(151)    Xue, K., Sarkar, R., Tosner, Z., Reif, B. Field and magic angle spinning frequency dependence of proton resonances in rotating solids. doi: 10.1016/j.pnmrs.2022.04.001, Prog. Nucl. Magn. Reson. 130, 45-59 (2022).

(150)    Reif, B., Deuteration for High-Resolution Detection of Protons in Protein Magic Angle Spinning (MAS) Solid-State NMR, 10.1021/acs.chemrev.1c00681, Chem. Rev. 122, 10019-10035 (2022).

(149)    Ozparpucu, M., Sanchez-Ferrer, A., Schuh, M., Wilhelm, B., Sarkar, R., Reif, B., Windeisen-Holzhauser, E., Richter, K., Acidic wood extractives accelerate the curing process of emulsion polymer isocyanate adhesives. doi: 10.1002/app.52189, J. Appl. Polym. Sci. 139, e52189 (2022).

(148)    Sahoo, B.R., Souders, C.L., Watanabe-Nakayama, T., Deng, Z., Linton, H., Suladze, S., Ivanova, M.I., Reif, B., Ando, T., Martyniuk, C.J., Ramamoorthy, A., Conformational Tuning of Amylin by Charged Styrene-Maleic-Acid Copolymers, doi: 10.1016/j.jmb.2021.167385; J. Mol. Biol. 434, e167385 (2022)

(147)    Mühlhofer, M.; Peters, C.; Kriehuber, T.; Kreuzeder, M.; Kazman, P.; Rodina, N.; Reif, B.; Haslbeck, M.; Weinkauf, S.; Buchner, J. Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble, doi: 10.1038/s41467-021-27036-7, Nat. Commun. 12, e6697 (2021).

(146)    Tošner, Z.; Brandl, M. J.; Blahut, J.; Glaser, S. J.; Reif, B., Maximizing efficiency of dipolar recoupling in solid-state NMR using optimal control sequences, doi: 10.1126/sciadv.abj5913, Sci. Adv. 7, eabj5913 (2021).

(145)    Schonfelder, J.; Pfeiffer, P. B.; Pradhan, T.; Bijzet, J.; Hazenberg, B. P. C.; Schonland, S. O.; Hegenbart, U.; Reif, B.; Haupt, C.; Fandrich, M. Protease resistance of ex vivo amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies, doi: 10.1080/13506129.13502021.11960501, Amyloid 28(4), 243-251 (2021).

(144)    Reif, B., Ashbrook, S.E., Emsley, L., Hong, M., Solid-state NMR spectroscopy, doi: 10.1038/s43586-020-00004-z, Nature Reviews Methods Primers 1: e2 (2021).

(143)    Pradhan, T., Annamalai, K., Weber, B., Sarkar, R., Hegenbart, U., Schönland, S., Buchner, J., Fändrich, M., Reif, B., Seeded fibrils of the germline variant of human λ-III immunoglobulin light chain FOR005 have a similar core as patient fibrils with reduced stability, doi: 10.1074/jbc.RA120.016006, J. Biol. Chem. 295: 18474–18484 (2020).
(142)    Weber, B., Hora, M., Kazman, P., Pradhan, T., Rührnößl, F., Reif, B., Buchner, J., Domain interactions determine the amyloidogenicity of antibody light chain mutants, doi: 10.1016/j.jmb.2020.10.005, J. Mol. Biol. 432: 6187-6199 (2020). 

(141)    Xue, K., Sarkar, R., Lalli, D., Koch, B., Pintacuda, G., Tošner, Z., Reif, B., Impact of the magnetic field strength on sensitivity and resolution of proton resonances in biological solids, doi: 10.1021/acs.jpcc.0c05407, J. Phys. Chem. C 124, 41, 22631-22637 (2020). 

(140)    Cox, S.J., Rodriguez Camargo, D.C., Lee, Y.-H., Dubini, R.C.A., Rovó, P., Ivanova, M.I., Padmini, V., Reif, B., Ramamoorthy, A. Small molecule induced toxic human-IAPP species characterized by NMR, doi: 10.1039/d0cc04803h, Chem. Commun. 56 (86), 13129-13132 (2020). 

(139)    Pradhan, T., Annamalai, K., Sarkar, R., Hegenbart, U., Schönland, S., Fändrich, M., Reif, B., Solid state NMR assignments of a human λ-III immunoglobulin light chain amyloid fibril, doi 10.1007/s12104-020-09975-2, Biol. NMR Assign. in press (2020).

(138)    Niu, Z., Sarkar, R., Aichler, M., Wester, H.-J., Yousefi, B.H., Reif B., Mapping of the binding interface of PET tracer molecules and Alzheimer Disease Aβ fibrils using MAS solid-state NMR, doi: 10.1002/cbic.202000143, ChemBioChem. 21(17): 2495-2502 (2020).

(137)    Niu, Z., Prade, E., Malideli, E., Hille, K., Jussupow, A., Mideksa, Y.G., Yan, L.-M., Qian, C., Fleisch, M., Messias, A.C., Sarkar, R., Sattler, M., Lamb, D.C., Feige, M., Camilloni, C., Kapurniotu, A., Reif B., Interaction Surface Mimic (ISM) Structural insight into IAPP-derived amyloid inhibitors and their mechanism of action, doi: 10.1002/anie.201914559, Angew. Chem. Int. Ed. 59(14): 5771 – 5781 (2020). 

(136)    Göbl, C., Morris, V.K., van Dam, L., Visscher, M., Polderman, P.E., Hartlmüller, C., de Ruiter, H., Hora, M., Birner-Gruenberger, R., Vos, H.R., Reif, B., Madl, T., Dansen, T.B., Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A, doi: 10.1016/j.redox.2019.101316, Redox Biology 28, e101316 (2020). 
(135)    Asami, S., Reif, B., Accessing methyl groups in proteins via 1H-detected MAS solid-state NMR spectroscopy employing random protonation, doi: 10.1038/s41598-019-52383-3, Sci. Rep. 9, e15903 (2019). 

