267. Roske Y, de Oliveira GAP, Cremer N, Diehl A, Schmieder P, Heinemann U, Oschkinat H, Pires JR (2020) Crystal structure of Q4D6Q6, a conserved kinetoplastid-specific protein from Trypanosoma cruzi. JSB accepted

266. Chow WY, Norman BP, Roberts NB, Ranganath LR, Teutloff C, Bittl R, Duer MJ, Gallagher JA, Oschkinat H (2020) Pigmentation chemistry and radical-based collagen degradation in alkaptonuria and osteoarthritic cartilage. Angew Chem Int Ed Engl 59, 1-7. DOI: 10.1002/anie.202000618

265. Friedrich D, Perodeau J, Nieuwkoop AJ, Oschkinat H (2020) MAS NMR detection of hydrogen bonds for protein secondary structure characterization. J Biomol NMR 74(4-5), 247-256. DOI: 10.1007/s10858-020-00307-z

264. Gerland L, Friedrich D, Hopf L, Donovan EJ, Wallmann A, Erdmann N, Diehl A, Bommer M, Buzar K, Ibrahim M, Schmieder P, Dobbek H, Zouni A, Bondar AN, Dau H, Oschkinat H (2020) pH-dependent protonation of surface carboxylate groups in PsbO enables local buffering and triggers structural changes. Chembiochem DOI: 10.1002/cbic.201900739

263. Friedrich D, Brüning FN, Nieuwkoop AJ, Netz RR, Hegemann P, Oschkinat H (2020) Collective exchange processes reveal an active site proton cage in bacteriorhodopsin. Commun Biol 3(1), 4. DOI: 10.1038/s42003-019-0733-7

262. Moura-Alves P, Puyskens A, Stinn A, Klemm M, Guhlich-Bornhof U, Dorhoi A, Furkert J, Kreuchwig A, Protze J, Lozza L, Pei G, Saikali P, Perdomo C, Mollenkopf HJ, Hurwitz R, Kirschhoefer F, Brenner-Weiss G, Weiner J, 3rd, Oschkinat H, Kolbe M, Krause G, Kaufmann SHE (2019) Host monitoring of quorum sensing during Pseudomonas aeruginosa infection. Science 366(6472), 1472. DOI: 10.1126/science.aaw1629

261. Jaudzems K, Polenova T, Pintacuda G, Oschkinat H, Lesage A (2019) DNP NMR of biomolecular assemblies. J Struct Biol 206(1), 90-98. DOI: 10.1016/j.jsb.2018.09.011

260. Hoffmann J, Ruta J, Shi C, Hendriks K, Chevelkov V, Franks WT, Oschkinat H, Giller K, Becker S, Lange A (2019) Protein resonance assignment by BSH-CP based 3D solid-state NMR experiments: A practical guide. MRC 58(5), 445-465. DOI: 10.1002/mrc.4945.

259. Goldberga I, Li R, Chow WY, Reid DG, Bashtanova U, Rajan R, Puszkarska A, Oschkinat H, Duer JM (2019) Detection of nucleic acids and other low abundance components in native bone and osteosarcoma extracellular matrix by isotope enrichment and DNP-enhanced NMR. RSC Adv 9(46), 26686-90. DOI: 10.1039/C9RA03198G

258. Müller KH, Hayward R, Rajan R, Whitehead M, Cobb AM, Ahmad S, Sun M, Goldberga I, Li R, Bashtanova U, Puszkarska AM, Reid DG, Brooks RA, Skepper JN, Bordoloi J, Chow WY, Oschkinat H, Groombridge A, Scherman OA, Harrison JA, Verhulst A, D'Haese PC, Neven E, Needham LM, Lee SF, Shanahan CM, Duer MJ (2019) Poly(ADP-Ribose) Links the DNA Damage Response and Biomineralization. Cell Rep 27(11), 3124-3138. DOI: 10.1016/j.celrep.2019.05.038

257. Gupta R, Zhang H, Lu M, Hou G, Caporini M, Rosay M, Maas W, Struppe J, Ahn J, Byeon IL, Oschkinat H, Jaudzems K, Barbet-Massin E, Emsley L, Pintacuda G, Lesage A, Gronenborn AM, Polenova T (2019) Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies. J Phys Chem B 123(24), 5048-5058. DOI: 10.1021/acs.jpcb.9b02293

256. Kesten C, Wallmann A, Schneider R, McFarlane HE, Diehl A, Khan GA, van Rossum BJ, Lampugnani ER, Szymanski WG, Cremer N, Schmieder P, Ford KL, Seiter F, Heazlewood JL, Sanchez-Rodriguez C, Oschkinat H, Persson S (2019) The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants.Nat Commun 10(1), 857. DOI: 10.1038/s41467-019-08780-3

255. Chow WY, Li R, Goldberga I, Reid DG, Rajan R, Clark J, Oschkinat H, Duer MJ, Hayward R, Shanahan CM (2018) Essential but sparse collagen hydroxylysyl post-translational modifications detected by DNP NMR. Chem Commun (Camb) 54, 12570-12573. DOI: 10.1039/c8cc04960b

254. de Freitas MS, Rezaei Araghi R, Brandenburg E, Leiterer J, Emmerling F, Folmert K, Gerling-Driessen UIM, Bardiaux B, Bottcher C, Pagel K, Diehl A, Berlepsch HV, Oschkinat H, Koksch B (2018) The protofilament architecture of a de novo designed coiled coil-based amyloidogenic peptide. J Struct Biol 203, 263-272. DOI: 10.1016/j.jsb.2018.05.009

253. Pellegrini E, Desfosses A, Wallmann A, Schulze WM, Rehbein K, Mas P, Signor L, Gaudon S, Zenkeviciute G, Hons M, Malet H, Gutsche I, Sachse C, Schoehn G, Oschkinat H, Cusack S (2018) RIP2 filament formation is required for NOD2 dependent NF-kappa B signalling. Nat Commun 9, 4043. DOI: 10.1038/s41467-018-06451-3

252. Iline-Vul T, Adiram-Filiba N, Matlahov I, Geiger Y, Abayev M, Keinan-Adamsky K, Akbey U, Oschkinat H, Goobes G (2018) Understanding the roles of functional peptides in designing apatite and silica nanomaterials biomimetically using NMR techniques. Curr Opin Colloid In 33, 44-52. DOI: 10.1016/j.cocis.2018.01.012

251. Stoepler D, Macpherson A, Smith-Penzel S, Basse N, Lecomte F, Deboves H, Taylor RD, Norman T, Porter J, Waters LC, Westwood M, Cossins B, Cain K, White J, Griffin R, Prosser C, Kelm S, Sullivan AH, Fox D 3rd, Carr MD, Henry A, Taylor R, Meier BH, Oschkinat H, Lawson AD (2018) Insight into small molecule binding to the neonatal Fc receptor by X-ray crystallography and 100 kHz magic-angle-spinning NMR. PLoS Biol 16(5), e2006192. DOI: 10.1371/journal.pbio.2006192

250. Geiger M, Jagtap A, Kaushik M, Sun H, Stöppler D, Sigurdsson S, Corzilius B, Oschkinat H (2018) Efficiency of water-soluble nitroxide biradicals for dynamic nuclear polarization in rotating solids at 9.4 T: bcTol-M and cyolyl-TOTAPOL as new polarizing agents. Chemistry 24(51), 13485-13494. DOI: 10.1002/chem.201801251

249. Diehl A, Roske Y, Ball L, Chowdhury A, Hiller M, Molière N, Kramer R, Stöppler D, Worth CL, Schlegel B, Leidert M, Cremer N, Erdmann N, Lopez D, Stephanowitz H, Krause E, van Rossum B-J, Schmieder P, Heinemann U, Turgay K, Akbey Ü, Oschkinat H(2018) Structural changes of TasA in biofilm formation of Bacillus subtilis. PNAS 115, 3237-3242. DOI: 10.1073/pnas.1718102115

248. Retel JS, Nieuwkoop AJ, Hiller M, Higman VA, Barbet-Massin E, Stanek J, Andreas LB, Franks WT, van Rossum BJ, Vinothkumar KR, Handel L, de Palma GG, Bardiaux B, Pintacuda G, Emsley L, Kühlbrandt W, Oschkinat H(2017) Structure of outer membrane protein G in lipid bilayers. Nature Communications 8, 2073

247. de Oliveira GAP, Marques MA, Cordeiro Y, Schuabb C, Moraes AH, Winter R, Oschkinat H, Foguel D, de Freitas MS, Silva JL(2017) Structural basis for the dissociation of alpha-synuclein fibrils triggered by pressure perturbation of the hydrophobic core. Scientific Reports 6,  Article number: 37990

