| Year |
Citation |
Score |
| 2024 |
Bell D, Lindemann F, Gerland L, Aucharova H, Klein A, Friedrich D, Hiller M, Grohe K, van Rossum B, Diehl A, Hughes J, Mueller LJ, Linser R, Miller AF, Oschkinat H. Sedimentation of large, soluble proteins up to 140 kDa for 1H-detected MAS NMR and 13C DNP NMR - practical aspects. Research Square. PMID 38464080 DOI: 10.21203/rs.3.rs-3972885/v1 |
0.348 |
|
| 2021 |
Busi B, Yarava JR, Bertarello A, Freymond F, Adamski W, Maurin D, Hiller M, Oschkinat H, Blackledge M, Emsley L. Similarities and Differences among Protein Dynamics Studied by Variable Temperature Nuclear Magnetic Resonance Relaxation. The Journal of Physical Chemistry. B. PMID 33635078 DOI: 10.1021/acs.jpcb.0c10188 |
0.468 |
|
| 2020 |
Dias D'Andréa É, Roske Y, de Oliveira GAP, Cremer N, Diehl A, Schmieder P, Heinemann U, Oschkinat H, Ricardo Pires J. Crystal structure of Q4D6Q6, a conserved kinetoplastid-specific protein from Trypanosoma cruzi. Journal of Structural Biology. 107536. PMID 32473201 DOI: 10.1016/J.Jsb.2020.107536 |
0.323 |
|
| 2020 |
Chow WY, Norman BP, Roberts NB, Ranganath LR, Teutloff C, Bittl R, Duer MJ, Gallagher JA, Oschkinat H. Pigmentation chemistry and radical-based collagen degradation in alkaptonuria and osteoarthritic cartilage. Angewandte Chemie (International Ed. in English). PMID 32219972 DOI: 10.1002/Anie.202000618 |
0.705 |
|
| 2020 |
Friedrich D, Perodeau J, Nieuwkoop AJ, Oschkinat H. MAS NMR detection of hydrogen bonds for protein secondary structure characterization. Journal of Biomolecular Nmr. PMID 32185644 DOI: 10.1007/S10858-020-00307-Z |
0.713 |
|
| 2020 |
Gerland LM, Friedrich D, Hopf L, Donovan E, Wallmann A, Erdmann N, Diehl A, Bommer M, Buzar K, Ibrahim M, Schmieder P, Dobbek H, Zouni A, Bondar AN, Dau H, ... Oschkinat H, et al. pH-Dependent Protonation of Surface Carboxylates in PsbO Enables Local Buffering and Triggers Structural Changes. Chembiochem : a European Journal of Chemical Biology. PMID 31930693 DOI: 10.1002/Cbic.201900739 |
0.304 |
|
| 2020 |
Friedrich D, Brünig FN, Nieuwkoop AJ, Netz RR, Hegemann P, Oschkinat H. Collective exchange processes reveal an active site proton cage in bacteriorhodopsin. Communications Biology. 3: 4. PMID 31925324 DOI: 10.1038/s42003-019-0733-7 |
0.688 |
|
| 2020 |
Chow WY, Norman BP, Roberts NB, Ranganath LR, Teutloff C, Bittl R, Duer MJ, Gallagher JA, Oschkinat H. Innentitelbild: Pigmentierungschemie und radikalbasierter Kollagenabbau bei Alkaptonurie und Arthrose (Angew. Chem. 29/2020) Angewandte Chemie. 132: 11770-11770. DOI: 10.1002/Ange.202005824 |
0.554 |
|
| 2019 |
Goldberga I, Li R, Chow WY, Reid DG, Bashtanova U, Rajan R, Puszkarska A, Oschkinat H, Duer MJ. Detection of nucleic acids and other low abundance components in native bone and osteosarcoma extracellular matrix by isotope enrichment and DNP-enhanced NMR. Rsc Advances. 9: 26686-26690. PMID 35528564 DOI: 10.1039/c9ra03198g |
0.701 |
|
| 2019 |
Hoffmann J, Ruta J, Shi C, Hendriks K, Chevelkov V, Franks WT, Oschkinat H, Giller K, Becker S, Lange A. Protein resonance assignment by BSH-CP based 3D solid-state NMR experiments: A practical guide. Magnetic Resonance in Chemistry : Mrc. PMID 31691361 DOI: 10.1002/Mrc.4945 |
0.73 |
|
| 2019 |
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, ... ... Oschkinat H, et al. Poly(ADP-Ribose) Links the DNA Damage Response and Biomineralization. Cell Reports. 27: 3124-3138.e13. PMID 31189100 DOI: 10.1016/J.Celrep.2019.05.038 |
0.688 |
|
| 2019 |
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, et al. Dynamic Nuclear Polarization Magic Angle Spinning NMR Combined with MD Simulations Permits Detection of Order and Disorder in Viral Assemblies. The Journal of Physical Chemistry. B. PMID 31125232 DOI: 10.1021/Acs.Jpcb.9B02293 |
0.582 |
|
| 2019 |
Goldberga I, Li R, Chow WY, Reid DG, Bashtanova U, Rajan R, Puszkarska A, Oschkinat H, Duer MJ. Detection of nucleic acids and other low abundance components in native bone and osteosarcoma extracellular matrix by isotope enrichment and DNP-enhanced NMR Rsc Advances. 9: 26686-26690. DOI: 10.1039/C9Ra03198G |
0.712 |
|
| 2018 |
Chow WY, Li R, Goldberga I, Reid DG, Rajan R, Clark J, Oschkinat H, Duer MJ, Hayward R, Shanahan CM. Essential but sparse collagen hydroxylysyl post-translational modifications detected by DNP NMR. Chemical Communications (Cambridge, England). PMID 30299444 DOI: 10.1039/C8Cc04960B |
0.741 |
|
| 2018 |
Jaudzems K, Polenova T, Pintacuda G, Oschkinat H, Lesage A. DNP NMR of biomolecular assemblies. Journal of Structural Biology. PMID 30273657 DOI: 10.1016/J.Jsb.2018.09.011 |
0.427 |
|
| 2018 |
de Freitas MS, Rezaei Araghi R, Brandenburg E, Leiterer J, Emmerling F, Folmert K, Gerling-Driessen UIM, Bardiaux B, Böttcher C, Pagel K, Diehl A, Berlepsch HV, Oschkinat H, Koksch B. The protofilament architecture of a de novo designed coiled coil-based amyloidogenic peptide. Journal of Structural Biology. PMID 29857134 DOI: 10.1016/J.Jsb.2018.05.009 |
0.32 |
|
| 2018 |
Stöppler 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, ... ... Oschkinat H, et al. Insight into small molecule binding to the neonatal Fc receptor by X-ray crystallography and 100 kHz magic-angle-spinning NMR. Plos Biology. 16: e2006192. PMID 29782488 DOI: 10.1371/Journal.Pbio.2006192 |
0.566 |
|
| 2018 |
Geiger M, Jagtap A, Kaushik M, Sun H, Stöppler D, Sigurdsson S, Corzilius B, Oschkinat H. 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 (Weinheim An Der Bergstrasse, Germany). PMID 29741214 DOI: 10.1002/Chem.201801251 |
0.364 |
|
| 2018 |
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, ... ... Oschkinat H, et al. Structural changes of TasA in biofilm formation of. Proceedings of the National Academy of Sciences of the United States of America. PMID 29531041 DOI: 10.1073/Pnas.1718102115 |
0.708 |
|
| 2018 |
Wallmann A, Oschkinat H. Backbone assignment of Rip2Card Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27555 |
0.344 |
|
| 2018 |
Norman B, Ying CW, Sutherland H, Wilson P, Roberts N, Duer M, Oschkinat H, Ranganath L, Gallagher J. Disruption of collagen triple helix hydrogen bonding in ochronotic human cartilage in alkaptonuria observed by dynamic nuclear polarisation-enhanced solid-state nuclear magnetic resonance spectroscopy Osteoarthritis and Cartilage. 26: S99. DOI: 10.1016/J.Joca.2018.02.214 |
0.613 |
|
| 2017 |
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, ... ... Oschkinat H, et al. Structure of outer membrane protein G in lipid bilayers. Nature Communications. 8: 2073. PMID 29233991 DOI: 10.1038/S41467-017-02228-2 |
0.753 |
|
| 2017 |
Erlendsson S, Gotfryd K, Larsen FH, Mortensen JS, Geiger MA, van Rossum BJ, Oschkinat H, Gether U, Teilum K, Loland CJ. Direct assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMR. Elife. 6. PMID 28117663 DOI: 10.7554/Elife.19314 |
0.306 |
|
| 2017 |
Retel J, Nieuwkoop A, Hiller M, Higman V, Barbet-Massin E, Stanek J, Andreas L, Franks W, vRB-,, Vinothkumar K, Handel L, Palma Gd, Bardiaux B, Pintacuda G, Emsley L, ... ... Oschkinat H, et al. Solid-state NMR Structure of outer membrane protein G in lipid bilayers Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr34088 |
0.738 |
|
| 2016 |
de Oliveira GA, Marques MA, Cruzeiro-Silva C, Cordeiro Y, Schuabb C, Moraes AH, Winter R, Oschkinat H, Foguel D, Freitas MS, Silva JL. Structural basis for the dissociation of α-synuclein fibrils triggered by pressure perturbation of the hydrophobic core. Scientific Reports. 6: 37990. PMID 27901101 DOI: 10.1038/Srep37990 |
