| Year |
Citation |
Score |
| 2024 |
Klukowski P, Damberger FF, Allain FH, Iwai H, Kadavath H, Ramelot TA, Montelione GT, Riek R, Güntert P. The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis. Scientific Data. 11: 30. PMID 38177162 DOI: 10.1038/s41597-023-02879-5 |
0.702 |
|
| 2022 |
Ashkinadze D, Kadavath H, Pokharna A, Chi CN, Friedmann M, Strotz D, Kumari P, Minges M, Cadalbert R, Königl S, Güntert P, Vögeli B, Riek R. Atomic resolution protein allostery from the multi-state structure of a PDZ domain. Nature Communications. 13: 6232. PMID 36266302 DOI: 10.1038/s41467-022-33687-x |
0.332 |
|
| 2022 |
Klukowski P, Riek R, Güntert P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA. Nature Communications. 13: 6151. PMID 36257955 DOI: 10.1038/s41467-022-33879-5 |
0.313 |
|
| 2021 |
Sawaya MR, Hughes MP, Rodriguez JA, Riek R, Eisenberg DS. The expanding amyloid family: Structure, stability, function, and pathogenesis. Cell. 184: 4857-4873. PMID 34534463 DOI: 10.1016/j.cell.2021.08.013 |
0.321 |
|
| 2021 |
Sawner AS, Ray S, Yadav P, Mukherjee S, Panigrahi R, Poudyal M, Patel K, Ghosh D, Kummerant E, Kumar A, Riek R, Maji SK. Modulating α-Synuclein Liquid-Liquid Phase Separation. Biochemistry. PMID 34431665 DOI: 10.1021/acs.biochem.1c00434 |
0.526 |
|
| 2020 |
Seuring C, Verasdonck J, Gath J, Ghosh D, Nespovitaya N, Wälti MA, Maji SK, Cadalbert R, Güntert P, Meier BH, Riek R. The three-dimensional structure of human β-endorphin amyloid fibrils. Nature Structural & Molecular Biology. PMID 33046908 DOI: 10.1038/s41594-020-00515-z |
0.541 |
|
| 2020 |
Strotz D, Orts J, Kadavath H, Friedmann M, Ghosh D, Olsson S, Chi C, Pokharna A, Güntert P, Vögeli B, Riek R. Protein allostery at atomic resolution. Angewandte Chemie (International Ed. in English). PMID 32797659 DOI: 10.1002/Ange.202008734 |
0.359 |
|
| 2020 |
Gerez JA, Prymaczok NC, Riek R. In-Cell NMR of Intrinsically Disordered Proteins in Mammalian Cells. Methods in Molecular Biology (Clifton, N.J.). 2141: 873-893. PMID 32696394 DOI: 10.1007/978-1-0716-0524-0_45 |
0.335 |
|
| 2020 |
Ke PC, Zhou R, Serpell LC, Riek R, Knowles TPJ, Lashuel HA, Gazit E, Hamley IW, Davis TP, Fändrich M, Otzen DE, Chapman MR, Dobson CM, Eisenberg DS, Mezzenga R. Half a century of amyloids: past, present and future. Chemical Society Reviews. PMID 32632432 DOI: 10.1039/C9Cs00199A |
0.338 |
|
| 2020 |
Orts J, Riek R. Protein-ligand structure determination with the NMR molecular replacement tool, NMR. Journal of Biomolecular Nmr. 74: 633-642. PMID 32621003 DOI: 10.1007/S10858-020-00324-Y |
0.377 |
|
| 2020 |
Ray S, Singh N, Kumar R, Patel K, Pandey S, Datta D, Mahato J, Panigrahi R, Navalkar A, Mehra S, Gadhe L, Chatterjee D, Sawner AS, Maiti S, Bhatia S, ... ... Riek R, et al. α-Synuclein aggregation nucleates through liquid-liquid phase separation. Nature Chemistry. PMID 32514159 DOI: 10.1038/S41557-020-0465-9 |
0.561 |
|
| 2020 |
Gerez JA, Riek R. Neurodegenerative diseases distinguished through protein-structure analysis. Nature. 578: 223-224. PMID 32042086 DOI: 10.1038/D41586-020-00131-3 |
0.374 |
|
| 2019 |
Bomba R, Rout SK, Bütikofer M, Kwiatkowski W, Riek R, Greenwald J. Carbonyl Sulfide as a Prebiotic Activation Agent for Stereo- and Sequence-Selective, Amyloid-Templated Peptide Elongation. Origins of Life and Evolution of the Biosphere : the Journal of the International Society For the Study of the Origin of Life. 49: 213-224. PMID 31845164 DOI: 10.1007/S11084-019-09586-5 |
0.3 |
|
| 2019 |
Guerrero-Ferreira R, Taylor NM, Arteni AA, Kumari P, Mona D, Ringler P, Britschgi M, Lauer ME, Makky A, Verasdonck J, Riek R, Melki R, Meier BH, Böckmann A, Bousset L, et al. Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy. Elife. 8. PMID 31815671 DOI: 10.7554/Elife.48907 |
0.343 |
|
| 2019 |
Burmann BM, Gerez JA, Matečko-Burmann I, Campioni S, Kumari P, Ghosh D, Mazur A, Aspholm EE, Šulskis D, Wawrzyniuk M, Bock T, Schmidt A, Rüdiger SGD, Riek R, Hiller S. Regulation of α-synuclein by chaperones in mammalian cells. Nature. PMID 31802003 DOI: 10.1038/S41586-019-1808-9 |
0.337 |
|
| 2019 |
Soste M, Charmpi K, Lampert F, Gerez JA, van Oostrum M, Malinovska L, Boersema PJ, Prymaczok NC, Riek R, Peter M, Vanni S, Beyer A, Picotti P. Proteomics-Based Monitoring of Pathway Activity Reveals that Blocking Diacylglycerol Biosynthesis Rescues from Alpha-Synuclein Toxicity. Cell Systems. PMID 31521608 DOI: 10.1016/J.Cels.2019.07.010 |
0.302 |
|
| 2019 |
Bayrhuber M, Maslennikov I, Kwiatkowski W, Sobol A, Wierschem C, Eichmann C, Frey L, Riek R. Nuclear Magnetic Resonance Solution Structure and Functional Behavior of the Human Proton Channel. Biochemistry. 58: 4017-4027. PMID 31365236 DOI: 10.1021/Acs.Biochem.9B00471 |
0.32 |
|
| 2019 |
Gerez JA, Prymaczok NC, Rockenstein E, Herrmann US, Schwarz P, Adame A, Enchev RI, Courtheoux T, Boersema PJ, Riek R, Peter M, Aguzzi A, Masliah E, Picotti P. A cullin-RING ubiquitin ligase targets exogenous α-synuclein and inhibits Lewy body-like pathology. Science Translational Medicine. 11. PMID 31167929 DOI: 10.1126/Scitranslmed.Aau6722 |
0.332 |
|
| 2018 |
Orts J, Wälti MA, Ghosh D, Campioni S, Saupe SJ, Riek R. Rational structure-based design of fluorescence probes for amyloid folds. Chembiochem : a European Journal of Chemical Biology. PMID 30548150 DOI: 10.1002/Cbic.201800664 |
0.391 |
|
| 2018 |
Bomba R, Kwiatkowski W, Sánchez-Ferrer A, Riek R, Greenwald J. Cooperative Induction of Ordered Peptide and Fatty Acid Aggregates. Biophysical Journal. 115: 2336-2347. PMID 30503535 DOI: 10.1016/J.Bpj.2018.10.031 |
0.349 |
|
| 2018 |
