Publications from PubMed: 215

Rogov VV, Stolz A, Ravichandran AC, Rios-Szwed DO, Suzuki H, Kniss A, Löhr F, Wakatsuki S, Dötsch V, Dikic I, Dobson RC, McEwan DG. Structural and functional analysis of the GABARAP interaction motif (GIM). EMBO Rep. 2018. 19 (12): . Link

Keller T, Gorboulev V, Mueller T, Dotsch V, Bernhard F, Koepsell H. Rat Organic Cation Transporter 1 Contains Three Binding Sites for Substrate 1-Methyl-4-phenylpyridinium per Monomer. Mol. Pharmacol. 2018.  (): . Link

Bock C, Löhr F, Tumulka F, Reichel K, Würz J, Hummer G, Schäfer L, Tampé R, Joseph B, Bernhard F, Dötsch V, Abele R. Structural and functional insights into the interaction and targeting hub TMD0 of the polypeptide transporter TAPL. Sci Rep 2018. 8 (1): 15662. Link

Dong F, Rues RB, Kazemi S, Dötsch V, Bernhard F. Molecular Determinants for Ligand Selectivity of the Cell-Free Synthesized Human Endothelin B Receptor. J. Mol. Biol. 2018. 430 (24): 5105-5119. Link

Henrich E, Löhr F, Pawlik G, Peetz O, Dötsch V, Morgner N, de Kroon AI, Bernhard F. Lipid Conversion by Cell-Free Synthesized Phospholipid Methyltransferase Opi3 in Defined Nanodisc Membranes Supports an in Trans Mechanism. Biochemistry 2018. 57 (40): 5780-5784. Link

Peetz O, Hellwig N, Henrich E, Mezhyrova J, Dötsch V, Bernhard F, Morgner N. LILBID and nESI: Different Native Mass Spectrometry Techniques as Tools in Structural Biology. J. Am. Soc. Mass Spectrom. 2018.  (): . Link

Di Rita A, Peschiaroli A, D Acunzo P, Strobbe D, Hu Z, Gruber J, Nygaard M, Lambrughi M, Melino G, Papaleo E, Dengjel J, El Alaoui S, Campanella M, Dötsch V, Rogov VV, Strappazzon F, Cecconi F. HUWE1 E3 ligase promotes PINK1/PARKIN-independent mitophagy by regulating AMBRA1 activation via IKKα. Nat Commun 2018. 9 (1): 3755. Link

Krauskopf K, Gebel J, Kazemi S, Tuppi M, Löhr F, Schäfer B, Koch J, Güntert P, Dötsch V, Kehrloesser S. Regulation of the Activity in the p53 Family Depends on the Organization of the Transactivation Domain. Structure 2018. 26 (8): 1091-1100.e4. Link

Kniss A, Kazemi S, Löhr F, Berger M, Rogov VV, Güntert P, Sommer T, Jarosch E, Dötsch V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9. J. Biomol. NMR 2018. 72 (1-2): 1-10. Link

Lazarova M, Löhr F, Rues RB, Kleebach R, Dötsch V, Bernhard F. Precursor-Based Selective Methyl Labeling of Cell-Free Synthesized Proteins. ACS Chem. Biol. 2018. 13 (8): 2170-2178. Link

Müller S, Ackloo S, Arrowsmith CH, Bauser M, Baryza JL, Blagg J, Böttcher J, Bountra C, Brown PJ, Bunnage ME, Carter AJ, Damerell D, Dötsch V, Drewry DH, Edwards AM, Edwards J, Elkins JM, Fischer C, Frye SV, Gollner A, Grimshaw CE, IJzerman A, Hanke T, Hartung IV, Hitchcock S, Howe T, Hughes TV, Laufer S, Li VM, Liras S, Marsden BD, Matsui H, Mathias J, O'Hagan RC, Owen DR, Pande V, Rauh D, Rosenberg SH, Roth BL, Schneider NS, Scholten C, Singh Saikatendu K, Simeonov A, Takizawa M, Tse C, Tho.... Donated chemical probes for open science. Elife 2018. 7 (): . Link

Kehrloesser S, Tuppi M, Dötsch V. CHK2 sets the stage for CK1 in oocyte quality control. Cell Death Differ. 2018. 25 (6): 1007-1009. Link

Hoffmann B, Löhr F, Laguerre A, Bernhard F, Dötsch V. Protein labeling strategies for liquid-state NMR spectroscopy using cell-free synthesis. Prog Nucl Magn Reson Spectrosc 2018. 105 (): 1-22. Link