0.302 |
|
| 2016 |
Stöppler D, Song C, van Rossum BJ, Geiger MA, Lang C, Mroginski MA, Pandurang Jagtap A, Sigurdsson ST, Matysik J, Hughes J, Oschkinat H. Dynamic Nuclear Polarization Provides New Insights into Chromophore Structure in Phytochrome Photoreceptors. Angewandte Chemie (International Ed. in English). PMID 27879035 DOI: 10.1002/Anie.201608119 |
0.428 |
|
| 2016 |
Geiger MA, Orwick-Rydmark M, Märker K, Franks WT, Akhmetzyanov D, Stöppler D, Zinke M, Specker E, Nazaré M, Diehl A, van Rossum BJ, Aussenac F, Prisner T, Akbey Ü, Oschkinat H. Temperature dependence of cross-effect dynamic nuclear polarization in rotating solids: advantages of elevated temperatures. Physical Chemistry Chemical Physics : Pccp. PMID 27791210 DOI: 10.1039/C6Cp06154K |
0.81 |
|
| 2016 |
Lange S, Franks WT, Rajagopalan N, Döring K, Geiger MA, Linden A, van Rossum BJ, Kramer G, Bukau B, Oschkinat H. Structural analysis of a signal peptide inside the ribosome tunnel by DNP MAS NMR. Science Advances. 2: e1600379. PMID 27551685 DOI: 10.1126/Sciadv.1600379 |
0.705 |
|
| 2016 |
Bretschneider CO, Akbey Ü, Aussenac F, Olsen GL, Feintuch A, Oschkinat H, Frydman L. On The Potential of Dynamic Nuclear Polarization Enhanced Diamonds in Solid-State and Dissolution (13) C NMR Spectroscopy. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 27416769 DOI: 10.1002/Cphc.201600301 |
0.742 |
|
| 2016 |
D'Andréa ÉD, Diehl A, Schmieder P, Oschkinat H, Pires JR. Chemical shift assignments and secondary structure prediction for Q4DY78, a conserved kinetoplastid-specific protein from Trypanosoma cruzi. Biomolecular Nmr Assignments. PMID 27356988 DOI: 10.1007/S12104-016-9693-8 |
0.35 |
|
| 2016 |
Jagtap AP, Geiger MA, Stöppler D, Orwick-Rydmark M, Oschkinat H, Sigurdsson ST. : a highly water-soluble biradical for efficient dynamic nuclear polarization of biomolecules. Chemical Communications (Cambridge, England). PMID 27161650 DOI: 10.1039/C6Cc01813K |
0.377 |
|
| 2016 |
Nagaraj M, Franks TW, Saeidpour S, Schubeis T, Oschkinat H, Ritter C, Van Rossum BJ. Surface binding of TOTAPOL assists structural investigations of amyloid fibrils by dynamic nuclear polarization NMR. Chembiochem : a European Journal of Chemical Biology. PMID 27147408 DOI: 10.1002/Cbic.201600185 |
0.411 |
|
| 2016 |
Akbey Ü, Oschkinat H. Structural biology applications of solid state MAS DNP NMR. Journal of Magnetic Resonance (San Diego, Calif. : 1997). PMID 27095695 DOI: 10.1016/J.Jmr.2016.04.003 |
0.751 |
|
| 2016 |
Bretschneider CO, Akbey Ü, Aussenac F, Olsen GL, Feintuch A, Oschkinat H, Frydman L. Cover Picture: On The Potential of Dynamic Nuclear Polarization Enhanced Diamonds in Solid-State and Dissolution 13C NMR Spectroscopy (ChemPhysChem 17/2016) Chemphyschem. 17: 2609. DOI: 10.1002/Cphc.201600878 |
0.411 |
|
| 2015 |
Gupta R, Lu M, Hou G, Caporini MA, Rosay M, Maas WE, Struppe JO, Suiter CL, Ahn J, Byeon IL, Franks WT, Orwick-Rydmark M, Bertarello A, Oschkinat H, Lesage A, et al. Dynamic Nuclear Polarization Enhanced MAS NMR for Structural Analysis of HIV-1 Protein Assemblies. The Journal of Physical Chemistry. B. PMID 26709853 DOI: 10.1021/Acs.Jpcb.5B12134 |
0.693 |
|
| 2015 |
Geiger Y, Gottlieb HE, Akbey Ü, Oschkinat H, Goobes G. Studying the Conformation of a Silaffin-Derived Pentalysine Peptide Embedded in Bioinspired Silica using Solution and DNP MAS NMR. Journal of the American Chemical Society. PMID 26451953 DOI: 10.1021/Jacs.5B07809 |
0.703 |
|
| 2015 |
Mentink-Vigier F, Akbey Ü, Oschkinat H, Vega S, Feintuch A. Theoretical aspects of Magic Angle Spinning - Dynamic Nuclear Polarization. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 258: 102-20. PMID 26232770 DOI: 10.1016/J.Jmr.2015.07.001 |
0.723 |
|
| 2015 |
Nieuwkoop AJ, Franks WT, Rehbein K, Diehl A, Akbey Ü, Engelke F, Emsley L, Pintacuda G, Oschkinat H. Sensitivity and resolution of proton detected spectra of a deuterated protein at 40 and 60 kHz magic-angle-spinning. Journal of Biomolecular Nmr. 61: 161-71. PMID 25663049 DOI: 10.1007/S10858-015-9904-0 |
0.805 |
|
| 2014 |
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, ... ... Oschkinat H, et al. Rapid proton-detected NMR assignment for proteins with fast magic angle spinning. Journal of the American Chemical Society. 136: 12489-97. PMID 25102442 DOI: 10.1021/Ja507382J |
0.824 |
|
| 2014 |
Akbey Ü, Nieuwkoop AJ, Wegner S, Voreck A, Kunert B, Bandara P, Engelke F, Nielsen NC, Oschkinat H. Quadruple-resonance magic-angle spinning NMR spectroscopy of deuterated solid proteins. Angewandte Chemie (International Ed. in English). 53: 2438-42. PMID 24474388 DOI: 10.1002/Anie.201308927 |
0.823 |
|
| 2014 |
Jain SK, Nielsen AB, Hiller M, Handel L, Ernst M, Oschkinat H, Akbey Ü, Nielsen NC. Low-power polarization transfer between deuterons and spin-1/2 nuclei using adiabatic (RESPIRATION)CP in solid-state NMR. Physical Chemistry Chemical Physics : Pccp. 16: 2827-30. PMID 24418905 DOI: 10.1039/C3Cp54419B |
0.432 |
|
| 2013 |
Jacso T, Bardiaux B, Broecker J, Fiedler S, Baerwinkel T, Mainz A, Fink U, Vargas C, Oschkinat H, Keller S, Reif B. The mechanism of denaturation and the unfolded state of the α-helical membrane-associated protein Mistic. Journal of the American Chemical Society. 135: 18884-91. PMID 24261476 DOI: 10.1021/Ja408644F |
0.363 |
|
| 2013 |
Akbey Ü, Altin B, Linden A, Özçelik S, Gradzielski M, Oschkinat H. Dynamic nuclear polarization of spherical nanoparticles. Physical Chemistry Chemical Physics : Pccp. 15: 20706-16. PMID 24192797 DOI: 10.1039/C3Cp53095G |
0.685 |
|
| 2013 |
Kingsley CN, Brubaker WD, Markovic S, Diehl A, Brindley AJ, Oschkinat H, Martin RW. Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin. Structure (London, England : 1993). 21: 2221-7. PMID 24183572 DOI: 10.1016/J.Str.2013.09.017 |
0.322 |
|
| 2013 |
Fiebig JE, Weidauer SE, Qiu LY, Bauer M, Schmieder P, Beerbaum M, Zhang JL, Oschkinat H, Sebald W, Mueller TD. The clip-segment of the von Willebrand domain 1 of the BMP modulator protein Crossveinless 2 is preformed. Molecules (Basel, Switzerland). 18: 11658-82. PMID 24071977 DOI: 10.3390/Molecules181011658 |
0.321 |
|
| 2013 |
Conley MP, Drost RM, Baffert M, Gajan D, Elsevier C, Franks WT, Oschkinat H, Veyre L, Zagdoun A, Rossini A, Lelli M, Lesage A, Casano G, Ouari O, Tordo P, et al. A well-defined Pd hybrid material for the Z-selective semihydrogenation of alkynes characterized at the molecular level by DNP SENS. Chemistry (Weinheim An Der Bergstrasse, Germany). 19: 12234-8. PMID 23959767 DOI: 10.1002/Chem.201302484 |
0.704 |
|
| 2013 |
Akbey U, Franks WT, Linden A, Orwick-Rydmark M, Lange S, Oschkinat H. Dynamic nuclear polarization enhanced NMR in the solid-state. Topics in Current Chemistry. 338: 181-228. PMID 23832684 DOI: 10.1007/128_2013_436 |
0.821 |
|
| 2013 |
Jayanthi S, Akbey Ü, Uluca B, Oschkinat H, Vega S. A Floquet description of phase alternated sequences for efficient homonuclear recoupling in solid perdeuterated systems. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 234: 10-20. PMID 23831836 DOI: 10.1016/J.Jmr.2013.05.007 |
0.69 |
|
| 2013 |
Barbet-Massin E, Pell AJ, Jaudzems K, Franks WT, Retel JS, Kotelovica S, Akopjana I, Tars K, Emsley L, Oschkinat H, Lesage A, Pintacuda G. Out-and-back 13C-13C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS. Journal of Biomolecular Nmr. 56: 379-86. PMID 23812971 DOI: 10.1007/S10858-013-9757-3 |
