhr F, Rogova NY, Bernhard F, Dötsch V. Modulation of the Rcs-mediated signal transfer by conformational flexibility. Biochemical Society Transactions. 36: 1427-32. PMID 19021569 DOI: 10.1042/BST0361427  0.96
2008 Durst FG, Ou HD, Löhr F, Dötsch V, Straub WE. The better tag remains unseen. Journal of the American Chemical Society. 130: 14932-3. PMID 18937478 DOI: 10.1021/ja806212j  0.96
2008 Schwarz D, Dötsch V, Bernhard F. Production of membrane proteins using cell-free expression systems. Proteomics. 8: 3933-46. PMID 18763710 DOI: 10.1002/pmic.200800171  0.96
2008 Koglin A, Löhr F, Bernhard F, Rogov VV, Frueh DP, Strieter ER, Mofid MR, Güntert P, Wagner G, Walsh CT, Marahiel MA, Dötsch V. Structural basis for the selectivity of the external thioesterase of the surfactin synthetase. Nature. 454: 907-11. PMID 18704089 DOI: 10.1038/nature07161  0.96
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 alpha-helical membrane proteins. Proceedings of the National Academy of Sciences of the United States of America. 105: 8262-7. PMID 18550820 DOI: 10.1073/pnas.0710843105  0.96
2008 Junge F, Schneider B, Reckel S, Schwarz D, Dötsch V, Bernhard F. Large-scale production of functional membrane proteins. Cellular and Molecular Life Sciences : Cmls. 65: 1729-55. PMID 18408885 DOI: 10.1007/s00018-008-8067-5  0.96
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: 4552-64. PMID 18361503 DOI: 10.1021/bi800060w  0.96
2008 Wagner S, Carpentier I, Rogov V, Kreike M, Ikeda F, Löhr F, Wu CJ, Ashwell JD, Dötsch V, Dikic I, Beyaert R. Ubiquitin binding mediates the NF-kappaB inhibitory potential of ABIN proteins. Oncogene. 27: 3739-45. PMID 18212736 DOI: 10.1038/sj.onc.1211042  0.96
2008 Klammt C, Schwarz D, Lehner I, Sobhanifar S, Löhr F, Zeelen J, Glaubitz C, Dötsch V, Bernhard F. Cell-Free Expression of Integral Membrane Proteins for Structural Studies Cell-Free Protein Synthesis: Methods and Protocols. 141-164. DOI: 10.1002/9783527622702.ch8  0.96
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: 2945-57. PMID 18007631 DOI: 10.1038/nprot.2007.426  0.96
2007 Klammt C, Schwarz D, Eifler N, Engel A, Piehler J, Haase W, Hahn S, Dötsch V, Bernhard F. Reprint of "Cell-free production of G protein-coupled receptors for functional and structural studies" [J. Struct. Biol. 158 (2007) 482-493]. Journal of Structural Biology. 159: 194-205. PMID 17660062 DOI: 10.1016/S1047-8477(07)00164-5  0.96
2007 Klammt C, Schwarz D, Dötsch V, Bernhard F. Cell-free production of integral membrane proteins on a preparative scale. Methods in Molecular Biology (Clifton, N.J.). 375: 57-78. PMID 17634596 DOI: 10.1007/978-1-59745-388-2_3  0.96
2007 Ikeda F, Hecker CM, Rozenknop A, Nordmeier RD, 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 Journal. 26: 3451-3462. PMID 17599067 DOI: 10.1038/sj.emboj.7601773  0.96
2007 Hoeller D, Hecker CM, Wagner S, Rogov V, Dötsch V, Dikic I. E3-Independent Monoubiquitination of Ubiquitin-Binding Proteins Molecular Cell. 26: 891-898. PMID 17588522 DOI: 10.1016/j.molcel.2007.05.014  0.96
2007 Ou HD, Löhr F, Vogel V, Mäntele W, Dötsch V. Structural evolution of C-terminal domains in the p53 family Embo Journal. 26: 3463-3473. PMID 17581633 DOI: 10.1038/sj.emboj.7601764  0.96
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. Journal of Structural Biology. 158: 482-93. PMID 17350285 DOI: 10.1016/j.jsb.2007.01.006  0.96