(134)    Kaiser, C., Peters, C., Schmid, P.W.N., Stavropoulou, M., Zou, J., Mymrikow, E., Rockel, B., Asami, S., Haslbeck, M., Rappsilber, J., Reif, B., Zacharias, M., Buchner, J., Weinkauf, S., The structure and oxidation of the eye lens chaperone αA-crystallin, doi: 10.1038/s41594-019-0332-9, Nature Struct. Mol. Biol. 26(12):1141-1150 (2019). 

(133)    Xue, K., Sarkar, R., Tošner, Z., Lalli, D., Motz, C., Koch, B., Pintacuda, G., Reif, B., MAS dependent Sensitivity of different Isotopomers in selectively methyl protonated Protein Samples in solid State NMR, doi: 10.1007/s10858-019-00274-0, J. Biomol. NMR 73(10-11): 625-631 (2019).

(132)    Xue, K., Mamone, S., Koch, B., Sarkar, R., Reif, B., Determination of methyl order parameters using solid state NMR under off magic angle spinning, doi: 10.1007/s10858-019-00253-5, J. Biomol. NMR 73: 471-475 (2019).

(131)    Brender, J.R., Ghosh, A., Kotler, S.A., Krishnamoorthy, J., Bera, S., Morris, V., Sil, T.B., Garai, K., Reif, B., Bhunia, A., Ramamoorthy, A., Probing transient non-native states in amyloid beta fiber elongation by NMR, doi: 10.1039/c9cc01067j, Chem. Commun. 55(31): 4483-4486 (2019).

(130) Xue, K., Mühlbauer, M., Mamone, S., Sarkar, S., Reif, B., Accurate determination of 1H-15N dipolar couplings using inaccurate settings of the Magic Angle in solid-state NMR, doi: 10.1002/anie.201814314, Angew. Chem. Int. Ed. Engl. 58: 4286-4290 (2019).

(129) Weber, B., Hora, M., Kazman, P., Göbl, C., Camilloni, C., Reif, B., Buchner, J., The antibody light chain linker is an important regulator for the orientation and stability of the two constituent domains, doi: 10.1016/j.jmb.2018.1010.1024, J. Mol. Biol. 430: 4925–4940 (2018).

(128) Weber, B., Brandl, M.J., Pulido-Cendales, M.D., Berner, C., Feind, G.M., Pradhan, T., Zacharias, M., Reif, B., Buchner, J., Principles of antibody domain integrity revealed by a single residue switch. 10.1074/jbc.RA118.005475 J. Biol. Chem. 293: 17107-17118 (2018).

(127) Tošner, Z., Sarkar, R., Becker-Baldus, J., Glaubitz, C., Wegner, S., Engelke, F., Glaser, S.J., Reif, B., Overcoming volume selectivity of dipolar recoupling in biological solid-state NMR, doi: 10.1002/anie.201805002, Angew. Chem. Int. Ed. 57, 14514-14518 (2018).

(126) Xue, K., Sarkar, R., Motz, C., Asami, S., Decker, V., Wegner, S., Tošner, Z., Reif, B., MAS rotations frequencies beyond 300 kHz are necessary to yield maximum sensitivity in selectively methyl protonated protein samples, doi: 10.1021/acs.jpcc.8b05600, J. Phys. Chem. C 122, 16437-16442 (2018).

(125) Cristóvão, J.S., Morris, V., Cardoso, I., Leal, S.S., Fernandez, J., Botelho, H.M., David, R., Göbl, C., Kierdorf, K., Madl, T., Fritz, G., Reif, B., Gomes, C.M., A new role for S100B in amyloid-β aggregation, doi: 10.1126/sciadv.aaq1702, Sci. Adv. 4, eaaq1702 (2018).

(124) Rodriguez Camargo, D.C., Garg, D., Buday, K., Franko, A., Rodriguez Camargo, A., Schmidt, F., Cox, S.J., Suladze, S., Haslbeck, M., Mideksa, Y.G., Gemmecker, G., Aichler, M., Mettenleiter, G., Schulz, M., Walch, A.K., Hrabě de Angelis, M., Feige, M.F., Sierra, C.A., Conrad, M., Tripsianes, K., Ramamoorthy, A., Reif, B., hIAPP forms toxic oligomers in plasma, doi: 10.1039/C8CC03097A, Chem. Commun. 54, 5426-5429 (2018).

(123) Barbet-Massin, E., van der Sluis, E., Musial, J., Beckmann, R., Reif, B., Reconstitution of isotopically labeled ribosomal protein L29 in the 50S large ribosomal subunit for solution-state and solid-state NMR, doi: 10.1007/978-1-4939-7759-8_6, Methods Mol. Biol. 1764, 87-100 (2018).

(122) Close, W., Neumann, M., Schmidt, A., Hora, M., Annamalai, K., Schmidt, M., Reif, B., Schmidt, V., Grigorieff, N., Faendrich, M., Physical basis of amyloid fibril polymorphism, doi: 10.1038/s41467-018-03164-5, Nature Commun. 9 e699 (2018).

(121) Franko, A., Rodriguez Camargo, D.C., Böddrich, A., Carg, D., Rodriguez Camargo, A., Rozman, J., Rathkolb, B., Janik, D., Aichler, M., Feuchtinger, A., Neff, F., Fuchs, H., Wanker, E.E., Reif, B., Häring, H.-U., Peter, A., Hrabě de Angelis, M., Green tea extract epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice, 10.1038/s41598-017-18807-8, Sci. Rep. 8 (1), 1116 (2018).

(120) Rodriguez Camargo, D.C. Korshavn, K., Jussupow, A., Raltchev, K., Goricanec, D., Camilloni, C., Sarkar, R., Xue, K., Aichler, M., Mettenleiter, M., Walch, A.K., Hagn, F., Reif, B., Ramamoorthy, A., Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate, doi: 10.7554/eLife.31226, eLife 6, e31226 (2017).

