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1. Correction: Unravelling potential reaction intermediates during catalytic pyrolysis of polypropylene with microscopy and spectroscopy

Author

Sub Inorganic Chemistry and Catalysis, Sub NMR Spectroscopy, Inorganic Chemistry and Catalysis, NMR Spectroscopy, Vollmer, I, Jenks, MJF, Rejman, S, Meirer, F, Gurinov, A, Baldus, M, Weckhuysen, BM, Sub Inorganic Chemistry and Catalysis, Sub NMR Spectroscopy, Inorganic Chemistry and Catalysis, NMR Spectroscopy, Vollmer, I, Jenks, MJF, Rejman, S, Meirer, F, Gurinov, A, Baldus, M, and Weckhuysen, BM

Published
2024

6. Adult AML: The Role of Chemotherapy Intensity and Duration. Two Studies of the AML Cooperative Group

Author

Büchner, T., Hiddemann, W., Blasius, S., Koch, P., Maschmeyer, G., Tirier, C., Sodomann, H., Kuse, R., Thiel, E., Ludwig, W. D., Seibt-Jung, H., Gassmann, W., Löffler, H., Aul, C., Heyll, A., Mertelsmann, R., Anders, C. H., Nowrousian, M. R., Straif, K., Hossfeld, D., Becker, K., Ho, A., Fülle, H. H., Hellriegel, K.-P., König, H. J., Lengfelder, E., Siegert, W., Bartels, H., Schwammborn, J., Donhuijsen-Ant, R., Vaupel, H. A., König, E., Planker, M., Emmerich, R., Middelhoff, G., Mainzer, K., Urbanitz, D., Zurborn, K.-H., Köppler, H., Nowicki, L., Augener, W., Karow, J., Schroeder, M., Eimermacher, H., Fuchs, R., Balleisen, L., Schmitz-Huebner, U., Leimer, L., Heitzelmann, K. H., Lathan, B., Meuthen, I., Baldus, M., Michels-Giermann, R., Fuhr, H. G., Sauerland, M. C., Heinecke, A., Büchner, T., editor, Schellong, G., editor, Hiddemann, W., editor, and Ritter, J., editor

Published
1990
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8. Correction:High-risk additional chromosomal abnormalities at low blast counts herald death by CML (Leukemia, (2020), 34, 8, (2074-2086), 10.1038/s41375-020-0826-9)

Author

Hehlmann, Rüdiger, Voskanyan, Astghik, Lauseker, Michael, Pfirrmann, Markus, Kalmanti, Lida, Rinaldetti, Sebastien, Kohlbrenner, Katharina, Haferlach, Claudia, Schlegelberger, Brigitte, Fabarius, Alice, Seifarth, Wolfgang, Spieß, Birgit, Wuchter, Patrick, Krause, Stefan, Kolb, Hans Jochem, Neubauer, Andreas, Hossfeld, Dieter K., Nerl, Christoph, Gratwohl, Alois, Baerlocher, Gabriela M., Burchert, Andreas, Brümmendorf, Tim H., Hasford, Jörg, Hochhaus, Andreas, Saußele, Susanne, Baccarani, Michele, von Weikersthal, L. Fischer, Hahn, M., Schlimok, G., Reichert, D., Janssen, J., Martens, U., Majunke, P., Reichert, Peter, Neben, K., Korsten, S., Scholz, Ch, Oldenkott, B., Heßling, J., Kingreen, D., Sperling, C., Schelenz, C., Blau, I., Urmersbach, A., Ludwig, W., Le Coutre, P., Arnold, R., de Wit, M., Pezzutto, A., Schäfer, E., Schroers, R., Lochter, A., Behringer, D., Ko, Y., Weidenhöfer, S., Verbeek, W., Brossart, P., Trenn, G., Pommerien, W., Krauter, J., Doering, G., Munzinger, H., Diekmann, C., Hertenstein, B., Stier, S., Möller-Faßbender, F., Hänel, M., Zöller, T., Lamberti, C., Koch, B., Henzel, A., Wagner, S., Schmalenbach, A., Hoffknecht, M., Ehninger, G., Kiani, A., Illmer, T., Aul, C., Flaßhove, M., Henneke, F., Simon, M., Müller, L., Becker, H., Janz, R., Eckart, M. J., Fuchs, R., Schlegel, F., Wattad, M., Rudolph, R., Beelen, D. W., Lindemann, A., Linck, D., Wassman, Jäger, E., Al-Batran, S., Reiber, T., Waller, C. F., Hoeffkes, H., Schulz, L., Tajrobehkar, K., Mittermüller, J., Pralle, H., Runde, V., Hoyer, A., Tessen, H., Trümper, L., Schmidt, C., Sieber, M., Eschenburg, H., Depenbusch, R., Rösel, S., Lindemann, H. W., Wolf, H., Spohn, C., Moeller, R., Hossfeld, D., Zander, A., Schafhausen, P., Köster, H., Hollburg, W., Schmitz, N., Dürk, H., Hemeier, M., Grote-Metke, A., Weischer, H., Bechtel, B., Balleisen, L., Sosada, M., Ho, A., Petersen, V., Dengler, J., Bildat, S., Hahn, L., Dietzfelbinger, H., Gröschel, W., Bartholomäus, A., Freier, W., Sievers, B., Pfreundschuh, I. M., Herrmann, T., Fauser, A., Menzel, J., Kemmerling, M., Hansen, R., Link, H., Schatz, M., Bentz, M., Prümmer, O., Kneba, M., Heymanns, J., Schmitz, S., Scheid, C., Lollert, A., Neise, M., Planker, M., Stauch, M., Schröder, M., Kempf, B., Vehling-Kaiser, U., Kremers, S., Köchling, G., Hartmann, F., Neuhaus, T., Fetscher, S., Kämpfe, D., Heil, G., Uppenkamp, M., Goldmann, B., Huber, T. Fischer, Hieber, U., Plöger, C., Griesshammer, M., Lange, C., Göttler, B., Lunscken, C., Schiel, X., Scheidegger, C., Stötzer, O., Hitz, H., Schick, H., Völkl, S., Spiekermann, K., Berdel, W., Hebart, H., Ladda, E., Schmidt, P., Burkhardt, U., Hentschke, S., Falge, C., Reschke, D., Köhne, C. A., Müller-Naendrup, C., Sauer, M., Frühauf, S., Ranft, K., Dencausse, Y., Sandritter, B., Baake, G., Hofknecht, M., Dengler, R., Edinger, M., Schenk, M., Wehmeier, A., Weidelich, H. P., Pihusch, R., Stahlhut, K., Baldus, M., Matzdorff, A., Geer, T., Schanz, S., Käfer, G., Gassmann, W., Priebe-Richter, C., Demandt, M., Springer, G., Fiechtner, H., Denzlinger, C., Schleicher, J., Assman, D., Gaeckler, R., Adam, G., Waladkhani, A., Rendenbach, B., Forstbauer, H., Kanz, L., Jacki, S., Stegelmann, F., Kalhori, N., Nusch, A., Langer, W., Müller, F., Brettner, S., Uebelmesser, B., Kamp, T., Schadeck-Gressel, C., Josten, K., Klein, O., Schwerdtfeger, R., Baurmann, H., Strotkötter, H., Fett, W., Raghavachar, A., Maintz, C., Goebler, M. C., Schlag, R., Elsel, W., Wernli, M., Heim, D., Wuillemin, W., Hess, U., Gmür, J., and Mayer, J.