Jemth P, Karlsson E, Vögeli B, Guzovsky B, Andersson E, Hultqvist G, Dogan J, Güntert P, Riek R, Chi CN. Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins. Science Advances. 4: eaau4130. PMID 30397651 DOI: 10.1126/Sciadv.Aau4130 |
0.388 |
|
| 2018 |
Guerrero-Ferreira R, Taylor NMI, Mona D, Ringler P, Lauer ME, Riek R, Britschgi M, Stahlberg H. Cryo-EM structure of alpha-synuclein fibrils. Elife. 7. PMID 29969391 DOI: 10.7554/Elife.36402 |
0.396 |
|
| 2018 |
Greenwald J, Kwiatkowski W, Riek R. Peptide Amyloids in the Origin of Life. Journal of Molecular Biology. 430: 3735-3750. PMID 29890117 DOI: 10.1016/J.Jmb.2018.05.046 |
0.378 |
|
| 2018 |
Young G, Hundt N, Cole D, Fineberg A, Andrecka J, Tyler A, Olerinyova A, Ansari A, Marklund EG, Collier MP, Chandler SA, Tkachenko O, Allen J, Crispin M, Billington N, ... ... Riek R, et al. Quantitative mass imaging of single biological macromolecules. Science (New York, N.Y.). 360: 423-427. PMID 29700264 DOI: 10.1126/Science.Aar5839 |
0.337 |
|
| 2018 |
Rout SK, Friedmann MP, Riek R, Greenwald J. A prebiotic template-directed peptide synthesis based on amyloids. Nature Communications. 9: 234. PMID 29339755 DOI: 10.1038/S41467-017-02742-3 |
0.304 |
|
| 2017 |
Chi C, Strotz D, Riek R, Vögeli BR. NOE-derived methyl distances from a 360 kDa proteasome complex. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 29265588 DOI: 10.1002/Chem.201705551 |
0.352 |
|
| 2017 |
Schütz AK, Hornemann S, Wälti MA, Greuter L, Tiberi C, Cadalbert R, Gantner M, Riek R, Hammarström P, Nilsson KPR, Böckmann A, Aguzzi A, Meier BH. Binding of Polythiophenes to Amyloids: Structural Mapping of the Pharmacophore. Acs Chemical Neuroscience. PMID 29178774 DOI: 10.1021/Acschemneuro.7B00397 |
0.371 |
|
| 2017 |
Meier BH, Riek R, Böckmann A. Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR. Trends in Biochemical Sciences. PMID 28916413 DOI: 10.1016/J.Tibs.2017.08.001 |
0.424 |
|
| 2017 |
Lakomek NA, Frey L, Bibow S, Böckmann A, Riek R, Meier BH. Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods. The Journal of Physical Chemistry. B. PMID 28737919 DOI: 10.1021/Acs.Jpcb.7B06944 |
0.358 |
|
| 2017 |
Strotz D, Orts J, Chi CN, Riek R, Vögeli B. The eNORA2 exact NOE analysis program. Journal of Chemical Theory and Computation. PMID 28727914 DOI: 10.1021/Acs.Jctc.7B00436 |
0.338 |
|
| 2017 |
Martinez D, Decossas M, Kowal J, Frey L, Stahlberg H, Dufourc E, Riek R, Habenstein B, Bibow S, Loquet A. Lipid internal dynamics probed in nanodiscs. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 28573816 DOI: 10.1002/Cphc.201700450 |
0.305 |
|
| 2017 |
Wälti MA, Riek R, Orts J. Fast NMR-Based Determination of the 3D Structure of the Binding Site of Protein-Ligand Complexes with Weak Affinity Binders. Angewandte Chemie (International Ed. in English). 56: 5208-5211. PMID 28387455 DOI: 10.1002/Anie.201612304 |
0.368 |
|
| 2017 |
Wälti MA, Orts J, Riek R. Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ(1-42) amyloid polymorph. Plos One. 12: e0172862. PMID 28319116 DOI: 10.1371/Journal.Pone.0172862 |
0.385 |
|
| 2017 |
Seuring C, Verasdonck J, Ringler P, Cadalbert R, Stahlberg H, Böckmann A, Meier BH, Riek R. Amyloid Fibril Polymorphism: Almost Identical on the Atomic Level, Mesoscopically Very Different. The Journal of Physical Chemistry. B. PMID 28075583 DOI: 10.1021/Acs.Jpcb.6B10624 |
0.375 |
|
| 2017 |
Frey L, Lakomek NA, Riek R, Bibow S. Micelles, Bicelles, and Nanodiscs: Comparing the Impact of Membrane Mimetics on Membrane Protein Backbone Dynamics. Angewandte Chemie (International Ed. in English). 56: 380-383. PMID 27882643 DOI: 10.1002/Anie.201608246 |
0.321 |
|
| 2017 |
Riek R. The Three-Dimensional Structures of Amyloids. Cold Spring Harbor Perspectives in Biology. 9. PMID 27793967 DOI: 10.1101/Cshperspect.A023572 |
0.457 |
|
| 2016 |
Riek R, Eisenberg DS. The activities of amyloids from a structural perspective. Nature. 539: 227-235. PMID 27830791 DOI: 10.1038/Nature20416 |
0.416 |
|
| 2016 |
Zelenay V, Arzt ME, Bibow S, Schwab ME, Riek R. The Neurite Outgrowth Inhibitory Nogo-A-Δ20 Region Is an Intrinsically Disordered Segment Harbouring Three Stretches with Helical Propensity. Plos One. 11: e0161813. PMID 27611089 DOI: 10.1371/Journal.Pone.0161813 |
0.381 |
|
| 2016 |
Greenwald J, Friedmann MP, Riek R. Amyloid Aggregates Arise from Amino Acid Condensations under Prebiotic Conditions. Angewandte Chemie (International Ed. in English). PMID 27511635 DOI: 10.1002/Anie.201605321 |
0.332 |
|
| 2016 |
Olsson S, Strotz D, Vögeli B, Riek R, Cavalli A. The Dynamic Basis for Signal Propagation in Human Pin1-WW. Structure (London, England : 1993). PMID 27499442 DOI: 10.1016/J.Str.2016.06.013 |
0.356 |
|
| 2016 |
Eichmann C, Tzitzilonis C, Nakamura T, Kwiatkowski W, Maslennikov I, Choe S, Lipton SA, Riek R. S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein. Journal of Molecular Biology. PMID 27473602 DOI: 10.1016/J.Jmb.2016.07.010 |
0.364 |
|
| 2016 |
Wälti MA, Ravotti F, Arai H, Glabe CG, Wall JS, Böckmann A, Güntert P, Meier BH, Riek R. Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril. Proceedings of the National Academy of Sciences of the United States of America. PMID 27469165 DOI: 10.1073/Pnas.1600749113 |
0.405 |
|
| 2016 |
Riek R, Saupe SJ. The HET-S/s Prion Motif in the Control of Programmed Cell Death. Cold Spring Harbor Perspectives in Biology. 8. PMID 27352624 DOI: 10.1101/Cshperspect.A023515 |
0.34 |
|
| 2016 |
Ravotti F, Wälti MA, Güntert P, Riek R, Böckmann A, Meier BH. Solid-state NMR sequential assignment of an Amyloid-β(1-42) fibril polymorph. Biomolecular Nmr Assignments. PMID 27165577 DOI: 10.1007/S12104-016-9682-Y |
0.4 |
|
| 2016 |