(119) Asami, S., Reif, B., Comparative study of REDOR and CPPI derived order parameters by 1H-detected MAS NMR and MD Simulations, doi: 10.1021/acs.jpcb.7b06812, J. Phys. Chem. B 121, 8719–8730 (2017).

(118) Tošner, Z., Purea, P., Wegner, S., Engelke, F., Glaser, S.J., Reif, B., Radiofrequency fields in solid state MAS probes, doi: 10.1016/j.jmr.2017.09.002, J. Magn. Reson. 284, 20-32 (2017).

(117) Xue, K., Sarkar, R., Motz, C., Rodriguez Camargo, D. C., Decker, V., Wegner, S., Asami, S., Tosner, Z., Reif, B., Comparison of deuterated and protonated microcrystalline protein samples at a MAS frequency of 110 kHz, doi: 10.1038/s41598-017-07253-1, Sci. Rep. 7, 7444 (2017).

(116) Hora, M., Sarkar, R., Morris, V., Xue, K., Prade, E., Harding, E., Buchner, J., Reif, B., Antibody light chain fibrils are similar to oligomeric precursors, doi: 10.1371/journal.pone.0181799, PloSOne 12(7), e0181799 (2017).

(115) Rodriguez Camargo, D.C., Tripsianes, K., Buday, K., Franko, A., Goebl, C., Hartlmueller, C., Sarkar, R., Aichler, M., Mettenleiter, G., Schulz, M., Boeddrich, A., Erck, C., Martens, H., Walch, A. K., Madl, T., Wanker, E. E., Conrad, M., Hrabě de Angelis, M., Reif, B., The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes, doi 10.1038/srep44041, Sci. Rep. 7, 44041 (2017).

(114) Hora, M., Carballo-Pacheco, M., Weber, B., Buchner, J., Strodel, B., Reif, B., Solid- and solution-state nuclear magnetic resonance spectroscopic studies on antibody light chain amyloid formation and interactions with epigallocatechin gallate, doi: 10.1080/13506129.2016.1269736, Amyloid 24, 10 (2017)

(113) Hora, M., Carballo-Pacheco, M., Weber, B., Morris, V., Wittkopf, A., Buchner, J., Strodel, B., Reif, B., Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains, doi 10.1038/srep41515, Sci. Rep. 7, 41515 (2017).

(112) Prade, E., Barucker, C., Sarkar, R., Althoff-Ospelt, G., Lopez del Amo, J.M., Multhaup, G., Reif, B., Sulindac Sulfide induces the formation of large oligomeric aggregates of the Alzheimer’s Disease Amyloid-β Peptide which exhibit reduced Neurotoxicity, doi 10.1021/acs.biochem.5b01272, Biochemistry 55, 1839–1849 (2016).

(111) Nokwe, C.N., Hora, M., Zacharias, M., Hisashi, Y., Peschek, J., Reif, B., Goto, Y., Buchner, J., A stable mutant predisposes antibody domains to amyloid formation through specific non-native interactions, doi 10.1016/j.jmb.2016.01.015, J. Mol. Biol. 216 1315-1332 (2016).

(110) Sarkar, R., Mainz, A., Busi, B., Barbet-Massin, E., Kranz, M., Hofmann, T., Reif, B., Immobilization of Soluble Protein Complexes in MAS solid-state NMR: Sedimentation versus Viscosity, Solid-State Nucl. Magn. Reson. 76-77, 7-14 (2016).

(109) Sarkar, R., Rodriguez Camargo, D.C., Reif, B., Spin-state selective 15N,1H correlation experiments in solid-state NMR to retain resolution under off-magic angle conditions, J. Phys. Chem. Lett. 6, 5040-5044 (2015).

(108) Prade, E., Bittner, H., Sarkar, R., Lopez del Amo, J.-M., Althoff-Ospelt, G., Multhaup, G., Hildebrand, P., Reif, B., Structural mechanism of the interaction of Alzheimer's disease Aβ fibrils with the NSAID sulindac sulfide, J. Biol. Chem. 290, 28737-28745 (2015).

(107) Nokwe, C.N., Hora, M., Zacharias, M., Hisashi, Y., John, C., Reif, B., Goto, Y., Buchner, J., The antibody light chain linker is important for domain stability and amyloid formation, J. Mol. Biol. 427, 3572-3586 (2015).

(106) Mainz, A., Peschek, J., Stavropoulou, M., Back, K., Bardiaux, B., Asami, S., Prade, E., Peters, C., Weinkauf, S., Buchner, J., Reif, B., The Molecular Chaperone αB­Crystallin Deploys Different Interfaces to Capture an Amorphous and an Amyloid Client, Nature Struct. Mol. Biol. 22, 898-905 (2015).

(105) Andreetto, E., Malideli, Yan, L.-M., Kracklauer, M., Farbiarz, K., Tatarek-Nossol, M., Rammes, G., Prade, E., Caporale, A., Spanopoulou, A., Bakou, M., Reif, B., Kapurniotu, A. A hot segment-based approach to design cross-amyloid interaction surface mimics as inhibitors of amyloid self-assembly, Angewandte Chemie Int. Edt. Engl. 54, 13095-13100 (2015).

(104) Barbet-Massin, E., Huang, C.-T., Daebel, V., Hsu, S.-T.D., Reif, B., Site-specific Solid-state NMR Studies of Trigger Factor in Complex with the Large Ribosomal Subunit 50S, doi: 10.1002/anie.201409393 Angewandte Chemie Int. Edt. Engl. 54 4367-4369 (2015).

(103) Chevelkov, V., Xiang, S., Giller, K., Becker, S., Lange, A., Reif, B., Perspectives for sensitivity enhancement in proton detected solid-state NMR of highly deuterated proteins by preserving water magnetization, J. Biomol. NMR 61 151-160 (2015).

(102) Asami, S., Porter, J., Lange, O.F., Reif, B., Access to Cα Backbone Dynamics of Biological Solids by 13C T1 and MD Simulations, J. Am. Chem. Soc. 137, 1094-1100 (2015).