Tuppi M, Kehrloesser S, Coutandin DW, Rossi V, Luh LM, Strubel A, Hötte K, Hoffmeister M, Schäfer B, De Oliveira T, Greten F, Stelzer EHK, Knapp S, De Felici M, Behrends C, Klinger FG, Dötsch V. Oocyte DNA damage quality control requires consecutive interplay of CHK2 and CK1 to activate p63. Nat. Struct. Mol. Biol. 2018. 25 (3): 261-269. Link

Rues RB, Dong F, Dötsch V, Bernhard F. Systematic optimization of cell-free synthesized human endothelin B receptor folding. Methods 2018. 147 (): 73-83. Link

Kniss A, Schuetz D, Kazemi S, Pluska L, Spindler PE, Rogov VV, Husnjak K, Dikic I, Güntert P, Sommer T, Prisner TF, Dötsch V. Chain Assembly and Disassembly Processes Differently Affect the Conformational Space of Ubiquitin Chains. Structure 2018. 26 (2): 249-258.e4. Link

Russo C, Osterburg C, Sirico A, Antonini D, Ambrosio R, Würz JM, Rinnenthal J, Ferniani M, Kehrloesser S, Schäfer B, Güntert P, Sinha S, Dötsch V, Missero C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome. Proc. Natl. Acad. Sci. U.S.A. 2018. 115 (5): E906-E915. Link

Reckel S, Gehin C, Tardivon D, Georgeon S, Kükenshöner T, Löhr F, Koide A, Buchner L, Panjkovich A, Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Güntert P, Dötsch V, Koide S, Gavin AC, Hantschel O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase. Nat Commun 2017. 8 (1): 2101. Link

Nemajerova A, Amelio I, Gebel J, Dötsch V, Melino G, Moll UM. Non-oncogenic roles of TAp73: from multiciliogenesis to metabolism. Cell Death Differ. 2018. 25 (1): 144-153. Link

Peetz O, Henrich E, Laguerre A, Löhr F, Hein C, Dötsch V, Bernhard F, Morgner N. Insights into Cotranslational Membrane Protein Insertion by Combined LILBID-Mass Spectrometry and NMR Spectroscopy. Anal. Chem. 2017. 89 (22): 12314-12318. Link

Foshag D, Henrich E, Hiller E, Schäfer M, Kerger C, Burger-Kentischer A, Diaz-Moreno I, García-Mauriño SM, Dötsch V, Rupp S, Bernhard F. The E. coli S30 lysate proteome: A prototype for cell-free protein production. N Biotechnol 2018. 40 (Pt B): 245-260. Link

Gebel J, Tuppi M, Krauskopf K, Coutandin D, Pitzius S, Kehrloesser S, Osterburg C, Dötsch V. Control mechanisms in germ cells mediated by p53 family proteins. J. Cell. Sci. 2017.  (): . Link

Wiechmann S, Gärtner A, Kniss A, Stengl A, Behrends C, Rogov VV, Rodriguez MS, Dötsch V, Müller S, Ernst A. Site-specific inhibition of the small ubiquitin-like modifier (SUMO)-conjugating enzyme Ubc9 selectively impairs SUMO chain formation. J. Biol. Chem. 2017. 292 (37): 15340-15351. Link

Rogov VV, Stolz A, Ravichandran AC, Rios-Szwed DO, Suzuki H, Kniss A, Löhr F, Wakatsuki S, Dötsch V, Dikic I, Dobson RC, McEwan DG. Structural and functional analysis of the GABARAP interaction motif (GIM). EMBO Rep. 2017. 18 (8): 1382-1396. Link

Henrich E, Sörmann J, Eberhardt P, Peetz O, Mezhyrova J, Morgner N, Fendler K, Dötsch V, Wachtveitl J, Bernhard F, Bamann C. From Gene to Function: Cell-Free Electrophysiological and Optical Analysis of Ion Pumps in Nanodiscs. Biophys. J. 2017. 113 (6): 1331-1341. Link

Rogov VV, Suzuki H, Marinković M, Lang V, Kato R, Kawasaki M, Buljubašić M, Šprung M, Rogova N, Wakatsuki S, Hamacher-Brady A, Dötsch V, Dikic I, Brady NR, Novak I. Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins. Sci Rep 2017. 7 (1): 1131. Link

Imre G, Berthelet J, Heering J, Kehrloesser S, Melzer IM, Lee BI, Thiede B, Dötsch V, Rajalingam K. Apoptosis inhibitor 5 is an endogenous inhibitor of caspase-2. EMBO Rep. 2017. 18 (5): 733-744. Link

Johansen T, Birgisdottir ÅB, Huber J, Kniss A, Dötsch V, Kirkin V, Rogov VV. Methods for Studying Interactions Between Atg8/LC3/GABARAP and LIR-Containing Proteins. Meth. Enzymol. 2017. 587 (): 143-169. Link

