Paul Schanda

Schanda Group

81 Publications

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[81]
2023 | Journal Article | IST-REx-ID: 13095 | OA
Troussicot, L., Vallet, A., Molin, M., Burmann, B. M., & Schanda, P. (2023). Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.3c01200
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[80]
2023 | Research Data | IST-REx-ID: 12820 | OA
Schanda, P. (2023). Research data of the publication “Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:12820
[Published Version] View | Files available | DOI
 
[79]
2023 | Journal Article | IST-REx-ID: 12114 | OA
Gauto, D. F., Lebedenko, O. O., Becker, L. M., Ayala, I., Lichtenecker, R., Skrynnikov, N. R., & Schanda, P. (2023). Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural Biology: X. Elsevier. https://doi.org/10.1016/j.yjsbx.2022.100079
[Published Version] View | Files available | DOI | PubMed | Europe PMC
 
[78]
2023 | Journal Article | IST-REx-ID: 13096 | OA
Degen, M., Santos, J. C., Pluhackova, K., Cebrero, G., Ramos, S., Jankevicius, G., … Hiller, S. (2023). Structural basis of NINJ1-mediated plasma membrane rupture in cell death. Nature. Springer Nature. https://doi.org/10.1038/s41586-023-05991-z
[Published Version] View | Files available | DOI | WoS
 
[77]
2023 | Other Publication | IST-REx-ID: 14861 | OA
Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B., … Schanda, P. (2023). Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues. Angewandte Chemie International Edition (Vol. 62). Wiley. https://doi.org/10.1002/anie.202304138
[Published Version] View | Files available | DOI | Download Published Version (ext.)
 
[76]
2023 | Journal Article | IST-REx-ID: 14835 | OA
Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B., … Schanda, P. (2023). Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten. Angewandte Chemie. Wiley. https://doi.org/10.1002/ange.202219314
[Published Version] View | Files available | DOI
 
[75]
2023 | Book Chapter | IST-REx-ID: 14847 | OA
Sučec, I., & Schanda, P. (2023). Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies. In S. Hiller, M. Liu, & L. He (Eds.), Biophysics of Molecular Chaperones (Vol. 29, pp. 136–161). Royal Society of Chemistry. https://doi.org/10.1039/bk9781839165986-00136
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[74]
2023 | Journal Article | IST-REx-ID: 14036 | OA
Napoli, F., Becker, L. M., & Schanda, P. (2023). Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. Current Opinion in Structural Biology. Elsevier. https://doi.org/10.1016/j.sbi.2023.102660
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[73]
2023 | Journal Article | IST-REx-ID: 12675 | OA
Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B., … Schanda, P. (2023). The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.202219314
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[72]
2023 | Research Data | IST-REx-ID: 12497 | OA
Becker, L. M., & Schanda, P. (2023). Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues. Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:12497
[Published Version] View | Files available | DOI
 
[71]
2022 | Journal Article | IST-REx-ID: 11179 | OA
Gauto, D. F., Macek, P., Malinverni, D., Fraga, H., Paloni, M., Sučec, I., … Schanda, P. (2022). Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-022-29423-0
[Published Version] View | Files available | DOI | WoS
 
[70]
2021 | Journal Article | IST-REx-ID: 10323 | OA
Sučec, I., Bersch, B., & Schanda, P. (2021). How do chaperones bind (partly) unfolded client proteins? Frontiers in Molecular Biosciences. Frontiers. https://doi.org/10.3389/fmolb.2021.762005
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[69]
2020 | Journal Article | IST-REx-ID: 8402 | OA
Rampelt, H., Sucec, I., Bersch, B., Horten, P., Perschil, I., Martinou, J.-C., … Pfanner, N. (2020). The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments. BMC Biology. Springer Nature. https://doi.org/10.1186/s12915-019-0733-6
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[68]
2020 | Preprint | IST-REx-ID: 8404 | OA
Weinhäupl, K., Wang, Y., Hessel, A., Brennich, M., Lindorff-Larsen, K., & Schanda, P. (n.d.). Architecture and subunit dynamics of the mitochondrial TIM9·10·12 chaperone. bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2020.03.13.990150
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[67]
2020 | Preprint | IST-REx-ID: 8403 | OA
Sučec, I., Wang, Y., Dakhlaoui, O., Weinhäupl, K., Jores, T., Costa, D., … Schanda, P. (n.d.). Structural basis of client specificity in mitochondrial membrane-protein chaperones. bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2020.06.08.140772
[Preprint] View | DOI | Download Preprint (ext.)
 
[66]
2019 | Journal Article | IST-REx-ID: 8405 | OA
Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., … Boisbouvier, J. (2019). Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-019-10490-9
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[65]
2019 | Journal Article | IST-REx-ID: 8406 | OA
Felix, J., Weinhäupl, K., Chipot, C., Dehez, F., Hessel, A., Gauto, D. F., … Fraga, H. (2019). Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors. Science Advances. American Association for the Advancement of Science. https://doi.org/10.1126/sciadv.aaw3818
[Published Version] View | DOI | Download Published Version (ext.)
 