(101) Rodriguez Camargo, D.C., Tripsianes, K., Kapp, T., Mendes, J., Schubert, J., Cordes, C., Reif, B., Cloning, expression and purification of the human hormone Islet Amyloid Polypeptide (hIAPP) from Escherichia coli, Protein Expr. Purif. 106, 49-56 (2015).

(100) Krushelnitzky, A., Zinkevich, Reif, B., Saalwächter, K., Slow motions in micro-crystalline proteins as observed by MAS-dependent 15N rotating-frame NMR relaxation, doi: 10.1016/j.jmr.2014.09.007, J. Magn. Reson. 248 8-12 (2014). (99) Nokwe, C.N., Zacharias, M., Yagi, H., Hora, M., Reif, B., Goto, Y., Buchner, J., A residue-specific shift in stability and amyloidogenicity of antibody variable domains, J. Biol. Chem. 289 26829-26846 (2014).

(98) Lopez del Amo, J.M., Agarwal, V., Sarkar, R., Porter, J., Asami, S., Rübbelke, M., Fink, U., Lange, O.F., Reif, B., Site-specific analysis of heteronuclear NOE effects in microcrystalline proteins, J. Biomol. NMR 59 241-249 (2014).

(97) Linser, R., Sarkar, R., Mainz, A., Reif, B., Dynamics in the Solid-State: Perspectives for the Investigation of Amyloid Aggregates, Membrane Proteins and Soluble Protein Complexes, J. Biomol. NMR 59 1-14 (2014).

(96) Prade, E., Lopez del Amo, J.-M., Reif, B., Advances in Biological Solid-State NMR: NMR studies of small molecules interacting amyloidogenic proteins, Separovic, F., and Naito, A., (Eds.), The Royal Society of Chemistry, Cambridge, pp 533-555 (2014).

(95) 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, J. Am. Chem. Soc. 135, 1884-18891 (2013).

(94) Zinkevich, T., Chevelkov, V., Reif, B., Saalwächter, K., Krushelnitzky, A., Multi-frequency 15N solid-state NMR relaxation analysis of protein dynamics validates motional models and offers surprising sensitivity to slow motions with very high order parameters, J. Biomol. NMR 57, 219-235 (2013).  

(93) Asami, S., Reif, B., Proton-detected solid-state NMR at aliphatic sites: Applications to Crystalline Systems, Acc. Chem. Res. 46 (9), 2089-2097 (2013).

(92) Lopez del Amo, J.M., Schneider, D., Lange, A., Reif, B., Field Cryogenic solid-state NMR studies of fibrils of the Alzheimer's disease amyloid-β peptide: Perspectives for DNP, J. Biomol. NMR 56, 359-363 (2013).  

(91) Mainz, A., Religa, T., Sprangers, R., Linser, R., Kay, L.E., Reif, B., Proton detection of MDa sized protein complexes in solution by MAS solid-state NMR, Angewandte Chemie Int. Edt. 52, 8746-8751 (2013).  

(90) Agarwal, V., Linser, R., Dasari, M., Fink, U., Lopez del Amo, J.M., Reif, B., Hydrogen bonding involving side chain exchangeable groups stabilizes amyloid quarternary structure, Phys. Chem. Chem. Phys. 15, 12551-12557 (2013).  

(89) Ravera, E., Parigi, G., Mainz, A., Religa, T. L., Reif, B., Luchinat, C., Experimental Determination of Microsecond Reorientation Correlation Times in Protein Solutions, J. Phys. Chem. B 117, 3548-3553 (2013).  

(88) Asami, S., Rakwalska-Bange, M., Carlomagno, T., Reif, B., Protein/RNA interfaces probed by 1H detected MAS solid-state NMR, Angewandte Chemie Int. Edt. Engl. 52 2345-2349 (2013).

(87) Asami, S., Szekely, K., Schanda, P., Meier, B.H., Reif, B., Optimal degree of protonation for 1H detection of aliphatic sites as a function of the MAS frequency, J. Biomol. NMR 54 155-168 (2012).

(86) Lopez del Amo, J.M., Dasari, M., Fink, U., Grelle, G., Wanker, E.E., Bieschke, J., Reif, B., Structural analysis of Alzheimer disease beta-amyloid oligomers induced by the green tea compound epigallocatechin-3-gallate (EGCG), J. Mol. Biol. 421 517-524 (2012).

(85) Lopez del Amo, J.M., Schmidt, M., Fink, U., Dasari, M., Fändrich, M., Reif, B., An asymmetric dimer can be the basic subunit in Alzheimer's disease β-amyloid fibrils, Angewandte Chemie Int. Edt. Engl. 51 6136-6139 (2012).

(84) Jacso, T., Schneider, E., Rupp, B., Reif, B., Substrate transport activation is mediated through the second periplasmic loop P2 of MalF in the maltose transport complex of Escherichia coli, J. Biol. Chem. 287 17040-17049 (2012).

(83) Reif, B., Ultra-high resolution in MAS solid-state NMR of perdeuterated proteins: Implications for Structure and Dynamcis, J. Magn. Reson. 216 1-12 (2012).

(82) Kaden, D., Munter, L.-M., Reif B., Multhaup, G., The Amyloid Precursor Protein and its homologues: Structural and functional aspects of native and pathogenic oligomerization, Eur. J. Cell Biol. 91 234-239 (2012).

(81) Asami, S., Reif, B., Assignment strategies for aliphatic protons in the solid-state in randomly protonated proteins, J. Biomol. NMR 52 31-39 (2012).

(80) Mainz, A., Bardiaux, B., Kuppler, F., Multhaup, G., Felli, I., Pierattelli, R., Reif, B., Strcutural and mechanistic implications of metal-binding in the small heat shock protein αB-crystallin, J. Biol. Chem. 287 1128-1138 (2012).

(79) Bieschke, J., Herbst, M., Wiglenda, T., Friedrich, R., Boeddrich, A., Schiele, F., Kleckers, D., Lopez del Amo, J.M., Gruening, B., Wang, Q., Schmidt, M., Lurz, R., Anwyl, R., Schnoegl, S., Fändrich, M., Frank, R., Reif, B., Guenther, S., Walsh, D., Wanker, E.E., Small-molecule conversion of toxic oligomers to non-toxic β-sheet-rich amyloid fibrils, Nature Chem. Biol. 8 93-101 (2012).