246. Erlendsson S, Gotfryd K, Larsen FH, Mortensen JS, Geiger MA, van Rossum BJ, Oschkinat H, Gether U, Teilum K, Loland CJ(2017) Direct assessment of substrate binding to the Neurotransmitter: Sodium Symporter LeuT by solid state NMR. Elife, Pii: e19314

245. Stöppler D, Song C, van Rossum BJ, Geiger MA, Lang C, Mroginski MA, Jagtap AP, Sigurdsson ST, Matysik J, Hughes J, Oschkinat H(2016) Dynamic Nuclear polarization provides new insights into chromophore structure in phytochrome photoreceptors. Angew Chem Int Ed 55(52): 16017-16020

244. Geiger M-A, Orwick-Rydmark M, Märker WT, Akhmetzyanov D, Stöppler D, Zinke M, Specker E, Nazaré M, Diehl A, van Rossum B-J, Aussenac F, Prisner T, Akbey Ü, Oschkinat H(2016) Temperature dependence of cross-effect dynamic nuclear polarization in rotating solid: advantages of elevated temperatures. PCCP 18(44): 30696-30704

243. D'Andréa ÉD, Diehl A, Schmieder P, Oschkinat H, Pires JR(2016) Chemical shift assignments and secondary structure prediction for Q4DY78, a conserved kinetoplastid-specific protein from Trypanosoma cruzi. Biomol NMR Assign 10(2): 325-328

242. Bretschneider CO, Akbey Ü, Aussenac F, Olsen GL, Feintuch A, Oschkinat H, Frydman L(2016) On the potential of dynamic nuclear polarization enhanced diamonds in solid-state and dissolution 13C NMR spectroscopy. ChemPhysChem 17(17): 2691-2701

241. Lange S, Franks WT, Rajagopalan N, Döring K, Geiger MA, Linden A, van Rossum B-J, Kramer G, Bukau B, Oschkinat H(2016) Structure analysis of a signal peptide inside the ribosome tunnel by DNP MAS NMR. Sci Adv 2(8): e1600379

240. Nagaraj M, Franks TW, Saeidpour S, Schubeis T, Oschkinat H, Ritter C, van Rossum BJ(2016) Surface binding of TOTAPOL assists structural investigations of amyloid fibrils by dynamic nuclear polarization NMR spectroscopy. ChemBioChem 17(14): 1308-1311

239.Soto M, Hiller M, Oschkinat H, Koschek K (2016) Multifunctional Benzoxazines Feature Low Polymerization Temperature and Diverse Polymer Structures. Polymers 8(8): Article Number: 278

238.Geiger Y, Gottlieb HE, Akbey Ü, Oschkinat H, Goobes G (2016) Studying the Conformation of a Silaffin-Derived Pentalysine Peptide Embedded in Bioinspired Silica using Solution and Dynamic Nuclear Polarization Magic-Angle Spinning NMR. JACS 138: 5561-5567

237.Loof D, Hiller M, Oschkinat H, Koschek K(2016) Quantitative and qualitative analysis of surface modified cellulose utilizing TGA-MS. Materials  9(6): 415-428

236.Jagtap AP, Geiger M-A, Stöppler D, Orwick-Rydmark M, Oschkinat H, Sigurdsson ST(2016) A highly water-soluble biradical for efficient dynamic nuclear polarization of biomolecules. ChemCommun  52(43): 7020-7023

235.Akbey Ü., Oschkinat H.(2016) Structural biology applications of solid state MAS DNP NMR. J Magn Reson [Epub ahead of print]

234.Muench F, Retel J, Jeuthe S, O H-Ici D, van Rossum B, Wassilew K, Schmerler P, Kuehne T, Berger F, Oschkinat H, Messroghli DR (2015) Alterations in creatine metabolism observed in experimental autoimmune myocarditis using ex vivo proton magic angle spinning MRS. NMR Biomed  28(12):1625-1633

234.Gupta R, Lu M, Hou G, Caporini MA, Rosay M, Maas W, Struppe J, Suiter C, Ahn J, Byeon IL, Franks WT, Orwick-Rydmark M, Bertarello A, Oschkinat H, Lesage A, Pintacuda G, Gronenborn AM, Polenova T (2015) Dynamic nuclear polarization enhanced MAS NMR spectroscopy for structural analysis of HIV-1 protein assemblies. J Phys Chem B  120(2):329-339

233.Geiger Y, Gottlieb HE, Akbey Ü, Oschkinat H, Goobes G (2015) Studying the conformation of a silaffin-derived pentalysine peptide embedded in bioinspired silica using solution and DNP MAS NMR. J Am Chem Soc.  138(17): 5561-5567

232.Bruun S, Stoeppler D, Keidel A, Kuhlmann U, Luck M, Diehl A, Geiger MA, Woodmansee D, Trauner D, Hegemann P, Oschkinat H, Hildebrandt P, Stehfest K (2015) Light-Dark Adaptation of Channelrhodopsin Involves Photoconversion Between the all-trans and 13-cis Retinal Isomers.Biochemistry 2015 Aug 3. [Epub ahead of print]

231.  Mentink-Vigier F, Akbey Ü, Oschkinat H, Vega S, Feintuch A (2015) Theoretical aspects of Magic Angle Spinning - Dynamic Nuclear Polarization.J Magn Reson 258:102-120

230. Opitz R, Müller M, Reuter C, Barone M, Soicke A, Roske Y, Piotukh K, Huy P, Beerbaum M, Wiesner B, Beyermann M, Schmieder P, Freund C, Volkmer R, Oschkinat H, Schmalz HG, Kühne R (2015) A modular toolkit to inhibit proline-rich motif-mediated protein-protein interactions.Proc Natl Acad Sci U S A. 112(16):5011-6

229. Moura-Alves P, Faé K, Houthuys E, Dorhoi A, Kreuchwig A, Furkert J, Barison N, Diehl A, Munder A, Constant P, Skrahina T, Guhlich-Bornhof U, Klemm M, Koehler AB, Bandermann S, Goosmann C, Mollenkopf HJ, Hurwitz R, Brinkmann V, Fillatreau S, Daffe M, Tümmler B, Kolbe M, Oschkinat H, Krause G, Kaufmann SH (2015) AhR sensing of bacterial pigments regulates antibacterial defence.Nature 512(7515):387-92

228.Nieuwkoop AJ, Franks WT, Rehbein K, Diehl A, Akbey Ü, Engelke F, Emsley L, Pintacuda G, Oschkinat H (2015) Sensitivity and resolution of proton detected spectra of a deuterated protein at 40 and 60 kHz magic-angle-spinning. J Biomol NMR  61(2), 161-171

227. Muench F, Retel J, Jeuthe S, Van Rossum B, Oh-Ici D, Berger F, Kuehne T, Oschkinat H, Messroghli D  (2014) Metabolic profiling in experimental autoimmune myocarditis rat model using ex-vivo proton magic angle spinning magnetic resonance spectroscopy (1H-MAS-MRS). Eur Heart J, 35, 114-115.

226. Moura-Alves P, Faé K, Houthuys E, Dorhoi A, Kreuchwig A, Furkert J, Barison N, Diehl A, Munder A, Constant P, Skrahina T, Guhlich-Bornhof U, Klemm M, Koehler AB, Bandermann S, Goosmann C, Mollenkopf HJ, Hurwitz R, Brinkmann V, Fillatreau S, Daffe M, Tümmler B, Kolbe M, Oschkinat H, Krause G, Kaufmann SH (2014) AhR sensing of bacterial pigments regulates anibacterial defence. Nature, 512(7515), 387-92

225. Barbet-Massin E, Pell AJ, Retel JS, Andreas LB, Jaudzems K, Franks WT, Nieuwkoop AJ, Hiller M, Higman V, Guerry P, Bertarello A, Knight MJ, Felletti M, Le Marchand T, Kotelovica S, Akopjana I, Tars K, Stoppini M, Bellotti V, Bolognesi M, Ricagno S, Chou JJ, Griffin RG, Oschkinat H, Lesage A, Emsley L, Herrmann T, Pintacuda G (2014) Rapid proton-detected NMR assignment for proteins with fast magic angle spinning. J Am Chem Soc, 136(35), 12489-97

224. Vargas C, Radziwill G, Krause G, Diehl A, Keller S, Kamdem N, Czekelius C, Kreuchwig A, Schmieder P, Doyle D, Moelling K, Hagen V, Schade M, Oschkinat H(2014) Small-molecule inhibitors of AF6 PDZ-mediated protein-protein interactions. ChemMedChem, 9(7), 1458-62