2007 Löhr F, Hänsel R, Rogov VV, Dötsch V. Improved pulse sequences for sequence specific assignment of aromatic proton resonances in proteins Journal of Biomolecular Nmr. 37: 205-224. PMID 17237975 DOI: 10.1007/s10858-006-9128-4  0.96
2007 Reese ML, Dakoji S, Bredt DS, Dötsch V. The guanylate kinase domain of the MAGUK PSD-95 binds dynamically to a conserved motif in MAP1a. Nature Structural & Molecular Biology. 14: 155-63. PMID 17220895 DOI: 10.1038/nsmb1195  0.96
2007 Rogov VV, Löhr F, Rogova N, Klammt C, Koglin A, Bernhard F, Dötsch V. NMR assignment of 1H, 13C and 15N resonances of the truncated Escherichia coli RcsC (700-949), including the phosphoreceiver domain [1] Journal of Biomolecular Nmr. 38: 165. PMID 17036162 DOI: 10.1007/s10858-006-9059-0  0.96
2007 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 (San Diego, Calif.). 41: 355-69. PMID 16938466 DOI: 10.1016/j.ymeth.2006.07.001  0.96
2007 Reckel S, Hänsel R, Löhr F, Dötsch V. In-cell NMR spectroscopy Progress in Nuclear Magnetic Resonance Spectroscopy. 51: 91-101. DOI: 10.1016/j.pnmrs.2007.02.002  0.96
2006 Serber Z, Selenko P, Hänsel R, Reckel S, Löhr F, Ferrell JE, Wagner G, Dötsch V. Investigating macromolecules inside cultured and injected cells by in-cell NMR spectroscopy. Nature Protocols. 1: 2701-9. PMID 17406526 DOI: 10.1038/nprot.2006.181  0.96
2006 Rogov VV, Rogova NY, 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 Journal of Molecular Biology. 364: 68-79. PMID 17005198 DOI: 10.1016/j.jmb.2006.07.052  0.96
2006 Ab E, Atkinson AR, Banci L, Bertini I, Ciofi-Baffoni S, Brunner K, Diercks T, Dötsch V, Engelke F, Folkers GE, Griesinger C, Gronwald W, Günther U, Habeck M, de Jong RN, et al. NMR in the SPINE Structural Proteomics project. Acta Crystallographica. Section D, Biological Crystallography. 62: 1150-61. PMID 17001092 DOI: 10.1107/S0907444906032070  0.96
2006 Klammt C, Schwarz D, Löhr F, Schneider B, Dötsch V, Bernhard F. Cell-free expression as an emerging technique for the large scale production of integral membrane protein. The Febs Journal. 273: 4141-53. PMID 16930130 DOI: 10.1111/j.1742-4658.2006.05432.x  0.96
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. Magnetic Resonance in Chemistry : Mrc. 44: S17-23. PMID 16826540 DOI: 10.1002/mrc.1833  0.96
2006 Petrosky KY, Löhr F, Dötsch V. NMR assignment of the L27 heterodimer from LIN-2 and LIN-7 scaffold proteins. Journal of Biomolecular Nmr. 36: 15. PMID 16721631 DOI: 10.1007/s10858-005-5391-z  0.96
2006 Koglin A, Mofid MR, Löhr F, Schäfer B, Rogov VV, Blum MM, Mittag T, Marahiel MA, Bernhard F, Dötsch V. Conformational switches modulate protein interactions in peptide antibiotic synthetases Science. 312: 273-276. PMID 16614225 DOI: 10.1126/science.1122928  0.96
2006 Nomura AM, Marnett AB, Shimba N, Dötsch V, Craik CS. One functional switch mediates reversible and irreversible inactivation of a herpesvirus protease. Biochemistry. 45: 3572-9. PMID 16533039 DOI: 10.1021/bi0523658  0.96
2006 Kelly AE, Kranitz H, Dötsch V, Mullins RD. Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex. The Journal of Biological Chemistry. 281: 10589-97. PMID 16403731 DOI: 10.1074/jbc.M507470200  0.96
2005 Klammt C, Schwarz D, Fendler K, Haase W, Dötsch V, Bernhard F. Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system. The Febs Journal. 272: 6024-38. PMID 16302967 DOI: 10.1111/j.1742-4658.2005.05002.x  0.96