Seuring C, Gath J, Verasdonck J, Cadalbert R, Rivier J, Böckmann A, Meier BH, Riek R. Solid-state NMR sequential assignment of the β-endorphin peptide in its amyloid form. Biomolecular Nmr Assignments. PMID 27165576 DOI: 10.1007/S12104-016-9681-Z |
0.36 |
|
| 2016 |
Orts J, Wälti MA, Marsh M, Vera L, Gossert AD, Güntert P, Riek R. NMR-Based Determination of the 3D Structure of the Ligand-Protein Interaction Site without Protein Resonance Assignment. Journal of the American Chemical Society. 138: 4393-400. PMID 26943491 DOI: 10.1021/Jacs.5B12391 |
0.392 |
|
| 2016 |
Eichmann C, Campioni S, Kowal J, Maslennikov I, Gerez J, Liu X, Verasdonck J, Nespovitaya N, Choe S, Meier B, Picotti P, Rizo J, Stahlberg H, Riek R. Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles. The Journal of Biological Chemistry. PMID 26846854 DOI: 10.1074/Jbc.M115.707968 |
0.317 |
|
| 2016 |
Vögeli B, Olsson S, Güntert P, Riek R. The Exact NOE as an Alternative in Ensemble Structure Determination. Biophysical Journal. 110: 113-126. PMID 26745415 DOI: 10.1016/J.Bpj.2015.11.031 |
0.414 |
|
| 2016 |
Ravotti F, Waelti M, Guentert P, Meier B, Riek R, Boeckmann A. Solid State NMR sequential assignment of Amyloid b(1-42) fibrils Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr26692 |
0.333 |
|
| 2015 |
Nespovitaya N, Gath J, Barylyuk K, Seuring C, Meier BH, Riek R. Dynamic assembly and disassembly of functional β-endorphin amyloid fibrils. Journal of the American Chemical Society. PMID 26699104 DOI: 10.1021/Jacs.5B08694 |
0.387 |
|
| 2015 |
Friedmann MP, Torbeev V, Zelenay V, Sobol A, Greenwald J, Riek R. Towards Prebiotic Catalytic Amyloids Using High Throughput Screening. Plos One. 10: e0143948. PMID 26650386 DOI: 10.1371/Journal.Pone.0143948 |
0.305 |
|
| 2015 |
Vögeli B, Olsson S, Riek R, Güntert P. Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3. Data in Brief. 5: 99-106. PMID 26504890 DOI: 10.1016/J.Dib.2015.08.020 |
0.362 |
|
| 2015 |
Saelices L, Johnson LM, Liang WY, Sawaya MR, Cascio D, Ruchala P, Whitelegge J, Jiang L, Riek R, Eisenberg DS. Uncovering the Mechanism of Aggregation of Human Transthyretin. The Journal of Biological Chemistry. PMID 26459562 DOI: 10.1074/Jbc.M115.659912 |
0.369 |
|
| 2015 |
Chi CN, Vögeli B, Bibow S, Strotz D, Orts J, Güntert P, Riek R. A Structural Ensemble for the Enzyme Cyclophilin Reveals an Orchestrated Mode of Action at Atomic Resolution. Angewandte Chemie (International Ed. in English). 54: 11657-61. PMID 26265096 DOI: 10.1002/Anie.201503698 |
0.305 |
|
| 2015 |
Vögeli B, Olsson S, Riek R, Güntert P. Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics. Journal of Structural Biology. 191: 306-17. PMID 26206511 DOI: 10.1016/J.Jsb.2015.07.008 |
0.368 |
|
| 2015 |
Ghosh D, Singh PK, Sahay S, Jha NN, Jacob RS, Sen S, Kumar A, Riek R, Maji SK. Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation. Scientific Reports. 5: 9228. PMID 25784353 DOI: 10.1038/Srep09228 |
0.651 |
|
| 2015 |
Chi CN, Strotz D, Riek R, Vögeli B. Extending the eNOE data set of large proteins by evaluation of NOEs with unresolved diagonals. Journal of Biomolecular Nmr. 62: 63-9. PMID 25749872 DOI: 10.1007/S10858-015-9917-8 |
0.374 |
|
| 2015 |
Wälti MA, Orts J, Vögeli B, Campioni S, Riek R. Solution NMR studies of recombinant Aβ(1-42): from the presence of a micellar entity to residual β-sheet structure in the soluble species. Chembiochem : a European Journal of Chemical Biology. 16: 659-69. PMID 25676345 DOI: 10.1002/Cbic.201402595 |
0.359 |
|
| 2015 |
Hähl H, Möller I, Kiesel I, Campioni S, Riek R, Verdes D, Seeger S. α-Synuclein insertion into supported lipid bilayers as seen by in situ X-ray reflectivity. Acs Chemical Neuroscience. 6: 374-9. PMID 25523270 DOI: 10.1021/Cn5002683 |
0.341 |
|
| 2015 |
Walti M, Orts J, Vogeli B, Campioni S, Riek R. Chemical shifts of amyloid beta (1-42) peptide in aqueous solution Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25218 |
0.309 |
|
| 2014 |
Eichmann C, Orts J, Tzitzilonis C, Vögeli B, Smrt S, Lorieau J, Riek R. Intermolecular detergent-membrane protein noes for the characterization of the dynamics of membrane protein-detergent complexes. The Journal of Physical Chemistry. B. 118: 14288-301. PMID 25419869 DOI: 10.1021/Jp509137Q |
0.378 |
|
| 2014 |
Eichmann C, Tzitzilonis C, Bordignon E, Maslennikov I, Choe S, Riek R. Solution NMR structure and functional analysis of the integral membrane protein YgaP from Escherichia coli. The Journal of Biological Chemistry. 289: 23482-503. PMID 24958726 DOI: 10.1074/Jbc.M114.571935 |
0.412 |
|
| 2014 |
Daskalov A, Gantner M, Wälti MA, Schmidlin T, Chi CN, Wasmer C, Schütz A, Ceschin J, Clavé C, Cescau S, Meier B, Riek R, Saupe SJ. Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability. Plos Pathogens. 10: e1004158. PMID 24945274 DOI: 10.1371/Journal.Ppat.1004158 |
0.446 |
|
| 2014 |
Bibow S, Carneiro MG, Sabo TM, Schwiegk C, Becker S, Riek R, Lee D. Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings. Protein Science : a Publication of the Protein Society. 23: 851-6. PMID 24752984 DOI: 10.1002/Pro.2482 |
0.346 |
|
| 2014 |
Nespovitaya N, Barylyuk K, Eichmann C, Zenobi R, Riek R. The production of recombinant (15)N, (13)C-labelled somatostatin 14 for NMR spectroscopy. Protein Expression and Purification. 99: 78-86. PMID 24698890 DOI: 10.1016/J.Pep.2014.03.011 |
0.315 |
|
| 2014 |
Vögeli B, Orts J, Strotz D, Chi C, Minges M, Wälti MA, Güntert P, Riek R. Towards a true protein movie: a perspective on the potential impact of the ensemble-based structure determination using exact NOEs. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 241: 53-9. PMID 24656080 DOI: 10.1016/J.Jmr.2013.11.016 |