223. Akbey Ü, Nieuwkoop AJ, Wegner S, Voreck A, Kunert B, Bandara P, Engelke F, Nielsen NC,Oschkinat H (2014) Quadruple-resonance magic-angle spinning NMR spectroscopy of deuterated solid proteins. Angew Chem Int Ed Engl., 53(9), 2438-42

222. Jain SK, Nielsen AB, Hiller M, Handel L, Ernst M, Oschkinat H, Akbey Ü, Nielsen NC (2014) Low-power polarization transfer between deuterons and spin-1/2 nuclei using adiabatic (RESPIRATION)CP in solid-state NMR. Phys Chem Chem Phys, 16(7), 2827-30

183. Zaminer J, Brockmann C, Huy P, Opitz R, Reuter C, Beyermann M, Freund C, Müller M, Oschkinat H, Kühne R, Schmalz HG (2010) Addressing protein-protein interactions with small molecules: a Pro-Pro dipeptide mimic with a PPII helix conformation as a module for the synthesis of PRD-binding ligands, Angew Chem Int Ed, 49:7111-71115

182. Akbey Ü, Franks WT, Linden A, Lange S, Griffin RG, van Rossum BJ, Oschkinat H(2010) Angew Chem Int Ed, 49:7803-7806

181. Akbey U, Lange S, Trent Franks W, Linser R, Rehbein K, Diehl A, van Rossum BJ, Reif B, Oschkinat H(2010) Optimum levels of exchangeable protons in perdeuterated proteins for proton detection in MAS solid-state NMR spectroscopy,J Biomol NMR, 46: 67-73

180. Jehle S, Rajagopal P, Bardiaux B, Markovic S, Kühne R, Stout JR, Higman VA, Klevit RE, van Rossum BJ, Oschkinat H (2010) Solid-state NMR and SAXS studies provide a structural basis for the activation of aB-crystallin oligomers, Nat Struct Mol Biol, 17: 1037-1042

179. Jehle S, Falb, M, Kirkpatrick JP, Oschkinat H, van Rossum BJ (2010) Intermolecular protein-RNA interactions revealed by 2D P-31-N-15 magic angle spinning solid-state NMR spectroscopy, JACS, 132: 3842-3846

178. Lange V, Becker-Baldus J, Kunert B, van Rossum BJ, Casagrande F, Engel A, Roske Y, Scheffel FM, Schneider E, Oschkinat H(2010) MAS NMR study of the bacterial ABC transporter ArtMP, ChemBioChem, 11: 547-555

177. Maritzen T, Schmidt MR, Kukhtina V, Higman VA, Strauss H, Volkmer R, Oschkinat H, Dotti CG, Haucke V (2010) A novel subtype of AP-1-binding motif within the Palmitoylated trans-Golgi Network/Endosomal Accessory Protein Gadkin/gamma-BAR, J Biol Chem, 285: 4074-4086

176. Nicolaus N, Zapke J, Riesterer P, Neudorfl JM, Prokop A, Oschkinat H, Schmalz HG (2010) Azides derived from colchicine and their use in library synthesis: a practical entry to new bioactive derivatives of an old natural drug, ChemMedChem, 5: 661-665

175. Saupe J, Roske Y, Kamdem N, Schillinger C, Radetzky S, Diehl A, Oschkinat H, Krause G, Heinemann U, Rademann J (2010) Tetrahydroquinoline carboxylates are potent inhibitors of the Shank PDZ domain, a putative target in autism disorders, J Med Chem, submitted

174. Akbey U, Oschkinat H, van Rossum BJ (2009) Double-nucleus enhanced recoupling for efficient C-13 MAS NMR correlation spectroscopy of perdeuterated proteins, JACS, 131: 17054- 17055

173. Higman VA, Flinders J, Hiller M, Jehle S, Markovic S, Fiedler S, van Rossum BJ, Oschkinat H (2009)Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively C-13-labelled proteins, J Biomol NMR, 44: 245-260

172. Jehle S, van Rossum B, Stout JR, Noguchi SM, Faelber K, Rehbein K, Oschkinat H, Klevit RE, Rajagopal P (2009) alpha B-Crystallin: a hybrid solid-state/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer, J Mol Biol, 385: 1481-1481

171.Krabben L, van Rossum BJ, Jehle S, Bocharov E, Lyukmanova EN, Schulga AA, Arseniev A, Hucho F, Oschkinat H (2009) Loop 3 of short neurotoxin II is an additional interaction site with membrane-bound nicotinic acetylcholine receptor as detected by solid-state NMR spectroscopy,J Mol Biol, 390: 662-671

170. Mainz A, Jehle S, van Rossum BJ, Oschkinat H, Reif B (2009) Large protein complexes with extreme rotational correlation times investigated in solution by magic-angle-spinning NMR spectroscopy, JACS, 131: 15968-15969

169. Rutkowska A, Beerbaum M, Rajagopalan N, Fiaux J, Schmieder P, Kramer G, Oschkinat H, Bukau B (2009) Large-scale purification of ribosome-nascent chain complexes for biochemical and structural studies, FEBS Lett, 583: 2407-2413

168.Schmidt MR, Maritzen T, Kukhtina V, Higman VA, Doglio L, Barak NN, Strauss H, Oschkinat H, Dotti CG, Haucke V (2009) Regulation of endosomal membrane traffic by a Gadkin/AP-1/kinesin KIF5 complex, PNAS, 106: 15344-15349

167. Weidauer SE, Schmieder P, Beerbaum M, Schmitz W, Oschkinat H, Mueller TD (2009) NMR structure of the Wnt modulator protein Sclerostin, Biochem and Biophy Res Comm, 380: 160-165

166.   Jehle S, van Rossum BJ, Stout JR, Noguchi SR, Falber K, Rehbein K, Oschkinat H, Klevit RE, Rajagopal P
alpha-B-Crystallin: A Hybrid Solid-Solution State NMR Investigation Reveals Structural Aspects of the Heterogeneous Oligomer.
J Mol Biol, 385, 1481–1497

165.   Konig R, Scholz G, Pawlik A, Jager C, van Rossum BJ, Oschkinat H, Kemnitz E
Crystalline aluminum hydroxy fluorides: Structural insights obtained by high field solid state NMR and trend analyses.
J Phys Chem C 112(40), 15708–15720

164.   Pellecchia M, Bertini I, Cowburn D, Dalvit C, Giralt E, Jahnke W, James TL, Homans SW, Kessler H, Luchinat C, Meyer B, Oschkinat H, Peng J, Schwalbe H, Siegal G
Perspectives on NMR in drug discovery: a technique comes of age.
Nat Rev Drug Discov, 7(9), 738-45

163.   Becker J, Ferguson N, Flinders J, van Rossum BJ, Fersht AR, Oschkinat H
A sequential assignment procedure for proteins that have intermediate line widths in MAS NMR spectra: amyloid fibrils of human CA 150, WW2. ChemBioChem 9(12), 1946-52

162.   Axelrod S, Oschkinat H, Enders J, Schlegel B, Brinkmann V, Kaufmann SH, Haas A, Schaible UE
Delay of phagosome maturation by a mycobacterial lipid is reversed by nitric oxide.
Cell Microbiol. Cell Microbiol 10(7), 1530-45

161. Hiller M, Higman VA, Jehle S, van Rossum BJ, Kühlbrandt W, Oschkinat H.
[2,3-(13)C]-labeling of aromatic residues--getting a head start in the magic-angle-spinning NMR assignment of membrane proteins.
J Am Chem Soc. 130(2):408-9

160. Ramirez-Espain X, Ruiz L, Martin-Malpartida P, Oschkinat H, Macias MJ.
Structural characterization of a new binding motif and a novel binding mode in group 2 WW domains.
J Mol Biol. 2007 Nov 9;373(5):1255

159. Podust LM, von Kries JP, Eddine AN, Kim Y, Yermalitskaya LV, Kuehne R, Ouellet H, Warrier T, Alteköster M, Lee JS, Rademann J, Oschkinat H, Kaufmann SH, Waterman MR.
Small-molecule scaffolds for CYP51 inhibitors identified by high-throughput screening and defined by X-ray crystallography.
Antimicrob Agents Chemother. 2007 Nov;51(11):3915-23

158. Fiedler S, Knocke C, Vogt J, Oschkinat H, Diehl A
Production of 2H-, 13C-, and 15N-Labeled OmpG via High Cell Density Fermentation
GEN, 27(9)

157. Scholz I, Jehle S, Schmieder P, Hiller M, Eisenmenger F, Oschkinat H, van Rossum B-J
J-deconvolution using maximum entropy reconstruction applied to 13C-13C solid-state cross-polarization magic-angle-spinning NMR of proteins
J Am Chem Soc. 129(21), 6682-3

156. Kohler C, Andersen OM, Diehl A, Krause G, Schmieder P, Oschkinat H
The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family
J Struct Funct Genomics. 7(3-4), 131-8