2005 Nomura AM, Marnett AB, Shimba N, Dötsch V, Craik CS. Induced structure of a helical switch as a mechanism to regulate enzymatic activity. Nature Structural & Molecular Biology. 12: 1019-20. PMID 16244665 DOI: 10.1038/nsmb1006  0.96
2005 Löhr F, Rogov VV, Shi M, Bernhard F, Dötsch V. Triple-resonance methods for complete resonance assignment of aromatic protons and directly bound heteronuclei in histidine and tryptophan residues Journal of Biomolecular Nmr. 32: 309-328. PMID 16211484 DOI: 10.1007/s10858-005-1195-4  0.96
2005 He C, Hus JC, Sun LJ, Zhou P, Norman DP, Dötsch V, Wei H, Gross JD, Lane WS, Wagner G, Verdine GL. A methylation-dependent electrostatic switch controls DNA repair and transcriptional activation by E. coli ada. Molecular Cell. 20: 117-29. PMID 16209950 DOI: 10.1016/j.molcel.2005.08.013  0.96
2005 Trbovic N, Klammt C, Koglin A, Löhr F, Bernhard F, Dötsch V. Efficient strategy for the rapid backbone assignment of membrane proteins Journal of the American Chemical Society. 127: 13504-13505. PMID 16190707 DOI: 10.1021/ja0540270  0.96
2005 Petrosky KY, Ou HD, Löhr F, Dötsch V, Lim WA. A general model for preferential hetero-oligomerization of LIN-2/7 domains: mechanism underlying directed assembly of supramolecular signaling complexes. The Journal of Biological Chemistry. 280: 38528-36. PMID 16147993 DOI: 10.1074/jbc.M506536200  0.96
2004 Shimba N, Kovacs H, Stern AS, Nomura AM, Shimada I, Hoch JC, Craik CS, Dötsch V. Optimization of 13C direct detection NMR methods. Journal of Biomolecular Nmr. 30: 175-9. PMID 15557804 DOI: 10.1023/B:JNMR.0000048855.35771.11  0.96
2004 Rogov VV, Bernhard F, Löhr F, Dötsch V. Solution structure of the Escherichia coli YojN histidine- phosphotransferase domain and its interaction with cognate phosphoryl receiver domains Journal of Molecular Biology. 343: 1035-1048. PMID 15476819 DOI: 10.1016/j.jmb.2004.08.096  0.96
2004 Rogov VV, Löhr F, Bernhard F, Dötsch V. Letter to the editor: Assignment of 1H, 13C and 15N resonances of the Escherichia coli YojN histidine-phosphotransferase (HPt) domain [3] Journal of Biomolecular Nmr. 30: 103-104. PMID 15452440 DOI: 10.1023/B:JNMR.0000042964.09428.4e  0.96
2004 Serber Z, Straub W, Corsini L, Nomura AM, Shimba N, Craik CS, Ortiz de Montellano P, Dötsch V. Methyl groups as probes for proteins and complexes in in-cell NMR experiments. Journal of the American Chemical Society. 126: 7119-25. PMID 15174883 DOI: 10.1021/ja049977k  0.96
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 European Journal of Biochemistry. 271: 568-580. PMID 14728684 DOI: 10.1111/j.1432-1033.2003.03959.x  0.96
2004 Dötsch V, Ito K, Jantke KP. Human-agent co-operation in accessing and communicating knowledge media - A case in medical therapy planning Lecture Notes in Artificial Intelligence (Subseries of Lecture Notes in Computer Science). 3359: 68-87.  0.96
2003 Reese ML, Dötsch V. Fast mapping of protein-protein interfaces by NMR spectroscopy. Journal of the American Chemical Society. 125: 14250-1. PMID 14624553 DOI: 10.1021/ja037640x  0.96
2003 Shimba N, Serber Z, Ledwidge R, Miller SM, Craik CS, Dötsch V. Quantitative identification of the protonation state of histidines in vitro and in vivo Biochemistry. 42: 9227-9234. PMID 12885258 DOI: 10.1021/bi0344679  0.96
2003 Shimba N, Stern AS, Craik CS, Hoch JC, Dötsch V. Elimination of 13Cα splitting in protein NMR spectra by deconvolution with maximum entropy reconstruction Journal of the American Chemical Society. 125: 2382-2383. PMID 12603112 DOI: 10.1021/ja027973e  0.96