0.405 |
|
| 2014 |
Jappelli R, Perrin MH, Lewis KA, Vaughan JM, Tzitzilonis C, Rivier JE, Vale WW, Riek R. Expression and functional characterization of membrane-integrated mammalian corticotropin releasing factor receptors 1 and 2 in Escherichia coli. Plos One. 9: e84013. PMID 24465390 DOI: 10.1371/Journal.Pone.0084013 |
0.32 |
|
| 2014 |
Campioni S, Carret G, Jordens S, Nicoud L, Mezzenga R, Riek R. The presence of an air-water interface affects formation and elongation of α-Synuclein fibrils. Journal of the American Chemical Society. 136: 2866-75. PMID 24460028 DOI: 10.1021/Ja412105T |
0.36 |
|
| 2013 |
Orts J, Vögeli B, Riek R, Güntert P. Stereospecific assignments in proteins using exact NOEs. Journal of Biomolecular Nmr. 57: 211-8. PMID 24136114 DOI: 10.1007/S10858-013-9780-4 |
0.368 |
|
| 2013 |
Sonati T, Reimann RR, Falsig J, Baral PK, O'Connor T, Hornemann S, Yaganoglu S, Li B, Herrmann US, Wieland B, Swayampakula M, Rahman MH, Das D, Kav N, Riek R, et al. The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein. Nature. 501: 102-6. PMID 23903654 DOI: 10.1038/Nature12402 |
0.334 |
|
| 2013 |
Ries J, Udayar V, Soragni A, Hornemann S, Nilsson KP, Riek R, Hock C, Ewers H, Aguzzi AA, Rajendran L. Superresolution imaging of amyloid fibrils with binding-activated probes. Acs Chemical Neuroscience. 4: 1057-61. PMID 23594172 DOI: 10.1021/Cn400091M |
0.384 |
|
| 2013 |
Rabe M, Soragni A, Reynolds NP, Verdes D, Liverani E, Riek R, Seeger S. On-surface aggregation of α-synuclein at nanomolar concentrations results in two distinct growth mechanisms. Acs Chemical Neuroscience. 4: 408-17. PMID 23509977 DOI: 10.1021/Cn3001312 |
0.32 |
|
| 2013 |
Tzitzilonis C, Eichmann C, Maslennikov I, Choe S, Riek R. Detergent/nanodisc screening for high-resolution NMR studies of an integral membrane protein containing a cytoplasmic domain. Plos One. 8: e54378. PMID 23349867 DOI: 10.1371/Journal.Pone.0054378 |
0.394 |
|
| 2013 |
Eichmann C, Sobol A, Pervushin K, Riek R. Polychromatic frequency encoding in indirect dimensions in NMR spectroscopy Molecular Physics. 111: 765-770. DOI: 10.1080/00268976.2012.745628 |
0.316 |
|
| 2013 |
Vögeli B, Güntert P, Riek R. Multiple-state ensemble structure determination from eNOE spectroscopy Molecular Physics. 111: 437-454. DOI: 10.1080/00268976.2012.728257 |
0.39 |
|
| 2012 |
Orts J, Vögeli B, Riek R. Relaxation Matrix Analysis of Spin Diffusion for the NMR Structure Calculation with eNOEs. Journal of Chemical Theory and Computation. 8: 3483-92. PMID 26592998 DOI: 10.1021/Ct3002249 |
0.333 |
|
| 2012 |
Seuring C, Greenwald J, Wasmer C, Wepf R, Saupe SJ, Meier BH, Riek R. The mechanism of toxicity in HET-S/HET-s prion incompatibility. Plos Biology. 10: e1001451. PMID 23300377 DOI: 10.1371/Journal.Pbio.1001451 |
0.339 |
|
| 2012 |
Vögeli B, Orts J, Strotz D, Güntert P, Riek R. Discrete three-dimensional representation of macromolecular motion from eNOE-based ensemble calculation. Chimia. 66: 787-90. PMID 23146266 DOI: 10.2533/Chimia.2012.787 |
0.369 |
|
| 2012 |
Vögeli B, Kazemi S, Güntert P, Riek R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs. Nature Structural & Molecular Biology. 19: 1053-7. PMID 22940676 DOI: 10.1038/Nsmb.2355 |
0.363 |
|
| 2012 |
Klammt C, Maslennikov I, Bayrhuber M, Eichmann C, Vajpai N, Chiu EJ, Blain KY, Esquivies L, Kwon JH, Balana B, Pieper U, Sali A, Slesinger PA, Kwiatkowski W, Riek R, et al. Facile backbone structure determination of human membrane proteins by NMR spectroscopy. Nature Methods. 9: 834-9. PMID 22609626 DOI: 10.1038/Nmeth.2033 |
0.415 |
|
| 2012 |
Greenwald J, Riek R. On the possible amyloid origin of protein folds. Journal of Molecular Biology. 421: 417-26. PMID 22542525 DOI: 10.1016/J.Jmb.2012.04.015 |
0.445 |
|
| 2012 |
Vilar M, Wang L, Riek R. Structural studies of amyloids by quenched hydrogen-deuterium exchange by NMR. Methods of Molecular Biology. 849: 185-198. PMID 22528091 DOI: 10.1007/978-1-61779-551-0_13 |
0.45 |
|
| 2012 |
Mathur V, Seuring C, Riek R, Saupe SJ, Liebman SW. Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity. Molecular and Cellular Biology. 32: 139-53. PMID 22037764 DOI: 10.1128/Mcb.06125-11 |
0.317 |
|
| 2012 |
Vogeli B, Kazemi S, Guntert P, Riek R. Three-State Ensemble obtained from eNOEs of the Third Immunoglobulin Binding Domain of Protein G (GB3) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Lum/Pdb |
0.308 |
|
| 2011 |
Reynolds NP, Soragni A, Rabe M, Verdes D, Liverani E, Handschin S, Riek R, Seeger S. Mechanism of membrane interaction and disruption by α-synuclein. Journal of the American Chemical Society. 133: 19366-75. PMID 21978222 DOI: 10.1021/Ja2029848 |
0.342 |
|
| 2011 |
Bayrhuber M, Riek R. Very simple combination of TROSY, CRINEPT and multiple quantum coherence for signal enhancement in an HN(CO)CA experiment for large proteins Journal of Magnetic Resonance. 209: 310-314. PMID 21353798 DOI: 10.1016/J.Jmr.2011.01.031 |
0.306 |
|
| 2011 |
Winner B, Jappelli R, Maji SK, Desplats PA, Boyer L, Aigner S, Hetzer C, Loher T, Vilar M, Campioni S, Tzitzilonis C, Soragni A, Jessberger S, Mira H, Consiglio A, ... ... Riek R, et al. In vivo demonstration that alpha-synuclein oligomers are toxic. Proceedings of the National Academy of Sciences of the United States of America. 108: 4194-9. PMID 21325059 DOI: 10.1073/Pnas.1100976108 |
0.585 |
|
| 2011 |
Riek RP, Graham RM. The elusive π-helix. Journal of Structural Biology. 173: 153-60. PMID 20828621 DOI: 10.1016/j.jsb.2010.09.001 |
0.314 |
|
| 2010 |
Greenwald J, Riek R. Biology of amyloid: structure, function, and regulation. Structure (London, England : 1993). 18: 1244-60. PMID 20947013 DOI: 10.1016/J.Str.2010.08.009 |