0.759 |
|
| 2013 |
Zagdoun A, Rossini AJ, Conley MP, Grüning WR, Schwarzwälder M, Lelli M, Franks WT, Oschkinat H, Copéret C, Emsley L, Lesage A. Improved dynamic nuclear polarization surface-enhanced NMR spectroscopy through controlled incorporation of deuterated functional groups. Angewandte Chemie (International Ed. in English). 52: 1222-5. PMID 23293096 DOI: 10.1002/Anie.201208699 |
0.742 |
|
| 2012 |
Mentink-Vigier F, Akbey U, Hovav Y, Vega S, Oschkinat H, Feintuch A. Fast passage dynamic nuclear polarization on rotating solids. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 224: 13-21. PMID 23000976 DOI: 10.1016/J.Jmr.2012.08.013 |
0.729 |
|
| 2012 |
Markley JL, Akutsu H, Asakura T, Baldus M, Boelens R, Bonvin A, Kaptein R, Bax A, Bezsonova I, Gryk MR, Hoch JC, Korzhnev DM, Maciejewski MW, Case D, Chazin WJ, ... ... Oschkinat H, et al. In support of the BMRB. Nature Structural & Molecular Biology. 19: 854-60. PMID 22955930 DOI: 10.1038/Nsmb.2371 |
0.378 |
|
| 2012 |
Bardiaux B, van Rossum BJ, Nilges M, Oschkinat H. Efficient modeling of symmetric protein aggregates from NMR data. Angewandte Chemie (International Ed. in English). 51: 6916-9. PMID 22653848 DOI: 10.1002/Anie.201201783 |
0.373 |
|
| 2012 |
Loening NM, van Rossum BJ, Oschkinat H. Broadband excitation pulses for high-field solid-state nuclear magnetic resonance spectroscopy. Magnetic Resonance in Chemistry : Mrc. 50: 284-8. PMID 22467565 DOI: 10.1002/Mrc.3800 |
0.345 |
|
| 2012 |
Akbey U, Rossum BJ, Oschkinat H. Practical aspects of high-sensitivity multidimensional ¹³C MAS NMR spectroscopy of perdeuterated proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 217: 77-85. PMID 22440428 DOI: 10.1016/J.Jmr.2012.02.015 |
0.745 |
|
| 2012 |
Lange S, Linden AH, Akbey U, Franks WT, Loening NM, van Rossum BJ, Oschkinat H. The effect of biradical concentration on the performance of DNP-MAS-NMR. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 216: 209-12. PMID 22285634 DOI: 10.1016/J.Jmr.2012.01.002 |
0.801 |
|
| 2012 |
Bjerring M, Paaske B, Oschkinat H, Akbey U, Nielsen NC. Rapid solid-state NMR of deuterated proteins by interleaved cross-polarization from ¹H and ²H nuclei. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 214: 324-8. PMID 22130517 DOI: 10.1016/J.Jmr.2011.10.020 |
0.74 |
|
| 2012 |
Loening NM, Bjerring M, Nielsen NC, Oschkinat H. A comparison of NCO and NCA transfer methods for biological solid-state NMR spectroscopy. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 214: 81-90. PMID 22116035 DOI: 10.1016/J.Jmr.2011.10.012 |
0.388 |
|
| 2012 |
Jacso T, Franks WT, Rose H, Fink U, Broecker J, Keller S, Oschkinat H, Reif B. Characterization of membrane proteins in isolated native cellular membranes by dynamic nuclear polarization solid-state NMR spectroscopy without purification and reconstitution. Angewandte Chemie (International Ed. in English). 51: 432-5. PMID 22113890 DOI: 10.1002/Anie.201104987 |
0.714 |
|
| 2012 |
Franks WT, Linden AH, Kunert B, van Rossum BJ, Oschkinat H. Solid-state magic-angle spinning NMR of membrane proteins and protein-ligand interactions. European Journal of Cell Biology. 91: 340-8. PMID 22019511 DOI: 10.1016/J.Ejcb.2011.09.002 |
0.719 |
|
| 2012 |
Akbey U, Linden AH, Oschkinat H. High-Temperature Dynamic Nuclear Polarization Enhanced Magic-Angle-Spinning NMR Applied Magnetic Resonance. 43: 81-90. DOI: 10.1007/S00723-012-0357-2 |
0.425 |
|
| 2012 |
Salnikov ES, Ouari O, Koers E, Sarrouj H, Franks T, Rosay M, Pawsey S, Reiter C, Bandara P, Oschkinat H, Tordo P, Engelke F, Bechinger B. Developing DNP/Solid-State NMR Spectroscopy of Oriented Membranes Applied Magnetic Resonance. 43: 91-106. DOI: 10.1007/S00723-012-0338-5 |
0.42 |
|
| 2012 |
Franks WT, van Rossum BJ, Bardiaux B, Ravera E, Parigi G, Luchinat C, Oschkinat H. Microcrystalline Proteins-An Ideal Benchmark for Methodology Development Nmr of Biomolecules: Towards Mechanistic Systems Biology. 376-392. DOI: 10.1002/9783527644506.ch22 |
0.632 |
|
| 2011 |
Wei D, Akbey Ü, Paaske B, Oschkinat H, Reif B, Bjerring M, Nielsen NC. Optimal (2)H rf Pulses and (2)H-(13)C Cross-Polarization Methods for Solid-State (2)H MAS NMR of Perdeuterated Proteins. The Journal of Physical Chemistry Letters. 2: 1289-94. PMID 26295423 DOI: 10.1021/Jz200511B |
0.714 |
|
| 2011 |
Linden AH, Lange S, Franks WT, Akbey U, Specker E, van Rossum BJ, Oschkinat H. Neurotoxin II bound to acetylcholine receptors in native membranes studied by dynamic nuclear polarization NMR. Journal of the American Chemical Society. 133: 19266-9. PMID 22039931 DOI: 10.1021/Ja206999C |
0.797 |
|
| 2011 |
Lalli D, Schanda P, Chowdhury A, Retel J, Hiller M, Higman VA, Handel L, Agarwal V, Reif B, van Rossum B, Akbey U, Oschkinat H. Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins. Journal of Biomolecular Nmr. 51: 477-85. PMID 22038621 DOI: 10.1007/S10858-011-9578-1 |
0.737 |
|
| 2011 |
Stevens TJ, Fogh RH, Boucher W, Higman VA, Eisenmenger F, Bardiaux B, van Rossum BJ, Oschkinat H, Laue ED. A software framework for analysing solid-state MAS NMR data. Journal of Biomolecular Nmr. 51: 437-47. PMID 21953355 DOI: 10.1007/S10858-011-9569-2 |
0.4 |
|
| 2011 |
Linden AH, Franks WT, Akbey Ü, Lange S, van Rossum BJ, Oschkinat H. Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR. Journal of Biomolecular Nmr. 51: 283-92. PMID 21826519 DOI: 10.1007/S10858-011-9535-Z |
0.792 |
|
| 2011 |
Akbey U, Camponeschi F, van Rossum BJ, Oschkinat H. Triple resonance cross-polarization for more sensitive 13C MAS NMR spectroscopy of deuterated proteins. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 12: 2092-6. PMID 21656893 DOI: 10.1002/Cphc.201100084 |
0.736 |
|
| 2011 |
Saupe J, Roske Y, Schillinger C, Kamdem N, Radetzki S, Diehl A, Oschkinat H, Krause G, Heinemann U, Rademann J. Discovery, structure-activity relationship studies, and crystal structure of nonpeptide inhibitors bound to the Shank3 PDZ domain. Chemmedchem. 6: 1411-22. PMID 21626699 DOI: 10.1002/Cmdc.201100094 |
0.331 |
|
| 2011 |
Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez del Amo JM, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B. Proton-detected solid-state NMR spectroscopy of fibrillar and membrane proteins. Angewandte Chemie (International Ed. in English). 50: 4508-12. PMID 21495136 DOI: 10.1002/Anie.201008244 |
0.394 |
|
| 2011 |
Jehle S, Vollmar BS, Bardiaux B, Dove KK, Rajagopal P, Gonen T, Oschkinat H, Klevit RE. N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proceedings of the National Academy of Sciences of the United States of America. 108: 6409-14. PMID 21464278 DOI: 10.1073/Pnas.1014656108 |
0.359 |
|
| 2011 |
Leskes M, Akbey U, Oschkinat H, van Rossum BJ, Vega S. Radio frequency assisted homonuclear recoupling - a Floquet description of homonuclear recoupling via surrounding heteronuclei in fully protonated to fully deuterated systems. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 209: 207-19. PMID 21316279 DOI: 10.1016/J.Jmr.2011.01.015 |
0.72 |
|
| 2011 |
Koehler C, Lighthouse J, Werther T, Andersen O, Diehl A, Schmieder P, Holdener B, Oschkinat H. NMR based model structure of mesoderm development (MESD) in solution. Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr11076 |
0.312 |
|
| 2011 |