[64]
2019 | Journal Article | IST-REx-ID: 8413
Rovó, P., Smith, C. A., Gauto, D., de Groot, B. L., Schanda, P., & Linser, R. (2019). Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.8b09258
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[63]
2019 | Journal Article | IST-REx-ID: 8412
Shannon, M. D., Theint, T., Mukhopadhyay, D., Surewicz, K., Surewicz, W. K., Marion, D., … Jaroniec, C. P. (2019). Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201800779
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[62]
2019 | Journal Article | IST-REx-ID: 8411
Marion, D., Gauto, D. F., Ayala, I., Giandoreggio-Barranco, K., & Schanda, P. (2019). Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201800935
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[61]
2019 | Journal Article | IST-REx-ID: 8409
Bougault, C., Ayala, I., Vollmer, W., Simorre, J.-P., & Schanda, P. (2019). Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency. Journal of Structural Biology. Elsevier. https://doi.org/10.1016/j.jsb.2018.07.009
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[60]
2019 | Journal Article | IST-REx-ID: 8407
Schanda, P. (2019). Relaxing with liquids and solids – A perspective on biomolecular dynamics. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2019.07.025
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[59]
2019 | Journal Article | IST-REx-ID: 8410 | OA
Schanda, P., & Chekmenev, E. Y. (2019). NMR for Biological Systems. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201801100
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[58]
2019 | Journal Article | IST-REx-ID: 8408
Gauto, D. F., Macek, P., Barducci, A., Fraga, H., Hessel, A., Terauchi, T., … Schanda, P. (2019). Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.9b04219
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[57]
2018 | Journal Article | IST-REx-ID: 8443
Kurauskas, V., Hessel, A., Ma, P., Lunetti, P., Weinhäupl, K., Imbert, L., … Schanda, P. (2018). How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine. The Journal of Physical Chemistry Letters. American Chemical Society. https://doi.org/10.1021/acs.jpclett.8b00269
View | DOI
 
[56]
2018 | Journal Article | IST-REx-ID: 8440
Weinhäupl, K., Brennich, M., Kazmaier, U., Lelievre, J., Ballell, L., Goldberg, A., … Fraga, H. (2018). The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. Journal of Biological Chemistry. American Society for Biochemistry & Molecular Biology. https://doi.org/10.1074/jbc.ra118.002251
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[55]
2018 | Journal Article | IST-REx-ID: 8442
Chipot, C., Dehez, F., Schnell, J. R., Zitzmann, N., Pebay-Peyroula, E., Catoire, L. J., … Schanda, P. (2018). Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. Chemical Reviews. American Chemical Society. https://doi.org/10.1021/acs.chemrev.7b00570
View | DOI
 
[54]
2018 | Journal Article | IST-REx-ID: 8441
Krushelnitsky, A., Gauto, D., Rodriguez Camargo, D. C., Schanda, P., & Saalwächter, K. (2018). Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-018-0191-4
[Published Version] View | DOI
 
[53]
2018 | Journal Article | IST-REx-ID: 8439
Laguri, C., Silipo, A., Martorana, A. M., Schanda, P., Marchetti, R., Polissi, A., … Simorre, J.-P. (2018). Solid state NMR studies of intact lipopolysaccharide endotoxin. ACS Chemical Biology. American Chemical Society. https://doi.org/10.1021/acschembio.8b00271
View | DOI
 
[52]
2018 | Journal Article | IST-REx-ID: 8437
Mas, G., Guan, J.-Y., Crublet, E., Debled, E. C., Moriscot, C., Gans, P., … Boisbouvier, J. (2018). Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. Science Advances. American Association for the Advancement of Science. https://doi.org/10.1126/sciadv.aau4196
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[51]
2018 | Journal Article | IST-REx-ID: 8436
Weinhäupl, K., Lindau, C., Hessel, A., Wang, Y., Schütze, C., Jores, T., … Schanda, P. (2018). Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. Elsevier. https://doi.org/10.1016/j.cell.2018.10.039
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[50]
2018 | Journal Article | IST-REx-ID: 8438
Kurauskas, V., Hessel, A., Dehez, F., Chipot, C., Bersch, B., & Schanda, P. (2018). Dynamics and interactions of AAC3 in DPC are not functionally relevant. Nature Structural & Molecular Biology. Springer Nature. https://doi.org/10.1038/s41594-018-0127-4
View | DOI
 
[49]
2017 | Journal Article | IST-REx-ID: 8446
Fraga, H., Arnaud, C., Gauto, D. F., Audin, M., Kurauskas, V., Macek, P., … Schanda, P. (2017). Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201700572
View | DOI
 
[48]
2017 | Journal Article | IST-REx-ID: 8445
Kurauskas, V., Izmailov, S. A., Rogacheva, O. N., Hessel, A., Ayala, I., Woodhouse, J., … Schanda, P. (2017). Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-017-00165-8
[Published Version] View | DOI
 
[47]
2017 | Journal Article | IST-REx-ID: 8444
Dehez, F., Schanda, P., King, M. S., Kunji, E. R. S., & Chipot, C. (2017). Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity. Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2017.09.019
View | DOI
 
[46]
2017 | Journal Article | IST-REx-ID: 8449
Rennella, E., Sára, T., Juen, M., Wunderlich, C., Imbert, L., Solyom, Z., … Brutscher, B. (2017). RNA binding and chaperone activity of the E.coli cold-shock protein CspA. Nucleic Acids Research. Oxford University Press. https://doi.org/10.1093/nar/gkx044
View | DOI
 
[45]
2017 | Journal Article | IST-REx-ID: 8447
Gauto, D. F., Hessel, A., Rovó, P., Kurauskas, V., Linser, R., & Schanda, P. (2017). Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.ssnmr.2017.04.002
View | DOI
 
[44]
2017 | Journal Article | IST-REx-ID: 8448
Franco, R., Favier, A., Schanda, P., & Brutscher, B. (2017). Optimized fast mixing device for real-time NMR applications. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2017.05.016
View | DOI
 