0.417 |
|
| 2010 |
Grace CR, Perrin MH, Gulyas J, Rivier JE, Vale WW, Riek R. NMR structure of the first extracellular domain of corticotropin-releasing factor receptor 1 (ECD1-CRF-R1) complexed with a high affinity agonist. The Journal of Biological Chemistry. 285: 38580-9. PMID 20843795 DOI: 10.1074/Jbc.M110.121897 |
0.322 |
|
| 2010 |
Greenwald J, Buhtz C, Ritter C, Kwiatkowski W, Choe S, Maddelein ML, Ness F, Cescau S, Soragni A, Leitz D, Saupe SJ, Riek R. The mechanism of prion inhibition by HET-S. Molecular Cell. 38: 889-99. PMID 20620958 DOI: 10.1016/J.Molcel.2010.05.019 |
0.369 |
|
| 2010 |
Schuetz A, Wasmer C, Habenstein B, Verel R, Greenwald J, Riek R, Böckmann A, Meier BH. Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227). Chembiochem : a European Journal of Chemical Biology. 11: 1543-51. PMID 20572250 DOI: 10.1002/Cbic.201000124 |
0.428 |
|
| 2010 |
Eichmann C, Preissler S, Riek R, Deuerling E. Cotranslational structure acquisition of nascent polypeptides monitored by NMR spectroscopy Proceedings of the National Academy of Sciences of the United States of America. 107: 9111-9116. PMID 20439768 DOI: 10.1073/Pnas.0914300107 |
0.401 |
|
| 2010 |
Wang L, Schubert D, Sawaya MR, Eisenberg D, Riek R. Multidimensional structure-activity relationship of a protein in its aggregated states. Angewandte Chemie (International Ed. in English). 49: 3904-8. PMID 20397175 DOI: 10.1002/Anie.201000068 |
0.439 |
|
| 2010 |
Goldschmidt L, Teng PK, Riek R, Eisenberg D. Identifying the amylome, proteins capable of forming amyloid-like fibrils. Proceedings of the National Academy of Sciences of the United States of America. 107: 3487-92. PMID 20133726 DOI: 10.1073/Pnas.0915166107 |
0.387 |
|
| 2010 |
Vögeli B, Riek R. Side chain: backbone projections in aromatic and ASX residues from NMR cross-correlated relaxation Journal of Biomolecular Nmr. 46: 135-147. PMID 19904498 DOI: 10.1007/S10858-009-9387-Y |
0.335 |
|
| 2010 |
Vögeli B, Segawa TF, Leitz D, Sobol A, Choutko A, Trzesniak D, van Gunsteren W, Riek R. Exact distances and internal dynamics of perdeuterated ubiquitin from NOE buildups. Journal of the American Chemical Society. 131: 17215-25. PMID 19891472 DOI: 10.1021/Ja905366H |
0.381 |
|
| 2010 |
Schuetz A, Wasmer C, Habenstein B, Verel R, Greenwald J, Riek R, Bockmann A, Meier B. Solid-state NMR assignment of the globular domain of HET-s(1-227) prion protein in microcrystalline form. Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16964 |
0.395 |
|
| 2009 |
Wasmer C, Schütz A, Loquet A, Buhtz C, Greenwald J, Riek R, Böckmann A, Meier BH. The molecular organization of the fungal prion HET-s in its amyloid form. Journal of Molecular Biology. 394: 119-27. PMID 19748509 DOI: 10.1016/J.Jmb.2009.09.015 |
0.425 |
|
| 2009 |
Maji SK, Wang L, Greenwald J, Riek R. Structure-activity relationship of amyloid fibrils. Febs Letters. 583: 2610-7. PMID 19596006 DOI: 10.1016/J.Febslet.2009.07.003 |
0.633 |
|
| 2009 |
Maji SK, Perrin MH, Sawaya MR, Jessberger S, Vadodaria K, Rissman RA, Singru PS, Nilsson KP, Simon R, Schubert D, Eisenberg D, Rivier J, Sawchenko P, Vale W, Riek R. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science (New York, N.Y.). 325: 328-32. PMID 19541956 DOI: 10.1126/Science.1173155 |
0.605 |
|
| 2009 |
Dvir H, Lundberg ME, Maji SK, Riek R, Choe S. Mistic: cellular localization, solution behavior, polymerization, and fibril formation. Protein Science : a Publication of the Protein Society. 18: 1564-70. PMID 19475664 DOI: 10.1002/Pro.148 |
0.567 |
|
| 2009 |
Wasmer C, Benkemoun L, Sabaté R, Steinmetz MO, Coulary-Salin B, Wang L, Riek R, Saupe SJ, Meier BH. Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids. Angewandte Chemie (International Ed. in English). 48: 4858-60. PMID 19472238 DOI: 10.1002/Anie.200806100 |
0.378 |
|
| 2009 |
Stroud RM, Choe S, Holton J, Kaback HR, Kwiatkowski W, Minor DL, Riek R, Sali A, Stahlberg H, Harries W. 2007 annual progress report synopsis of the Center for Structures of Membrane Proteins. Journal of Structural and Functional Genomics. 10: 193-208. PMID 19148774 DOI: 10.1007/S10969-008-9058-3 |
0.365 |
|
| 2009 |
Siemer A, Wasmer C, Lange A, Melckebeke HV, Ernst M, Ritter C, Steinmetz M, Riek R, Meier B. Solid-state NMR assignment of the rigid core of the HET-s(218-289) prion protein in its amyloid conformation. Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr11028 |
0.423 |
|
| 2009 |
Wasmer C, Benkemoun L, Sabaté R, Steinmetz M, Coulary‐Salin B, Wang L, Riek R, Saupe S, Meier B. Festkörper‐NMR‐Spektroskopie zeigt: Die Einschlusskörperchen von HET‐s(218–289) inE. colisind Amyloide Angewandte Chemie. 121: 4952-4954. DOI: 10.1002/Ange.200806100 |
0.363 |
|
| 2008 |
Wang L, Maji SK, Sawaya MR, Eisenberg D, Riek R. Bacterial inclusion bodies contain amyloid-like structure. Plos Biology. 6: e195. PMID 18684013 DOI: 10.1371/Journal.Pbio.0060195 |
0.634 |
|
| 2008 |
Grace CRR, Erchegyi J, Reubi JC, Rivier JE, Riek R. Three-dimensional consensus structure of sst2-selective somatostatin (SRIF) antagonists by NMR. Biopolymers. 89: 1077-1087. PMID 18655144 DOI: 10.1002/Bip.21060 |
0.316 |
|
| 2008 |
Vilar M, Chou HT, Lührs T, Maji SK, Riek-Loher D, Verel R, Manning G, Stahlberg H, Riek R. The fold of alpha-synuclein fibrils. Proceedings of the National Academy of Sciences of the United States of America. 105: 8637-42. PMID 18550842 DOI: 10.1073/Pnas.0712179105 |
0.597 |
|
| 2008 |
Wasmer C, Soragni A, Sabaté R, Lange A, Riek R, Meier BH. Infectious and noninfectious amyloids of the HET-s(218-289) prion have different NMR spectra. Angewandte Chemie (International Ed. in English). 47: 5839-41. PMID 18548467 DOI: 10.1002/Anie.200704896 |