(78) Jacso, T., Franks, T.W., Rose, H.M., 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 Int. Edt. 51 432-435 (2012).

(77) Lalli, D., Schanda, P., Chowdhury, A., Retel, J., Hiller, M., Agarwal, V., Reif, B., van Rossum, B., Akbey, U., Oschkinat, H., Three-Dimensional Deuterium-Carbon Correlation for High-Resolution Solid-State MAS NMR Spectroscopy of Large Proteins, J. Biomol. NMR. 51 477-485 (2011).

(76) Bertini, I., Luchinat, C., Parigi, G., Ravera, E., Reif, B., Turano, P., Solid-state NMR of proteins sedimented by ultracentrifugation, Proc. Natl. Acad. Sci. U.S.A. 108 10396-10399 (2011).

(75) Wei, D., Akbey, U., Paaske, B., Oschkinat, H., Reif, B., Bjerring, M., Nielsen, N.C., Optimal 2H Rf Pulses and 2H,13C Cross-Polarization Methods for Solid-State 2H MAS NMR of Perdeuterated Proteins, J. Phys. Chem. Lett. 2 1289-1294 (2011).  

(74) Linser, R., Dasari, M., Hiller, M., Higman, V., Fink, U., Lopez del Amo, J.-M., Handel, L., Kessler, B., Schmieder, P., Oesterhelt, D., Oschkinat, H. & Reif, B., Proton detected solid-state NMR of fibrillar and membrane proteins, Angewandte Chemie Int. Edt. 50 4508-4512 (2011).

(73) Linser, R., Bardiaux, B., Higman, V., Fink, U., Reif, B., Structure calculation from unambiguous long-range amide and methyl 1H-1H distance restraints for a micro-crystalline protein with MAS solid-state NMR spectroscopy, J. Am. Chem. Soc. 133 5905-5912 (2011).

(72) Christian, F., Szaszák, M., Friedl, S., Drewianka, S., Lorenz, D., Goncalves, A., Furkert, J., Vargas, C., Schmieder, P., Götz, F., Zühlke, K., Moutty, H., Göttert, H., Joshi, M., Reif, B., Haase, H., Morano, I., Solveig, G., Klukovit, A., Verli, J., Gaspar, R., Noack, C., Bergmann, M., Kass, R., Hampel, K., Kashin, D., Genieser, H.-G., Herberg, F. W., Willoughby, D., Cooper, D. M. F., Baillie, G. S., Houslay, M. D., von Kries, J. P., Zimmermann, B., Rosenthal, W., Klussmann, E., Small molecule AKAP/PKA interaction disruptors that activate PKA interfere with compartmentalized cAMP signaling in cardiac myocytes, J. Biol. Chem. 286 (11) 9079-9096 (2011).

(71) Dasari, M., Espargaro, A., Sabate, R., Lopez del Amo, J.-M., Fink, U., Grelle, G., Bieschke, J., Ventura, S., Reif, B., Bacterial Inclusion Bodies of the Alzheimer Disease beta-Amyloid Peptides can be employed to study Native like Aggregation Intermediate States, ChemBioChem. 12 407-423 (2011).

(70) Lopez del Amo, J.-M., Fink, U., Reif, B., Quantification of Protein Backbone Hydrogen-Deuterium Exchange Rates by MAS solid-state NMR Spectroscopy, J. Biomol. NMR 48, 203-212 (2010).

(69) Asami, S., Schmieder, P., Reif, B., High resolution 1H-detected solid-state NMR spectroscopy of protein aliphatic resonances: Access to tertiary structure information, J. Am. Chem. Soc. 132, 15133-15135 (2010).

(68) Krushelnitsky, A., Zinkevich, T., Reichert, D., Chevelkov, V., Reif B., Microsecond time scale mobility in a solid protein as studied by the 15N R1 site-specific NMR relaxation rates, J. Am. Chem. Soc. 132, 11850-11853 (2010).

(67) Richter, L., Munter, L.-M., Ness, J., Hildebrand, P.W., Dasari, M., Unterreitmeier, S., Bulic, B., Beyermann, M., Gust, R., Reif, B., Weggen, S., Langosch, D., Multhaup, G., Aß42-lowering compounds directly bind to Aß and interfere with APP transmembrane dimerization, Proc. Natl. Acad. Sci. USA 107, 14597–14602 (2010).

(66) Linser, R., Fink, U., Reif, B., Detection of dynamic regions in biological solids enabled by spin-state selective NMR experiments, J. Am. Chem. Soc. 132 8891–8893 (2010).

(65) Linser, R., Fink, U., Reif, B., Narrow Carbonyl Resonances in Proton-Diluted Proteins facilitate NMR Assignments in the Solid-State, J. Biomol. NMR 47, 1-6 (2010).

(64) Chevelkov, V., Xue, Y., Linser, R., Skrynnikov, N.R., Reif, B., Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics, J. Am. Chem. Soc. 132, 5015-5017 (2010).

(63) Agarwal, V., Linser, R., Fink, U., Faelber, K., Reif, B., Identification of Hydroxyl Protons, Determination of their Exchange Dynamics, and Characterization of Hydrogen Bonding by MAS solid-state NMR spectroscopy in a Microcrystalline Protein, J. Am. Chem. Soc. 132, 3187–3195 (2010).

(62) Hundsrucker, C., Skroblin, P., Christian, F., Zenn, M., Popara, V., Joshi, M., Eichhorst, J., Wiesner, B., Herberg, F. W., Reif, B., Rosenthal, W., Klussmann, E., Glycogen synthase kinase 3β interaction protein functions as an A-kinase anchoring protein, J. Biol. Chem. 285, 5507-5521 (2010).  