[43]
2017 | Journal Article | IST-REx-ID: 8451
Bersch, B., Dörr, J. M., Hessel, A., Killian, J. A., & Schanda, P. (2017). Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.201610441
View | DOI
 
[42]
2017 | Book Chapter | IST-REx-ID: 8450
Kurauskas, V., Schanda, P., & Sounier, R. (2017). Methyl-specific isotope labeling strategies for NMR studies of membrane proteins. In Membrane protein structure and function characterization (Vol. 1635, pp. 109–123). Springer Nature. https://doi.org/10.1007/978-1-4939-7151-0_6
View | DOI
 
[41]
2016 | Journal Article | IST-REx-ID: 8455
Kurauskas, V., Crublet, E., Macek, P., Kerfah, R., Gauto, D. F., Boisbouvier, J., & Schanda, P. (2016). Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit. Chemical Communications. Royal Society of Chemistry. https://doi.org/10.1039/c6cc04484k
View | DOI
 
[40]
2016 | Journal Article | IST-REx-ID: 8453
Kurauskas, V., Weber, E., Hessel, A., Ayala, I., Marion, D., & Schanda, P. (2016). Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics measurements. The Journal of Physical Chemistry B. American Chemical Society. https://doi.org/10.1021/acs.jpcb.6b06129
View | DOI
 
[39]
2016 | Journal Article | IST-REx-ID: 8452
Rodrigues, C. D. A., Henry, X., Neumann, E., Kurauskas, V., Bellard, L., Fichou, Y., … Morlot, C. (2016). A ring-shaped conduit connects the mother cell and forespore during sporulation in Bacillus subtilis. Proceedings of the National Academy of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.1609604113
View | DOI
 
[38]
2016 | Journal Article | IST-REx-ID: 8454
Schanda, P., & Ernst, M. (2016). Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules. Progress in Nuclear Magnetic Resonance Spectroscopy. Elsevier. https://doi.org/10.1016/j.pnmrs.2016.02.001
View | DOI
 
[37]
2015 | Journal Article | IST-REx-ID: 8456
Ma, P., Xue, Y., Coquelle, N., Haller, J. D., Yuwen, T., Ayala, I., … Schanda, P. (2015). Observing the overall rocking motion of a protein in a crystal. Nature Communications. Springer Nature. https://doi.org/10.1038/ncomms9361
[Published Version] View | DOI
 
[36]
2015 | Journal Article | IST-REx-ID: 8457
Ma, P., & Schanda, P. (2015). Conformational exchange processes in biological systems: Detection by solid-state NMR. EMagRes. Wiley. https://doi.org/10.1002/9780470034590.emrstm1418
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[35]
2014 | Journal Article | IST-REx-ID: 8459
Morin, S., Linnet, T. E., Lescanne, M., Schanda, P., Thompson, G. S., Tollinger, M., … d’Auvergne, E. J. (2014). Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. Bioinformatics. Oxford University Press. https://doi.org/10.1093/bioinformatics/btu166
View | Files available | DOI
 
[34]
2014 | Journal Article | IST-REx-ID: 8458
Schanda, P., Triboulet, S., Laguri, C., Bougault, C. M., Ayala, I., Callon, M., … Simorre, J.-P. (2014). Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja5105987
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[33]
2014 | Journal Article | IST-REx-ID: 8460
Ma, P., Haller, J. D., Zajakala, J., Macek, P., Sivertsen, A. C., Willbold, D., … Schanda, P. (2014). Probing transient conformational states of proteins by solid-state R1ρ relaxation-dispersion NMR spectroscopy. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.201311275
View | DOI
 
[32]
2013 | Journal Article | IST-REx-ID: 8461
Haller, J. D., & Schanda, P. (2013). Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-013-9787-x
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[31]
2013 | Journal Article | IST-REx-ID: 8462
Rennella, E., Cutuil, T., Schanda, P., Ayala, I., Gabel, F., Forge, V., … Brutscher, B. (2013). Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2013.04.028
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[30]
2012 | Journal Article | IST-REx-ID: 8463
Asami, S., Szekely, K., Schanda, P., Meier, B. H., & Reif, B. (2012). Optimal degree of protonation for 1H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-012-9659-9
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[29]
2012 | Journal Article | IST-REx-ID: 8465
Tollinger, M., Sivertsen, A. C., Meier, B. H., Ernst, M., & Schanda, P. (2012). Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja303591y
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[28]
2012 | Journal Article | IST-REx-ID: 8466
Rennella, E., Cutuil, T., Schanda, P., Ayala, I., Forge, V., & Brutscher, B. (2012). Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja302598j
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[27]
2012 | Journal Article | IST-REx-ID: 8467
Huber, M., With, O., Schanda, P., Verel, R., Ernst, M., & Meier, B. H. (2012). A supplementary coil for 2H decoupling with commercial HCN MAS probes. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2011.10.010
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[26]
2011 | Journal Article | IST-REx-ID: 8469
Schanda, P., Meier, B. H., & Ernst, M. (2011). Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2011.03.015
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[25]
2011 | Journal Article | IST-REx-ID: 8470
Huber, M., Hiller, S., Schanda, P., Ernst, M., Böckmann, A., Verel, R., & Meier, B. H. (2011). A proton-detected 4D solid-state NMR experiment for protein structure determination. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201100062
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[24]
2011 | Journal Article | IST-REx-ID: 8464
Schanda, P., Huber, M., Boisbouvier, J., Meier, B. H., & Ernst, M. (2011). Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.201103944
View | Files available | DOI
 