0.388 |
|
| 2008 |
Rodgers L, Gamez A, Riek R, Ghosh P. The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE. The Journal of Biological Chemistry. 283: 20857-63. PMID 18502763 DOI: 10.1074/Jbc.M802339200 |
0.338 |
|
| 2008 |
Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science (New York, N.Y.). 319: 1523-6. PMID 18339938 DOI: 10.1126/Science.1151839 |
0.444 |
|
| 2008 |
Maji SK, Schubert D, Rivier C, Lee S, Rivier JE, Riek R. Amyloid as a depot for the formulation of long-acting drugs. Plos Biology. 6: e17. PMID 18254658 DOI: 10.1371/Journal.Pbio.0060017 |
0.58 |
|
| 2008 |
Riek RP, Finch AA, Begg GE, Graham RM. Wide turn diversity in protein transmembrane helices implications for G-protein-coupled receptor and other polytopic membrane protein structure and function. Molecular Pharmacology. 73: 1092-104. PMID 18202304 DOI: 10.1124/mol.107.043042 |
0.305 |
|
| 2007 |
Grace CR, Perrin MH, Cantle JP, Vale WW, Rivier JE, Riek R. Common and divergent structural features of a series of corticotropin releasing factor-related peptides. Journal of the American Chemical Society. 129: 16102-14. PMID 18052377 DOI: 10.1021/Ja0760933 |
0.363 |
|
| 2007 |
Maslennikov I, Kefala G, Johnson C, Riek R, Choe S, Kwiatkowski W. NMR spectroscopic and analytical ultracentrifuge analysis of membrane protein detergent complexes. Bmc Structural Biology. 7: 74. PMID 17988403 DOI: 10.1186/1472-6807-7-74 |
0.345 |
|
| 2007 |
Perrin MH, Grace CR, Digruccio MR, Fischer WH, Maji SK, Cantle JP, Smith S, Manning G, Vale WW, Riek R. Distinct structural and functional roles of conserved residues in the first extracellular domain of receptors for corticotropin-releasing factor and related G-protein-coupled receptors. The Journal of Biological Chemistry. 282: 37529-36. PMID 17940290 DOI: 10.1074/Jbc.M703748200 |
0.581 |
|
| 2007 |
Grace CRR, Cervini L, Gulyas J, Rivier J, Riek R. Astressin-amide and astressin-acid are structurally different in dimethylsulfoxide. Biopolymers. 87: 196-205. PMID 17657708 DOI: 10.1002/Bip.20818 |
0.389 |
|
| 2007 |
Pegan S, Tan J, Huang A, Slesinger PA, Riek R, Choe S. NMR studies of interactions between C-terminal tail of Kir2.1 channel and PDZ1,2 domains of PSD95. Biochemistry. 46: 5315-22. PMID 17437338 DOI: 10.1021/Bi062228Q |
0.36 |
|
| 2007 |
Grace CR, Perrin MH, Gulyas J, Digruccio MR, Cantle JP, Rivier JE, Vale WW, Riek R. Structure of the N-terminal domain of a type B1 G protein-coupled receptor in complex with a peptide ligand. Proceedings of the National Academy of Sciences of the United States of America. 104: 4858-63. PMID 17360332 DOI: 10.1073/Pnas.0700682104 |
0.339 |
|
| 2007 |
Riek R. Structural investigations of ordered aggregates The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A95-E |
0.348 |
|
| 2006 |
Riek R. Cell biology: infectious Alzheimer's disease? Nature. 444: 429-431. PMID 17122841 DOI: 10.1038/444429A |
0.316 |
|
| 2006 |
Nishina KA, Deleault NR, Mahal SP, Baskakov I, Luhrs T, Riek R, Supattapone S. The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro. Biochemistry. 45: 14129-39. PMID 17115708 DOI: 10.1021/Bi061526K |
0.331 |
|
| 2006 |
Siemer AB, Arnold AA, Ritter C, Westfeld T, Ernst M, Riek R, Meier BH. Observation of highly flexible residues in amyloid fibrils of the HET-s prion. Journal of the American Chemical Society. 128: 13224-8. PMID 17017802 DOI: 10.1021/Ja063639X |
0.443 |
|
| 2006 |
Liu Y, Ritter C, Riek R, Schubert D. The formation of bioactive amyloid species by prion proteins in vitro and in cells. Neuroscience Letters. 406: 200-4. PMID 16916580 DOI: 10.1016/J.Neulet.2006.07.047 |
0.36 |
|
| 2006 |
Perrin MH, Grace CR, Riek R, Vale WW. The three-dimensional structure of the N-terminal domain of corticotropin-releasing factor receptors: sushi domains and the B1 family of G protein-coupled receptors. Annals of the New York Academy of Sciences. 1070: 105-19. PMID 16888152 DOI: 10.1196/Annals.1317.065 |
0.356 |
|
| 2006 |
Keller R, Grace CRR, Riek R. Fast multidimensional NMR spectroscopy by spin-state selective off-resonance decoupling (SITAR). Magnetic Resonance in Chemistry. 44. PMID 16823901 DOI: 10.1002/Mrc.1818 |
0.33 |
|
| 2006 |
Tzakos AG, Grace CRR, Lukavsky PJ, Riek R. NMR techniques for very large proteins and rnas in solution. Annual Review of Biophysics and Biomolecular Structure. 35: 319-342. PMID 16689639 DOI: 10.1146/Annurev.Biophys.35.040405.102034 |
0.35 |
|
| 2006 |
Siemer AB, Ritter C, Steinmetz MO, Ernst M, Riek R, Meier BH. 13C, 15N resonance assignment of parts of the HET-s prion protein in its amyloid form. Journal of Biomolecular Nmr. 34: 75-87. PMID 16518695 DOI: 10.1007/S10858-005-5582-7 |
0.385 |
|
| 2005 |
Lührs T, Ritter C, Adrian M, Riek-Loher D, Bohrmann B, Döbeli H, Schubert D, Riek R. 3D structure of Alzheimer's amyloid-beta(1-42) fibrils. Proceedings of the National Academy of Sciences of the United States of America. 102: 17342-7. PMID 16293696 DOI: 10.1073/Pnas.0506723102 |
0.376 |
|
| 2005 |
Ritter C, Maddelein ML, Siemer AB, Lührs T, Ernst M, Meier BH, Saupe SJ, Riek R. Correlation of structural elements and infectivity of the HET-s prion. Nature. 435: 844-8. PMID 15944710 DOI: 10.1038/Nature03793 |
0.438 |
|
| 2005 |
Siemer AB, Ritter C, Ernst M, Riek R, Meier BH. High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation. Angewandte Chemie (International Ed. in English). 44: 2441-4. PMID 15770629 DOI: 10.1002/Anie.200462952 |
0.452 |
|
| 2005 |
Roosild TP, Greenwald J, Vega M, Castronovo S, Riek R, Choe S. NMR structure of Mistic, a membrane-integrating protein for membrane protein expression. Science (New York, N.Y.). 307: 1317-21. PMID 15731457 DOI: 10.1126/Science.1106392 |