Henrich E, Peetz O, Hein C, Laguerre A, Hoffmann B, Hoffmann J, Dötsch V, Bernhard F, Morgner N. Analyzing native membrane protein assembly in nanodiscs by combined non-covalent mass spectrometry and synthetic biology. Elife 2017. 6 (): . Link

Hein C, Löhr F, Schwarz D, Dötsch V. Acceleration of protein backbone NMR assignment by combinatorial labeling: Application to a small molecule binding study. Biopolymers 2017. 107 (5): . Link

Stolz A, Putyrski M, Kutle I, Huber J, Wang C, Major V, Sidhu SS, Youle RJ, Rogov VV, Dötsch V, Ernst A, Dikic I. Fluorescence-based ATG8 sensors monitor localization and function of LC3/GABARAP proteins. EMBO J. 2017. 36 (4): 549-564. Link

Waberer L, Henrich E, Peetz O, Morgner N, Dötsch V, Bernhard F, Volknandt W. The synaptic vesicle protein SV31 assembles into a dimer and transports Zn. J. Neurochem. 2017. 140 (2): 280-293. Link

Gebel J, Luh LM, Coutandin D, Osterburg C, Löhr F, Schäfer B, Frombach AS, Sumyk M, Buchner L, Krojer T, Salah E, Mathea S, Güntert P, Knapp S, Dötsch V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization. Cell Death Differ. 2016. 23 (12): 1930-1940. Link

Laguerre A, Löhr F, Henrich E, Hoffmann B, Abdul-Manan N, Connolly PJ, Perozo E, Moore JM, Bernhard F, Dötsch V. From Nanodiscs to Isotropic Bicelles: A Procedure for Solution Nuclear Magnetic Resonance Studies of Detergent-Sensitive Integral Membrane Proteins. Structure 2016. 24 (10): 1830-1841. Link

Kehrloesser S, Osterburg C, Tuppi M, Schäfer B, Vousden KH, Dötsch V. Intrinsic aggregation propensity of the p63 and p73 TI domains correlates with p53R175H interaction and suggests further significance of aggregation events in the p53 family. Cell Death Differ. 2016. 23 (12): 1952-1960. Link

Focke PJ, Hein C, Hoffmann B, Matulef K, Bernhard F, Dötsch V, Valiyaveetil FI. Combining in Vitro Folding with Cell Free Protein Synthesis for Membrane Protein Expression. Biochemistry 2016. 55 (30): 4212-9. Link

von Delbrück M, Kniss A, Rogov VV, Pluska L, Bagola K, Löhr F, Güntert P, Sommer T, Dötsch V. The CUE Domain of Cue1 Aligns Growing Ubiquitin Chains with Ubc7 for Rapid Elongation. Mol. Cell 2016. 62 (6): 918-928. Link

Chillemi G, Kehrloesser S, Bernassola F, Desideri A, Dötsch V, Levine AJ, Melino G. Structural Evolution and Dynamics of the p53 Proteins. Cold Spring Harb Perspect Med 2017. 7 (4): . Link

Coutandin D, Osterburg C, Srivastav RK, Sumyk M, Kehrloesser S, Gebel J, Tuppi M, Hannewald J, Schäfer B, Salah E, Mathea S, Müller-Kuller U, Doutch J, Grez M, Knapp S, Dötsch V. Quality control in oocytes by p63 is based on a spring-loaded activation mechanism on the molecular and cellular level. Elife 2016. 5 (): . Link

Habisov S, Huber J, Ichimura Y, Akutsu M, Rogova N, Loehr F, McEwan DG, Johansen T, Dikic I, Doetsch V, Komatsu M, Rogov VV, Kirkin V. Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation. J. Biol. Chem. 2016. 291 (17): 9025-41. Link

Rues RB, Dötsch V, Bernhard F. Co-translational formation and pharmacological characterization of beta1-adrenergic receptor/nanodisc complexes with different lipid environments. Biochim. Biophys. Acta 2016. 1858 (6): 1306-16. Link

Klionsky DJ, Abdelmohsen K, Abe A, Abedin MJ, Abeliovich H, Acevedo Arozena A, Adachi H, Adams CM, Adams PD, Adeli K, Adhihetty PJ, Adler SG, Agam G, Agarwal R, Aghi MK, Agnello M, Agostinis P, Aguilar PV, Aguirre-Ghiso J, Airoldi EM, Ait-Si-Ali S, Akematsu T, Akporiaye ET, Al-Rubeai M, Albaiceta GM, Albanese C, Albani D, Albert ML, Aldudo J, Algül H, Alirezaei M, Alloza I, Almasan A, Almonte-Beceril M, Alnemri ES, Alonso C, Altan-Bonnet N, Altieri DC, Alvarez S, Alvarez-Erviti L, Alves S, Amad.... Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy 2016. 12 (1): 1-222. Link