155. Balayssac S, Bertini I, Falber K, Fragai M, Jehle S, Lelli M, Luchinat C, Oschkinat H, Yeo KJ
Solid-State NMR of Matrix Metalloproteinase 12: An Approach Complementary to Solution NMR
Chembiochem. 8(5), 486-9

154. Fedorov OY, Higman VA, Schmieder P, Leidert M, Diehl A, Elkins J, Soundarajan M, Oschkinat H, Ball LJ
Resonance assignment of the RGS domain of human RGS10
J Biomol NMR, 38(2), 191

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153. Jehle S, Hiller M, Rehbein K, Diehl A, Oschkinat H, van Rossum BJ
Spectral editing: selection of methyl groups in multidimensional solid-state magic-angle spinning NMR
J Biomol NMR. 2006 Nov;36(3):169-77

151. Ferguson N, Becker J, Tidow H, Tremmel S, Sharpe TD, Krause G, Flinders J, Petrovich M, Berriman J, Oschkinat H, Fersht AR General structural motifs of amyloid protofilaments
Proc Natl Acad Sci U S A. 103:16248-53

150. Higman VA, Leidert M, Diehl A, Elkins J, Soundararajan M, Oschkinat H, Ball LJ
NMR assignment of human RGS18
J Biomol NMR. 36(5):72

149. Aido-Machado RD, Salmon D, Diehl A, Leidert M, Schmetzer O, de Lima AP, Scharfstein J, Oschkinat H, Pires JR
(1)H, (15) N and (13)C assignments of the cysteine protease inhibitor Chagasin from Trypanosoma cruzi
J Biomol NMR. 36(1):30

148. Joshi M, Vargas C, Boisguerin P, Diehl A, Krause G, Schmieder P, Moelling K, Hagen V, Schade M, Oschkinat H
Discovery of Low-Molecular-Weight Ligands for the AF6 PDZ Domain
Angew Chem Int Ed Engl. 45(23):3790-95

147. Salmon D, do Aido-Machado R, Diehl A, Leidert M, Schmetzer O, de A Lima AP, Scharfstein J, Oschkinat H, Pires JR
Solution structure and backbone dynamics of the Trypanosoma cruzi cysteine protease inhibitor chagasin
J Mol Biol. 2006 Apr 14;357(5):1511-21

146. Mac TT, Beyermann M, Pires JR, Schmieder P, Oschkinat H
High yield expression and purification of isotopically labelled human endothelin-1 for use in NMR studies Protein Expr Purif. 48(2):253-60

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145. Adam P, Gutlich M, Oschkinat H, Bacher A, Eisenreich W
Studies of the intermediary metabolism in cultured cells of the insect Spodoptera frugiperda using 13C- or 15N-labelled tracers
BMC Biochem. 2005 Nov 14;6:24

144. Fossi M, Castellani F, Nilges M, Oschkinat H, van Rossum BJ
SOLARIA: a protocol for automated cross-peak assignment and structure calculation for solid-state magic-angle spinning NMR spectroscopy
Angew Chem Int Ed Engl. 2005 Sep 26;44(38):6151-4

143. Hiller M, Krabben L, Vinothkumar KR, Castellani F, van Rossum BJ, Kuhlbrandt W, Oschkinat H
Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli
Chembiochem. 2005 Sep;6(9):1679-84

142. Appelt C, Wessolowski A, Soderhall JA, Dathe M, Schmieder P
Structure of the Antimicrobial, Cationic Hexapeptide Cyclo(RRWWRF) and Its Analogues in Solution and Bound to Detergent Micelles
Chembiochem. 2005 Sep;6(9):1654-62

141. Tremmel S, Beyermann M, Oschkinat H, Bienert M, Naumann D, Fabian H
(13)C-Labeled Tyrosine Residues as Local IR Probes for Monitoring Conformational Changes in Peptides and Proteins
Angew Chem Int Ed Engl. 2005 Jul 18;44(29):4631-5

140. Leitner D, Wahl M, Labudde D, Krause G, Diehl A, Schmieder P, Pires JR, Fossi M, Wiedemann U, Leidert M, Oschkinat H
The solution structure of an N-terminally truncated version of the yeast CDC24p PB1 domain shows a different beta-sheet topology
FEBS Lett. 2005 Jul 4;579(17):3534-8

139. Fossi M, Oschkinat H, Nilges M, Ball LJ
Quantitative study of the effects of chemical shift tolerances and rates of SA cooling on structure calculation from automatically assigned NOE data
J Magn Reson. 2005 Jul;175(1):92-102

138. Chevelkov V, Faelber K, Diehl A, Heinemann U, Oschkinat H, Reif B
Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR
J Biomol NMR. 2005 Apr;31(4):295-310

137. Schade M, Oschkinat H
NMR fragment screening: tackling protein-protein interaction targets
Curr Opin Drug Discov Devel. 2005 May;8(3):365-73

136. Ball LJ, Kuhne R, Schneider-Mergener J, Oschkinat H
Recognition of Proline-Rich Motifs by Protein-Protein-Interaction Domains
Angew Chem Int Ed Engl. 2005 May 3;44(19):2852-2869

135. Pires JR, Parthier C, Aido-Machado R, Wiedemann U, Otte L, Bohm G, Rudolph R, Oschkinat H
Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain
J Mol Biol. 2005 Apr 29;348(2):399-408

134. Schubert M, Labudde D, Leitner D, Oschkinat H, Schmieder P.
A modified strategy for sequence specific assignment of protein NMR spectra based on amino acid type selective experiments
J Biomol NMR. 2005 Feb;31(2):115-28

133. Fossi M, Linge J, Labudde D, Leitner D, Nilges M, Oschkinat H.
Influence of chemical shift tolerances on NMR structure calculations using ARIA protocols for assigning NOE data
J Biomol NMR. 2005 Jan;31(1):21-34

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132. Quantification of PDZ Domain Specificity, Prediction of Ligand Affinity and Rational Design of Super-binding Peptides
Wiedemann, U., Boisguerin, P., Leben, R., Leitner, D., Krause, G., Moelling, K., Volkmer-Engert, R. and Oschkinat, H.
J. Mol. Biol. 343, 703–718 (2004)

131. Letter to the Editor: 1H, 13C and 15N resonance assignment of the human Spred2 EVH1 do-main
Zimmermann, J., Jarchau, T., Walter, U., Oschkinat, H. & Ball L.J.
J. Biomol. NMR 29, 435-436 (2004)

130. The solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitro
Kahmann, J.D., Wecking, D.A., Putter, V., Lowenhaupt, K., Kim, Y.-G., Schmieder, P., Oschkinat, H., Rich, A., and Schade, M.
PNAS 101(9), 2712-2717 (2004)

129. Identifying cis/trans conformation of proline using backbone and Cb chemical shifts and secondary structure information for decision tree learning
Pahlke, D., Labudde, D., Leitner, D., and Oschkinat, H.
J. Biomol. NMR, submitted 2004

128. Solution structure of the OPCA domain of yeast CDC24p: Insights on the structural and functional evolution within the PB1 family
Impacts on domain and functional evolution derived from a structurally new member of the PB1 family: The solution structure of the OPCA domain of yeast CDC24p
Leitner, D., Wahl, M., Labudde, D., Krause, G., Diehl, A., Schmieder, P., Pires, J.R., Fossi, M., Wiedemann, U., Leidert, M., and Oschkinat, H., J. Mol. Biol., submitted

127. Sulindac-Derived Ras Pathway Inhibitors Target the Ras-Ra Interaction and Downstream Effectors in the Ras Pathway
Waldmann, H., Karaguni I.M., Carpintero, M., Gourzoulidou, E., Herrm, C., Brockmann, C., Oschkinat, H., Muller O.
Angew. Chem. Int. Ed. Engl. 43(4), 454-458 (2004)

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126. Determination of solid-state NMR structures of proteins by means of three-dimensional 15N-13C-13C dipolar correlation spectroscopy and chemical shift analysis
Castellani, F., van Rossum, B.J., Diehl, A., Rehbein, K., Oschkinat, H.
Biochemistry 42(39), 11476-83 (2003)

125. Design of N-substituted Peptomer Ligands for EVH1 Domains.
Zimmermann, J., Kuhne, R., Volkmer-Engert, R., Jarchau, T., Walter, U., Oschkinat, H., Ball, L.J.
J. Biol. Chem. 278(38):36810-36818 (2003)

124. 1H detection in MAS solid-state NMR spectroscopy of biomacromolecules employing pulsed field gradients for residue solvent suppression
Chevelkov, V., van Rossum, B.J., Castellani, F., Rehbein, K., Diehl, A., Hoh, M., Steuernagel, S., Engelke, F., Oschkinat, H., Reif, B.
J. Am. Soc. 125(26), 7788-7789 (2003)