[23]
2011 | Journal Article | IST-REx-ID: 8468
Lalli, D., Schanda, P., Chowdhury, A., Retel, J., Hiller, M., Higman, V. A., … Oschkinat, H. (2011). Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-011-9578-1
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[22]
2011 | Journal Article | IST-REx-ID: 8471
Van Melckebeke, H., Schanda, P., Gath, J., Wasmer, C., Verel, R., Lange, A., … Böckmann, A. (2011). Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2010.11.004
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[21]
2010 | Journal Article | IST-REx-ID: 8473
Corazza, A., Rennella, E., Schanda, P., Mimmi, M. C., Cutuil, T., Raimondi, S., … Esposito, G. (2010). Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. Journal of Biological Chemistry. American Society for Biochemistry & Molecular Biology. https://doi.org/10.1074/jbc.m109.061168
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[20]
2010 | Journal Article | IST-REx-ID: 8472
Schanda, P., Meier, B. H., & Ernst, M. (2010). Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja100726a
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[19]
2009 | Journal Article | IST-REx-ID: 8479
Gal, M., Kern, T., Schanda, P., Frydman, L., & Brutscher, B. (2009). An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-008-9284-9
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[18]
2009 | Journal Article | IST-REx-ID: 8478
Brüschweiler, S., Schanda, P., Kloiber, K., Brutscher, B., Kontaxis, G., Konrat, R., & Tollinger, M. (2009). Direct observation of the dynamic process underlying allosteric signal transmission. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja809947w
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[17]
2009 | Journal Article | IST-REx-ID: 8476
Farjon, J., Boisbouvier, J., Schanda, P., Pardi, A., Simorre, J.-P., & Brutscher, B. (2009). Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja901633y
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[16]
2009 | Journal Article | IST-REx-ID: 8477
Amero, C., Schanda, P., Durá, M. A., Ayala, I., Marion, D., Franzetti, B., … Boisbouvier, J. (2009). Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja809880p
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[15]
2009 | Journal Article | IST-REx-ID: 8474
Schanda, P., Huber, M., Verel, R., Ernst, M., & Meier, B. (2009). Direct detection of 3hJN’ hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.200904411
View | DOI
 
[14]
2009 | Journal Article | IST-REx-ID: 8475
Schanda, P. (2009). Fast-pulsing longitudinal relaxation optimized techniques: Enriching the toolbox of fast biomolecular NMR spectroscopy. Progress in Nuclear Magnetic Resonance Spectroscopy. Elsevier. https://doi.org/10.1016/j.pnmrs.2009.05.002
View | DOI
 
[13]
2008 | Journal Article | IST-REx-ID: 8481
Bersch, B., Favier, A., Schanda, P., van Aelst, S., Vallaeys, T., Covès, J., … Wattiez, R. (2008). Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2008.05.017
View | DOI
 
[12]
2008 | Journal Article | IST-REx-ID: 8480
Schanda, P., Brutscher, B., Konrat, R., & Tollinger, M. (2008). Folding of the KIX domain: Characterization of the equilibrium analog of a folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2008.05.040
View | DOI
 
[11]
2008 | Journal Article | IST-REx-ID: 8482
Kern, T., Schanda, P., & Brutscher, B. (2008). Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced radiofrequency load. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2007.11.015
View | DOI
 
[10]
2007 | Journal Article | IST-REx-ID: 8483
Schanda, P., Forge, V., & Brutscher, B. (2007). Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy. Proceedings of the National Academy of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.0702069104
View | DOI
 
[9]
2007 | Journal Article | IST-REx-ID: 8487
Gal, M., Schanda, P., Brutscher, B., & Frydman, L. (2007). UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja066915g
View | DOI
 
[8]
2007 | Journal Article | IST-REx-ID: 8485
Schanda, P., Lescop, E., Falge, M., Sounier, R., Boisbouvier, J., & Brutscher, B. (2007). Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-006-9138-2
View | DOI
 
[7]
2007 | Journal Article | IST-REx-ID: 8486
Lescop, E., Schanda, P., Rasia, R., & Brutscher, B. (2007). Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja068949u
View | DOI
 
[6]
2007 | Journal Article | IST-REx-ID: 8484
Lescop, E., Schanda, P., & Brutscher, B. (2007). A set of BEST triple-resonance experiments for time-optimized protein resonance assignment. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2007.04.002
View | DOI
 
[5]
2006 | Journal Article | IST-REx-ID: 8489
Schanda, P., Forge, V., & Brutscher, B. (2006). HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains. Magnetic Resonance in Chemistry. Wiley. https://doi.org/10.1002/mrc.1825
View | DOI
 
[4]
2006 | Journal Article | IST-REx-ID: 8488
Schanda, P., Van Melckebeke, H., & Brutscher, B. (2006). Speeding up three-dimensional protein NMR experiments to a few minutes. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja062025p
View | DOI
 
[3]
2006 | Journal Article | IST-REx-ID: 8490
Schanda, P., & Brutscher, B. (2006). Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein NMR. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2005.10.007
View | DOI
 
[2]
2005 | Journal Article | IST-REx-ID: 8491
Schanda, P., Kupče, Ē., & Brutscher, B. (2005). SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-005-4425-x
View | DOI
 
[1]
2005 | Journal Article | IST-REx-ID: 8492
Schanda, P., & Brutscher, B. (2005). Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja051306e
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[81]
2023 | Journal Article | IST-REx-ID: 13095 | OA
Troussicot, L., Vallet, A., Molin, M., Burmann, B. M., & Schanda, P. (2023). Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.3c01200
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[80]
2023 | Research Data | IST-REx-ID: 12820 | OA
Schanda, P. (2023). Research data of the publication “Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:12820
[Published Version] View | Files available | DOI
 