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 the Lipid II Synthesis Pathway. J. Biol. Chem. 2016. 291 (5): 2535-46. Link

LaGuerre A, Löhr F, Bernhard F, Dötsch V. Labeling of membrane proteins by cell-free expression. Meth. Enzymol. 2015. 565 (): 367-88. Link

Heering J, Jonker HR, Löhr F, Schwalbe H, Dötsch V. Structural investigations of the p53/p73 homologs from the tunicate species Ciona intestinalis reveal the sequence requirements for the formation of a tetramerization domain. Protein Sci. 2016. 25 (2): 410-22. Link

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. Bioorg. Med. Chem. Lett. 2015. 25 (22): 5243-6. Link

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. Mol. Cell 2015. 60 (1): 89-104. Link

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. J. Biol. Chem. 2015. 290 (46): 27712-22. Link

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. Biol. Chem. 2015. 396 (9-10): 1097-107. Link

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. J. Biol. Chem. 2015. 290 (26): 16415-30. Link

Löhr F, Tumulka F, Bock C, Abele R, Dötsch V. An extended combinatorial 15N, 13Cα, and 13C' labeling approach to protein backbone resonance assignment. J. Biomol. NMR 2015. 62 (3): 263-79. Link

Henrich E, Hein C, Dötsch V, Bernhard F. Membrane protein production in Escherichia coli cell-free lysates. FEBS Lett. 2015. 589 (15): 1713-22. Link

Henrich E, Dötsch V, Bernhard F. Screening for lipid requirements of membrane proteins by combining cell-free expression with nanodiscs. Meth. Enzymol. 2015. 556 (): 351-69. Link

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, Joos S, Rieker RJ, Agaimy A, Söder S, Reid-Lombardo KM, Kendrick ML, Bardsley MR, Hayashi Y, Asuzu DT, Syed SA, Ordog T, Zörnig M. FAM96A is a novel pro-apoptotic tumor suppressor in gastrointestinal stromal tumors. Int. J. Cancer 2015. 137 (6): 1318-29. Link

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. Mol. Cell 2015. 57 (6): 995-1010. Link

Orbán E, Proverbio D, Haberstock S, Dötsch V, Bernhard F. Cell-free expression of G-protein-coupled receptors. Methods Mol. Biol. 2015. 1261 (): 171-95. Link

Kai L, Orbán E, Henrich E, Proverbio D, Dötsch V, Bernhard F. Co-translational stabilization of insoluble proteins in cell-free expression systems. Methods Mol. Biol. 2015. 1258 (): 125-43. Link

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. J. Magn. Reson. 2014. 248 (): 81-95. Link

Stindt MH, Muller PA, Ludwig RL, Kehrloesser S, Dötsch V, Vousden KH. Functional interplay between MDM2, p63/p73 and mutant p53. Oncogene 2015. 34 (33): 4300-10. Link

Rues RB, Orbán E, Dötsch V, Bernhard F. Cell-free expression of G-protein coupled receptors: new pipelines for challenging targets. Biol. Chem. 2014. 395 (12): 1425-34. Link

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. Biochim. Biophys. Acta 2014. 1842 (10): 1538-47. Link

Hänsel R, Luh LM, Corbeski I, Trantirek L, Dötsch V. In-cell NMR and EPR spectroscopy of biomacromolecules. Angew. Chem. Int. Ed. Engl. 2014. 53 (39): 10300-14. Link

Boland C, Li D, Shah STA, Haberstock S, Dötsch V, Bernhard F, Caffrey M. Cell-free expression and in meso crystallisation of an integral membrane kinase for structure determination. Cell. Mol. Life Sci. 2014. 71 (24): 4895-4910. Link

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. Chem. Biol. 2014. 21 (4): 552-562. Link

Tikole S, Jaravine V, Rogov V, Dötsch V, Güntert P. Peak picking NMR spectral data using non-negative matrix factorization. BMC Bioinformatics 2014. 15 (): 46. Link

Rogov V, Dötsch V, Johansen T, Kirkin V. Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy. Mol. Cell 2014. 53 (2): 167-78. Link

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 Mol. Biol. 2014. 1118 (): 109-30. Link

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 2013. 8 (9): e72925. Link

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. J. Biomol. NMR 2013. 57 (2): 141-54. Link