123. Measurement of multiple psi torsion angles in uniformly 13C,15N-labeled alpha-spectrin SH3 domain using 3D 15N-13C-13C-15N MAS dipolar-chemical shift correlation spectroscopy.
Ladizhansky, V., Jaroniec, C.P., Diehl, A., Oschkinat, H., Griffin, R.G.
J. Am. Chem. Soc., 125(22), 6827-33 (2003)

122. Combinig SPOT Synthesis and Nature Peptide Ligation to Create Large Arrays of WW Domains
Toepert, F, Knaute, T, Guffler, S, Pires, JR, Matzdorf, T, Oschkinat, H, Schneider-Mergener,
J: Angew Chem Int Ed Engl., 42(10), 1136-1140 (2003)

121. WW domain sequence activity relationships identified using ligand recognition propensities of 42 WW domains
Otte, L., Wiedemann, U., Schlegel, B., Pires, J.R., Beyermann, M., Schmieder, P., Krause, G., Volkmer-Engert, R., Schneider-Mergener, J., and Oschkinat, H.
Protein Science, 12, 491-500 (2003)

120. The solution structure of the SODD BAG-domain and a model of the SODD-BAG/HAP70 complex reveal additional SODD subfamily-specific electrostatic interactions
Brockmann, C., Leitner, D., Labudde, D., Diehl, A., Sievert, V., Büssow, K., Kühne, R., and Oschkinat, H.
FEBS, submitted

119. The ScPex13p SH3 domain exposes two distinct binding sites for Pex5p and Pex14p
Pires, J.R., Hong, X., Brockmann, C., Volkmer-Engert, R., Schneider-Mergener, J., Oschkinat, H., and Erdmann, R.
J. Mol. Biol.; 326(5), 1427-35 (2003)

118. Characterization of 1H-1H distances in a uniformly 2H, 15N-labeled SH3 domain by MAS solid-state NMR spectroscopy
Reif, B., van Rossum, B., Castellani, F., Rehbein, K., Diehl, A., and Oschkinat, H.
J. Am. Chem. Soc., 125, 1488-1489 (2003)

117. Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR correlation spectra
van Rossum, B., Castellani, F., Pauli, J., Rehbein, K., Hollander, J, de Groot, H., Oschkinat, H.
J. Biomol. NMR, 25(3), 217-223 (2003)

116. Prediction algorithm for amino acid type with its secondary structure in proteins (PLATON) using chemical shifts
Labudde, D., Leitner, D., Krüger, and Oschkinat, H.
J. Biomol. NMR, 25(1), 41-53 (2003)

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115. Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
Castellani, F., van Rossum, B.J., Diehl, A., Schubert, M., Rehbein, K., and Oschkinat, H.
Nature 420, 98-102 (2002)

114. Biosynthesis of riboflavin in archaea. Studies on the mechanism of 3,4-dihydroxy-2-butanone4-phosphate synthase of methanococcus jannaschii
Fischer, M.J., Romisch, W., Schiffmann, S., Kelly, M., Oschkinat, H., Steinbacher, S., Huber, R., Eisenreich, W., Richter, G., and Bacher, A.
J. Biol. Chem. 277(44), 41410-6 (2002)

113. A software tool for the prediction of xaa-pro peptide bond conformations in proteins based on 13C chemical shift statistic
Schubert, M., Labudde, D., Oschkinat, H., Schmieder, P.
J. Biomol. NMR 24(2), 149-54 (2002)

112. A 3-D structural model of solid self-assembled chlorophyll a/H(2)O from multispin labeling and MAS NMR 2-D dipolar correlation spectroscopy in high magnetic field
van Rossum, B.J., Schulten, E.A., Raap, J., Oschkinat, H., and de Groot, H.
J. Magn. Reson. 155(1), 1-14 (2002)

111. Relaxation, equilibrium oligomerization, and molecular symmetry of the VASP (336-380) EVH2 tetramer
Zimmermann, J., Labudde, D., Jarchau, T., Walter, U., Oschkinat, H., and Ball, L.J.
Biochemistry 41(37), 11143-11151 (2002)

110. 2D(13)C-(13)C MAS NMR correlation spectroscopy with mixing by true (1)H spin diffusion reveals long-range intermolecular distance restraints in ultra high magnetic field
de Boer, I., Bosman, L., Raap, J., Oschkinat, H., and de Groot H.
J. Magn. Reson. 157(2), 286 (2002)

109. Automated Setup of NMR Experiments by new versions of PASTE and PAPST
Labudde, D., Leitner, D., Winter, R., Schmieder, P., Schubert, M., and Oschkinat, H.
International Genomic/Proteomic Technology, 1(2) 24-28 (2002) Bruker Report 150, 8-12 (2002)

108. Solution structures of the YAP65 WW domain and the variant L30 K in complex with the peptides GTPPPPYTVG, N-(n-octyl)-GPPPY and PLPPY and the application of peptide libraries reveal a minimal binding epitope
Pires, J.R., Fatemeh T.-N., Toepert, F., Ast, T.,Hoffmüller, U., Schneider-Mergener, J., Kühne, R., Macias, M.J., and Oschkinat, H.
J. Mol. Biol. 314, 1147-1156 (2002)

107. EVH1 domains: structure, function and interactions
Ball, L.J., Jarchau, T., Oschkinat, H., and Walter, U.
FEBS Letters 513, 45-52 (2002)

106. The structure of the active center in dark-adapted Bacteriorhodopsin by solution-state NMR spectroscopy
Patzelt, H., Simon, B., terLaak, A., Keßler, B., Kühne, R., Schmieder, P., Oesterhelt, D., and Oschkinat, H.
PNAS, 99(15), 9765-9770 (2002)

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105. High-throughput three-dimensional protein structure determination.
Heinemann, U., Illing, G., and Oschkinat, H.
Current Opinion in Biotechnology 12, 348-354 (2001)

104. Ultrafast folding of WW domain without structured aromatic clusters in the denatured state.
Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., and Fersht, A.R.
PNAS 98(23), 13002-13007 (2001)

103. Using flexible loop mimetics to extend -value analysis to secondary structure interactions.
Ferguson, N., Pires, J.R., Toepert, F., Johnson, C.M., Pan, Y.P., Volkmer-Engert, R., Schneider-Mergener, J., Daggett, V., Oschkinat, H., and Fersht, A.R.
PNAS 98(23), 13008-13013 (2001)

102. The NMR structure of the 47 kD dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site.
Kelly, M.J.S., Ball, L.J., Krieger, C., Yu, Y., Fischer, M., Schiffmann, S., Schmieder, P., Kühne, R., Bremel, W., Bacher, A., Richter, G., and Oschkinat, H.
PNAS 98(23), 13025-13030 (2001)

101. High-resolution structures of the YAP65 domain and the variant L30K in complex with the peptides GTPPPPYTVG, N-(n-octyl)-GPPPY and PLPPY and the application of peptide libraries reveal a minimal binding epitope.
Pires, J.R., Taha-Nejad, F., Töpert, F., Ast, T., Hoffmüller, U., Schneider-Mergener, J., Kühne, R., Macias, M. J., and Oschkinat, H.
J Mol Biol 314(5), 1147-1156 (2001)

100. Amino acid type-selective backbone 1H-15N-correlations for Arg and Lys.
Schubert, M., Oschkinat, H., and Schmieder, P.
J. Biomol. NMR 20, 379-384 (2001)

99. Secondary chemical shifts in immobilized peptides and proteins: A qualitative basis for structure refinement under Magic Angle Spinning.
Luca, S., Filippov, D.V., van Boom, J.H., Oschkinat, H., de Groot, H.J.M., and Baldus, M.
J. Biomol. NMR 20, 325-331 (2001)

98. Assignment of the non-exchanging protons of the a-spectrin SH3 Domain by 2-D and 3-D 1H-13C solid-state MAS NMR and comparison of solution and solid-state proton chemical shifts.
van Rossum, B.-J., Castellani, F., Rehbein, K., Pauli, J., and Oschkinat, H.
CHEMBIOCHEM 2(12), 906-914 (2001)

97. Synthesis of an array comprising 837 variants of the hYAP WW protein domain.
Toepert, F., Pires, J.R., Landgraf, C., Oschkinat, H., and Schneider-Mergener, J.
Angew. Chem. Int. Ed. 40(5), 897-900 (2001)

96. Backbone and side chain 13C and 15N resonance assignments of the a-Spectrin SH3 domain by Magic Angle Spinning Solid State NMR at 17.6 Tesla.
Pauli, J., Baldus, M., van Rossum, B., de Groot, H., and Oschkinat, H.
CHEMBIOCHEM 2, 272 - 281 (2001)