Lewandowski JR, Dumez JN, Akbey U, Lange S, Emsley L, Oschkinat H. Enhanced resolution and coherence lifetimes in the solid-state NMR spectroscopy of perdeuterated proteins under ultrafast magic-angle spinning Journal of Physical Chemistry Letters. 2: 2205-2211. DOI: 10.1021/Jz200844N |
0.599 |
|
| 2011 |
Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez del Amo J, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B. Cover Picture: Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins (Angew. Chem. Int. Ed. 19/2011) Angewandte Chemie International Edition. 50: 4237-4237. DOI: 10.1002/Anie.201101732 |
0.394 |
|
| 2011 |
Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez del Amo J, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B. Titelbild: Festkörper-NMR-Spektroskopie mit Protonendetektion an fibrillären Proteinen und Membranproteinen (Angew. Chem. 19/2011) Angewandte Chemie. 123: 4325-4325. DOI: 10.1002/Ange.201101732 |
0.415 |
|
| 2011 |
Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez del Amo J, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B. Festkörper-NMR-Spektroskopie mit Protonendetektion an fibrillären Proteinen und Membranproteinen Angewandte Chemie. 123: 4601-4605. DOI: 10.1002/Ange.201008244 |
0.411 |
|
| 2010 |
Zaminer J, Brockmann C, Huy P, Opitz R, Reuter C, Beyermann M, Freund C, Müller M, Oschkinat H, Kühne R, Schmalz HG. 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. Angewandte Chemie (International Ed. in English). 49: 7111-5. PMID 20803590 DOI: 10.1002/Anie.201001739 |
0.3 |
|
| 2010 |
Jehle S, Rajagopal P, Bardiaux B, Markovic S, Kühne R, Stout JR, Higman VA, Klevit RE, Van Rossum BJ, Oschkinat H. Solid-state NMR and SAXS studies provide a structural basis for the activation of αb-crystallin oligomers Nature Structural and Molecular Biology. 17: 1037-1042. PMID 20802487 DOI: 10.1038/Nsmb.1891 |
0.341 |
|
| 2010 |
Akbey Ü, Franks WT, Linden A, Lange S, Griffin RG, van Rossum BJ, Oschkinat H. Dynamic nuclear polarization of deuterated proteins. Angewandte Chemie (International Ed. in English). 49: 7803-6. PMID 20726023 DOI: 10.1002/Anie.201002044 |
0.743 |
|
| 2010 |
Jehle S, Falb M, Kirkpatrick JP, Oschkinat H, Van Rossum BJ, Althoff G, Carlomagno T. Intermolecular protein-RNA interactions revealed by 2D31P- 15N magic angle spinning solid-state NMR spectroscopy Journal of the American Chemical Society. 132: 3842-3846. PMID 20184366 DOI: 10.1021/Ja909723F |
0.375 |
|
| 2010 |
Lange V, Becker-Baldus J, Kunert B, van Rossum BJ, Casagrande F, Engel A, Roske Y, Scheffel FM, Schneider E, Oschkinat H. A MAS NMR study of the bacterial ABC transporter ArtMP. Chembiochem : a European Journal of Chemical Biology. 11: 547-55. PMID 20099290 DOI: 10.1002/Cbic.200900472 |
0.385 |
|
| 2010 |
Akbey U, Lange S, Trent Franks W, Linser R, Rehbein K, Diehl A, van Rossum BJ, Reif B, Oschkinat H. Optimum levels of exchangeable protons in perdeuterated proteins for proton detection in MAS solid-state NMR spectroscopy. Journal of Biomolecular Nmr. 46: 67-73. PMID 19701607 DOI: 10.1007/S10858-009-9369-0 |
0.734 |
|
| 2010 |
Freitas MS, Oschkinat H. An Atomic View of Fibril Structure Using Solid State NMR Approaches Biophysical Journal. 98: 453a. DOI: 10.1016/J.Bpj.2009.12.2461 |
0.367 |
|
| 2010 |
Akbey Ü, Franks WT, Linden A, Lange S, Griffin RG, van Rossum B, Oschkinat H. Dynamische Kernpolarisation bei deuterierten Proteinen Angewandte Chemie. 122: 7971-7974. DOI: 10.1002/Ange.201002044 |
0.62 |
|
| 2009 |
Akbey U, Oschkinat H, van Rossum BJ. Double-nucleus enhanced recoupling for efficient 13C MAS NMR correlation spectroscopy of perdeuterated proteins. Journal of the American Chemical Society. 131: 17054-5. PMID 19929015 DOI: 10.1021/Ja907493P |
0.738 |
|
| 2009 |
Mainz A, Jehle S, van Rossum BJ, Oschkinat H, Reif B. Large protein complexes with extreme rotational correlation times investigated in solution by magic-angle-spinning NMR spectroscopy. Journal of the American Chemical Society. 131: 15968-9. PMID 19839609 DOI: 10.1021/Ja904733V |
0.397 |
|
| 2009 |
Higman VA, Flinders J, Hiller M, Jehle S, Markovic S, Fiedler S, van Rossum BJ, Oschkinat H. Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins. Journal of Biomolecular Nmr. 44: 245-60. PMID 19609683 DOI: 10.1007/S10858-009-9338-7 |
0.47 |
|
| 2009 |
Rutkowska A, Beerbaum M, Rajagopalan N, Fiaux J, Schmieder P, Kramer G, Oschkinat H, Bukau B. Large-scale purification of ribosome-nascent chain complexes for biochemical and structural studies. Febs Letters. 583: 2407-13. PMID 19560460 DOI: 10.1016/J.Febslet.2009.06.041 |
0.329 |
|
| 2009 |
Krabben L, van Rossum BJ, Jehle S, Bocharov E, Lyukmanova EN, Schulga AA, Arseniev A, Hucho F, Oschkinat H. Loop 3 of Short Neurotoxin II is an Additional Interaction Site with Membrane-bound Nicotinic Acetylcholine Receptor as Detected by Solid-state NMR Spectroscopy Journal of Molecular Biology. 390: 662-671. PMID 19447114 DOI: 10.1016/J.Jmb.2009.05.016 |
0.336 |
|
| 2009 |
Jehle S, van Rossum B, Stout JR, Noguchi SM, Falber K, Rehbein K, Oschkinat H, Klevit RE, Rajagopal P. αB-Crystallin: A Hybrid Solid-State/Solution-State NMR Investigation Reveals Structural Aspects of the Heterogeneous Oligomer Journal of Molecular Biology. 385: 1481-1497. PMID 19041879 DOI: 10.1016/J.Jmb.2008.10.097 |
0.358 |
|
| 2009 |
Jehle S, Rossum B, Markovic S, Rajagopal P, Klevit R, Oschkinat H. 13C and 15N Chemical Shift Assignments for human alphaB-crystallin Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16391 |
0.742 |
|
| 2008 |
Koehler C, Bishop S, Dowler EF, Schmieder P, Diehl A, Oschkinat H, Ball LJ. Backbone and sidechain 1H, 13C and 15N resonance assignments of the Bright/ARID domain from the human JARID1C (SMCX) protein. Biomolecular Nmr Assignments. 2: 9-11. PMID 19636912 DOI: 10.1007/S12104-007-9071-7 |
0.361 |
|
| 2008 |
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. Nature Reviews. Drug Discovery. 7: 738-45. PMID 19172689 DOI: 10.1038/Nrd2606 |
0.473 |
|
| 2008 |
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 CA150.WW2. Chembiochem : a European Journal of Chemical Biology. 9: 1946-52. PMID 18642254 DOI: 10.1002/Cbic.200700706 |
0.396 |
|
| 2008 |
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. Journal of the American Chemical Society. 130: 408-9. PMID 18092784 DOI: 10.1021/Ja077589N |
0.446 |
|
| 2008 |
König R, Scholz G, Pawlik A, Jäger C, Van Rossum B, Oschkinat H, Kemnitz E. Crystalline aluminum hydroxy fluorides: Structural insights obtained by high field solid state NMR and trend analyses Journal of Physical Chemistry C. 112: 15708-15720. DOI: 10.1021/Jp804662F |
0.353 |
|
| 2007 |
Dowler EF, Diehl A, Schmieder P, Brockmann C, Elkins J, Soundararajan M, Oschkinat H, Ball LJ. Backbone and sidechain 1H, 13C and 15N resonance assignments of the RGS domain from human RGS14. Biomolecular Nmr Assignments. 1: 95-7. PMID 19636837 DOI: 10.1007/S12104-007-9029-9 |
0.361 |
|
| 2007 |
Scholz I, Jehle S, Schmieder P, Hiller M, Eisenmenger F, Oschkinat H, van Rossum BJ. J-deconvolution using maximum entropy reconstruction applied to 13C-13C solid-state cross-polarization magic-angle-spinning NMR of proteins. Journal of the American Chemical Society. 129: 6682-3. PMID 17488078 DOI: 10.1021/Ja070849G |
0.441 |
|
| 2007 |
Balayssac S, Bertini I, Fälber 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 : a European Journal of Chemical Biology. 8: 486-9. PMID 17300109 DOI: 10.1002/Cbic.200600408 |