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. J. Am. Chem. Soc. 2013. 135 (37): 13796-803. Link

Hein C, Wittinghofer A, Dötsch V. How to switch a master switch. Elife 2013. 2 (): e01159. Link

Denic V, Dötsch V, Sinning I. Endoplasmic reticulum targeting and insertion of tail-anchored membrane proteins by the GET pathway. Cold Spring Harb Perspect Biol 2013. 5 (8): a013334. Link

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. Biochem. J. 2013. 454 (3): 459-66. Link

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. Biochim. Biophys. Acta 2013. 1828 (9): 2182-92. Link

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. 20 (8): 1008-16. Link

Kai L, Dötsch V, Kaldenhoff R, Bernhard F. Artificial environments for the co-translational stabilization of cell-free expressed proteins. PLoS ONE 2013. 8 (2): e56637. Link

Hänsel R, Löhr F, Trantirek L, Dötsch V. High-resolution insight into G-overhang architecture. J. Am. Chem. Soc. 2013. 135 (7): 2816-24. Link

Mörs K, Roos C, Scholz F, Wachtveitl J, Dötsch V, Bernhard F, Glaubitz C. Modified lipid and protein dynamics in nanodiscs. Biochim. Biophys. Acta 2013. 1828 (4): 1222-9. Link

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. J. Biomol. NMR 2012. 54 (4): 401-13. Link

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 2012. 28 (24): 3282-9. Link

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. 2012. 86 (2): 120-6. Link

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 2012. 1818 (12): 3098-106. Link

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. 2012. 109 (38): 15312-7. Link

Hänsel R, Foldynová-Trantírková S, Dötsch V, Trantírek L. Investigation of quadruplex structure under physiological conditions using in-cell NMR. Top Curr Chem 2013. 330 (): 47-65. Link

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. 2013. 30 (1): 75-89. Link

Gottstein D, Reckel S, Dötsch V, Güntert P. Requirements on paramagnetic relaxation enhancement data for membrane protein structure determination by NMR. Structure 2012. 20 (6): 1019-27. Link

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. EMBO J. 2012. 31 (11): 2615-28. Link

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 2012. 13 (7): 964-7. Link

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 2012. 13 (7): 959-63. Link

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. 2012. 82 (2): 308-16. Link

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 2012. 13 (4): 534-7. Link

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 2012. 52 (3): 197-210. Link

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 2012. 6 (1): 961-71. Link

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 Chem. Biol. 2012. 7 (2): 378-86. Link

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. 2011. 50 (50): 11942-6. Link

Hahn S, Achenbach J, Buscató E, Klingler FM, Schroeder M, Meirer K, Hieke M, Heering J, Barbosa-Sicard E, Loehr F, Fleming I, Doetsch V, Schubert-Zsilavecz M, Steinhilber D, Proschak E. Complementary screening techniques yielded fragments that inhibit the phosphatase activity of soluble epoxide hydrolase. ChemMedChem 2011. 6 (12): 2146-9. Link

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 Mol. Biol. 2012. 800 (): 201-25. Link

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. J. Biol. Chem. 2011. 286 (45): 38844-53. Link

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. 2011. 413 (3): 593-603. Link

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. J. Biol. Chem. 2011. 286 (43): 37874-86. Link

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. 2011. 286 (37): 32525-32. Link

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 2011. 333 (6043): 758-62. Link

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. J. Cell. Sci. 2011. 124 (Pt 13): 2200-7. Link

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. J. Biomol. NMR 2011. 50 (2): 167-90. Link

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. J. Mol. Biol. 2011. 410 (3): 477-87. Link

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 2011. 333 (6039): 228-33. Link

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. Am. J. Med. Genet. A 2011. 155A (6): 1432-6. Link

Dötsch V. How to create a specific recognition for an unspecific interaction. Structure 2011. 19 (5): 601-2. Link

Deutsch GB, Zielonka EM, Coutandin D, Dötsch V. Quality control in oocytes: domain-domain interactions regulate the activity of p63. Cell Cycle 2011. 10 (12): 1884-5. Link

Krstić I, Hänsel R, Romainczyk O, Engels JW, Dötsch V, Prisner TF. Long-range distance measurements on nucleic acids in cells by pulsed EPR spectroscopy. Angew. Chem. Int. Ed. Engl. 2011. 50 (22): 5070-4. Link

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. J. Struct. Biol. 2011. 174 (3): 434-42. Link

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 2011. 19 (4): 577-87. Link

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. J. Biol. Chem. 2011. 286 (21): 18775-83. Link

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. 2011. 39 (13): 5768-75. Link

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, 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 2011. 144 (4): 566-76. Link