0.371 |
|
| 2005 |
Grace CRR, Durrer L, Koerber SC, Erchegyi J, Reubi JC, Rivier JE, Riek R. Somatostatin receptor 1 selective analogues: 4. Three-dimensional consensus structure by NMR. Journal of Medicinal Chemistry. 48: 523-533. PMID 15658866 DOI: 10.1021/Jm049518U |
0.353 |
|
| 2005 |
Siemer AB, Ritter C, Ernst M, Riek R, Meier BH. Hochauflösende Festkörper-NMR-Spektroskopie am Prionprotein HET-s in seiner amyloiden Form Angewandte Chemie. 117: 2494-2497. DOI: 10.1002/Ange.200462952 |
0.333 |
|
| 2004 |
Grace CR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, Riek R. NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor. Proceedings of the National Academy of Sciences of the United States of America. 101: 12836-41. PMID 15326300 DOI: 10.1073/Pnas.0404702101 |
0.362 |
|
| 2004 |
Ritter C, Lührs T, Kwiatkowski W, Riek R. 3D TROSY-HNCA(coded)CB and TROSY-HNCA(coded)CO experiments: triple resonance NMR experiments with two sequential connectivity pathways and high sensitivity. Journal of Biomolecular Nmr. 28: 289-294. PMID 14752261 DOI: 10.1023/B:Jnmr.0000013698.89582.Dc |
0.345 |
|
| 2003 |
Grace CRR, Erchegyi J, Koerber SC, Reubi JC, Rivier J, Riek R. Novel sst2-Selective Somatostatin Agonists. Three-Dimensional Consensus Structure by NMR Journal of Medicinal Chemistry. 49: 4487-4496. PMID 16854054 DOI: 10.1021/Jm060363V |
0.345 |
|
| 2003 |
Pegan S, Kwiatkowski W, Choe S, Riek R. High-throughput backbone resonance assignment of small 13C,15N-labeled proteins by a triple-resonance experiment with four sequential connectivity pathways using chemical shift-dependent, apparent 1J(1H,13C): HNCACBcodedHAHB. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 165: 315-9. PMID 14643715 DOI: 10.1016/J.Jmr.2003.08.012 |
0.339 |
|
| 2003 |
Kwiatkowski W, Riek R. Chemical shift-dependent apparent scalar couplings: An alternative concept of chemical shift monitoring in multi-dimensional NMR experiments Journal of Biomolecular Nmr. 25: 281-290. PMID 12766391 DOI: 10.1023/A:1023083911125 |
0.308 |
|
| 2003 |
Riek R, Lührs T. Three-dimensional structures of the prion protein and its doppel. Clinics in Laboratory Medicine. 23: 209-225. PMID 12733433 DOI: 10.1016/S0272-2712(02)00070-7 |
0.35 |
|
| 2003 |
Balguerie A, Dos Reis S, Ritter C, Chaignepain S, Coulary-Salin B, Forge V, Bathany K, Lascu I, Schmitter JM, Riek R, Saupe SJ. Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. The Embo Journal. 22: 2071-81. PMID 12727874 DOI: 10.1093/Emboj/Cdg213 |
0.406 |
|
| 2003 |
Lührs T, Riek R, Güntert P, Wüthrich K. NMR structure of the human doppel protein. Journal of Molecular Biology. 326: 1549-57. PMID 12595265 DOI: 10.1016/S0022-2836(02)01471-7 |
0.52 |
|
| 2002 |
Riek R, Fiaux J, Bertelsen EB, Horwich AL, Wuthrich K. Solution NMR techniques for large molecular and supramolecular structures. Journal of the American Chemical Society. 124: 12144-53. PMID 12371854 DOI: 10.1021/Ja026763Z |
0.496 |
|
| 2002 |
Frickel EM, Riek R, Jelesarov I, Helenius A, Wuthrich K, Ellgaard L. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proceedings of the National Academy of Sciences of the United States of America. 99: 1954-9. PMID 11842220 DOI: 10.1073/Pnas.042699099 |
0.53 |
|
| 2001 |
Riek R, Güntert P, Döbeli H, Wipf B, Wüthrich K. NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, A beta(1-40)(ox) and A beta(1-42)(ox). European Journal of Biochemistry / Febs. 268: 5930-6. PMID 11722581 DOI: 10.1046/J.0014-2956.2001.02537.X |
0.479 |
|
| 2001 |
Riek R, Pervushin K, Fernández C, Kainosho M, Wüthrich K. [(13)C,(13)C]- and [(13)C,(1)H]-TROSY in a triple resonance experiment for ribose-base and intrabase correlations in nucleic acids. Journal of the American Chemical Society. 123: 658-64. PMID 11456577 DOI: 10.1021/Ja9938276 |
0.47 |
|
| 2001 |
Wüthrich K, Riek R. Three-dimensional structures of prion proteins. Advances in Protein Chemistry. 57: 55-82. PMID 11447697 DOI: 10.1016/S0065-3233(01)57018-7 |
0.55 |
|
| 2001 |
Ellgaard L, Riek R, Herrmann T, Güntert P, Braun D, Helenius A, Wüthrich K. NMR structure of the calreticulin P-domain. Proceedings of the National Academy of Sciences of the United States of America. 98: 3133-8. PMID 11248044 DOI: 10.1073/Pnas.051630098 |
0.528 |
|
| 2001 |
Ellgaard L, Riek R, Braun D, Herrmann T, Helenius A, Wüthrich K. Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment. Febs Letters. 488: 69-73. PMID 11163798 DOI: 10.1016/S0014-5793(00)02382-6 |
0.543 |
|
| 2000 |
Riek R, Pervushin K, Wüthrich K. TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution. Trends in Biochemical Sciences. 25: 462-8. PMID 11050425 DOI: 10.1016/S0968-0004(00)01665-0 |
0.559 |
|
| 2000 |
Calzolai L, Lysek DA, Guntert P, von Schroetter C, Riek R, Zahn R, Wüthrich K. NMR structures of three single-residue variants of the human prion protein. Proceedings of the National Academy of Sciences of the United States of America. 97: 8340-5. PMID 10900000 DOI: 10.1073/Pnas.97.15.8340 |
0.578 |
|
| 2000 |
López Garcia F, Zahn R, Riek R, Wüthrich K. NMR structure of the bovine prion protein. Proceedings of the National Academy of Sciences of the United States of America. 97: 8334-9. PMID 10899999 DOI: 10.1073/Pnas.97.15.8334 |
0.58 |
|
| 2000 |
Liu A, Riek R, Wider G, von Schroetter C, Zahn R, Wüthrich K. NMR experiments for resonance assignments of 13C, 15N doubly-labeled flexible polypeptides: application to the human prion protein hPrP(23-230). Journal of Biomolecular Nmr. 16: 127-38. PMID 10723992 DOI: 10.1023/A:1008305022907 |
0.511 |
|
| 2000 |