(61) Akbey, Ü., Lange, S., Franks, T.W., Linser, R., Diehl, A., van Rossum, B.-J., Reif, B., Oschkinat, H., Optimum Levels of Exchangeable Protons in Perdeuterated Proteins for Proton Detection in MAS Solid-State NMR Spectroscopy, J. Biomol. NMR 46, 67-73  (2010).

(60) Mainz, A., Jehle, S., van Rossum, B.-J., Oschkinat, H., Reif, B., Large Soluble Protein Complexes with Extreme Rotational Correlation Times investigated by MAS Solid-State NMR J. Am. Chem. Soc. 131, 15968-15969 (2009).

(59) Chevelkov, V., Fink, U., Reif, B., Accurate Determination of Order Parameters from 1H, 15N dipolar couplings in MAS solid-state NMR experiments, J. Am. Chem. Soc. 131, 14018-14022 (2009).

(58) Linser, R., Fink, U., Reif, B., Probing Surface Accessibility using Paramagnetic Relaxation in Solid-State NMR, J. Am. Chem. Soc. 131, 13703-13708 (2009).

(57) Chevelkov, V., Fink, U., Reif, B., Quantitative Analysis of Backbone Motion in Proteins using MAS solid-state NMR spectroscopy, J. Biomol. NMR 45 197–206  (2009).

(56) Krushelnitsky, A., de Azevedo, E., Linser, R., Reif, B., Saalwächter, K., Reichert, D., Direct Observation of Millisecond to Second Motions in Proteins by Dipolar CODEX NMR, J. Am. Chem. Soc. 131 12097–12099 (2009).  

(55) Thoms, S., Max, K.E.A., Wunderlich, M., Jacso, T., Lilie, H., Reif, B., Heinemann, U., Schmid, F. X., Dimer formation of a stabilized Gß1 variant. A structural and energetic analysis. J. Mol. Biol. 391 (5) 918-932 (2009).

(54) Jacso, T., Grote, M., Daus, M. L., Keller, S., Schneider, E., Reif, B. The perplasmic loop P2 of the MalF subunit of the ATP binding cassette maltose transporter is sufficient to bind the maltose transport protein MBP. Biochemistry 48 (10) 2216-2225 (2009).

(53) Jacso, T., Grote, M., Schneider, E., Reif, B., NMR assignments of the second periplasmic loop of the MalF subunit of the maltose ATP binding cassette transporter Biomol. NMR Assignments 3 (1) 21-23 (2009).

(52) Agarwal, V., Faelber, K., Schmieder, P., Reif, B., High Resolution Double Quantum Deuterium MAS solid-state NMR Spectroscopy of Perdeuterated Proteins, J. Am. Chem. Soc. 131 (1) 2-3 (2009).

(51) Agarwal, V., Xue, Y., Reif, B., Skrynnikov N.R., Protein side-chain dynamics as observed by solution- and solid-state NMR: a similarity revealed. J. Am. Chem. Soc. 130, 16611-16621 (2008).

(50) Agarwal, V., Reif, B., Residual Methyl Protonation in Perdeuterated Proteins for Multidimensional Correlation Experiments in MAS solid-state NMR Spectroscopy, J. Magn. Res. 194 (1) 16-24 (2008).

(49) Linser, R., Fink, U., Reif, B., Proton-detected Scalar Coupling based Assignment Strategies in MAS Solid-State NMR Spectroscopy applied to Perdeuterated Proteins, J. Magn. Reson. 193 (1) 89-93 (2008).

(48) Chevelkov, V., Reif, B., TROSY effects in MAS solid-state NMR, Concepts Magn. Reson. A 32 (2), 143-156 (2008).

(47) Kaden, D., Munter, L.-M., Joshi, M., Treiber, C., Weise, C., Beyermann, M., Reif, B., Multhaup, G., Homophilic interactions of the APP ectodomain are regulated by the loop-region and affect ß-secretase cleavage of APP, J. Biol. Chem. 283 (11) 7271-7279 (2008).

(46) Chevelkov, V., Diehl, A., Reif, B., Measurement of 15N- T1 Relaxation Rates in a Perdeuterated Protein by MAS Solid-State NMR Spectroscopy, J. Chem. Phys. 128 052316-1-5 (2008).

(45) Agarwal, V., Fink, U., Schuldiner, S., Reif, B., MAS Solid-State NMR Studies on the Multidrug Transporter EmrE, Biochim. Biophys. Acta - Biomembranes 1768, 3036-3043 (2007).

(44) Chevelkov, V., Diehl, A., Reif, B., Measurement of Differential 15N-Hα/β T2 Relaxation Times in a Perdeuterated Protein by MAS Solid-State NMR, Mag. Res. Chem. 45 (S1) S156-S160 (2007).

(43) Linser, R., Chevelkov, V., Diehl, A., Reif, B., Sensitivity Enhancement Using Paramagnetic Relaxation in MAS Solid State NMR of Perdeuterated Proteins, J. Magn. Reson. 189, 209-216 (2007).

(42) Chevelkov, V., Zhuravleva, A. V., Xue, Y., Reif, B., Skrynnikov, N. R., Combined Analysis of 15N Relaxation Data from Solid- and Solution-State NMR Spectroscopy, J. Am. Chem. Soc. 129, 12594-12595 (2007).

(41) Chevelkov, V., Faelber, K., Schrey, A., Rehbein, K., Diehl, A., Reif, B., Differential Line Broadening in MAS solid-state NMR due to Dynamic Interference, J. Am. Chem. Soc. 129, 10195-10200 (2007).

(40) Xue, Y., Pavlova, M. S., Ryabov, Y. E., Reif, B., Skrynnikov, N. R., Methyl rotation barriers in proteins from 2H relaxation data. Implications for protein structure, J. Am. Chem. Soc. 129, 6827-6838  (2007).

(39) Narayanan, S., Kamps, B., Boelens, W., Reif, B., αB-crystalline competes with Alzheimer's disease beta-amyloid peptide for peptide-peptide interactions and induces oxidation of Abeta-Met35, FEBS Lett. 580, 5941-5946 (2006).  