[79]
2023 | Journal Article | IST-REx-ID: 12114 | OA
Gauto, D. F., Lebedenko, O. O., Becker, L. M., Ayala, I., Lichtenecker, R., Skrynnikov, N. R., & Schanda, P. (2023). Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural Biology: X. Elsevier. https://doi.org/10.1016/j.yjsbx.2022.100079
[Published Version] View | Files available | DOI | PubMed | Europe PMC
 
[78]
2023 | Journal Article | IST-REx-ID: 13096 | OA
Degen, M., Santos, J. C., Pluhackova, K., Cebrero, G., Ramos, S., Jankevicius, G., … Hiller, S. (2023). Structural basis of NINJ1-mediated plasma membrane rupture in cell death. Nature. Springer Nature. https://doi.org/10.1038/s41586-023-05991-z
[Published Version] View | Files available | DOI | WoS
 
[77]
2023 | Other Publication | IST-REx-ID: 14861 | OA
Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B., … Schanda, P. (2023). Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues. Angewandte Chemie International Edition (Vol. 62). Wiley. https://doi.org/10.1002/anie.202304138
[Published Version] View | Files available | DOI | Download Published Version (ext.)
 
[76]
2023 | Journal Article | IST-REx-ID: 14835 | OA
Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B., … Schanda, P. (2023). Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten. Angewandte Chemie. Wiley. https://doi.org/10.1002/ange.202219314
[Published Version] View | Files available | DOI
 
[75]
2023 | Book Chapter | IST-REx-ID: 14847 | OA
Sučec, I., & Schanda, P. (2023). Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies. In S. Hiller, M. Liu, & L. He (Eds.), Biophysics of Molecular Chaperones (Vol. 29, pp. 136–161). Royal Society of Chemistry. https://doi.org/10.1039/bk9781839165986-00136
[Preprint] View | DOI | Download Preprint (ext.)
 
[74]
2023 | Journal Article | IST-REx-ID: 14036 | OA
Napoli, F., Becker, L. M., & Schanda, P. (2023). Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. Current Opinion in Structural Biology. Elsevier. https://doi.org/10.1016/j.sbi.2023.102660
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[73]
2023 | Journal Article | IST-REx-ID: 12675 | OA
Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B., … Schanda, P. (2023). The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.202219314
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[72]
2023 | Research Data | IST-REx-ID: 12497 | OA
Becker, L. M., & Schanda, P. (2023). Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues. Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:12497
[Published Version] View | Files available | DOI
 
[71]
2022 | Journal Article | IST-REx-ID: 11179 | OA
Gauto, D. F., Macek, P., Malinverni, D., Fraga, H., Paloni, M., Sučec, I., … Schanda, P. (2022). Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-022-29423-0
[Published Version] View | Files available | DOI | WoS
 
[70]
2021 | Journal Article | IST-REx-ID: 10323 | OA
Sučec, I., Bersch, B., & Schanda, P. (2021). How do chaperones bind (partly) unfolded client proteins? Frontiers in Molecular Biosciences. Frontiers. https://doi.org/10.3389/fmolb.2021.762005
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[69]
2020 | Journal Article | IST-REx-ID: 8402 | OA
Rampelt, H., Sucec, I., Bersch, B., Horten, P., Perschil, I., Martinou, J.-C., … Pfanner, N. (2020). The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments. BMC Biology. Springer Nature. https://doi.org/10.1186/s12915-019-0733-6
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[68]
2020 | Preprint | IST-REx-ID: 8404 | OA
Weinhäupl, K., Wang, Y., Hessel, A., Brennich, M., Lindorff-Larsen, K., & Schanda, P. (n.d.). Architecture and subunit dynamics of the mitochondrial TIM9·10·12 chaperone. bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2020.03.13.990150
[Preprint] View | DOI | Download Preprint (ext.)
 
[67]
2020 | Preprint | IST-REx-ID: 8403 | OA
Sučec, I., Wang, Y., Dakhlaoui, O., Weinhäupl, K., Jores, T., Costa, D., … Schanda, P. (n.d.). Structural basis of client specificity in mitochondrial membrane-protein chaperones. bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2020.06.08.140772
[Preprint] View | DOI | Download Preprint (ext.)
 
[66]
2019 | Journal Article | IST-REx-ID: 8405 | OA
Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., … Boisbouvier, J. (2019). Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-019-10490-9
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[65]
2019 | Journal Article | IST-REx-ID: 8406 | OA
Felix, J., Weinhäupl, K., Chipot, C., Dehez, F., Hessel, A., Gauto, D. F., … Fraga, H. (2019). Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors. Science Advances. American Association for the Advancement of Science. https://doi.org/10.1126/sciadv.aaw3818
[Published Version] View | DOI | Download Published Version (ext.)
 