Abstract

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

Published
2020

18. NgCKK (N.Gruberi CKK) decorated 13pf taxol-GDP microtubule

Author

Atherton, J.M., primary, Luo, Y., additional, Xiang, S., additional, Yang, C., additional, Jiang, K., additional, Stangier, M., additional, Vemu, A., additional, Cook, A., additional, Wang, S., additional, Roll-Mecak, A., additional, Steinmetz, M.O., additional, Akhmanova, A., additional, Baldus, M., additional, and Moores, C.A., additional

Published
2019
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19. NgCKK (Naegleria Gruberi CKK) decorated 14pf taxol-GDP microtubule

Author

Atherton, J.M., primary, Luo, Y., additional, Xiang, S., additional, Yang, C., additional, Jiang, K., additional, Stangier, M., additional, Vemu, A., additional, Cook, A., additional, Wang, S., additional, Roll-Mecak, A., additional, Steinmetz, M.O., additional, Akhmanova, A., additional, Baldus, M., additional, and Moores, C.A., additional

Published
2019
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20. HsCKK (human CAMSAP1) decorated 14pf taxol-GDP microtubule

Author

Atherton, J.M., primary, Luo, Y., additional, Xiang, S., additional, Yang, C., additional, Jiang, K., additional, Stangier, M., additional, Vemu, A., additional, Cook, A., additional, Wang, S., additional, Roll-Mecak, A., additional, Steinmetz, M.O., additional, Akhmanova, A., additional, Baldus, M., additional, and Moores, C.A., additional

Published
2019
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23. Probing through-bond connectivities and through-space distances in solids by magic-angle-spinning nuclear magnetic resonance

Author

Baldus, M., Iuliucci, R.J., and Meier, B.H.

Subjects
Organic compounds -- Research, Solid state chemistry -- Research, Nuclear magnetic resonance spectroscopy -- Research, Chemistry
Abstract

High-resolution magic-angle sample spinning experiments using total through-bond correlation spectroscopy and total through-space spectroscopy were carried out to examine the structure of organic solids. The results demonstrated the feasibility of probing both through-bond and through-space connectivities of calcium acetate monohydrate. However, both methods are limited to maximum distances of five angstrom and through-bond connectivities of up to three bonds only.

Published
1997

24. Characterization of deactivated and regenerated zeolite ZSM-5-based catalyst extrudates used in catalytic pyrolysis of biomass

Author

NMR Spectroscopy, Sub Inorganic Chemistry and Catalysis, Sub NMR Spectroscopy, Sub Organic Chemistry and Catalysis, Inorganic Chemistry and Catalysis, Organic Chemistry and Catalysis, Heracleous, E., Pachatouridou, E., Hernández-Giménez, A. M., Hernando, H., Fakin, T., Lucini Paioni, A., Baldus, M., Serrano, D. P., Bruijnincx, P. C.A., Weckhuysen, B. M., Lappas, A. A., NMR Spectroscopy, Sub Inorganic Chemistry and Catalysis, Sub NMR Spectroscopy, Sub Organic Chemistry and Catalysis, Inorganic Chemistry and Catalysis, Organic Chemistry and Catalysis, Heracleous, E., Pachatouridou, E., Hernández-Giménez, A. M., Hernando, H., Fakin, T., Lucini Paioni, A., Baldus, M., Serrano, D. P., Bruijnincx, P. C.A., Weckhuysen, B. M., and Lappas, A. A.

Published
2019

25. Structure investigation on anhydrous disodium hydrogen phosphate using solid-state NMR and X-ray techniques

Author

Baldus, M., Meier, B.H., Ernst, R.R., Kentgens, A.P.M., Altenschildesche, H. Meyer zu, and Nesper, R.

Subjects
Hydrogen sulfide -- Research, Nuclear magnetic resonance -- Usage, Symmetry (Physics) -- Analysis, Chemistry
Abstract

Nuclear magnetic resonance and power X-ray diffraction techniques have been used to study the crystal structure of anhydrous disodium hydrogen phosphate. NMR spectra reveal the superposition of several second-order quadrupolar centerband patterns and three inequivalent sodium sites consistent with a P2(sub1)/c space group and not the predicted P2(sub1)/m structure. Simultaneous double rotation experiments were further conducted to check number of sodium sites. The results of the test are presented.

Published
1995

26. Adult AML: The Role of Chemotherapy Intensity and Duration. Two Studies of the AML Cooperative Group

Author

Büchner, T., primary, Hiddemann, W., additional, Blasius, S., additional, Koch, P., additional, Maschmeyer, G., additional, Tirier, C., additional, Sodomann, H., additional, Kuse, R., additional, Thiel, E., additional, Ludwig, W. D., additional, Seibt-Jung, H., additional, Gassmann, W., additional, Löffler, H., additional, Aul, C., additional, Heyll, A., additional, Mertelsmann, R., additional, Anders, C. H., additional, Nowrousian, M. R., additional, Straif, K., additional, Hossfeld, D., additional, Becker, K., additional, Ho, A., additional, Fülle, H. H., additional, Hellriegel, K.-P., additional, König, H. J., additional, Lengfelder, E., additional, Siegert, W., additional, Bartels, H., additional, Schwammborn, J., additional, Donhuijsen-Ant, R., additional, Vaupel, H. A., additional, König, E., additional, Planker, M., additional, Emmerich, R., additional, Middelhoff, G., additional, Mainzer, K., additional, Urbanitz, D., additional, Zurborn, K.-H., additional, Köppler, H., additional, Nowicki, L., additional, Augener, W., additional, Karow, J., additional, Schroeder, M., additional, Eimermacher, H., additional, Fuchs, R., additional, Balleisen, L., additional, Schmitz-Huebner, U., additional, Leimer, L., additional, Heitzelmann, K. H., additional, Lathan, B., additional, Meuthen, I., additional, Baldus, M., additional, Michels-Giermann, R., additional, Fuhr, H. G., additional, Sauerland, M. C., additional, and Heinecke, A., additional

Published
1990
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27. Overhauser effects in insulating solids.