(38) Heller, M., Sukopp, M., Tsomaia, N., John, M., Mierke, D. F., Reif, B., Kessler, H., The Conformation of Cyclo(−D-Pro−Ala4−) as a Model for Cyclic Pentapeptides of the DL4 Type, J. Am. Chem. Soc. 128, 13806-13814 (2006).

(37) Agarwal, V., Diehl, A., Skrynnikov, N., Reif, B., High resolution proton detected proton-carbon correlation spectra of a protein in MAS solid-state NMR spectroscopy, J. Am. Chem. Soc. 128, 12620-12621 (2006).

(36) Reif, B., Xue, Y., Agarwal, V., Pavlova, M. S., Hologne, M., Diehl, A., Ryabov, Y. E., Skrynnikov, N. R., Protein Side-Chain Dynamics Observed by Solution- and Solid-state NMR: Comparative Analysis of Methyl 2H Relaxation Data, J. Am. Chem. Soc. 128, 12354-12355 (2006).

(35) Chevelkov, V., Rehbein, K., Diehl, A., Reif, B., Ultra-high resolution in solid-state NMR at high levels of deuteration, Angewandte Chem. Int. Edt. 45, 3878-3881 (2006).

(34) Narayanan, S., Walter, S., Reif, B., Yeast prion protein, Sup35, fibril formation proceeds by addition and substraction of oligomers, ChemBioChem. 7, 757-765 (2006).

(33) Hologne, M., Chen, Z., Reif, B., Characterization of dynamic processes using deuterium in uniformly 2H,13C,15N enriched peptides by MAS solid-state NMR, J. Magn. Reson. 178, 20-28 (2006).

(32) Chen, Z., Krause, G., Reif, B., Structure and Orientation of Peptide Inhibitors Bound to Alzheimer's disease beta-amyloid fibrils, J. Mol. Biol. 354, 760-776 (2005).

(31) Hologne, M., Faelber, K., Diehl, A., Reif, B., Characterization of dynamics by MAS Solid-State NMR of uniformly deuterated proteins, J. Am. Chem. Soc. 127 (32), 11208-11209 (2005).

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

(29) Narayanan, S., Reif, B., Characterization of chemical exchange between soluble and aggregated states of β-amyloid by solution state NMR upon variation of the salt conditions, Biochemistry 44 (5), 1444-1452 (2005).

(28) Chevelkov, V., Chen, Z., Bermel, W., Reif, B., Resolution enhancement in MAS solid-state NMR by application of 13C homonuclear scalar decoupling during acquisition J. Magn. Reson. 172, 56-62 (2005).

(27) Chen, Z., Reif, B., Measurement of residual dipolar couplings in peptidic inhibitors weakly aligned by transient binding to peptide amyloid fibrils, J. Biomol. NMR 29, 525-530 (2004).

(26) Reif, B., Narayanan, S., Bösl, B., Walter, S., The yeast prion system: Molecular interactions between Sup35 and Hsp104 characterized by solution state NMR spectroscopy, Biophys. J. 86, 176 (2004).

(25) Narayanan, S., Boelens, W.C., Reif, B., Interaction sites between αB-crystalline and β- amyloid as mapped by solution state NMR spectroscopy, Biophys. J. 86, 76  (2004).  

(24) Ventura, S., Zurdo, J., Narayanan, S., Parreño, M., Mangues, R., Reif, B., Chiti, F., Giannoni, E., Dobson, C. M., Aviles F. X., Serrano, L., Short amino acid stretches play an important role in protein amyloid formation. The SH3 case, Proc. Natl. Acad. Sci. USA 101, 7258-7263 (2004).  

(23) Narayanan, S., Bösl, B., Walter, S., Reif, B., Importance of low oligomeric weight species for prion propagation in the yeast prion system Sup35/Hsp104, Proc. Natl. Acad. Sci. USA 100, 9286-9291 (2003).

(22) Chevelkov, V., van Rossum, B.-J., Castellani, F., Rehbein, K., Diehl, A., Hohwy, M., Steuernagel, S., Engelke, F., Oschkinat, H., Reif, B., 1H detection in MAS solid state NMR employing pulsed field gradients for residual solvent, J. Am. Chem. Soc. 125, 7788-7789 (2003).  

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

(20) Reif, B., Griffin, R. G., 1H detected 1H,15N correlation spectroscopy in rotating solids, J. Magn. Reson. 160, 78-83 (2003).

(19) Rienstra, C. M., Tucker-Kelly, L., Jaroniec, C. P., Hohwy, M., Reif, B., McMahon, M. T., Tidor, B., Lozano-Pérez, T., Griffin, R. G., De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy, Proc. Natl. Acad. Sci. USA 93, 10260-10265 (2002).

(18) Rienstra, C. M., Hohwy, M., Jaroniec, C. P., Mueller, L., Reif, B., Griffin, R. G., Determination of Multiple Torsion-Angle Constraints in U-13C,15N-labeled peptides: 3D 1H-15N-13C-1H Dipolar Chemical Shift NMR Spectroscopy in Rotating Solids, J. Am. Chem. Soc. 124, 11908-11922 (2002).

(17) Duchardt, E., Richter, C., Reif, B., Glaser, S. J., Engels, J. W., Griesinger, C., Schwalbe, H., Measurement of 2J(H,C) and 3J(H,C) Coupling Constants in the / selective HC(C)H-TOCSY,  J. Biomol. NMR  21, 117-126 (2001).

(16) Reif, B., Jaroniec, J. P., Rienstra, C. M., Hohwy, M., Griffin, R. G., 1H-1H MAS Correlation Spectroscopy and Distance Measurements in a Deuterated Peptide by Solid-State NMR, J. Magn. Reson. 151, 320-327 (2001).

(15) Reif, B., Hohwy, M., Jaroniec, J. P., Rienstra, C. M., Griffin, R. G., NH-NH Vector Correlation in Peptides by Solid-State NMR, J. Magn. Reson. 145, 132-141 (2000).

(14) Hohwy, M., Jaroniec, J. P., Reif, B., Rienstra, C. M., Griffin, R. G., Determination of local structure and relaxation properties in solid-state NMR: Accurate measurement of amide N-H bond lengths and H-N-H bond angles, J. Am. Chem. Soc. 122, 3218-3219 (2000).