[64]
2019 | Journal Article | IST-REx-ID: 8413
Rovó, P., Smith, C. A., Gauto, D., de Groot, B. L., Schanda, P., & Linser, R. (2019). Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.8b09258
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[63]
2019 | Journal Article | IST-REx-ID: 8412
Shannon, M. D., Theint, T., Mukhopadhyay, D., Surewicz, K., Surewicz, W. K., Marion, D., … Jaroniec, C. P. (2019). Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201800779
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[62]
2019 | Journal Article | IST-REx-ID: 8411
Marion, D., Gauto, D. F., Ayala, I., Giandoreggio-Barranco, K., & Schanda, P. (2019). Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201800935
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[61]
2019 | Journal Article | IST-REx-ID: 8409
Bougault, C., Ayala, I., Vollmer, W., Simorre, J.-P., & Schanda, P. (2019). Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency. Journal of Structural Biology. Elsevier. https://doi.org/10.1016/j.jsb.2018.07.009
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[60]
2019 | Journal Article | IST-REx-ID: 8407
Schanda, P. (2019). Relaxing with liquids and solids – A perspective on biomolecular dynamics. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2019.07.025
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[59]
2019 | Journal Article | IST-REx-ID: 8410 | OA
Schanda, P., & Chekmenev, E. Y. (2019). NMR for Biological Systems. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201801100
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[58]
2019 | Journal Article | IST-REx-ID: 8408
Gauto, D. F., Macek, P., Barducci, A., Fraga, H., Hessel, A., Terauchi, T., … Schanda, P. (2019). Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.9b04219
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[57]
2018 | Journal Article | IST-REx-ID: 8443
Kurauskas, V., Hessel, A., Ma, P., Lunetti, P., Weinhäupl, K., Imbert, L., … Schanda, P. (2018). How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine. The Journal of Physical Chemistry Letters. American Chemical Society. https://doi.org/10.1021/acs.jpclett.8b00269
View | DOI
 
[56]
2018 | Journal Article | IST-REx-ID: 8440
Weinhäupl, K., Brennich, M., Kazmaier, U., Lelievre, J., Ballell, L., Goldberg, A., … Fraga, H. (2018). The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. Journal of Biological Chemistry. American Society for Biochemistry & Molecular Biology. https://doi.org/10.1074/jbc.ra118.002251
View | DOI
 
[55]
2018 | Journal Article | IST-REx-ID: 8442
Chipot, C., Dehez, F., Schnell, J. R., Zitzmann, N., Pebay-Peyroula, E., Catoire, L. J., … Schanda, P. (2018). Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. Chemical Reviews. American Chemical Society. https://doi.org/10.1021/acs.chemrev.7b00570
View | DOI
 
[54]
2018 | Journal Article | IST-REx-ID: 8441
Krushelnitsky, A., Gauto, D., Rodriguez Camargo, D. C., Schanda, P., & Saalwächter, K. (2018). Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-018-0191-4
[Published Version] View | DOI
 
[53]
2018 | Journal Article | IST-REx-ID: 8439
Laguri, C., Silipo, A., Martorana, A. M., Schanda, P., Marchetti, R., Polissi, A., … Simorre, J.-P. (2018). Solid state NMR studies of intact lipopolysaccharide endotoxin. ACS Chemical Biology. American Chemical Society. https://doi.org/10.1021/acschembio.8b00271
View | DOI
 
[52]
2018 | Journal Article | IST-REx-ID: 8437
Mas, G., Guan, J.-Y., Crublet, E., Debled, E. C., Moriscot, C., Gans, P., … Boisbouvier, J. (2018). Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. Science Advances. American Association for the Advancement of Science. https://doi.org/10.1126/sciadv.aau4196
View | DOI
 
[51]
2018 | Journal Article | IST-REx-ID: 8436
Weinhäupl, K., Lindau, C., Hessel, A., Wang, Y., Schütze, C., Jores, T., … Schanda, P. (2018). Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. Elsevier. https://doi.org/10.1016/j.cell.2018.10.039
View | DOI
 
[50]
2018 | Journal Article | IST-REx-ID: 8438
Kurauskas, V., Hessel, A., Dehez, F., Chipot, C., Bersch, B., & Schanda, P. (2018). Dynamics and interactions of AAC3 in DPC are not functionally relevant. Nature Structural & Molecular Biology. Springer Nature. https://doi.org/10.1038/s41594-018-0127-4
View | DOI
 
[49]
2017 | Journal Article | IST-REx-ID: 8446
Fraga, H., Arnaud, C., Gauto, D. F., Audin, M., Kurauskas, V., Macek, P., … Schanda, P. (2017). Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201700572
View | DOI
 
[48]
2017 | Journal Article | IST-REx-ID: 8445
Kurauskas, V., Izmailov, S. A., Rogacheva, O. N., Hessel, A., Ayala, I., Woodhouse, J., … Schanda, P. (2017). Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-017-00165-8
[Published Version] View | DOI
 
[47]
2017 | Journal Article | IST-REx-ID: 8444
Dehez, F., Schanda, P., King, M. S., Kunji, E. R. S., & Chipot, C. (2017). Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity. Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2017.09.019
View | DOI
 
[46]
2017 | Journal Article | IST-REx-ID: 8449
Rennella, E., Sára, T., Juen, M., Wunderlich, C., Imbert, L., Solyom, Z., … Brutscher, B. (2017). RNA binding and chaperone activity of the E.coli cold-shock protein CspA. Nucleic Acids Research. Oxford University Press. https://doi.org/10.1093/nar/gkx044
View | DOI
 
[45]
2017 | Journal Article | IST-REx-ID: 8447
Gauto, D. F., Hessel, A., Rovó, P., Kurauskas, V., Linser, R., & Schanda, P. (2017). Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.ssnmr.2017.04.002
View | DOI
 
[44]
2017 | Journal Article | IST-REx-ID: 8448
Franco, R., Favier, A., Schanda, P., & Brutscher, B. (2017). Optimized fast mixing device for real-time NMR applications. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2017.05.016
View | DOI
 
[43]
2017 | Journal Article | IST-REx-ID: 8451
Bersch, B., Dörr, J. M., Hessel, A., Killian, J. A., & Schanda, P. (2017). Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.201610441
View | DOI
 