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95. Improving the refolding yield of interleukin-4 through the optimization of local interactions.
Domingues, H., Peters, J., Schneider, K., Apeler, H., Sebald, W., Oschkinat, H., and Serrano, L.
J Biotechnol. 84(3):217-230 (2000)

94. An integrated approach to structural genomics.
Heinemann, U., Frevert, J., Hofmann, K.-P., Illing, G., Maurer, C., Oschkinat, H., and Saenger, W.
Progress in Biophysics & Molecular Biology 73, 347-362 (2000)

93. MUSIC, selective pulses, and tuned delays: Amino acid type-selective 1H-15N correlations, II.
Schubert, M., Oschkinat, H., and Schmieder, P.
J. Magn. Reson. 148, 61-72 (2000)

92. Bridging the gap: A set of selective 1H-15N-correlations to link sequential neighbours of prolines.
Schubert, M., Ball, L.J., Oschkinat, H., and Schmieder, P.
J. Biomol. NMR 17, 331-335 (2000)

91. Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity.
Ball, L.J., Kühne, R., Hoffmann, B., Häfner, A., Schmieder, P., Volkmer-Engert, R., Hof, M., Wahl, M., Schneider-Mergener, J., Walter, U., Oschkinat, H., and Jarchau, T.
EMBO J. 19 (18), 4903-4914 (2000)

90. Structural analysis of WW domains and design of a WW prototype.
Macias, M.J., Gervais, V., Civera, C., and Oschkinat, H.
Nat. Struc. Biol. 7, 375-379 (2000)

89. Sample optimization and identification of signal patterns of amino acid side chains in 2D RFDR Spectra of the a-spectrin SH3 domain.
Pauli, J., van Rossum, B., Förster, H., de Groot, H.J.M., and Oschkinat, H.
J. Magn. Reson. 143, 411-416 (2000)

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88. Rational design of a GCN4-derived mimetic of interleukin-4.
Domingues, H., Cregut, D., Sebald, W., Oschkinat, H., and Serrano, L.
Nat. Struc. Biol. 7, 652-656 (1999)

87. The solution structure of the Za domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA.
Schade, M., Turner, C.J., Kühne, R., Schmieder, P., Lowenhaupt, K., Herbert, A., Rich, A., and Oschkinat, H.
PNAS, 96, 12465-12470 (1999)

86. A 6 bp Z-DNA hairpin binds two Z domains from the human RNA editing enzyme ADAR1.
Schade, M., Behlke, J., Lowenhaupt, K., Herbert, A., Rich, A., and Oschkinat, H.
FEBS Letters 458, 27-31 (1999)

85. Signal selection in high-resolution NMR by pulsed field gradients: II. The design of gradient pulse sequence.
Thomas, D.J., Mitschang, L., Simon, B., and Oschkinat, H.
J. Magn. Reson. 137, 10-24 (1999)

84. Interaction of a syntrophin PDZ domain with a synthetic library of all human protein C-termini.
Hoffmüller, U., Russwurm, M., Kleinjung, F., Ashurst, J., Vokmer-Engert, R.,
Oschkinat, H., Koesling, D., and Schneider-Mergener, J.
Angew. Chem. Int. Ed. 38, 2000-2004 (1999)

83. The solution structure of the SAM domain from the receptor tyrosine kinase EphB2.
Smalla, M., Schmieder, P., Kelly, M., ter Laak, T., Krause, G., Ball, L., Wahl, M., Bork, P., and Oschkinat, H.
Protein Science 8, 1954-1961, (1999)

82. MUSIC in triple-resonance experiments: Amino acid type selective 15N-HSQCs.
Schubert, M., Smalla, M., Schmieder, P., and Oschkinat, H.
J. Magn. Reson. 141, 34-43 (1999)

81. A new type of PDZ domain recognition.
Oschkinat, H.
Nat. Struc. Biol. 6, 408-410 (1999)

80. NMR studies on the 46-kDa dimeric protein, 3,4-dihydroxy-2-butanone 4-phosphate synthase, using 2H, 13C, and 15N-labelling.
Richter, G., Kelly, M., Krieger, C., Yu, Y., Bermel, W., Karlsson, G., Bacher, A., and Oschkinat, H.
Eur. J. Biochem. 261, 57-65 (1999)

79. Application of amino acid type-specific 1H- and 14N- labelling in a 2H-, 15N-labelled background to a 47kDa homodimer: Potential for NMR structure determination of large proteins.
Kelly, M.J.S., Krieger, C., Ball, L.J., Yu, Y., Richter, G., Schmieder, P., Bacher, A., and Oschkinat, H.
J. Biomol. NMR 14, 79-83 (1999)

78. The entire metabolite spectrum of the green alga scenedesmus obliquus in isotope-labelled form.
Patzelt, B., Keßler, H., Oschkinat, H., and Oesterhelt, D.
Phytochemistry 50, 215-217 (1999)

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77. Heteronuclear relaxation study of the PH domain of b-spectrin: restriction of loop motions upon binding inositol trisphosphate.
Gryk, M., Abseher, R., Simon, B., Nilges, M., and Oschkinat, H.
J. Mol. Biol. 280, 879-896 (1998)

76. Multiplicity-selective coherence transfer steps for the design of amino-acid selective experiments - A triple-resonance experiment selective for Asn and Gln.
Schmieder, P., Leidert, M., Kelly, M., and Oschkinat, H.
J. Magn. Reson. 131, 199-202 (1998)

75. Specific interactions between the syntrophin PDZ domain and voltage-gates sodium channels.
Schultz, J., Hoffmüller, U., Krause, G., Ashurst, J., Macias, M.J., Schmieder, P., Schneider-Mergener, J., and Oschkinat, H.
Nat. Struc. Biol. 5, 19-24 (1998)

74. Multidimensional CP-MAS 13C-NMR of uniformly enriched chlorophyll.
van Rossum, B.-J., Boender, G.J., Mulder, F.M., Raap, J., Balaban, T.S., Holzwarth, A., Schaffner, K., Prytulla, S., Oschkinat, H., and de Groot, H.J.M.
Spectrochimica Acta A 54, 1167-1176 (1998)

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73. Towards structural investigations on isotope labelled native bacteriorhodopsin in detergent micelles by solution-state NMR spectroscopy.
Patzelt, H., Ulrich, A.S., Egbringhoff, H., Düx, P., Ashurst, J., Simon, B., Oschkinat, H., and Oesterhelt, D.
J. Biomol. NMR 10, 95-106 (1997)

72. A small region in phosducin inhibits G-protein-bg subunit function.
Blüml, K., Schnepp, W., Schröder, S., Beyermann, M., Macias, M., Oschkinat, H., and Lohse, M.J.
EMBO J. 16, 4908-4915 (1997)

71. Tools for the automated assignment of high-resolution three-dimensional protein NMR spectra based on pattern recognition techniques.
Croft, D., Kemmink, J., Neidig, K-P., and Oschkinat, H.
J. Biomol. NMR 10, 207-219 (1997)

70. Resonance assignments of the sugar chains of the recombinant human granulocyte colony-stimulating factor.
Gervais, V., Zerial, A., and Oschkinat, H.
Eur. J. Biochem. 247, 386-395 (1997)

69. NMR characterization of protein-pheophytin interactions in rhodobacter sphaeroides R26 photosynthetic reaction centers, from multispin pheophytin enrichment and 2-D MAS NMR dipolar correlation spectroscopy.
Egorova-Zachernyuk, T., van Rossum, B., Boender, G-J., Franken, E., Ashurst, J., Raap, J., Gast, P., Hoff, A., Oschkinat, H. and de Groot, H.
Biochemistry 36, 7513-7519 (1997)

68. Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from ß-Spectrin.
Nilges, M., Macias, M.J., O’Donoghue, S.I., and Oschkinat, H.
J. Mol. Biol. 269, 408-422 (1997)

67. Rab7: NMR and kinetics analysis of intact and C-terminal truncated constructs.
Neu, M., Brachvogel, V., Oschkinat, H., Zerial, M., and Metcalf, P.
Proteins 27, 204-209 (1997)

66. Constant-time HQQC experiment for protein NMR spectroscopy.
Shaw, Müller, T., Mott, H.R., Oschkinat, H., Campbell, I.D. and Mitschang, L.
J. Magn. Reson. 124, 479-483 (1997)

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65. An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residue types.
Smith, B.O., Ito, Y., Raine, A., Teichmann, S., Ben-Tovim, L., Nietlispach, D., Broadhurst, R.W., Terada, T., Kelly, M., Oschkinat, O., Shibata, T., Yokoyama, S. and Laue, E.D.
J. Biomol. NMR 8, 360-368 (1996)

64. Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide.
Macias, M.J., Hyvnen, M., Baraldi, E., Schultz, J., Sudol, M., Saraste, M., and Oschkinat, H.
Nature 382, 646-649 (1996)

63. NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies on the interaction of riboflavin synthase with trifluoromethyl-substituted intermediates.
Scheuring, J., Fischer, M., Cushmans, M., Lee, J., Bacher, A., and Oschkinat H.
Biochemistry 35, 9637-9646 (1996)

62. An approach to the structure determination of larger proteins using triple-resonance NMR experiments in conjunction with random fractional deuteration.
Nietlisbach, D., Clowes, R.T., Broadhurst, R.W., Ito, Y., Keeler, J., Kelly, M., Ashurst, J., Oschkinat, H., Domaille, P.J., and Laue, E.D.
J. Am. Chem. Soc. 118, 407-415 (1996)

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61. Structure of the binding site for inositol phosphates in a PH domain.
Hyvönen, M., Macias, M.J., Nilges, M., Oschkinat, H., Saraste, M., and Wilmanns, M.
EMBO J. 14, 4676-4685 (1995)

60. Assignment and secondary-structure determination of monomeric bovine seminal ribonuclease employing computer-assisted evaluation of homonuclear three-dimensional 1H-NMR spectra.
D'Ursi, A., Oschkinat, H., Cieslar, C., Picone, D., D'Alessio, G., Amodeo, P., Temussi, P.A.
Eur. J. Biochem. 229, 494-502 (1995)

59. MAS NMR structure refinement of uniformly 13C enriched chlorophyll a/water aggregates with 2D dipolar correlation spectroscopy.
Boender, G.J., Raap, J., Prytulla, S., Oschkinat, H., and de Groot, H.J.M.
Chem. Phys. Lett. 237, 502-508 (1995)

58. Geometrical representation of coherence transfer selection by pulsed field gradients in high-resolution nuclear magnetic resonance.
Mitschang, L., Ponstingl, H., Grindrod D., and Oschkinat, H.
J. Chem. Phys. 102, 3089-3098 (1995)

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57. Antagonist design through forced electrostatic mismatch.
Müller, T., Sebald W., and Oschkinat, H.
Nat. Stuc. Biol. 1, 674-676 (1994)

56. Structure of the pleckstrin homology domain from b-spectrin.
Macias-Hernandez, M., Musacchio, A., Ponstingl, H., Nilges, M., Saraste, M., and Oschkinat, H.
Nature 369, 675-677 (1994)

55. Receptor binding properties of four-helix-bundle growth factors deduced from electrostatic analysis.
Demchuk, E., Müller, T., Oschkinat, H., Sebald, W., and Wade, R.C.
Protein Science 3, 920-935 (1994)

54. Aspects of receptor binding and signalling of interleukin-4 investigated by site-directed mutagenesis and NMR spectroscopy.
Müller, T., Dieckmann, T., Sebald, W., and Oschkinat, H.
J. Mol. Biol. 237, 423-436 (1994)

53. Automated assignment of multidimensional nuclear magnetic resonance spectra.
Oschkinat, H., and Croft, D.
Meth. Enzymol. 239, (1994)

52b. Proteinstrukturaufklärung mit drei- und vierdimensionaler NMR-Spektroskopie.
Oschkinat, H., Müller, T., and Dieckmann, T.
Angewandte Chemie 33, 277-293 (1994)

52a. Protein structure determination with three- and four-dimensional NMR spectroscopy.
Oschkinat, H., Müller, T., and Dieckmann, T.
Angewandte Chemie 33, 277-293 (1994)

51. 19F NMR studies on the mechanism of riboflavin synthase.
Scheuring, J., Cushman, M., Oschkinat, H., and Bacher, A.
Flavins and Flavoproteins 1993, K. Yagi (Editor), W. deGryuter, Berlin/New York, 79-82 (1994)

50. 19F NMR studies on lumazine protein from photobacterium phosphoreum.
Scheuring, J., Lee, J., Cushman, M., Oschkinat, H., and Bacher, A.
Flavins and Flavoproteins 1993, K. Yagi (Editor), W. deGryuter, Berlin/New York, 75-78 (1994)

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49. Conformational variability of chicken cystatin: comparison of structures determined by X-ray diffraction and NMR spectroscopy.
Engh, R.A., Dieckmann, T., Bode, W., Auerswald, E., Turk, V., Huber, R., and Oschkinat, H.
Mol. Biol. 234, 1060-1069 (1993)

48. Structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution.
Dieckmann, T., Mitschang, L., Hofmann, M., Kos, J., Turk, V., Auerswald, E., Jaenicke, R., and Oschkinat, H. Mol. Biol. 234, 1048-1059 (1993)

47. Computer-assisted assignment of multidimensional NMR spectra of proteins: application to 3D NOESY-HMQC and TOCSY-HMQC spectra.
Bernstein, R., Cieslar, C., Ross, A., Oschkinat, H., Freund, J., and Holak, T.A.
J. Biomol. NMR 3, 245-251 (1993)

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46. Removal of zero-quantum interference in NOESY spectra of proteins by utilizing the natural inhomogeneity of the radiofrequency field.
Mitschang, L., Keeler, J., Davis, A.L., and Oschkinat, H.
J. Biomol. NMR 2, 545-556 (1992)

45. Two-dimensional nuclear magnetic resonance studies of an intercalation complex between the novel semisynthetic anthracycline 3'-deamino-3'-(2-methoxy-4-morpholinyl)-doxorubicin and the hexanucleotide duplex d(CGTACG).
Odefey, C., Westendorf, J., Dieckmann, T., and Oschkinat, H.
Chem.-Biol. Interactions 85, 117-126 (1992)

44. Evidence for tyrosine-linked glycosaminoglycan in a bacterial surface protein.
Peters, J., Rudolf, S., Oschkinat, H., Mengele, R., Sumper, M., Kellermann, J., Lottspeich, F., and Baumeister, W.
Biol. Chem. 373, 171-176 (1992)

43. The interaction of thrombin with fibrinogen. A structural basis for its specificity.
Stubbs, M.T., Oschkinat, H., Mayr, I., Huber, R., Angliker, H., Stone, S.R., and Bode, W.
Eur. J. Biochem. 206, 187-195 (1992)

42. Conformation of 6,7-dimethyl-8-ribityllumazine bound to ß-subunits of heavy riboflavin synthase. Transferred nuclear Overhauser effect (TrNOE) studies employing 1-13C-filtered NOESY including a novel technique for zero quantum suppression.
Oschkinat, H., Schott, K., and Bacher, A.
J. of Biomolecular NMR, 2, 19-32 (1992)

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41. Homonuclear three-dimesional NOE-NOE nuclear magnetic resonance spectroscopy of proteins in water.
Ross, A., Freund, J., Cieslar, C., Oschkinat, H., Schleicher, M., and Horak, T. A.
J. Magn. Reson. 95, 567-573 (1991)

40. Purification and characterization of a chicken egg ehite cystatin variant expressed in an escherichia coli pINIII ompA - system.
Auerswald, E. A., Genenger, G., Mentele, R., Lenzen, S., Assfalg-Machleidt, I., Mitschang, L., Oschkinat, H., and Fritz, H.
Eur. J. of Biochemistry 200, 131-138 (1991)

39. Structures of proteins in solution derived from homonuclear three-dimensional NOE-NOE nuclear magnetic resonance spectroscopy. High resolution structure of squash trypsin inhibitor.
Holak, T., Habazettl A.J., Oschkinat, H., and Otlewski, J.
J. Am. Chem. Soc. 113, 3196-3198 (1991)

38. NMR structures of proteins using stereospecific assignments and relaxation matrix refinement in a hybrid method of distance geometry and simulated annealing protocol.
Habazettl, J., Nilges, M., Oschkinat, H., Brünger, A. T., & Holak, T. A.
In: "Computational Aspects of the Study of Biological Macromolecules" Ed. J. H. Hoch, Plenum (1991)

37. Application of the Karhunen-Loéve Transformation (KLT) to the suppression of undesired resonances in 3D-NMR.
Mitschang, L., Cieslar, C., Holak, T.A., and Oschkinat, H.
J. Magn. Reson. 92, 208-217 (1991)

36. Assignment of protein NMR spectra in the light of homonuclear 3D-spectroscopy. An automatable procedure based on 3D-TOCSY-TOCSY and 3D-TOCSY-NOESY.
Oschkinat, H., Holak, T. A., and Cieslar, C.
Biopolymers 31, 699-712 (1991)