Author

Can, T. V., Caporini, M. A., Mentink-Vigier, F., Corzilius, B., Walish, J. J., Rosay, M., Maas, W. E., Baldus, M., Vega, S., Swager, T. M., and Griffi, R. G.

Subjects
OVERHAUSER effect (Nuclear physics), DYNAMIC nuclear polarisation, GLYCERIN, WATER, BIPHENYLENE, HYPERFINE interactions, COMPUTER simulation, MAGNETIC fields
Abstract

We report magic angle spinning, dynamic nuclear polarization (DNP) experiments at magnetic fields of 9.4 T, 14.1 T, and 18.8 T using the narrow line polarizing agents 1,3-bisdiphenylene-2-phenylallyl (BDPA) dispersed in polystyrene, and sulfonated-BDPA (SA-BDPA) and trityl OX063 in glassy glycerol/water matrices. The ¹H DNP enhancement field profiles of the BDPA radicals exhibit a significant DNP Overhauser effect (OE) as well as a solid effect (SE) despite the fact that these samples are insulating solids. In contrast, trityl exhibits only a SE enhancement. Data suggest that the appearance of the OE is due to rather strong electron-nuclear hyperfine couplings present in BDPA and SA-BDPA, which are absent in trityl and perdeuterated BDPA (d21 -BDPA). In addition, and in contrast to other DNP mechanisms such as the solid effect or cross effect, the experimental data suggest that the OE in non-conducting solids scales favorably with magnetic field, increasing in magnitude in going from 5 T, to 9.4 T, to 14.1 T, and to 18.8 T. Simulations using a model two spin system consisting of an electron hyperfine coupled to a ¹H reproduce the essential features of the field profiles and indicate that the OE in these samples originates from the zero and double quantum cross relaxation induced by fluctuating hyperfine interactions between the intramolecular delocalized unpaired electrons and their neighboring nuclei, and that the size of these hyperfine couplings is crucial to the magnitude of the enhancements. Microwave power dependent studies show that the OE saturates at considerably lower power levels than the solid effect in the same samples. Our results provide new insights into the mechanism of the Overhauser effect, and also provide a new approach to perform DNP experiments in chemical, biophysical, and physical systems at high magnetic fields. [ABSTRACT FROM AUTHOR]

Published
2014
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28. Relevance of the Mo-precursor state in H-ZSM-5 for methane dehydroaromatization

Author

Vollmer, I., Li, Guanna, Yarulina, I., Kosinov, N., Hensen, E.J.M., Houben, K., Mance, D., Baldus, M., Gascon, J., Kapteijn, F., Vollmer, I., Li, Guanna, Yarulina, I., Kosinov, N., Hensen, E.J.M., Houben, K., Mance, D., Baldus, M., Gascon, J., and Kapteijn, F.

Abstract

Although the local geometry of Mo in Mo/HZSM-5 has been characterized before, we present a systematic way to manipulate the configuration of Mo and link it to its catalytic properties. The location and geometry of cationic Mo-complexes, the precursor of the active metal site for methane dehydroaromatization, are altered by directing the way they anchor to the framework of the zeolite. The feature used to direct the anchoring of Mo is the location of Al in the zeolite framework. According to DFT calculations, the local geometry of Mo should change, while UV-vis and pyridine FTIR spectroscopy indicated differences in the dispersion of Mo. Both aspects, however, did not influence the catalytic behavior of Mo/HZSM-5, indicating that as long as enough isolated Mo species are present inside the pores of the zeolite, the catalytic behavior is unaffected. This paves the way to better understand how the Mo oxo precursor transforms into the active phase under the reaction conditions.

Published
2018

29. A tailored multi-frequency EPR approach to accurately determine the magnetic resonance parameters of dynamic nuclear polarization agents: application to AMUPol

Author

Gast, P, Mance, D, Zurlo, E, Ivanov, K L, Baldus, M, Huber, M, Sub NMR Spectroscopy, NMR Spectroscopy, Sub NMR Spectroscopy, and NMR Spectroscopy

Subjects
010405 organic chemistry, Chemistry, Physics::Medical Physics, Exchange interaction, General Physics and Astronomy, Electron, 010402 general chemistry, Polarization (waves), 01 natural sciences, Molecular physics, Spectral line, 0104 chemical sciences, law.invention, Magnetic field, Dipole, Nuclear magnetic resonance, law, Physical and Theoretical Chemistry, Electron paramagnetic resonance, Anisotropy
Abstract

To understand the dynamic nuclear polarization (DNP) enhancements of biradical polarizing agents, the magnetic resonance parameters need to be known. We describe a tailored EPR approach to accurately determine electron spin-spin coupling parameters using a combination of standard (9 GHz), high (95 GHz) and ultra-high (275 GHz) frequency EPR. Comparing liquid- and frozen-solution continuous-wave EPR spectra provides accurate anisotropic dipolar interaction D and isotropic exchange interaction J parameters of the DNP biradical AMUPol. We found that D was larger by as much as 30% compared to earlier estimates, and that J is 43 MHz, whereas before it was considered to be negligible. With the refined data, quantum mechanical calculations confirm that an increase in dipolar electron-electron couplings leads to higher cross-effect DNP efficiencies. Moreover, the DNP calculations qualitatively reproduce the difference of TOTAPOL and AMUPol DNP efficiencies found experimentally and suggest that AMUPol is particularly effective in improving the DNP efficiency at magnetic fields higher than 500 MHz. The multi-frequency EPR approach will aid in predicting the optimal structures for future DNP agents.