2002 Serber Z, Lai HC, Yang A, Ou HD, Sigal MS, Kelly AE, Darimont BD, Duijf PH, Van Bokhoven H, McKeon F, Dötsch V. A C-terminal inhibitory domain controls the activity of p63 by an intramolecular mechanism. Molecular and Cellular Biology. 22: 8601-11. PMID 12446779 DOI: 10.1128/MCB.22.24.8601-8611.2002  0.96
2002 Kelly AE, Ou HD, Withers R, Dötsch V. Low-conductivity buffers for high-sensitivity NMR measurements. Journal of the American Chemical Society. 124: 12013-9. PMID 12358548 DOI: 10.1021/ja026121b  0.96
2002 Duijf PH, Vanmolkot KR, Propping P, Friedl W, Krieger E, McKeon F, Dötsch V, Brunner HG, van Bokhoven H. Gain-of-function mutation in ADULT syndrome reveals the presence of a second transactivation domain in p63. Human Molecular Genetics. 11: 799-804. PMID 11929852  0.96
2001 Serber Z, Richter C, Dötsch V. Carbon-detected NMR experiments to investigate structure and dynamics of biological macromolecules Chembiochem. 2: 247-251. PMID 11828451  0.96
2001 Ou HD, Lai HC, Serber Z, Dötsch V. Efficient identification of amino acid types for fast protein backbone assignments Journal of Biomolecular Nmr. 21: 269-273. PMID 11775743 DOI: 10.1023/A:1012920832184  0.96
2001 Serber Z, Ledwidge R, Miller SM, Dötsch V. Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy Journal of the American Chemical Society. 123: 8895-8901. PMID 11552796 DOI: 10.1021/ja0112846  0.96
2001 Dötsch V. Protein-DNA interactions Methods in Enzymology. 339: 343-357. PMID 11462820 DOI: 10.1016/S0076-6879(01)39321-7  0.96
2001 Serber Z, Keatinge-Clay AT, Ledwidge R, Kelly AE, Miller SM, Dötsch V. High-resolution macromolecular NMR spectroscopy inside living cells. Journal of the American Chemical Society. 123: 2446-7. PMID 11456903 DOI: 10.1021/ja0057528  0.96
2001 Lin Y, Dötsch V, Wintner T, Peariso K, Myers LC, Penner-Hahn JE, Verdine GL, Wagner G. Structural basis for the functional switch of the E. coli Ada protein. Biochemistry. 40: 4261-71. PMID 11284682 DOI: 10.1021/bi002109p  0.96
2001 Gerber BO, Meng EC, Dotsch V, Baranski TJ, Bourne HR. An activation switch in the ligand binding pocket of the C5a receptor. The Journal of Biological Chemistry. 276: 3394-400. PMID 11062244 DOI: 10.1074/jbc.M007748200  0.96
2001 James TL, Dötsch V, Schmitz U. Methods in Enzymology: Preface Methods in Enzymology. 338: xi. DOI: 10.1016/S0076-6879(02)38212-0  0.96
2001 James TL, Dötsch V, Schmitz U. Nuclear magnetic resonance of biological macromolecules Methods in Enzymology. 339: xi. DOI: 10.1016/S0076-6879(01)39304-7  0.96
2000 Serber Z, Richter C, Moskau D, Böhlen JM, Gerfin T, Marek D, Häberli M, Baselgia L, Laukien F, Stern AS, Hoch JC, Dötsch V. New carbon-detected protein NMR experiments using cryoprobes [17] Journal of the American Chemical Society. 122: 3554-3555. DOI: 10.1021/ja991371m  0.96
2000 Dötsch V, Grieser G, Lange S. Applying formal concepts to learning systems validation Journal of Experimental and Theoretical Artificial Intelligence. 12: 433-445.  0.96
1999 Freund C, Dötsch V, Nishizawa K, Reinherz EL, Wagner G. The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences. Nature Structural Biology. 6: 656-60. PMID 10404223 DOI: 10.1038/10712  0.72
1999 Sun ZY, Dötsch V, Kim M, Li J, Reinherz EL, Wagner G. Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies. The Embo Journal. 18: 2941-9. PMID 10357807 DOI: 10.1093/emboj/18.11.2941  0.96