[42]
2017 | Book Chapter | IST-REx-ID: 8450
Kurauskas, V., Schanda, P., & Sounier, R. (2017). Methyl-specific isotope labeling strategies for NMR studies of membrane proteins. In Membrane protein structure and function characterization (Vol. 1635, pp. 109–123). Springer Nature. https://doi.org/10.1007/978-1-4939-7151-0_6
View | DOI
 
[41]
2016 | Journal Article | IST-REx-ID: 8455
Kurauskas, V., Crublet, E., Macek, P., Kerfah, R., Gauto, D. F., Boisbouvier, J., & Schanda, P. (2016). Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit. Chemical Communications. Royal Society of Chemistry. https://doi.org/10.1039/c6cc04484k
View | DOI
 
[40]
2016 | Journal Article | IST-REx-ID: 8453
Kurauskas, V., Weber, E., Hessel, A., Ayala, I., Marion, D., & Schanda, P. (2016). Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics measurements. The Journal of Physical Chemistry B. American Chemical Society. https://doi.org/10.1021/acs.jpcb.6b06129
View | DOI
 
[39]
2016 | Journal Article | IST-REx-ID: 8452
Rodrigues, C. D. A., Henry, X., Neumann, E., Kurauskas, V., Bellard, L., Fichou, Y., … Morlot, C. (2016). A ring-shaped conduit connects the mother cell and forespore during sporulation in Bacillus subtilis. Proceedings of the National Academy of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.1609604113
View | DOI
 
[38]
2016 | Journal Article | IST-REx-ID: 8454
Schanda, P., & Ernst, M. (2016). Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules. Progress in Nuclear Magnetic Resonance Spectroscopy. Elsevier. https://doi.org/10.1016/j.pnmrs.2016.02.001
View | DOI
 
[37]
2015 | Journal Article | IST-REx-ID: 8456
Ma, P., Xue, Y., Coquelle, N., Haller, J. D., Yuwen, T., Ayala, I., … Schanda, P. (2015). Observing the overall rocking motion of a protein in a crystal. Nature Communications. Springer Nature. https://doi.org/10.1038/ncomms9361
[Published Version] View | DOI
 
[36]
2015 | Journal Article | IST-REx-ID: 8457
Ma, P., & Schanda, P. (2015). Conformational exchange processes in biological systems: Detection by solid-state NMR. EMagRes. Wiley. https://doi.org/10.1002/9780470034590.emrstm1418
View | DOI
 
[35]
2014 | Journal Article | IST-REx-ID: 8459
Morin, S., Linnet, T. E., Lescanne, M., Schanda, P., Thompson, G. S., Tollinger, M., … d’Auvergne, E. J. (2014). Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. Bioinformatics. Oxford University Press. https://doi.org/10.1093/bioinformatics/btu166
View | Files available | DOI
 
[34]
2014 | Journal Article | IST-REx-ID: 8458
Schanda, P., Triboulet, S., Laguri, C., Bougault, C. M., Ayala, I., Callon, M., … Simorre, J.-P. (2014). Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja5105987
View | DOI
 
[33]
2014 | Journal Article | IST-REx-ID: 8460
Ma, P., Haller, J. D., Zajakala, J., Macek, P., Sivertsen, A. C., Willbold, D., … Schanda, P. (2014). Probing transient conformational states of proteins by solid-state R1ρ relaxation-dispersion NMR spectroscopy. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.201311275
View | DOI
 
[32]
2013 | Journal Article | IST-REx-ID: 8461
Haller, J. D., & Schanda, P. (2013). Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-013-9787-x
View | DOI
 
[31]
2013 | Journal Article | IST-REx-ID: 8462
Rennella, E., Cutuil, T., Schanda, P., Ayala, I., Gabel, F., Forge, V., … Brutscher, B. (2013). Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2013.04.028
View | DOI
 
[30]
2012 | Journal Article | IST-REx-ID: 8463
Asami, S., Szekely, K., Schanda, P., Meier, B. H., & Reif, B. (2012). Optimal degree of protonation for 1H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-012-9659-9
View | DOI
 
[29]
2012 | Journal Article | IST-REx-ID: 8465
Tollinger, M., Sivertsen, A. C., Meier, B. H., Ernst, M., & Schanda, P. (2012). Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja303591y
View | DOI
 
[28]
2012 | Journal Article | IST-REx-ID: 8466
Rennella, E., Cutuil, T., Schanda, P., Ayala, I., Forge, V., & Brutscher, B. (2012). Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja302598j
View | DOI
 
[27]
2012 | Journal Article | IST-REx-ID: 8467
Huber, M., With, O., Schanda, P., Verel, R., Ernst, M., & Meier, B. H. (2012). A supplementary coil for 2H decoupling with commercial HCN MAS probes. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2011.10.010
View | DOI
 
[26]
2011 | Journal Article | IST-REx-ID: 8469
Schanda, P., Meier, B. H., & Ernst, M. (2011). Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2011.03.015
View | DOI
 
[25]
2011 | Journal Article | IST-REx-ID: 8470
Huber, M., Hiller, S., Schanda, P., Ernst, M., Böckmann, A., Verel, R., & Meier, B. H. (2011). A proton-detected 4D solid-state NMR experiment for protein structure determination. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201100062
View | DOI
 
[24]
2011 | Journal Article | IST-REx-ID: 8464
Schanda, P., Huber, M., Boisbouvier, J., Meier, B. H., & Ernst, M. (2011). Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.201103944
View | Files available | DOI
 