Published
2017

30. Exploring the interactions of irbesartan and irbesartan–2-hydroxypropyl-β-cyclodextrin complex with model membranes

Author

Α. S. Liossi , D. Ntountaniotis, T.F. Kellici, M.V. Chatziathanasiadou, G. Megariotis, M. Mania, J. Becker-Baldus, M. Kriechbaum, A. Krajnc, E. Christodoulou, C. Glaubitz , M. Rappolt, H. Amenitsch, Gregor Mali, D.N. Theodorou, G. Valsami, M. Pitsikalis, H. Iatrou, A. Tzakos, T. Mavromoustakos

Subjects
Θετικές Επιστήμες, Science
Abstract

The interactions of irbesartan (IRB) and irbesartan–2-hydroxypropyl-βcyclodextrin (HP-β-CD) complex with Dipalmitoyl Phosphatidylcholine (DPPC) bilayers have been explored utilizing an array of biophysical techniques ranging from Differential Scanning Calorimetry (DSC), Small angle X-ray Scattering (SAXS), ESI Mass-Spectrometry (ESI-MS) and solid state Nuclear Magnetic Resonance (ssNMR). Molecular Dynamics (MD) calculations have been also conducted to complement the experimental results. Irbesartan was found to be embedded in the lipid membrane core and to affect the phase transition properties of the DPPC bilayers. SAXS studies revealed that irbesartan alone does not display perfect solvation since some coexisting irbesartan crystallites are present. In its complexed form IRB gets fully solvated in the membranes showing that encapsulation of IRB in HP-β-CD may have beneficial effects in the ADME properties of this drug. MD experiments revealed the topological and orientational integration of irbesartan into the phospholipid bilayer being placed at about 1 nm from the membrane centre.

Published
2017

35. Overhauser effects in insulating solids

Author

Massachusetts Institute of Technology. Department of Chemistry, Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology), Can, Thach Van, Corzilius, Bjorn, Walish, Joseph John, Swager, Timothy M, Griffin, Robert Guy, Caporini, M. A., Mentink-Vigier, F., Rosay, M., Maas, W. E., Baldus, M., Vega, S., Can, Thach V, Massachusetts Institute of Technology. Department of Chemistry, Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology), Can, Thach Van, Corzilius, Bjorn, Walish, Joseph John, Swager, Timothy M, Griffin, Robert Guy, Caporini, M. A., Mentink-Vigier, F., Rosay, M., Maas, W. E., Baldus, M., Vega, S., and Can, Thach V

Abstract

We report magic angle spinning, dynamic nuclear polarization (DNP) experiments at magnetic fields of 9.4 T, 14.1 T, and 18.8 T using the narrow line polarizing agents 1,3-bisdiphenylene-2-phenylallyl (BDPA) dispersed in polystyrene, and sulfonated-BDPA (SA-BDPA) and trityl OX063 in glassy glycerol/water matrices. The 1H DNP enhancement field profiles of the BDPA radicals exhibit a significant DNP Overhauser effect (OE) as well as a solid effect (SE) despite the fact that these samples are insulating solids. In contrast, trityl exhibits only a SE enhancement. Data suggest that the appearance of the OE is due to rather strong electron-nuclear hyperfine couplings present in BDPA and SA-BDPA, which are absent in trityl and perdeuterated BDPA (d21-BDPA). In addition, and in contrast to other DNP mechanisms such as the solid effect or cross effect, the experimental data suggest that the OE in non-conducting solids scales favorably with magnetic field, increasing in magnitude in going from 5 T, to 9.4 T, to 14.1 T, and to 18.8 T. Simulations using a model two spin system consisting of an electron hyperfine coupled to a 1H reproduce the essential features of the field profiles and indicate that the OE in these samples originates from the zero and double quantum cross relaxation induced by fluctuating hyperfine interactions between the intramolecular delocalized unpaired electrons and their neighboring nuclei, and that the size of these hyperfine couplings is crucial to the magnitude of the enhancements. Microwave power dependent studies show that the OE saturates at considerably lower power levels than the solid effect in the same samples. Our results provide new insights into the mechanism of the Overhauser effect, and also provide a new approach to perform DNP experiments in chemical, biophysical, and physical systems at high magnetic fields., National Institute of General Medical Sciences (U.S.) (Grant No. GM095843), National Institute for Biomedical Imaging and Bioengineering (U.S.) (NIBIB, Grant No. EB-002804)), National Institute for Biomedical Imaging and Bioengineering (U.S.) (NIBIB, Grant No. EB002026)

Published
2017

36. Rapid prediction of multi-dimensional NMR data sets

Author

Gradmann, S.H.E., Ader, C., Heinrich, I., Nand, D., Dittmann, M., Cukkemane, A.A., van Dijk, M., Bonvin, A.M.J.J., Engelhard, M., Baldus, M., NMR Spectroscopy, Sub NMR Spectroscopy, NMR Spectroscopy, Sub NMR Spectroscopy, Molecular and Computational Toxicology, and AIMMS

Subjects
Channel (digital image), Data set, Databases, Factual, In silico, Analytical chemistry, Cyclic Nucleotide-Gated Cation Channels, Context (language use), Experimental data, 010402 general chemistry, 01 natural sciences, Biochemistry, Solid-state NMR, Nuclear magnetic resonance, 03 medical and health sciences, Software, Taverne, Sensory Rhodopsins, Nuclear Magnetic Resonance, Biomolecular, Spectroscopy, Sensory rhodopsin II, 030304 developmental biology, 0303 health sciences, Binding Sites, Chemistry, business.industry, Chemical shift, Protein, Membrane, Multi dimensional, Computational environment, NMR, 0104 chemical sciences, Solid-state nuclear magnetic resonance, Content (measure theory), Biological system, business, Algorithms
Abstract

We present a computational environment for Fast Analysis of multidimensional NMR DAta Sets (FANDAS) that allows assembling multidimensional data sets from a variety of input parameters and facilitates comparing and modifying such "in silico" data sets during the various stages of the NMR data analysis. The input parameters can vary from (partial) NMR assignments directly obtained from experiments to values retrieved from in silico prediction programs. The resulting predicted data sets enable a rapid evaluation of sample labeling in light of spectral resolution and structural content, using standard NMR software such as Sparky. In addition, direct comparison to experimental data sets can be used to validate NMR assignments, distinguish different molecular components, refine structural models or other parameters derived from NMR data. The method is demonstrated in the context of solid-state NMR data obtained for the cyclic nucleotide binding domain of a bacterial cyclic nucleotide-gated channel and on membrane-embedded sensory rhodopsin II. FANDAS is freely available as web portal under WeNMR ( http://www.wenmr.eu/services/FANDAS ).