1998 Dötsch V, Wagner G. New approaches to structure determination by NMR spectroscopy. Current Opinion in Structural Biology. 8: 619-23. PMID 9818267 DOI: 10.1016/S0959-440X(98)80154-1  0.96
1998 Yang A, Kaghad M, Wang Y, Gillett E, Fleming MD, Dötsch V, Andrews NC, 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: 305-16. PMID 9774969  0.96
1998 Zhu J, Shibasaki F, Price R, Guillemot JC, 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: 851-61. PMID 9630228 DOI: 10.1016/S0092-8674(00)81445-2  0.96
1998 Zhou P, Sun LJ, Dötsch V, Wagner G, Verdine GL. Solution structure of the core NFATC1/DNA complex. Cell. 92: 687-96. PMID 9506523 DOI: 10.1016/S0092-8674(00)81136-8  0.96
1997 Feltham JL, Dötsch V, Raza S, Manor D, Cerione RA, Sutcliffe MJ, Wagner G, Oswald RE. Definition of the switch surface in the solution structure of Cdc42Hs. Biochemistry. 36: 8755-66. PMID 9220962 DOI: 10.1021/bi970694x  0.96
1997 Wolfe SA, Zhou P, Dötsch V, Chen L, You A, Ho SN, Crabtree GR, Wagner G, Verdine GL. Unusual Rel-like architecture in the DNA-binding domain of the transcription factor NFATc. Nature. 385: 172-6. PMID 8990122 DOI: 10.1038/385172a0  0.96
1996 Dötsch V, Oswald RE, Wagner G. Selective identification of threonine, valine, and isoleucine sequential connectivities with a TVI-CBCACONH experiment. Journal of Magnetic Resonance. Series B. 110: 304-8. PMID 8867447  0.96
1996 Schiffer CA, Dötsch V. The role of protein-solvent interactions in protein unfolding Current Opinion in Biotechnology. 7: 428-432. PMID 8768902 DOI: 10.1016/S0958-1669(96)80119-4  0.96
1996 Dötsch V, Wagner G. Editing for amino-acid type in CBCACONH experiments based on the 13C beta-13C gamma coupling. Journal of Magnetic Resonance. Series B. 111: 310-3. PMID 8680747  0.96
1996 Dötsch V, Matsuo H, Wagner G. Amino-acid-type identification for deuterated proteins with a beta-carbon-edited HNCOCACB experiment. Journal of Magnetic Resonance. Series B. 112: 95-100. PMID 8661315  0.96
1996 Dötsch V, Oswald RE, Wagner G. Amino-acid-type-selective triple-resonance experiments. Journal of Magnetic Resonance. Series B. 110: 107-11. PMID 8556233 DOI: 10.1006/jmrb.1996.0017  0.96
1996 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. DOI: 10.1016/0031-6865(95)00042-9  0.96
1995 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. PMID 7789518 DOI: 10.1016/0014-5793(95)00459-M  0.96
1995 Dötsch V, Oswald RE, Wagner G. Water suppression by coherence selection with absorptive lineshape without loss in sensitivity. Journal of Magnetic Resonance. Series B. 108: 285-8. PMID 7670759 DOI: 10.1006/jmrb.1995.1135  0.96
1995 Schiffer CA, Dötsch V, Wüthrich K, van Gunsteren WF. 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: 15057-67. PMID 7578118  0.96
1995 Dötsch V, Wider G, Siegal G, Wüthrich K. Salt-stabilized globular protein structure in 7 M aqueous urea solution. Febs Letters. 372: 288-90. PMID 7556686 DOI: 10.1016/0014-5793(95)01004-X  0.96
1995 Dötsch V, Wider G. Exchange rates of internal water molecules in proteins measured using pulsed field gradients Journal of the American Chemical Society. 117: 6064-6069.  0.96
1992 Güntert P, Dötsch V, Wider G, Wüthrich K. Processing of multi-dimensional NMR data with the new software PROSA Journal of Biomolecular Nmr. 2: 619-629. DOI: 10.1007/BF02192850  0.96
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