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35. 3D- 15N-1H NOESY-HMQC in water without presaturation: jump twice, return later.
Oschkinat, H., Cieslar, C., Mitschang, L., Ross, A., Holak, T.A., Auerwald, E.A.
Bruker Report 2, 1-4 (1990) 34. 3D heteronuclear NMR techniques for carbon-13 in natural abundance.
Kessler, H., Schmieder, P., and Oschkinat, H.
J. Am. Chem. Soc. 112, 8599-8600 (1990)

33. 1H NMR assignments of sidechain conformations in proteins using a high-dimensional potential in the simulated annealing calculations.
Habazettl, J., Cieslar, C., Oschkinat, H., and Holak, T. A.
FEBS Lett. 268, 141-145 (1990)

32. The solution conformation of thymosin b4: A nuclear magnetic resonance and simulated annealing study.
Zarbock, J., Oschkinat, H., Hannapel, E. Kalbacher, H., Voelter, W., and Holak, T. A.
Biochemistry 29, 7814-7821 (1990)

31. 3D-TOCSY-TOCSY processed using Linear prediction is a potential technique for automated assignment.
Cieslar, C., Holak, T. A. and Oschkinat, H.
J. Magn. Reson. 89, 184-190 (1990)

30. Fast heteronuclear 3D-spectroscopy.
Schmieder, P., Kessler, H. and Oschkinat, H.
Angew. Chem. Int. Ed. Engl. 29, 546-548 (1990)

29. A program for the evaluation of 3D spectra applied to the sequential assignment of BPTI utilizing 3D-TOCSY-NOESY.
Cieslar, C., Holak, T.A. and Oschkinat, H.
J. Magn. Reson. 87, 400-407 (1990)

28. Recognition of secondary structure elements in 3D-TOCSY-NOESY spectra of proteins.
Oschkinat, H., Cieslar, C. and Griesinger, C.
J. Magn. Reson. 86, 453-469 (1990)

27. Detection of metabolites in body fluids and biological tissue by a 1D soft COSY technique.
Stryjewski, D., Oschkinat, H. and Leibfritz, D.
Magn. Reson. Med. 13, 158-161 (1990)

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26. A specific metabolite editing technique in H1-NMR spectra by a soft COSY-technique in body fluids and tissue.
Stryjewski, D., Oschkinat, H., Leibfritz, D.
In: "Magnetic Resonance Spectroscopy of Biofluids", ed. de Certaines, J. J., World Scientific Publishing, Singapore.

25. The cysteine proteinase inhibitor chicken cystatin is a phosphoprotein II: NMR-investigations.
Hofmann, M., Oschkinat, H.
In: Proteinases and Their Inhibitors: Recent Developments KFA Jülich, (Eds. Auerswald, H., Fritz, E., Turk, V.)

24. Practical and theoretical aspects of three-dimensional HOHAHA-NOESY spectroscopy of proteins.
Oschkinat, H., Cieslar, C., Holak, T. A., Gronenborn A. M. and Clore, G. M.
J. Magn. Reson. 83, 450-472 (1989)

23. Improved strategies for the determination of protein structures from NMR data: the solution structure from acyl carrier protein.
Holak, T.A., Nilges, M. and Oschkinat, H.
FEBS Lett. 242, 218-224 (1989)

22. Application of the soft NOESY technique to the measurement of individual transition probabilities.
Oschkinat, H. and Bermel, W.
J. Magn. Reson. 81, 220-225 (1989)

21. Three-dimensional homonuclear Hartmann Hahn- Nuclear Overhauser enhancement spectroscopy: A powerful three-dimensional NMR technique for applications to proteins.
Oschkinat, H., Cieslar, C., Gronenborn, A. M. and Clore, G. M.
J. Magn. Reson. 81, 212-216 (1989)

20. Longitudinal relaxation pathways in scalar coupled systems.
Oschkinat, H., Limat, D., Emsley, L. and Bodenhausen, G.
J. Magn. Reson 81, 13-42 (1989)

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19. A two-dimensional nuclear Overhauser enhancement experiment using semiselective soft pulses, and its applications to proteins.
Oschkinat, H.G., Clore, M. and Gronenborn, A. M.
J. Magn. Reson. 78, 371-375 (1988)

18. Three-dimensional NMR-spectroscopy of a protein in solution.
Oschkinat, H., Griesinger, C., Kraulis, P. J., SÀrensen, O. W., Ernst, R. R., Gronenborn, A. M., and Clore, G.M.
Nature 332, 374-376 (1988)

17. Refinement of the solution structure of the DNA dodecamer 5'd(CGCGPATTCGCG)2 containing a stable purine-thymine base pair: combined use of nuclear magnetic resonance and restrained molecular dynamics.
Clore, G. M., Oschkinat, H., McLaughlin, L. W., Benseler, F., Scalfi-Happ, C., Happ, E. and Gronenborn, A. M.
Biochemistry 27, 4185-4197 (1988)

16. 2D-NMR spectroscopy of peptides.
Kessler, H., Oschkinat, H., and Loosli, H.R. in "2D-NMR-Spectroscopy"
Carlsson, R.M., Croasmon, W.R. (Eds.) VCH-Publ. Deerfield Beech, FL USA, Chap. 4 (1988)

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15. Application of the z-COSY technique with a modified pulse sequence to measurement of coupling constants in macromolecules.
Oschkinat, H., Clore, G. M., Nilges, M. and Gronenborn, A. M. J. Magn. Reson. 75, 534-539 (1987)

14. Multiplet effects in double quantum spectra.
Oschkinat, H. and Bodenhausen, G.
J. Magn. Reson. 73, 565-567 (1987)

13. z-filtered double-quantum NMR spectra and automated analysis by pattern recognition.
Novic, M., Oschkinat, H., Pfändler, P. and Bodenhausen, G.
J. Magn. Reson. 73, 493-511 (1987).

12. Determination of relaxation pathways in coupled spins systems by two-dimensional NMR exchange spectroscopy with small flip angles.
Oschkinat, H., Pastore, A. and Bodenhausen, G.
Am. Chem. Soc. 109, 4110-4111 (1987)

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11. Two-dimensional correlation of directly and remotely connected transitions by z-filtered COSY.
Oschkinat, H., Pastore, A., Pfändler, P. and Bodenhausen, G.
J. Magn. Reson. 69, 559-566 (1986)

10. Transformations of homonuclear two-dimensional-NMR techniques into one-dimensional using gaussian pulses.
Kessler, H., Oschkinat, H., Griesinger, C. and Bermel, W.
J. Magn. Reson. 70, 106-133 (1986)

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9. Die Struktur des Flechten-Makrolids (+)-Aspicillin
Quinkert, G., Heim, N., Bats, J. W., Oschkinat, H. and Kessler, H.
Angew. Chem. 97, 985-986 (1985)

8. Differences and sums of traces within COSY-spectra (DISCO) for the extraction of coupling constants.
Kessler, H., Müller, A. and Oschkinat, H.
Magn. Reson. Chem. 23, 844-852 (1985)

7. Simplification of spectra for the determination of coupling constants from COSY-spectra.
Kessler, H. and Oschkinat, H.
Angew. Chem. Int. Ed. 24, 690-692 (1985)

6. The conformation of cyclosporin in the crystal and in solution.
Loosli, H. R., Kessler, H., Oschkinat, H., Weber, H. P., Petcher, J. and Widmer, A.
Helv. Chim. Acta 68, 682-704 (1985)

5. Assignment of the 1H-, 13C-, and 15N-NMR spectra of cyclosporin A in CDCl3 and C6D6 by a combination of homo- and heteronuclear two dimensional techniques.
Kessler, H., Loosli, H. R. and Oschkinat, H.
Helv. Chim. Acta 68, 661-681 (1985)

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4. Investigation of peptides by two-dimensional NMR-spectroscopy.
Kessler, H., Loosli, H. R. and Oschkinat, H.
In: "Proceedings of the 18th European Peptide Symposium", U. Ragnarsson (Ed.), Almquist and Wiksell International, Stockholm, Schweden, p. 65-79 (1984)

3. Fine structure in two-dimensional NMR correlation spectroscopy.
Oschkinat, H. and Freeman, R.
J. Magn. Reson. 60, 164-169 (1984)

2. Anwendung der hochaufgelösten Festkörper-NMR-Spektroskopie zur Bestimmung der Ring-Ketten-Tautomerie.
Kessler, H., Oschkinat, H., Zimmermann, G., Möhrle, H., Bieghold, M., Arz W. and Förster, H.
Chem. Ber. 117, 702-709 (1984)

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1. Double-quantum-filtering in 2DJ-spectra.
Kessler, H., Oschkinat, H., Sørensen, O., Kogler, H. and Ernst, R. R.
J. Magn. Reson. 42, 329 (1983)

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