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. Am. J. Med. Genet. A 2011. 155A (1): 228-32. Link

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. J. Biomol. NMR 2011. 49 (2): 75-84. Link

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 2010. 5 (9): e12972. Link

Siemoneit U, Koeberle A, Rossi A, Dehm F, Verhoff M, Reckel S, Maier TJ, Jauch J, Northoff H, Bernhard F, Doetsch V, Sautebin L, Werz O. Inhibition of microsomal prostaglandin E2 synthase-1 as a molecular basis for the anti-inflammatory actions of boswellic acids from frankincense. Br. J. Pharmacol. 2011. 162 (1): 147-62. Link

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 2010. 49 (41): 8988-98. Link

Coutandin D, Ou HD, Löhr F, Dötsch V. Tracing the protectors path from the germ line to the genome. Proc. Natl. Acad. Sci. U.S.A. 2010. 107 (35): 15318-25. Link

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. N Biotechnol 2011. 28 (3): 262-71. Link

Koglin A, Doetsch V, Bernhard F. Molecular engineering aspects for the production of new and modified biosurfactants. Adv. Exp. Med. Biol. 2010. 672 (): 158-69. Link

Dötsch V, Bernassola F, Coutandin D, Candi E, Melino G. p63 and p73, the ancestors of p53. Cold Spring Harb Perspect Biol 2010. 2 (9): a004887. Link

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. J. Struct. Biol. 2010. 172 (1): 94-106. Link

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. Proc. Natl. Acad. Sci. U.S.A. 2010. 107 (21): 9644-9. Link

Reckel S, Sobhanifar S, Durst F, Löhr F, Shirokov VA, Dötsch V, Bernhard F. Strategies for the cell-free expression of membrane proteins. Methods Mol. Biol. 2010. 607 (): 187-212. Link

Schwarz D, Daley D, Beckhaus T, Dötsch V, Bernhard F. Cell-free expression profiling of E. coli inner membrane proteins. Proteomics 2010. 10 (9): 1762-79. Link

Schneider B, Junge F, Shirokov VA, Durst F, Schwarz D, Dötsch V, Bernhard F. Membrane protein expression in cell-free systems. Methods Mol. Biol. 2010. 601 (): 165-86. Link

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 Dis 2010. 1 (): e5. Link

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 Rep. 2010. 11 (1): 45-51. Link

Dikic I, Dötsch V. Ubiquitin linkages make a difference. Nat. Struct. Mol. Biol. 2009. 16 (12): 1209-10. Link

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. J. Pharmacol. Exp. Ther. 2010. 332 (3): 840-8. Link

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. 2009. 394 (5): 852-63. Link

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. J. Am. Chem. Soc. 2009. 131 (43): 15761-8. Link

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 Differ. 2009. 16 (12): 1582-9. Link

Dötsch V. On track to tenure-track. EMBO Rep. 2009. 10 (9): 936-7. Link

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 2010. 46 (1): 33-43. Link

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. Angew. Chem. Int. Ed. Engl. 2009. 48 (33): 6128-31. Link

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. J. Biomol. Struct. Dyn. 2009. 26 (6): 755-61. Link

Rogov VV, Schmöe K, Löhr F, Rogova NY, Bernhard F, Dötsch V. Modulation of the Rcs-mediated signal transfer by conformational flexibility. Biochem. Soc. Trans. 2008. 36 (Pt 6): 1427-32. Link

Durst FG, Ou HD, Löhr F, Dötsch V, Straub WE. The better tag remains unseen. J. Am. Chem. Soc. 2008. 130 (45): 14932-3. Link

Schwarz D, Dötsch V, Bernhard F. Production of membrane proteins using cell-free expression systems. Proteomics 2008. 8 (19): 3933-46. Link

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 2008. 454 (7206): 907-11. Link

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. Proc. Natl. Acad. Sci. U.S.A. 2008. 105 (24): 8262-7. Link

Junge F, Schneider B, Reckel S, Schwarz D, Dötsch V, Bernhard F. Large-scale production of functional membrane proteins. Cell. Mol. Life Sci. 2008. 65 (11): 1729-55. Link

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 2008. 47 (15): 4552-64. Link

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 2008. 27 (26): 3739-45. Link

Dötsch V. Investigation of proteins in living bacteria with in-cell NMR experiments. Top Curr Chem 2008. 273 (): 203-14. Link

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. Nat Protoc 2007. 2 (11): 2945-57. Link

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]. J. Struct. Biol. 2007. 159 (2): 194-205. Link

Klammt C, Schwarz D, Dötsch V, Bernhard F. Cell-free production of integral membrane proteins on a preparative scale. Methods Mol. Biol. 2007. 375 (): 57-78. Link