0.344 |
|
| 2007 |
Fedorov OY, Higman VA, Schmieder P, Leidert M, Diehl A, Elkins J, Soundararajan M, Oschkinat H, Ball LJ. Resonance assignment of the RGS domain of human RGS10. Journal of Biomolecular Nmr. 38: 191. PMID 17180548 DOI: 10.1007/S10858-006-9111-0 |
0.355 |
|
| 2006 |
Köhler 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. Journal of Structural and Functional Genomics. 7: 131-8. PMID 17342452 DOI: 10.1007/S10969-007-9016-5 |
0.333 |
|
| 2006 |
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. Proceedings of the National Academy of Sciences of the United States of America. 103: 16248-53. PMID 17060612 DOI: 10.1073/Pnas.0607815103 |
0.33 |
|
| 2006 |
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. Journal of Biomolecular Nmr. 36: 169-77. PMID 17031530 DOI: 10.1007/S10858-006-9078-X |
0.385 |
|
| 2006 |
Higman VA, Leidert M, Diehl A, Elkins J, Soundararajan M, Oschkinat H, Ball LJ. NMR assignment of human RGS18. Journal of Biomolecular Nmr. 36: 72. PMID 16964532 DOI: 10.1007/S10858-006-9061-6 |
0.347 |
|
| 2006 |
Aido-Machado Rd, Salmon D, Diehl A, Leidert M, Schmetzer O, de Lima AP, Scharfstein J, Oschkinat H, Pires JR. 1H, 15N and 13C assignments of the cysteine protease inhibitor chagasin from Trypanosoma cruzi. Journal of Biomolecular Nmr. 36: 30. PMID 16680406 DOI: 10.1007/S10858-006-0014-X |
0.313 |
|
| 2006 |
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 Expression and Purification. 48: 253-60. PMID 16584890 DOI: 10.1016/J.Pep.2006.01.022 |
0.317 |
|
| 2006 |
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. Journal of Molecular Biology. 357: 1511-21. PMID 16490204 DOI: 10.1016/J.Jmb.2006.01.064 |
0.311 |
|
| 2006 |
Higman V, Leidert M, Elkins J, Soundararajan M, Brockmann C, Schmieder P, Sundstrom M, Arrowsmith C, Weigelt J, Edwards A, Diehl A, Oschkinat H, Ball L. NMR Assignment of human RGS18 (regulator of G-protein signalling) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr7106 |
0.332 |
|
| 2005 |
Adam P, Gütlich 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 Biochemistry. 6: 24. PMID 16285881 DOI: 10.1186/1471-2091-6-24 |
0.303 |
|
| 2005 |
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. Angewandte Chemie (International Ed. in English). 44: 6151-4. PMID 16175529 DOI: 10.1002/Anie.200501884 |
0.414 |
|
| 2005 |
Hiller M, Krabben L, Vinothkumar KR, Castellani F, van Rossum BJ, Kühlbrandt W, Oschkinat H. Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli. Chembiochem : a European Journal of Chemical Biology. 6: 1679-84. PMID 16138308 DOI: 10.1002/Cbic.200500132 |
0.455 |
|
| 2005 |
Tremmel S, Beyermann M, Oschkinat H, Bienert M, Naumann D, Fabian H. 13C-labeled tyrosine residues as local IR probes for monitoring conformational changes in peptides and proteins. Angewandte Chemie (International Ed. in English). 44: 4631-5. PMID 15977271 DOI: 10.1002/Anie.200500547 |
0.328 |
|
| 2005 |
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 Letters. 579: 3534-8. PMID 15961083 DOI: 10.1016/J.Febslet.2005.05.025 |
0.315 |
|
| 2005 |
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. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 175: 92-102. PMID 15949752 DOI: 10.1016/J.Jmr.2005.03.020 |
0.397 |
|
| 2005 |
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. Journal of Biomolecular Nmr. 31: 295-310. PMID 15928996 DOI: 10.1007/S10858-005-1718-Z |
0.432 |
|
| 2005 |
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. Journal of Biomolecular Nmr. 31: 115-28. PMID 15772751 DOI: 10.1007/S10858-004-8263-Z |
0.647 |
|
| 2005 |
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. Journal of Biomolecular Nmr. 31: 21-34. PMID 15692736 DOI: 10.1007/S10858-004-5359-4 |
0.38 |
|
| 2004 |
Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kühne R, Oschkinat H, Heinemann U. Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1. Biochemistry. 43: 15983-95. PMID 15609993 DOI: 10.1021/Bi049550Q |
0.36 |
|
| 2004 |
Zimmermann J, Jarchau T, Walter U, Oschkinat H, Ball LJ. 1H, 13C and 15N resonance assignment of the human Spred2 EVH1 domain. Journal of Biomolecular Nmr. 29: 435-6. PMID 15213456 DOI: 10.1023/B:Jnmr.0000032526.17586.8C |
0.347 |
|
| 2004 |
Krabben L, Van Rossum BJ, Castellani F, Bocharov E, Schulga AA, Arseniev AS, Weise C, Hucho F, Oschkinat H. Towards structure determination of neurotoxin II bound to nicotinic acetylcholine receptor: A solid-state NMR approach Febs Letters. 564: 319-324. PMID 15111116 DOI: 10.1016/S0014-5793(04)00252-2 |
0.4 |
|
| 2003 |
Castellani F, van Rossum BJ, Diehl A, Rehbein K, Oschkinat H. Determination of solid-state NMR structures of proteins by means of three-dimensional 15N-13C-13C dipolar correlation spectroscopy and chemical shift analysis. Biochemistry. 42: 11476-83. PMID 14516199 DOI: 10.1021/Bi034903R |
0.377 |
|
| 2003 |
Zimmermann J, Kühne R, Volkmer-Engert R, Jarchau T, Walter U, Oschkinat H, Ball LJ. Design of N-substituted peptomer ligands for EVH1 domains. The Journal of Biological Chemistry. 278: 36810-8. PMID 12857736 DOI: 10.1074/Jbc.M305934200 |
0.319 |
|
| 2003 |
Chevelkov V, van Rossum BJ, Castellani F, Rehbein K, Diehl A, Hohwy M, Steuernagel S, Engelke F, Oschkinat H, Reif B. 1H detection in MAS solid-state NMR spectroscopy of biomacromolecules employing pulsed field gradients for residual solvent suppression. Journal of the American Chemical Society. 125: 7788-9. PMID 12822982 DOI: 10.1021/Ja029354B |
0.385 |
|
| 2003 |
Ladizhansky V, Jaroniec CP, Diehl A, Oschkinat H, Griffin RG. 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. Journal of the American Chemical Society. 125: 6827-33. PMID 12769594 DOI: 10.1021/Ja029082C |
0.391 |
|
| 2003 |
van Rossum BJ, Castellani F, Pauli J, Rehbein K, Hollander J, de Groot HJ, Oschkinat H. Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR correlation spectra. Journal of Biomolecular Nmr. 25: 217-23. PMID 12652133 DOI: 10.1023/A:1022819921584 |
0.455 |
|
| 2003 |
Reif B, Van Rossum BJ, Castellani F, Rehbein K, Diehl A, Oschkinat H. Characterization of (1)H-(1)H distances in a uniformly (2)H,(15)N-labeled SH3 domain by MAS solid-state NMR spectroscopy (section sign). Journal of the American Chemical Society. 125: 1488-9. PMID 12568603 DOI: 10.1021/Ja0283697 |
0.386 |
|
| 2002 |
Schubert M, Labudde D, Oschkinat H, Schmieder P. A software tool for the prediction of Xaa-Pro peptide bond conformations in proteins based on 13C chemical shift statistics. Journal of Biomolecular Nmr. 24: 149-54. PMID 12495031 DOI: 10.1023/A:1020997118364 |
0.627 |
|
| 2002 |
Castellani F, van Rossum B, Diehl A, Schubert M, Rehbein K, Oschkinat H. Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy. Nature. 420: 98-102. PMID 12422222 DOI: 10.1038/Nature01070 |
0.7 |
|
| 2002 |
de Boer I, Bosman L, Raap J, Oschkinat H, de Groot HJ. 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. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 157: 286-91. PMID 12323147 DOI: 10.1006/Jmre.2002.2588 |
0.41 |
|
| 2002 |
Zimmermann J, Labudde D, Jarchau T, Walter U, Oschkinat H, Ball LJ. Relaxation, equilibrium oligomerization, and molecular symmetry of the VASP (336-380) EVH2 tetramer. Biochemistry. 41: 11143-51. PMID 12220179 DOI: 10.1021/Bi020379X |
0.395 |
|
| 2002 |