Published
2012

37. Limited clinical relevance of imaging techniques in the follow-up of patients with advanced chronic lymphocytic leukemia: results of a meta-analysis

Author

Eichhorst, Barbara F, Fischer, Kirsten, Fink, Anna Maria, Elter, Thomas, Wendtner, Clemens M, Goede, Valentin, Bergmann, Manuela, Stilgenbauer, Stephan, Hopfinger, Georg, Ritgen, Matthias, Bahlo, Jasmin, Busch, Raymonde, Hallek, Michael, Oduncu, F, Dreyling, M, Forstpointner, R, Schneller, F, Bogner, C, Peschel, C, Ringshausen, I, Götze, K, Goebeler, Me, Rückle, Lanz, Ritgen, M, Schawitzke, A, Heydrich, B, Kern, K, Böttcher, S, Irmer, S, Strack, U, Borries, V, Klima, Km, Scholz, C, Herold, M, Härtwig, K, Dürig, J, Dührsen, U, Müller Beissenhirtz, H, Noppeney, R, Schüttrumpf, S, Hohloch, K, Binder, C, Hasenkamp, J, Trümper, L, Bäsecke, J, Rieger, M, Witzens Harig, M, Friedrichs, B, Rieger, K, Uharek, L, Kubuschok, B, Murawski, N, Held, G, Zwick, C, Pfreundschuh, M, Fingerle Rowson, G, Reiser, M, Elter, T, Eichhorst, B, Pallasch, C, Hallek, M, Borchmann, P, Hacker, U, Schinkel, S, Wieker, K, Sökler, M, Wolf, Hh, Eucker, J, Staib, P, Schlegel, F, Kropff, M, Kahl, C, Hess, G, Beck, J, Wölfel, T, Bokemeyer, C, Schilling, G, Dierlamm, J, Schüler, F, Busemann, C, Dölken, G, Trendelenburg, Tk, Bühler, A, Stilgenbauer, S, Viardot, A, Greiner, J, Zenz, T, Gaidzik, V, Langer, C, Döhner, H, Werner, I, Dienst, A, Habersang, K, Härtel, N, Leitner, A, Kehrer, G, Middeke, H, Heinisch, K, Adorf, D, Ismer, B, Hering Schubert, C, Jäckle, J, Aulmann, C, Söllner, S, Majunke, P, Fuss, H, Käfer, G, Potenberg, J, Dietrich, G, Hartung, E, Pronath, A, Riedhammer, Fj, Zehrfeld, T, Prümmer, O, Gatter, J, Meier, A, Wattad, M, Heit, W, Sauer, I, Hilgers, K, Geissler, M, Bauer, J, Stein, W, Voigtmann, R, Natt, F, Nickelsen, M, Zeis, M, Schmitz, N, Lange, E, Stoltefuss, A, Schubert, J, Dürk, Ha, Kloke, O, Fauser, A, Roemer, E, Kraut, L, Musch, E, Kohl, S, Link, H, Kirsch, Jf, Schatz, M, Mezger, J, Kempf, B, Heil, G, Derigs, Hg, Roll, C, Kettner, E, Dübbers, Hw, Lutz, L, Hentrich, M, Hoffmann, U, Ibe, M, Falge, C, Schäfer Eckart, K, Rothmann, F, Raghavachar, A, Beckmann, K, Behringer, D, Stauder, H, Hempfling, C, Matzdorff, A, Hähling, D, Kaesberger, Kj, Mück, R, Waladkhani, Ar, Clemens, M, Kraft, J, Ehlert, T, N. N., Schloen, A, Sandritter, B, Scholz, Diekmann, C, Pflüger, Kh, Hausner, G, Fetscher, S, Aulitzky, W, Brugger, W, Frickhofen, N, Fuhr, Lange, C, Lambertz, H, Schulz, L, Schmier, M, Bentz, M, Tauchmann, Gm, Schmidt, M, Meiler, J, Sandmann, M, Kürschner, D, Maier Bay, B, Lindemann, W, Diers, J, Riemeier Sievers, C, Daun, M, Mergenthaler, Hg, Hiller, S, Schirmer, V, Kirchner, H, Langer, W, Günther, B, Gassmann, W, Franke, K, Burghardt, F, Abele, U, Celikel Becker, D, von Weikersthal LF, Brög, G, Hauch, U, Heinrich, B, Brudler, O, Häcker, B, Eckart, Mj, Bolouri, H, Göttler, B, Kindler, M, Zuchold, K, Strohbach, F, Plingen, Ml, Seibt Jung, H, Kirsch, A, Herrenberger, J, Doering, G, von Grünhagen, U, Franke, H, Weniger, J, Kerzel, W, Schmalfeld, M, Rohrberg, R, Hurtz, Hj, Gehbauer, G, Hahnfeld, S, Vehling Kaiser, U, Abenhardt, W, Bosse, D, Böning, L, Schmidt, B, Schick, Hd, Jacobs, G, Stauch, M, Hoffmann, R, Müller, S, Hahn, M, Freier, W, Dietzfelbinger, H, Rassmann, I, Söling, U, Siehl, S, Rudolph, R, Weinert, R, Sauer, A, Meyer, B, Eschenburg, H, Schadeck Gressel, C, Grabenhorst, U, Perker, M, Otremba, B, Reschke, D, Hinrichs, Hf, Zirpel, I, Höring, E, Respondek, M, Köppler, H, Heymanns, J, Weide, R, Hünermund, K, Thiel, C, Reiber, T, Spohn, C, Springer, G, Fiechtner, H, Hübner, A, Kurschel, E, Weiss, J, Schlag, R, Schäfer, E, Hartwich, G, Schmitz, S, Steinmetz, T, Kim, Ts, Lerchenmüller, C, Wehmeyer, J, Laubenstein, Hp, Rendenbach, B, Lebahn, H, Kröning, H, Uhle, R, Balló, H, Gaede, B, Zumbrink, S, Eckert, R, Kamp, T, Reimann, B, Burkhard, O, Mittermüller, J, Hansen, R, Hitz, H, Schliesser, G, Schmitt, Hr, Forstbauer, H, Grundeis, M, Schulze, M, Baldus, M, Lakner, V, Haen, M, Müller, C, Dörfel, S, Göhler, T, Welslau, M, Achtzehn, V, Culmann, H, Gerhardt, S, Ulshöfer, T, Koschuth, A, Schmidt, P, Müller, L, Schneider, M, Koniczek, K, Porowski, P, Glados, M, Knoblich, J, Ben Yehuda, D, Jäger, U, Gaiger, A, Schwarzmeier, J, Nösslinger, T, Smith, M, Patton, N, Gibbons, S, Bouabdallah, R, Gandhi, M, Marlton, P, Mills, T, Angelucci, E, Sorano, Gg, Casula, P, Berneman, Z, Kohser, P, Hudcova Burgetova, A, Machová, R, Papajik, T, Kubová, Z, Fineman, R, Mayer, J, Doubek, M, Brychtova, Y, Ciceri, F, Caligaris Cappio, F, Crocchiolo, R, Dauriac, C, Bernard, M, Escoffre Barbe, M, Lamy, T, Zikesova, E, Karban, J, Salkova, J, Trnený, M, Pytlik, R, Tiley, C, Forsyth, C, Vokurka, S, Koza, V, Van Hoof, A, Selleslag, D, Sebban, C, Baker, B, Belada, D, Jebavy, L, Smolej, L, Pavel, Z, Di Ianni, M, Castaigne, S, Del Poeta, G, Amadori, S, Catalano, J, Ganju, V, Hertzberg, M, Laurenti, L, Dalseg, Am, Bron, D, Morton, J, Durrant, S, Casado, Lf, Theunissen, K, Atias, D, Berkhan, L, Seymour, J, Wolf, M, Bosly, A, Osma Cordoba MM, Portois, C, Jaubert, J, Ferrant, A, Lambert, C, Maerevoet, E, Van den Neste, E, Gadeberg, O, Carney, B, Cannell, P, Eghbali, H, Legouffe, E, Bordessoule, D, Chaury, M, Moreau, S, Pierri, I, Gobbi, M, Berrebi, A, Lishner, M, Yerushazim, R, Yermiaku, T, Kosolov, V, Ambrosetti, Achille, Andreoli, Al, Huguet, F, Laurent, G, Orsucci, L, Forconi, F, Musuraca, G, Zinzani, Pl, Loscertales, J, Mcquillan, A, Cordingley, F, Leahy, M, Cazin, B, Taylor, Mulligan, S, Herbrecht, Cull, G, Seldon, M, Rowlings, P, Ludwig, H, Zojer, N, Solal Céligny, P, Pomponi, F, Savdkova, L, Kozák, T, Christiansen, I, Pérez, I, Campbell, P, Canales Albendea, M, De Paz, R, Arthur, C, Gisselbrecht, C., Eichhorst B.F., Fischer K., Fink A.M., Elter T., Wendtner C.M., Goede V., Bergmann M., Stilgenbauer S., Hopfinger G., Ritgen M., Bahlo J., Busch R., Hallek M., and Zinzani P.L.