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 J. 2007. 26 (14): 3451-62. Link

Hoeller D, Hecker CM, Wagner S, Rogov V, Dötsch V, Dikic I. E3-independent monoubiquitination of ubiquitin-binding proteins. Mol. Cell 2007. 26 (6): 891-8. Link

Ou HD, Löhr F, Vogel V, Mäntele W, Dötsch V. Structural evolution of C-terminal domains in the p53 family. EMBO J. 2007. 26 (14): 3463-73. Link

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. 2007. 274 (13): 3257-69. Link

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. Nat Protoc 2006. 1 (6): 2701-9. Link

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. 2007. 158 (3): 482-93. Link

Löhr F, Hänsel R, Rogov VV, Dötsch V. Improved pulse sequences for sequence specific assignment of aromatic proton resonances in proteins. J. Biomol. NMR 2007. 37 (3): 205-24. Link

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. Nat. Struct. Mol. Biol. 2007. 14 (2): 155-63. Link

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. J. Biomol. NMR 2007. 38 (2): 165. Link

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. J. Mol. Biol. 2006. 364 (1): 68-79. Link

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, Kalbitzer HR, Kieffer B, Leeflang BR, Loss S, Luchinat C, Marquardsen T, Moskau D, Neidig KP, Nilges M, Piccioli M, Pierattelli R, Rieping W, Schippmann T, Schwalbe H, Travé G, Trenner J, Wöhnert J, Zweckstetter M, Kaptein R. NMR in the SPINE Structural Proteomics project. Acta Crystallogr. D Biol. Crystallogr. 2006. 62 (Pt 10): 1150-61. Link

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 2007. 41 (4): 355-69. Link

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. FEBS J. 2006. 273 (18): 4141-53. Link

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 2006. 44 Spec No (): S17-23. Link

Petrosky KY, Löhr F, Dötsch V. NMR assignment of the L27 heterodimer from LIN-2 and LIN-7 scaffold proteins. J. Biomol. NMR 2006. 36 Suppl 1 (): 15. Link

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 2006. 312 (5771): 273-6. Link

Nomura AM, Marnett AB, Shimba N, Dötsch V, Craik CS. One functional switch mediates reversible and irreversible inactivation of a herpesvirus protease. Biochemistry 2006. 45 (11): 3572-9. Link

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. J. Biol. Chem. 2006. 281 (15): 10589-97. Link

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. FEBS J. 2005. 272 (23): 6024-38. Link

Nomura AM, Marnett AB, Shimba N, Dötsch V, Craik CS. Induced structure of a helical switch as a mechanism to regulate enzymatic activity. Nat. Struct. Mol. Biol. 2005. 12 (11): 1019-20. Link

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. J. Biomol. NMR 2005. 32 (4): 309-28. Link

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. Mol. Cell 2005. 20 (1): 117-29. Link

Trbovic N, Klammt C, Koglin A, Löhr F, Bernhard F, Dötsch V. Efficient strategy for the rapid backbone assignment of membrane proteins. J. Am. Chem. Soc. 2005. 127 (39): 13504-5. Link

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. J. Biol. Chem. 2005. 280 (46): 38528-36. Link

Reckel S, Löhr F, Dötsch V. In-cell NMR spectroscopy. Chembiochem 2005. 6 (9): 1601-6. Link

Serber Z, Corsini L, Durst F, Dötsch V. In-cell NMR spectroscopy. Meth. Enzymol. 2005. 394 (): 17-41. Link

Shimba N, Kovacs H, Stern AS, Nomura AM, Shimada I, Hoch JC, Craik CS, Dötsch V. Optimization of 13C direct detection NMR methods. J. Biomol. NMR 2004. 30 (2): 175-9. Link

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. J. Mol. Biol. 2004. 343 (4): 1035-48. Link

V Rogov V, Löhr F, Bernhard F, Dötsch V. Assignment of (1)H, (13)C and (15)N resonances of the Escherichia coli YojN histidine-phosphotransferase (HPt) domain. J. Biomol. NMR 2004. 30 (1): 103-4. Link

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. J. Am. Chem. Soc. 2004. 126 (22): 7119-25. Link

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. 2004. 271 (3): 568-80. Link

Reese ML, Dötsch V. Fast mapping of protein-protein interfaces by NMR spectroscopy. J. Am. Chem. Soc. 2003. 125 (47): 14250-1. Link

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 2003. 42 (30): 9227-34. Link

Shimba N, Stern AS, Craik CS, Hoch JC, Dötsch V. Elimination of 13Calpha splitting in protein NMR spectra by deconvolution with maximum entropy reconstruction. J. Am. Chem. Soc. 2003. 125 (9): 2382-3. Link