Patzelt H, Simon B, terLaak A, Kessler B, Kühne R, Schmieder P, Oesterhelt D, Oschkinat H. The structures of the active center in dark-adapted bacteriorhodopsin by solution-state NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 99: 9765-70. PMID 12119389 DOI: 10.1073/Pnas.132253899 |
0.341 |
|
| 2002 |
van Rossum BJ, Castellani F, Rehbein K, Pauli J, Oschkinat H. Assignment of the nonexchanging protons of the alpha-spectrin SH3 domain by two- and three-dimensional 1H-13C solid-state magic-angle spinning NMR and comparison of solution and solid-state proton chemical shifts. Chembiochem : a European Journal of Chemical Biology. 2: 906-14. PMID 11948879 DOI: 10.1002/1439-7633(20011203)2:12<906::Aid-Cbic906>3.0.Co;2-M |
0.475 |
|
| 2002 |
van Rossum BJ, Schulten EA, Raap J, Oschkinat H, de Groot HJ. 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. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 155: 1-14. PMID 11945028 DOI: 10.1006/Jmre.2002.2502 |
0.44 |
|
| 2002 |
Ball LJ, Jarchau T, Oschkinat H, Walter U. EVH1 domains: structure, function and interactions. Febs Letters. 513: 45-52. PMID 11911879 DOI: 10.1016/S0014-5793(01)03291-4 |
0.306 |
|
| 2002 |
Pires JR, Taha-Nejad F, Toepert F, Ast T, Hoffmüller U, Schneider-Mergener J, Kühne R, Macias MJ, Oschkinat H. 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. Journal of Molecular Biology. 314: 1147-56. PMID 11743730 DOI: 10.1006/Jmbi.2000.5199 |
0.302 |
|
| 2002 |
Schubert M, Oschkinat H, Schmieder P. Amino acid type-selective backbone 1H-15N-correlations for Arg and Lys. Journal of Biomolecular Nmr. 20: 379-84. PMID 11563560 DOI: 10.1023/A:1011206131623 |
0.627 |
|
| 2001 |
Pauli J, Baldus M, Van Rossum B, De Groot H, Oschkinat H. Backbone and side-chain13C and15N signal assignments of the α-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 tesla Chembiochem. 2: 272-281. PMID 11828455 DOI: 10.1002/1439-7633(20010401)2:4<272::Aid-Cbic272>3.0.Co;2-2 |
0.44 |
|
| 2001 |
Schubert M, Oschkinat H, Schmieder P. MUSIC and aromatic residues: amino acid type-selective (1)H-(15)N correlations, III. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 153: 186-92. PMID 11740893 DOI: 10.1006/Jmre.2001.2447 |
0.616 |
|
| 2001 |
Kelly MJ, Ball LJ, Krieger C, Yu Y, Fischer M, Schiffmann S, Schmieder P, Kühne R, Bermel W, Bacher A, Richter G, Oschkinat H. The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site. Proceedings of the National Academy of Sciences of the United States of America. 98: 13025-30. PMID 11687623 DOI: 10.1073/Pnas.231323598 |
0.352 |
|
| 2001 |
Ferguson N, Pires JR, Toepert F, Johnson CM, Pan YP, Volkmer-Engert R, Schneider-Mergener J, Daggett V, Oschkinat H, Fersht A. Using flexible loop mimetics to extend phi-value analysis to secondary structure interactions. Proceedings of the National Academy of Sciences of the United States of America. 98: 13008-13. PMID 11687614 DOI: 10.1073/Pnas.221467398 |
0.352 |
|
| 2001 |
Ferguson N, Johnson CM, Macias M, Oschkinat H, Fersht A. Ultrafast folding of WW domains without structured aromatic clusters in the denatured state. Proceedings of the National Academy of Sciences of the United States of America. 98: 13002-7. PMID 11687613 DOI: 10.1073/Pnas.221467198 |
0.328 |
|
| 2001 |
Luca S, Filippov DV, van Boom JH, Oschkinat H, de Groot HJ, Baldus M. Secondary chemical shifts in immobilized peptides and proteins: a qualitative basis for structure refinement under magic angle spinning. Journal of Biomolecular Nmr. 20: 325-31. PMID 11563556 DOI: 10.1023/A:1011278317489 |
0.427 |
|
| 2001 |
Heinemann U, Illing G, Oschkinat H. High-throughput three-dimensional protein structure determination. Current Opinion in Biotechnology. 12: 348-54. PMID 11551462 DOI: 10.1016/S0958-1669(00)00226-3 |
0.324 |
|
| 2001 |
Schubert M, Oschkinat H, Schmieder P. MUSIC, selective pulses, and tuned delays: amino acid type-selective (1)H-(15)N correlations, II. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 148: 61-72. PMID 11133277 DOI: 10.1006/Jmre.2000.2222 |
0.614 |
|
| 2001 |
Heinemann U, Frevert J, Hofmann K, Illing G, Maurer C, Oschkinat H, Saenger W. An integrated approach to structural genomics. Progress in Biophysics and Molecular Biology. 73: 347-62. PMID 11063780 DOI: 10.1016/S0079-6107(00)00009-2 |
0.34 |
|
| 2001 |
Schubert M, Ball LJ, Oschkinat H, Schmieder P. Bridging the gap: A set of selective 1H-15N-correlations to link sequential neighbors of prolines. Journal of Biomolecular Nmr. 17: 331-5. PMID 11014597 DOI: 10.1023/A:1008362904205 |
0.625 |
|
| 2000 |
Ball LJ, Kühne R, Hoffmann B, Häfner A, Schmieder P, Volkmer-Engert R, Hof M, Wahl M, Schneider-Mergener J, Walter U, Oschkinat H, Jarchau T. Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity. The Embo Journal. 19: 4903-14. PMID 10990454 DOI: 10.1093/Emboj/19.18.4903 |
0.328 |
|
| 2000 |
Macias MJ, Gervais V, Civera C, Oschkinat H. Structural analysis of WW domains and design of a WW prototype. Nature Structural Biology. 7: 375-9. PMID 10802733 DOI: 10.1038/75144 |
0.316 |
|
| 2000 |
Pauli J, van Rossum B, Förster H, de Groot HJ, Oschkinat H. Sample optimization and identification of signal patterns of amino acid side chains in 2D RFDR spectra of the alpha-spectrin SH3 domain. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 143: 411-6. PMID 10729269 DOI: 10.1006/Jmre.2000.2029 |
0.402 |
|
| 1999 |
Smalla M, Schmieder P, Kelly M, Ter Laak A, Krause G, Ball L, Wahl M, Bork P, Oschkinat H. Solution structure of the receptor tyrosine kinase EphB2 SAM domain and identification of two distinct homotypic interaction sites. Protein Science : a Publication of the Protein Society. 8: 1954-61. PMID 10548040 DOI: 10.1110/Ps.8.10.1954 |
0.33 |
|
| 1999 |
Schubert M, Smalla M, Schmieder P, Oschkinat H. MUSIC in Triple-Resonance Experiments: Amino Acid Type-Selective 1H–15N Correlations Journal of Magnetic Resonance. 141: 34-43. PMID 10527741 DOI: 10.1006/Jmre.1999.1881 |
0.356 |
|
| 1999 |
Richter G, Kelly M, Krieger C, Yu Y, Bermel W, Karlsson G, Bacher A, Oschkinat H. NMR studies on the 46-kDa dimeric protein, 3,4-dihydroxy-2-butanone 4-phosphate synthase, using 2H, 13C, and 15N-labelling. European Journal of Biochemistry. 261: 57-65. PMID 10103033 DOI: 10.1046/J.1432-1327.1999.00211.X |
0.392 |
|
| 1999 |
Patzelt H, Kessler B, Oschkinat H, Oesterhelt D. The entire metabolite spectrum of the green alga Scenedesmus obliquus in isotope-labelled form Phytochemistry. 50: 215-217. DOI: 10.1016/S0031-9422(98)00374-4 |
0.319 |
|
| 1999 |
Hoffmüller U, Russwurm M, Kleinjung F, Ashurst J, Oschkinat H, Volkmer-Engert R, Koesling D, Schneider-Mergener J. Interaction of a PDZ Protein Domain with a Synthetic Library of All Human Protein C Termini Angewandte Chemie International Edition. 38: 2000-2004. DOI: 10.1002/(Sici)1521-3773(19990712)38:13/14<2000::Aid-Anie2000>3.0.Co;2-V |
0.318 |
|
| 1997 |
Gervais V, Zerial A, Oschkinat H. NMR investigations of the role of the sugar moiety in glycosylated recombinant human granulocyte-colony-stimulating factor. European Journal of Biochemistry. 247: 386-95. PMID 9249051 DOI: 10.1111/J.1432-1033.1997.00386.X |
0.347 |
|
| 1997 |
Egorova-Zachernyuk TA, van Rossum B, Boender GJ, Franken E, Ashurst J, Raap J, Gast P, Hoff AJ, Oschkinat H, de Groot HJ. Characterization of pheophytin ground states in Rhodobacter sphaeroides R26 photosynthetic reaction centers from multispin pheophytin enrichment and 2-D 13C MAS NMR dipolar correlation spectroscopy. Biochemistry. 36: 7513-9. PMID 9200701 DOI: 10.1021/Bi962770M |