Pervushin K, Fernández C, Riek R, Ono A, Kainosho M, Wüthrich K. Determination of h2J(NN) and h1J(HN) coupling constants across Watson-Crick base pairs in the Antennapedia homeodomain-DNA complex using TROSY. Journal of Biomolecular Nmr. 16: 39-46. PMID 10718611 DOI: 10.1023/A:1008367405025 |
0.459 |
|
| 2000 |
Zahn R, Liu A, Lührs T, Riek R, von Schroetter C, López García F, Billeter M, Calzolai L, Wider G, Wüthrich K. NMR solution structure of the human prion protein. Proceedings of the National Academy of Sciences of the United States of America. 97: 145-50. PMID 10618385 DOI: 10.1073/Pnas.97.1.145 |
0.582 |
|
| 2000 |
Liu A, Riek R, Wider G, Schroetter Cv, Zahn R, Wuthrich K. 1H, 13C and 15N chemical shift assignment of human prion protein hPrP(23-230) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4402 |
0.333 |
|
| 1999 |
Pervushin KV, Wider G, Riek R, Wüthrich K. The 3D NOESY-[(1)H,(15)N,(1)H]-ZQ-TROSY NMR experiment with diagonal peak suppression. Proceedings of the National Academy of Sciences of the United States of America. 96: 9607-12. PMID 10449740 DOI: 10.1073/Pnas.96.17.9607 |
0.47 |
|
| 1999 |
Riek R, Prêcheur B, Wang Y, Mackay EA, Wider G, Güntert P, Liu A, Kägi JH, Wüthrich K. NMR structure of the sea urchin (Strongylocentrotus purpuratus) metallothionein MTA. Journal of Molecular Biology. 291: 417-28. PMID 10438629 DOI: 10.1006/Jmbi.1999.2967 |
0.507 |
|
| 1999 |
Liu A, Riek R, Zahn R, Hornemann S, Glockshuber R, Wüthrich K. Peptides and proteins in neurodegenerative disease: helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy. Biopolymers. 51: 145-52. PMID 10397798 DOI: 10.1002/(Sici)1097-0282(1999)51:2<145::Aid-Bip4>3.0.Co;2-4 |
0.583 |
|
| 1999 |
Riek R, Wider G, Pervushin K, Wüthrich K. Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules. Proceedings of the National Academy of Sciences of the United States of America. 96: 4918-23. PMID 10220394 DOI: 10.1073/pnas.96.9.4918 |
0.423 |
|
| 1999 |
Wüthrich K, Riek R, Wider G, Garcia FL, Liu A, Zahn R, Billeter M, Hornemann S, Glockshuber R. Structural biology of prion proteins Transfusion Clinique Et Biologique. 6: 31. DOI: 10.1016/S1246-7820(99)80051-2 |
0.394 |
|
| 1998 |
Riek R, Wider G, Billeter M, Hornemann S, Glockshuber R, Wüthrich K. Prion protein NMR structure and familial human spongiform encephalopathies. Proceedings of the National Academy of Sciences of the United States of America. 95: 11667-72. PMID 9751723 DOI: 10.1073/Pnas.95.20.11667 |
0.567 |
|
| 1998 |
Glockshuber R, Hornemann S, Billeter M, Riek R, Wider G, Wüthrich K. Prion protein structural features indicate possible relations to signal peptidases. Febs Letters. 426: 291-6. PMID 9600253 DOI: 10.1016/S0014-5793(98)00372-X |
0.542 |
|
| 1998 |
Pervushin K, Riek R, Wider G, Wüthrich K. Transverse Relaxation-Optimized Spectroscopy (TROSY) for NMR Studies of Aromatic Spin Systems in13C-Labeled Proteins Journal of the American Chemical Society. 120: 6394-6400. DOI: 10.1021/Ja980742G |
0.485 |
|
| 1997 |
Korth C, Stierli B, Streit P, Moser M, Schaller O, Fischer R, Schulz-Schaeffer W, Kretzschmar H, Raeber A, Braun U, Ehrensperger F, Hornemann S, Glockshuber R, Riek R, Billeter M, et al. Prion (PrPSc)-specific epitope defined by a monoclonal antibody Nature. 390: 74-77. PMID 9363892 DOI: 10.1038/36337 |
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| 1997 |
Pervushin K, Riek R, Wider G, Wüthrich K. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proceedings of the National Academy of Sciences of the United States of America. 94: 12366-71. PMID 9356455 DOI: 10.1073/Pnas.94.23.12366 |
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| 1997 |
Riek R, Hornemann S, Wider G, Glockshuber R, Wüthrich K. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). Febs Letters. 413: 282-8. PMID 9280298 DOI: 10.1016/S0014-5793(97)00920-4 |
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| 1997 |
Hornemann S, Korth C, Oesch B, Riek R, Wider G, Wüthrich K, Glockshuber R. Recombinant full-length murine prion protein, mPrP(23-231): purification and spectroscopic characterization. Febs Letters. 413: 277-81. PMID 9280297 DOI: 10.1016/S0014-5793(97)00921-6 |
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| 1997 |
Glockshuber R, Hornemann S, Riek R, Wider G, Billeter M, Wüthrich K. Three-dimensional NMR structure of a self-folding domain of the prion protein PrP(121-231) Trends in Biochemical Sciences. 22: 241-2. PMID 9255063 DOI: 10.1016/S0968-0004(97)01070-0 |
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| 1997 |
Billeter M, Riek R, Wider G, Hornemann S, Glockshuber R, Wüthrich K. Prion protein NMR structure and species barrier for prion diseases. Proceedings of the National Academy of Sciences of the United States of America. 94: 7281-5. PMID 9207082 DOI: 10.1073/Pnas.94.14.7281 |
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| 1996 |
Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wüthrich K. NMR structure of the mouse prion protein domain PrP(121-231). Nature. 382: 180-2. PMID 8700211 DOI: 10.1038/382180A0 |
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| 1996 |
Wüthrich K, Billeter M, Güntert P, Luginbühl P, Riek R, Wider G. NMR studies of the hydration of biological macromolecules Faraday Discuss.. 103: 245-253. DOI: 10.1039/Fd9960300245 |
0.508 |
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| 1996 |
Wider G, Riek R, Wüthrich K. Diffusion filters for separation of solvent-protein and protein-protein nuclear Overhauser effects (HYDRA) Journal of the American Chemical Society. 118: 11629-11634. DOI: 10.1021/Ja9607188 |
0.514 |
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