Subjects
Male, medicine.medical_specialty, Cyclophosphamide, Chronic lymphocytic leukemia, Immunology, Medizin, Antineoplastic Combined Chemotherapy Protocols, Blood Cell Count, Disease Progression, Disease-Free Survival, Female, Follow-Up Studies, Humans, Leukemia, Lymphocytic, Chronic, B-Cell, Middle Aged, Prognosis, Recurrence, Remission Induction, Tomography, X-Ray Computed, Physical examination, Biochemistry, Chemoimmunotherapy, medicine, Chronic, Tomography, Leukemia, medicine.diagnostic_test, business.industry, B-Cell, Cancer, Cell Biology, Hematology, medicine.disease, Lymphocytic, imaging techniques, X-Ray Computed, Fludarabine, Surgery, chronic lymphocytic leukemia, Radiology, business, Progressive disease, medicine.drug
Abstract

The clinical value of imaging is well established for the follow-up of many lymphoid malignancies but not for chronic lymphocytic leukemia (CLL). A meta-analysis was performed with the dataset of 3 German CLL Study Group phase 3 trials (CLL4, CLL5, and CLL8) that included 1372 patients receiving first-line therapy for CLL. Response as well as progression during follow-up was reassessed according to the National Cancer Institute Working Group1996 criteria. A total of 481 events were counted as progressive disease during treatment or follow-up. Of these, 372 progressions (77%) were detected by clinical symptoms or blood counts. Computed tomography (CT) scans or ultrasound were relevant in 44 and 29 cases (9% and 6%), respectively. The decision for relapse treatment was determined by CT scan or ultrasound results in only 2 of 176 patients (1%). CT scan results had an impact on the prognosis of patients in complete remission only after the administration of conventional chemotherapy but not after chemoimmunotherapy. In conclusion, physical examination and blood count remain the methods of choice for staging and clinical follow-up of patients with CLL as recommended by the International Workshop on Chronic Lymphocytic Leukemia 2008 guidelines. These trials are registered at http://www.isrctn.org as ISRCTN 75653261 and ISRCTN 36294212 and at http://www.clinicaltrials.gov as NCT00281918.

Published
2011

38. Interaction of Epothilone B (Patupilone) with Microtubules as Detected by Two-Dimensional Solid-State NMR Spectroscopy

Author

Kumar, A., Heise, H., Blommers, M. J. J., Krastel, P., Schmitt, E., Petersen, F., Jeganathan, S., Mandelkow, E. -M, Carlomagno, T., Griesinger, C., Baldus, M., NMR Spectroscopy, Sub NMR Spectroscopy, NMR Spectroscopy, and Sub NMR Spectroscopy

Subjects
Models, Molecular, Epothilones, Tubulin, Neoplasms, Humans, Antineoplastic Agents, Myxococcales, General Chemistry, Microtubules, Nuclear Magnetic Resonance, Biomolecular, Tubulin Modulators, Catalysis
Abstract

Solid evidence: Induction of the polymerization of β-tubulin dimers into microtubules by epothilones, such as patupilone, by an as yet unknown mechanism leads to the apoptosis of cancer cells. Solid-state NMR spectroscopy of patupilone bound to microtubules has now enabled the identification of atomic positions of the drug that undergo clear chemical-shift changes upon binding (see correlation spectra of free (black) and complexed patupilone (red)).