0.413 |
|
| 1997 |
Nilges M, Macias MJ, O'Donoghue SI, Oschkinat H. Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin. Journal of Molecular Biology. 269: 408-22. PMID 9199409 DOI: 10.1006/Jmbi.1997.1044 |
0.37 |
|
| 1997 |
Shaw GL, Müller T, Mott HR, Oschkinat H, Campbell ID, Mitschang L. Constant-Time HQQC Experiment for Protein NMR Spectroscopy Journal of Magnetic Resonance. 124: 479-483. DOI: 10.1006/Jmre.1996.1062 |
0.389 |
|
| 1996 |
Smith BO, Ito Y, Raine A, Teichmann S, Ben-Tovim L, Nietlispach D, Broadhurst RW, Terada T, Kelly M, Oschkinat H, Shibata T, Yokoyama S, Laue ED. An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residue types. Journal of Biomolecular Nmr. 8: 360-8. PMID 20686886 DOI: 10.1007/BF00410335 |
0.343 |
|
| 1996 |
Macias MJ, Hyvönen M, Baraldi E, Schultz J, Sudol M, Saraste M, Oschkinat H. Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature. 382: 646-9. PMID 8757138 DOI: 10.1038/382646A0 |
0.308 |
|
| 1996 |
Scheuring J, Fischer M, Cushman M, Lee J, Bacher A, Oschkinat H. NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies on the interaction of riboflavin synthase with trifluoromethyl-substituted intermediates. Biochemistry. 35: 9637-46. PMID 8703935 DOI: 10.1021/Bi9600916 |
0.335 |
|
| 1996 |
Nietlispach D, Clowes RT, Broadhurst RW, Ito Y, Keeler J, Kelly M, Ashurst J, Oschkinat H, Domaille PJ, Laue ED. An Approach to the Structure Determination of Larger Proteins Using Triple Resonance NMR Experiments in Conjunction with Random Fractional Deuteration Journal of the American Chemical Society. 118: 407-415. DOI: 10.1021/Ja952207B |
0.422 |
|
| 1995 |
Hyvonen M, Macias MJ, Nilges M, Oschkinat H, Saraste M, Wilmanns M. Structure of the binding site for inositol phosphates in a PH domain. The Embo Journal. 14: 4676-4685. DOI: 10.2210/Pdb1Btn/Pdb |
0.305 |
|
| 1995 |
Mitschang L, Ponstingl H, Grindrod D, Oschkinat H. Geometrical representation of coherence transfer selection by pulsed field gradients in high‐resolution nuclear magnetic resonance The Journal of Chemical Physics. 102: 3089-3098. DOI: 10.1063/1.468618 |
0.307 |
|
| 1994 |
Macias MJ, Musacchio A, Ponstingl H, Nilges M, Saraste M, Oschkinat H. Structure of the pleckstrin homology domain from beta-spectrin. Nature. 369: 675-7. PMID 8208297 DOI: 10.1038/369675A0 |
0.319 |
|
| 1994 |
Oschkinat H, Müller T, Dieckmann T. Protein Structure Determination with Three- and Four-Dimensional NMR Spectroscopy Angewandte Chemie International Edition in English. 33: 277-293. DOI: 10.1002/Anie.199402771 |
0.397 |
|
| 1994 |
Oschkinat H, Müller T, Dieckmann T. Proteinstrukturaufklärung mit drei- und vierdimensionaler NMR-Spektroskopie Angewandte Chemie. 106: 284-300. DOI: 10.1002/Ange.19941060305 |
0.352 |
|
| 1993 |
Engh RA, Dieckmann T, Bode W, Auerswald EA, Turk V, Huber R, Oschkinat H. Conformational variability of chicken cystatin. Comparison of structures determined by X-ray diffraction and NMR spectroscopy. Journal of Molecular Biology. 234: 1060-9. PMID 8263913 DOI: 10.1006/Jmbi.1993.1659 |
0.325 |
|
| 1993 |
Dieckmann T, Mitschang L, Hofmann M, Kos J, Turk V, Auerswald EA, Jaenicke R, Oschkinat H. The structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution Journal of Molecular Biology. 234: 1048-1059. PMID 8263912 DOI: 10.1006/Jmbi.1993.1658 |
0.323 |
|
| 1993 |
Odefey C, Westendorf J, Dieckmann T, Oschkinat H. 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). Chemico-Biological Interactions. 85: 117-26. PMID 1493604 DOI: 10.1016/0009-2797(92)90056-Q |
0.314 |
|
| 1993 |
Bernstein R, Cieslar C, Ross A, Oschkinat H, Freund J, Holak T. Computer-assisted assignment of multidimensional NMR spectra of proteins: Application to 3D NOESY-HMQC and TOCSY-HMQC spectra Journal of Biomolecular Nmr. 3. DOI: 10.1007/Bf00178267 |
0.368 |
|
| 1992 |
Stubbs MT, Oschkinat H, Mayr I, Huber R, Angliker H, Stone SR, Bode W. The interaction of thrombin with fibrinogen. A structural basis for its specificity. European Journal of Biochemistry. 206: 187-95. PMID 1587268 DOI: 10.1111/J.1432-1033.1992.Tb16916.X |
0.315 |
|
| 1992 |
Habazettl J, Ross A, Oschkinat H, Holak TA. Secondary NOE pathways in 2D NOESY spectra of proteins estimated from homonuclear three-dimensional NOE-NOE nuclear magnetic resonance spectroscopy Journal of Magnetic Resonance (1969). 97: 511-521. DOI: 10.1016/0022-2364(92)90031-2 |
0.303 |
|
| 1992 |
Mitschang L, Keeler J, Davis AL, Oschkinat H. Removal of zero-quantum interference in NOESY spectra of proteins by utilizing the natural inhomogeneity of the radiofrequency field Journal of Biomolecular Nmr. 2: 545-556. DOI: 10.1007/Bf02192844 |
0.336 |
|
| 1992 |
Oschkinat H, Schott K, Bacher A. Conformation of 6,7-dimethyl-8-ribityllumazine bound to β-subunits of heavy riboflavin synthase: Transferred nuclear overhauser effect (TrNOE) studies employing ω1-13C-filtered NOESY including a novel technique for zero quantum suppression Journal of Biomolecular Nmr. 2: 19-32. DOI: 10.1007/Bf02192798 |
0.308 |
|
| 1991 |
Zarbock J, Oschkinat H, Hannappel E, Kalbacher H, Voelter W, Holak TA. Solution conformation of thymosin beta 4: a nuclear magnetic resonance and simulated annealing study. Biochemistry. 29: 7814-21. PMID 2261438 DOI: 10.1021/Bi00486A006 |
0.36 |
|
| 1991 |
Oschkinat H, Holak TA, Cieslar C. Assignment of protein NMR spectra in the light of homonuclear 3D spectroscopy: an automatable procedure based on 3D TOCSY-TOCSY and 3D TOCSY-NOESY. Biopolymers. 31: 699-712. PMID 1932568 DOI: 10.1002/Bip.360310615 |
0.35 |
|
| 1991 |
Holak TA, Habazettl J, Oschkinat H, Otlewski J. Structures of proteins in solution derived from homonuclear three-dimensional NOE-NOE nuclear magnetic resonance spectroscopy. High-resolution structure of squash trypsin inhibitor Journal of the American Chemical Society. 113: 3196-3198. DOI: 10.1021/Ja00008A072 |
0.37 |
|
| 1991 |
Mitschang L, Cieslar C, Holak T, Oschkinat H. Application of the Karhunen-Loéve transformation to the suppression of undesired resonances in three-dimensional NMR Journal of Magnetic Resonance (1969). 92: 208-217. DOI: 10.1016/0022-2364(91)90264-T |
0.333 |
|
| 1991 |
Ross A, Freund J, Cieslar C, Oschkinat H, Schleicher M, Holak TA. Homonuclear three-dimensional NOE-NOE Nuclear magnetic resonance spectroscopy of proteins in water Journal of Magnetic Resonance (1969). 95: 567-573. DOI: 10.1016/0022-2364(91)90170-X |
0.33 |
|
| 1990 |
Habazettl J, Cieslar C, Oschkinat H, Holak TA. 1H NMR assignments of sidechain conformations in proteins using a high-dimensional potential in the simulated annealing calculations. Febs Letters. 268: 141-5. PMID 2384151 DOI: 10.1016/0014-5793(90)80993-S |
0.373 |
|
| 1990 |
Kessler H, Schmieder P, Oschkinat H. 3D Heteronuclear NMR techniques for carbon-13 in natural abundance Journal of the American Chemical Society. 112: 8599-8600. DOI: 10.1021/Ja00179A064 |
0.385 |
|
| 1990 |
Cieslar C, Holak T, Oschkinat H. 3D TOCSY-TOCSY processing using linear prediction, as a potential technique for automated assignment Journal of Magnetic Resonance (1969). 89: 184-190. DOI: 10.1016/0022-2364(90)90174-8 |
0.43 |
|
| 1990 |
Oschkinat H, Cieslar C, Griesinger C. Recognition of secondary-structure elements in 3D TOCSY-NOESY spectra of proteins. Interpretation of 3D cross-peak amplitudes Journal of Magnetic Resonance (1969). 86: 453-469. DOI: 10.1016/0022-2364(90)90024-4 |
0.484 |
|