(13) Junker, J., Reif, B., Steinhagen, H., Junker, B., Felli, I. C., Reggelin, M., Griesinger, C., Structure Determination of a Key-Intermediate of the Enantioselective Pd-Complex-Catalyzed Allylic Substitution-Reaction, Chem. Eur. J. 6, 3281-3286 (2000).

(12) Richter, C., Reif, B., Griesinger, C., Schwalbe, H., NMR-Spectroscopic Determination of Angles  and  in RNA from 13C 1H-Dipole, 31P-CSA Cross Correlated Relaxation, J. Am. Chem. Soc. 122, 12728-12731 (2000).

(11) Reif, B., Diener, A., Hennig, M., Maurer, M., Griesinger, C., Cross Correlated Relaxation for the Measurement of Angles between Tensorial Interactions, J. Magn. Reson. 143, 45-68 (2000).

(10) Reif, B., Steinhagen, H., Junker, B., Reggelin, M., Griesinger, C. Determination of the Orientation of a Distant Bond Vector in a Molecular Reference Frame by Cross Correlated Relaxation of Nuclear Spins in an Organometallic Compound, Angew. Chemie Int. Ed. Engl. 37, 1903-1906 (1998).

(9) Richter, C., Reif, B., Wörner, K., Quant, S., Marino, J. P., Engels, J. W., Griesinger, C., Schwalbe, H., A New Experiment for the Measurement of nJ(C,P) Coupling Constants including 3J(C4’i Pi) and 3J(C4’i  Pi+1) in Oligonucleotides, J. Biomol. NMR 12, 223-230 (1998).

(8) Reif, B., Wittmann, V., Schwalbe, H., Wörner, K., Jahn- Hoffmann, K., Engels, J. W., Bermel, W., Griesinger, C., Structural Comparison of Oligonucleotides and their 2'-Deoxy-2'-Fluoro Analogs by Heteronuclear NMR Spectroscopy, Chim. Helv. Acta. 80, 1952-1971 (1997).

(7) Reif, B., Hennig, M., Griesinger, C., Direct Measurement of Angles between Bond Vectors in High Resolution NMR, Science 276, 1230-1233 (1997).

(6) Reif, B., Köck, M., Kerssebaum, R., Schleucher, J., Griesinger, C., Determination of 1J, 2J and 3J Carbon Carbon Coupling Constants at Natural Abundance J. Magn. Reson. B 112, 295-301 (1996).

(5) Köck, M., Reif, B., Gerlach, M., Reggelin, M., Application of the 1,n-ADEQUATE Experiment in the Assignment of Highly Substituted Aromatic Compounds Molecules 1, 41-42 (1996).

(4) Köck, M., Reif, B., Fenical, W., Griesinger, C., Differentiation of HMBC Two- and Three-Bond Correlations: A Method to Simplify the Structure Determination of Natural Products Tetrahedron Letters 37, 363-366 (1996).

(3) Reif, B., Köck, M., Kerssebaum, R., Kang, H., Fenical, W., Griesinger, C. ADEQUATE, a New Set of Experiments to Determine the Constitution of Small Molecules at Natural Abundance J. Magn. Reson. A 118, 282-285 (1996).

(2) Griesinger, C., Schwalbe, H., Marino, J. P., Rexroth, A., Maurer, M., Bellinger, V., Schmidt, P., Quant, S., Wechselberger, R., Reif, B., Naumann, T., Bermel, W., Anklin, C., Glaser, S. J., King, G., Crothers D. M., New Experiments directed to the Assignment and Measurement of Coupling-Constants in Proteins and Oligonucleotides J. Cell. Biol. 21B, 17-18 (1995).

(1) Limmer, S., Reif, B., Ott, G., Arnold, L., Sprinzl, M., NMR evidence for helix geometry modifications by a G-U wobble base pair in the acceptor stem of E.Coli tRNAAla FEBS Letters 385, 15-20 (1996). 


Book Contributions

(7) B. Reif, Deuterated Peptides and Proteins: Structure and Dynamics Studies by MAS solid-state NMR, Eds. D. Burz, A. Shekhtman, Humana Press, Methods in Molecular Biology: Protein NMR Techniques, Vol. 831, 279-301, 2012.

(6) B. Reif, Bestimmung von Struktur und Dynamik von Biopolymeren mittels MAS Festkörper-NMR Spektroskopie, BIOspektrum, Spektrum Akademischer Verlag, Springer, Ausgabe 4, 15. Jahrgang, 406-407, 2009.

(5) B. Reif, Deuterated Peptides and Proteins in MAS solid-state NMR, Encyclopedia of Nuclear Magnetic Resonance, Eds. D.M. Grant, R.K. Harris, Wiley: Chichester, Published 15th December 2009, DOI: 10.1002/9780470034590.emrstm1080.

(4) B. Reif, S. Narayanan, Characterization of Interactions Between Misfolding Proteins and Molecular Chaperones by NMR Spectroscopy, Edt. Thomas Peters, Topics in Current Chemistry 272, pp. 117-168, 2007.

(3) M. Hologne, V. Chevelkov, B. Reif, Deuteration of Peptides and Proteins in MAS Solid-State NMR, in Progress in NMR Spectroscopy 48, pp. 211-232, 2006.

(2) H. Schwalbe, T. Carlomagno, M. Hennig, J. Junker, B. Reif, C. Richter, C. Griesinger, in Nuclear Magnetic Resonance of Biological Macromolecules, Part A, Eds. T. L. James, V. Dötsch and U. Schmitz, Methods in Enzymology Vol. 338, pp. 35-81, 2001.

(1) C. Griesinger, M. Hennig, J. P. Marino, B. Reif, C. Richter, H. Schwalbe, in Modern Techniques in Protein NMR, Eds.: N. R. Krishna and L. J. Berliner, Vol. 16 of Biological Magetic Resonance Series, Plenum Press, pp. 259-367, 1999.