Published
2010

39. Mechanism of microtubule minus-end recognition and protection by CAMSAP proteins

Author

Akhmanova, A., primary, Moores, C.A., additional, Baldus, M., additional, Steinmetz, M.O., additional, Topf, M., additional, Roberts, A.J., additional, Grant, B.J., additional, Scarabelli, G., additional, Joseph, A.-P., additional, van Hooff, J.J.E., additional, Houben, K., additional, Hua, S., additional, Luo, Y., additional, Stangier, M.M., additional, Jiang, K., additional, and Atherton, J., additional

Published
2017
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40. Clonal Evolution and Blast Crisis Correlate with Enhanced Proteolytic Activity of Separase in BCR-ABL b3a2 Fusion Type CML under Imatinib Therapy

Author

Haaß, Wiltrud, Kleiner, Helga, Schweizerische Arbeitsgemeinschaft für Klinische Krebsforschung, Morgner, A., Herbst, R., Matek, W., Lamberti, C., Zöller, T., Koch, B., Marth, T., Henzel, A., Wagner, S., Woska, E., German CML Study Group, Neumann, F., Hoffknecht, M. M., Illmer, T., Wolf, T., Ehninger, G., Kiani, A., Platzbecker, U., Aul, C., Badrakhan, C. D., Giagounidis, A., Wernli, M., Flaßhove, M., Henneke, F., Moritz, T., Simon, M., Müller, L. L., Janz, R., Eckart, M., Häcker, B., Rech, D., Mackensen, A., Bargetzi, M., Krause, S. W., Staib, P., Schlegel, F., Wätzig, K., Rudolph, R., Wattad, M., Baur, F. K., Heit, W., Beelen, D. W., Hüttmann, A., Fischer von Weikersthal, L., Novotny, J., Trenschel, R., Lindemann, A., Linck, D., Jäger, E., Al-Batran, Salah-Eddin, Ottmann, O. G., Serve, H., Reiber, T., Semsek, D., Gro, V., Waller, C., Kühnemund, A., Hoeffkes, H. G., Lambertz, H., Schulz, L., Tajrobehkar, K., Mittermüller, J., Rummel, M. J., Burchardt, A., Pralle, H., Müller, S., Runde, V., Klei, M., Westheider, J., Hoyer, A., Tessen, H. W., Hesse, A., Trümper, L., Binder, C., Schmidt, C. A., Hirt, C., Hahn, M., Sieber, M., Eschenburg, H., Wilhelm, S., Depenbusch, R., Rösel, S., Eimermacher, H., Spohn, C., Moeller, R., Schmitz, N., Nickelsen, M., Schlimok, G., Engel, E., Haatanen, T., Hollburg, W., Platz, D., Köster, H., Bokemeyer, C., Schafhausen, P., Grote-Metke, A., Bechtel, B., Hemeier, M., Reichert, D., Sosada, M., Ganser, A., Schlegelberger, B., Ho, A. D., Rohlfing, S., Dengler, J., Petersen, V., Porowski, P., Hahn, L., Dietzfelbinger, H., Weiß, Christel, Janssen, J., Gröschel, W., Bartholomäus, A., Pfreundschuh, M., Kemmerling, M., Hansen, R., Reeb, M., Link, H., Mahlmann, S., Mezger, J., Schatz, M., Furkert, J., Schmier, M., Gatter, J., Neumann, S., Heymanns, J., Steinmetz, H. T., Schmitz, S., Scheid, C., Planker, M., Frieling, T., Lollert, A., Mandel, T., Neise, M., Schröder, M., Greif, D., Kempf, B., März, W., Kremers, S., Müller, L., Hartmann, F., Heil, G., Goldmann, B., Majunke, P. J., Heinkele, P., Gregor, M., Theobald, M., Fischer, T., Thomas, S., Hensel, M., Plöger, C., Schuster, D., Brust, J., Hieber, U., Paliege, R., Hehlmann, R., Neubauer, A., Burchert, A., Graeven, U., Lange, C., Schmidt, G., Völkl, S., Schmidt, B., Hitz, H., Spiekermann, K., Reichert, P., Hiddemann, W., Haferlach, T., Haferlach, C., Schnittger, S., Stötzer, O., Scheidegger, C., Fischer, C., Berdel, W. E., Koppele, A., Hebart, H., Fuss, H., Snaga, A., Schmidt, P., Hoffmann, R., Reschke, D., Zirpel, I., Sauer, M., Lenk, G., Theilmann, L., Sandritter, B., Neben, K., Schenk, M., Dengler, R., Herr, W., Krause, S., Braun, B., Günther, E., Wacker, A., Pihusch, R., Baldus, M., Matzdorff, A., Staiger, H. J., Pollmeier, G., Grimminger, W., Geer, T., Schanz, S., Jür, C., Gassmann, W., Seitz, K., Kaesberger, J., Mück, R., Heim, D., Illerhaus, G., Denzlinger, C., Fiechtner, H., Springer, G., Hoffmann, D., Jacki, S. H., Kanz, L., Bross-Bach, U., Döhner, H., Stegelmann, F., Haferlach, Claudia, Gratwohl, A., Kalhori, N., Langer, W., Nusch, A., Wei, J., Kamp, T., Schadeck-Gressel, C., Schwerdtfeger, R., Josten, K. M., Klein, O., Fett, W., Tichelli, A., Strotkötter, H., Maintz, C., Groschek, M., Schlag, R., Elsel, W., Schüler, F., Dölken, G., Lindemann, H. W., Wolf, H. H., Schmoll, H. J., Korsten, S., Braumann, D., Hoelzer, P., Kleeberg, U., Hossfeld, D., Lange, E., Schubert, J., Weischer, H., Dürk, H. A., Kirchner, H. H., Bu, E C., Henesser, D., Sievers, B., Freier, W., Kaiser, U., Peest, D., Römer, E., Hermann, T., Fauser, A., Valverde, M. L., Menzel, J., Kemper, J., le Coutre, P., Hochhaus, A., La Rosée, P., Bentz, M., Prümmer, O., Kneba, M., Strack, U., Schoch, R., Severin, K., Stauch, M., Arnold, R., Karbach, U., Vehling-Kaiser, U., Köchling, G., Wei, U., Middeke, H., Neuhaus, T., Martin, H., Fetscher, S., Schmielau, J., Kämpfe, D., Ludwig, W. D., Uppenkamp, M., Wei, B., Thum, P., Wuillemin, W., Hofmann, W. K., Griesshammer, M., Tischler, H. J., Becker, M., Hanfstein, B., Müller, M., Ratei, R., Saußele, S., Lunscken, C., Kolb, H. J., Lutz, L., Hentrich, M., Nerl, C., Wendtner, C., Ladda, E., Gnad, M., Teutsch, C., Suna, H., Schmidt, E., Koschmieder, S., Falge, C., Wandt, H., Wilhelm, M., Köhne, C. H., Schweiger, C., Müller-Naendrup, C., Frühauf, S., Ludwig, F., Ranft, K., Dencausse, Y., Baake, G., Ritter, P. R., Kloke, O., Göttler, B., Schick, H. D., Schlegelberger, Brigitte, Urmersbach, A., Weidenhöfer, S., Weidinger, P., Wacker, D., Wehmeyer, J., Kreuser, E. D., Schlenska-Lange, A., Edinger, R., Andreesen, R., Wehmeier, A., Stahlhut, K., Blau, I., Käfer, G., Cerny, T., Hess, U., Priebe-Richter, C., Stange-Budumlu, O., Demandt, M., Freunek, G., Heidemann, E., Schleicher, J., Mergenthaler, H. G., Ihle, H., Boewer, C., Zeller, C., Laubenstein, H. P., Rendenbach, B., Clemens, M., Waladkhani, A. R., Forstbauer, H., Müller, F., Brettner, S., Raghavachar, A., Sperling, C., Kunzmann, V., Goebeler, M. E., Gmür, J., Schelenz, C., Koschuth, A., Kingreen, D., Heßling, J., Derwahl, K. M., Oldenkott, B., Müller, Martin C., Englisch, H. J., Thiel, E., Burmeister, T., Notter, M., de Wit, M., Rothaug, W., Büschel, G., Beyer, J., Dahmen, E., Hehlmann, Rüdiger, Biaggi, C., Lämmle, B., Friess, D., Baerlocher, G., Oppliger Leibundgut, E., Tobler, A., Just, M., Schäfer, E., Behringer, D., Brandt, M., Hofmann, Wolf-Karsten, Schmiegel, W., Vaupel, H. A., Verbeek, W., Ko, Y. D., Sauerbruch, T., Hahn-Ast, C., Janzen, V., Schmidt-Wolf, Ingo G. H., Trenn, G., Fabarius, Alice, van der Linde, M., Pommerien, W., Fritz, L., Krauter, J., Lordick, F., Fritsch, G., Pflüger, K. H., Diekmann, C., Kullmer, J., Doering, G., Seifarth, Wolfgang, Munzinger, H., Hertenstein, B., Peyn, A., Mayer, J., Zácková, D., Kujickova, J., Stier, S., Wejda, B., Möller-Faßbender, F., and Hänel, M.