| 1990 |
Schmieder P, Kessler H, Oschkinat H. Fast Heteronuclear 3D NMR Spectroscopy Angewandte Chemie International Edition in English. 29: 546-548. DOI: 10.1002/Anie.199005461 |
0.357 |
|
| 1990 |
Schmieder P, Kessler H, Oschkinat H. Schnelle Heterokern-3D-NMR-Spektroskopie Angewandte Chemie. 102: 588-589. DOI: 10.1002/Ange.19901020534 |
0.477 |
|
| 1989 |
Holak TA, Nilges M, Oschkinat H. Improved strategies for the determination of protein structures from NMR data: The solution structure of acyl carrier protein Febs Letters. 242: 218-224. PMID 2914604 DOI: 10.1016/0014-5793(89)80473-9 |
0.364 |
|
| 1989 |
Oschkinat H, Cieslar C, Holak TA, Marius Clore G, Gronenborn AM. Practical and theoretical aspects of three-dimensional homonuclear Hartmann-Hahn-nuclear overhauser enhancement spectroscopy of proteins Journal of Magnetic Resonance (1969). 83: 450-472. DOI: 10.1016/0022-2364(89)90342-9 |
0.342 |
|
| 1989 |
Oschkinat H, Cieslar C, Gronenborn AM, Clore G. Three-dimensional homonuclear Hartmann-Hahn-nuclear overhauser enhancement spectroscopy in H2O and its application to proteins Journal of Magnetic Resonance (1969). 81: 212-216. DOI: 10.1016/0022-2364(89)90283-7 |
0.35 |
|
| 1989 |
Oschkinat H, Limat D, Emsley L, Bodenhausen G. Longitudinal relaxation pathways in scalar-coupled systems Journal of Magnetic Resonance (1969). 81: 13-42. DOI: 10.1016/0022-2364(89)90264-3 |
0.569 |
|
| 1988 |
Oschkinat H, Griesinger C, Kraulis PJ, Sørensen OW, Ernst RR, Gronenborn AM, Clore GM. Three-dimensional NMR spectroscopy of a protein in solution. Nature. 332: 374-6. PMID 3352736 DOI: 10.1038/332374A0 |
0.579 |
|
| 1988 |
Oschkinat H, Marius Clore G, Gronenborn AM. A two-dimensional nuclear overhauser enhancement experiment using semiselective soft pulses, and its applications to proteins Journal of Magnetic Resonance (1969). 78: 371-375. DOI: 10.1016/0022-2364(88)90285-5 |
0.374 |
|
| 1988 |
OSCHKINAT H, GRIESINGER C, KRAULIS PJ, SORENSEN OW, ERNST RR, GRONENBORN AM, CLORE GM. ChemInform Abstract: Three-Dimensional NMR Spectroscopy of a Protein in Solution. Cheminform. 19. DOI: 10.1002/chin.198830053 |
0.465 |
|
| 1987 |
Oschkinat H, Pastore A, Bodenhausen G. Determination of relaxation pathways in coupled spin systems by two-dimensional NMR exchange spectroscopy with small flip angles Journal of the American Chemical Society. 109: 4110-4111. DOI: 10.1021/Ja00247A045 |
0.538 |
|
| 1987 |
Oschkinat H, Marius Clore G, Nilges M, Gronenborn AM. Application of the z-COSY technique with a modified pulse sequence to measurement of coupling constants in macromolecules Journal of Magnetic Resonance (1969). 75: 534-539. DOI: 10.1016/0022-2364(87)90111-9 |
0.311 |
|
| 1987 |
Oschkinat H, Bodenhausen G. Multiplet effects in double-quantum spectra Journal of Magnetic Resonance (1969). 73: 565-567. DOI: 10.1016/0022-2364(87)90025-4 |
0.376 |
|
| 1987 |
Nović M, Oschkinat H, Pfändler P, Bodenhausen G. z-Filtered double-quantum NMR spectra and automated analysis by pattern recognition Journal of Magnetic Resonance (1969). 73: 493-511. DOI: 10.1016/0022-2364(87)90012-6 |
0.501 |
|
| 1987 |
OSCHKINAT H, PASTORE A, BODENHAUSEN G. ChemInform Abstract: Determination of Relaxation Pathways in Coupled Spin Systems by Two-Dimensional NMR Exchange Spectroscopy with Small Flip Angles. Cheminform. 18. DOI: 10.1002/chin.198743044 |
0.483 |
|
| 1986 |
Kessler H, Oschkinat H, Griesinger C, Bermel W. Transformation of homonuclear two-dimensional NMR techniques into one-dimensional techniques using Gaussian pulses Journal of Magnetic Resonance (1969). 70: 106-133. DOI: 10.1016/0022-2364(86)90366-5 |
0.595 |
|
| 1986 |
Oschkinat H, Pastore A, Pfändler P, Bodenhausen G. Two-dimensional correlation of directly and remotely connected transitions by z-filtered COSY Journal of Magnetic Resonance (1969). 69: 559-566. DOI: 10.1016/0022-2364(86)90176-9 |
0.484 |
|
| 1986 |
QUINKERT G, HEIM N, BATS JW, OSCHKINAT H, KESSLER H. ChemInform Abstract: Structure of the Lichen Macrolide (+)-Aspicilin Chemischer Informationsdienst. 17. DOI: 10.1002/Chin.198609061 |
0.438 |
|
| 1985 |
Kessler H, Müller A, Oschkinat H. Differences andsums of traces within,COSY spectra (DISCO) for the extraction of coupling constants: ‘Decoupling’ after the measurement Magnetic Resonance in Chemistry. 23: 844-852. DOI: 10.1002/Mrc.1260231012 |
0.513 |
|
| 1985 |
Loosli H, Kessler H, Oschkinat H, Weber H, Petcher TJ, Widmer A. Peptide conformations. Part 31. The conformation of cyclosporin a in the crystal and in solution Helvetica Chimica Acta. 68: 682-704. DOI: 10.1002/Hlca.19850680319 |
0.498 |
|
| 1985 |
Kessler H, Loosli H, Oschkinat H. Peptide conformations. Part 30. Assignment of the1H-,13C-, and15N-NMR spectra of cyclosporin A in CDCl3 and C6D6 by a combination of homo- and heteronuclear two-dimensional techniques Helvetica Chimica Acta. 68: 661-681. DOI: 10.1002/Hlca.19850680318 |
0.555 |
|
| 1985 |
LOOSLI H, KESSLER H, OSCHKINAT H, WEBER H, PETCHER TJ, WIDMER A. ChemInform Abstract: PEPTIDE CONFORMATIONS. PART 31. THE CONFORMATION OF CYCLOSPORIN A IN THE CRYSTAL AND IN SOLUTION Chemischer Informationsdienst. 16. DOI: 10.1002/Chin.198535047 |
0.434 |
|
| 1985 |
KESSLER H, LOOSLI H, OSCHKINAT H. ChemInform Abstract: PEPTIDE CONFORMATIONS. PART 30. ASSIGNMENT OF THE PROTON, CARBON-13, NITROGEN-15 NMR SPECTRA OF CYCLOSPORIN A IN D-CHLOROFORM AND D6-BENZENE BY A COMBINATION OF HOMO- AND HETERONUCLEAR TWO-DIMENSIONAL TECHNIQUES Chemischer Informationsdienst. 16. DOI: 10.1002/Chin.198535042 |
0.5 |
|
| 1985 |
Quinkert G, Heim N, Bats JW, Oschkinat H, Kessler H. The Structure of the Lichen Macrolide(+)-Aspicilin Angewandte Chemie International Edition in English. 24: 987-988. DOI: 10.1002/Anie.198509871 |
0.428 |
|
| 1985 |
Kessler H, Oschkinat H. Simplification of Spectra for the Determination of Coupling Constants from Homonuclear Correlated 2D NMR Spectra Angewandte Chemie International Edition in English. 24: 690-692. DOI: 10.1002/Anie.198506901 |
0.504 |
|
| 1985 |
Quinkert G, Heim N, Bats JW, Oschkinat H, Kessler H. Die Struktur des Flechten-Makrolids (+)-Aspicilin Angewandte Chemie. 97: 985-986. DOI: 10.1002/Ange.19850971125 |
0.373 |
|
| 1985 |
Kessler H, Oschkinat H. Spektrenvereinfachung zur Ermittlung von Kopplungskonstanten aus homonuclear-korrelierten 2D-NMR-Spektren Angewandte Chemie. 97: 689-690. DOI: 10.1002/Ange.19850970811 |
0.472 |
|
| 1984 |
Oschkinat H, Freeman R. Fine structure in two-dimensional NMR correlation spectroscopy Journal of Magnetic Resonance (1969). 60: 164-169. DOI: 10.1016/0022-2364(84)90044-1 |
0.427 |
|
| 1984 |
KESSLER H, OSCHKINAT H, ZIMMERMANN G, MOEHRLE H, BIEGHOLDT M, ARZ W, FOERSTER H. ChemInform Abstract: APPLICATION OF HIGH-RESOLUTION SOLID-STATE NMR SPECTROSCOPY TO THE DETERMINATION OF THE RING-CHAIN TAUTOMERISM Chemischer Informationsdienst. 15. DOI: 10.1002/Chin.198418077 |
0.499 |
|
| 1984 |
Kessler H, Oschkinat H, Zimmermann G, Möhrle H, Biegholdt M, Arz W, Förster H. Anwendung der hochaufgelösten Festkörper-NMR-Spektroskopie zur Bestimmung der Ring-Ketten-Tautomerie Chemische Berichte. 117: 702-709. DOI: 10.1002/Cber.19841170223 |
0.554 |
|
| 1983 |
Kessler H, Oschkinat H, Sørensen O, Kogler H, Ernst R. Multiple-quantum-filtered homonuclear J,δ spectra Journal of Magnetic Resonance (1969). 55: 329-333. DOI: 10.1016/0022-2364(83)90244-5 |
0.419 |
|
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