[23]
2011 | Journal Article | IST-REx-ID: 8468
Lalli, D., Schanda, P., Chowdhury, A., Retel, J., Hiller, M., Higman, V. A., … Oschkinat, H. (2011). Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-011-9578-1
View | DOI
 
[22]
2011 | Journal Article | IST-REx-ID: 8471
Van Melckebeke, H., Schanda, P., Gath, J., Wasmer, C., Verel, R., Lange, A., … Böckmann, A. (2011). Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2010.11.004
View | DOI
 
[21]
2010 | Journal Article | IST-REx-ID: 8473
Corazza, A., Rennella, E., Schanda, P., Mimmi, M. C., Cutuil, T., Raimondi, S., … Esposito, G. (2010). Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. Journal of Biological Chemistry. American Society for Biochemistry & Molecular Biology. https://doi.org/10.1074/jbc.m109.061168
View | DOI
 
[20]
2010 | Journal Article | IST-REx-ID: 8472
Schanda, P., Meier, B. H., & Ernst, M. (2010). Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja100726a
View | DOI
 
[19]
2009 | Journal Article | IST-REx-ID: 8479
Gal, M., Kern, T., Schanda, P., Frydman, L., & Brutscher, B. (2009). An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-008-9284-9
View | DOI
 
[18]
2009 | Journal Article | IST-REx-ID: 8478
Brüschweiler, S., Schanda, P., Kloiber, K., Brutscher, B., Kontaxis, G., Konrat, R., & Tollinger, M. (2009). Direct observation of the dynamic process underlying allosteric signal transmission. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja809947w
View | DOI
 
[17]
2009 | Journal Article | IST-REx-ID: 8476
Farjon, J., Boisbouvier, J., Schanda, P., Pardi, A., Simorre, J.-P., & Brutscher, B. (2009). Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja901633y
View | DOI
 
[16]
2009 | Journal Article | IST-REx-ID: 8477
Amero, C., Schanda, P., Durá, M. A., Ayala, I., Marion, D., Franzetti, B., … Boisbouvier, J. (2009). Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja809880p
View | DOI
 
[15]
2009 | Journal Article | IST-REx-ID: 8474
Schanda, P., Huber, M., Verel, R., Ernst, M., & Meier, B. (2009). Direct detection of 3hJN’ hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.200904411
View | DOI
 
[14]
2009 | Journal Article | IST-REx-ID: 8475
Schanda, P. (2009). Fast-pulsing longitudinal relaxation optimized techniques: Enriching the toolbox of fast biomolecular NMR spectroscopy. Progress in Nuclear Magnetic Resonance Spectroscopy. Elsevier. https://doi.org/10.1016/j.pnmrs.2009.05.002
View | DOI
 
[13]
2008 | Journal Article | IST-REx-ID: 8481
Bersch, B., Favier, A., Schanda, P., van Aelst, S., Vallaeys, T., Covès, J., … Wattiez, R. (2008). Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2008.05.017
View | DOI
 
[12]
2008 | Journal Article | IST-REx-ID: 8480
Schanda, P., Brutscher, B., Konrat, R., & Tollinger, M. (2008). Folding of the KIX domain: Characterization of the equilibrium analog of a folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2008.05.040
View | DOI
 
[11]
2008 | Journal Article | IST-REx-ID: 8482
Kern, T., Schanda, P., & Brutscher, B. (2008). Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced radiofrequency load. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2007.11.015
View | DOI
 
[10]
2007 | Journal Article | IST-REx-ID: 8483
Schanda, P., Forge, V., & Brutscher, B. (2007). Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy. Proceedings of the National Academy of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.0702069104
View | DOI
 
[9]
2007 | Journal Article | IST-REx-ID: 8487
Gal, M., Schanda, P., Brutscher, B., & Frydman, L. (2007). UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja066915g
View | DOI
 
[8]
2007 | Journal Article | IST-REx-ID: 8485
Schanda, P., Lescop, E., Falge, M., Sounier, R., Boisbouvier, J., & Brutscher, B. (2007). Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-006-9138-2
View | DOI
 
[7]
2007 | Journal Article | IST-REx-ID: 8486
Lescop, E., Schanda, P., Rasia, R., & Brutscher, B. (2007). Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja068949u
View | DOI
 
[6]
2007 | Journal Article | IST-REx-ID: 8484
Lescop, E., Schanda, P., & Brutscher, B. (2007). A set of BEST triple-resonance experiments for time-optimized protein resonance assignment. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2007.04.002
View | DOI
 
[5]
2006 | Journal Article | IST-REx-ID: 8489
Schanda, P., Forge, V., & Brutscher, B. (2006). HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains. Magnetic Resonance in Chemistry. Wiley. https://doi.org/10.1002/mrc.1825
View | DOI
 
[4]
2006 | Journal Article | IST-REx-ID: 8488
Schanda, P., Van Melckebeke, H., & Brutscher, B. (2006). Speeding up three-dimensional protein NMR experiments to a few minutes. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja062025p
View | DOI
 
[3]
2006 | Journal Article | IST-REx-ID: 8490
Schanda, P., & Brutscher, B. (2006). Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein NMR. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2005.10.007
View | DOI
 
[2]
2005 | Journal Article | IST-REx-ID: 8491
Schanda, P., Kupče, Ē., & Brutscher, B. (2005). SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-005-4425-x
View | DOI
 
[1]
2005 | Journal Article | IST-REx-ID: 8492
Schanda, P., & Brutscher, B. (2005). Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja051306e
View | DOI
 
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