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. Mol. Cell. Biol. 2002. 22 (24): 8601-11. Link

Kelly AE, Ou HD, Withers R, Dötsch V. Low-conductivity buffers for high-sensitivity NMR measurements. J. Am. Chem. Soc. 2002. 124 (40): 12013-9. Link

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. Hum. Mol. Genet. 2002. 11 (7): 799-804. Link

Serber Z, Richter C, Dötsch V. Carbon-detected NMR experiments to investigate structure and dynamics of biological macromolecules. Chembiochem 2001. 2 (4): 247-51. Link

Ou HD, Lai HC, Serber Z, Dötsch V. Efficient identification of amino acid types for fast protein backbone assignments. J. Biomol. NMR 2001. 21 (3): 269-73. Link

Serber Z, Dötsch V. In-cell NMR spectroscopy. Biochemistry 2001. 40 (48): 14317-23. Link

Serber Z, Ledwidge R, Miller SM, Dötsch V. Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy. J. Am. Chem. Soc. 2001. 123 (37): 8895-901. Link

Dötsch V. Protein-DNA interactions. Meth. Enzymol. 2001. 339 (): 343-57. Link

Serber Z, Keatinge-Clay AT, Ledwidge R, Kelly AE, Miller SM, Dötsch V. High-resolution macromolecular NMR spectroscopy inside living cells. J. Am. Chem. Soc. 2001. 123 (10): 2446-7. Link

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 2001. 40 (14): 4261-71. Link

McGrath JA, Duijf PH, Doetsch V, Irvine AD, de Waal R, Vanmolkot KR, Wessagowit V, Kelly A, Atherton DJ, Griffiths WA, Orlow SJ, van Haeringen A, Ausems MG, Yang A, McKeon F, Bamshad MA, Brunner HG, Hamel BC, van Bokhoven H. Hay-Wells syndrome is caused by heterozygous missense mutations in the SAM domain of p63. Hum. Mol. Genet. 2001. 10 (3): 221-9. Link

Gerber BO, Meng EC, Dotsch V, Baranski TJ, Bourne HR. An activation switch in the ligand binding pocket of the C5a receptor. J. Biol. Chem. 2001. 276 (5): 3394-400. Link

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. Nat. Struct. Biol. 1999. 6 (7): 656-60. Link

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. EMBO J. 1999. 18 (11): 2941-9. Link

Dötsch V, Wagner G. New approaches to structure determination by NMR spectroscopy. Curr. Opin. Struct. Biol. 1998. 8 (5): 619-23. Link

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. Mol. Cell 1998. 2 (3): 305-16. Link

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 1998. 93 (5): 851-61. Link

Zhou P, Sun LJ, Dötsch V, Wagner G, Verdine GL. Solution structure of the core NFATC1/DNA complex. Cell 1998. 92 (5): 687-96. Link

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 1997. 36 (29): 8755-66. Link

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 1997. 385 (6612): 172-6. Link

Schiffer CA, Dötsch V. The role of protein-solvent interactions in protein unfolding. Curr. Opin. Biotechnol. 1996. 7 (4): 428-32. Link

Dötsch V, Matsuo H, Wagner G. Amino-acid-type identification for deuterated proteins with a beta-carbon-edited HNCOCACB experiment. J Magn Reson B 1996. 112 (1): 95-100. Link

Dötsch V, Wagner G. Editing for amino-acid type in CBCACONH experiments based on the 13C beta-13C gamma coupling. J Magn Reson B 1996. 111 (3): 310-3. Link

Dötsch V, Oswald RE, Wagner G. Selective identification of threonine, valine, and isoleucine sequential connectivities with a TVI-CBCACONH experiment. J Magn Reson B 1996. 110 (3): 304-8. Link

Dötsch V, Oswald RE, Wagner G. Amino-acid-type-selective triple-resonance experiments. J Magn Reson B 1996. 110 (1): 107-11. Link

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 1995. 34 (46): 15057-67. Link

Dötsch V, Wider G, Siegal G, Wüthrich K. Salt-stabilized globular protein structure in 7 M aqueous urea solution. FEBS Lett. 1995. 372 (2-3): 288-90. Link

Dötsch V, Oswald RE, Wagner G. Water suppression by coherence selection with absorptive lineshape without loss in sensitivity. J Magn Reson B 1995. 108 (3): 285-8. Link

Dötsch V, Wider G, Siegal G, Wüthrich K. Interaction of urea with an unfolded protein. The DNA-binding domain of the 434-repressor. FEBS Lett. 1995. 366 (1): 6-10. Link