Subjects
Adult, Aged, 80 and over, Chromosome Aberrations, Adolescent, Fusion Proteins, bcr-abl, Antineoplastic Agents, Chromosome Breakage, Middle Aged, Clonal Evolution, Young Adult, hemic and lymphatic diseases, Cell Line, Tumor, Leukemia, Myelogenous, Chronic, BCR-ABL Positive, Proteolysis, Imatinib Mesylate, Humans, Blast Crisis, Separase, Research Article, Aged
Abstract

PLoS ONE 10(6), e0129648 (2015). doi:10.1371/journal.pone.0129648, Published by PLoS, Lawrence, Kan.

Published
2015
Full Text
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42. Importance of lipid-pore loop interface for potassium channel structure and function

Author

van der Cruijsen, E.A.W., Nand, D., Weingarth, M.H., Prokofyev, A., Hornig, S., Cukkemane, A.A., Bonvin, A.M.J.J., Becker, S., Hulse, R.E., Perozo, E., Pongs, O., Baldus, M., NMR Spectroscopy, and Sub NMR Spectroscopy

Subjects
Models, Molecular, Magnetic Resonance Spectroscopy, Potassium Channels, Protein Conformation, Recombinant Fusion Proteins, Xenopus, Lipid Bilayers, Molecular Sequence Data, KcsA potassium channel, Molecular Dynamics Simulation, 010402 general chemistry, 01 natural sciences, Membrane Potentials, 03 medical and health sciences, Bacterial Proteins, Taverne, Animals, Amino Acid Sequence, Lipid bilayer, Ion channel, 030304 developmental biology, 0303 health sciences, Multidisciplinary, Binding Sites, Kv1.3 Potassium Channel, Sequence Homology, Amino Acid, Chemistry, Voltage-gated potassium channel, Biological Sciences, Tandem pore domain potassium channel, Potassium channel, 0104 chemical sciences, Protein Structure, Tertiary, Crystallography, Transmembrane domain, Mutation, Oocytes, Ligand-gated ion channel, Female, Ion Channel Gating, Protein Binding
Abstract

Potassium (i.e., K + ) channels allow for the controlled and selective passage of potassium ions across the plasma membrane via a conserved pore domain. In voltage-gated K + channels, gating is the result of the coordinated action of two coupled gates: an activation gate at the intracellular entrance of the pore and an inactivation gate at the selectivity filter. By using solid-state NMR structural studies, in combination with electrophysiological experiments and molecular dynamics simulations, we show that the turret region connecting the outer transmembrane helix (transmembrane helix 1) and the pore helix behind the selectivity filter contributes to K + channel inactivation and exhibits a remarkable structural plasticity that correlates to K + channel inactivation. The transmembrane helix 1 unwinds when the K + channel enters the inactivated state and rewinds during the transition to the closed state. In addition to well-characterized changes at the K + ion coordination sites, this process is accompanied by conformational changes within the turret region and the pore helix. Further spectroscopic and computational results show that the same channel domain is critically involved in establishing functional contacts between pore domain and the cellular membrane. Taken together, our results suggest that the interaction between the K + channel turret region and the lipid bilayer exerts an important influence on the selective passage of potassium ions via the K + channel pore.

Published
2013

43. Protein oligomers studied by solid-state NMR the case of the full-length nucleoid-associated protein histone-like nucleoid structuring protein

Author

Renault, M.A.M., García, J., Cordeiro, T.N., Baldus, M., Pons, M., NMR Spectroscopy, Sub NMR Spectroscopy, NMR Spectroscopy, Sub NMR Spectroscopy, and Universitat de Barcelona

Subjects
Models, Molecular, Magnetic Resonance Spectroscopy, ADN, Biology, 010402 general chemistry, Medical sciences, 01 natural sciences, Biochemistry, Protein Structure, Secondary, Ressonància magnètica nuclear, Nuclear magnetic resonance, Cromatina, Histones, 03 medical and health sciences, chemistry.chemical_compound, Gene expression, Escherichia coli, Nucleoid, Protein Interaction Domains and Motifs, Protein Structure, Quaternary, Molecular Biology, 030304 developmental biology, Ciències de la salut, Oligòmers, 0303 health sciences, Binding Sites, Accession number (library science), Escherichia coli Proteins, Proteins, Biological activity, Cell Biology, DNA, Chromatin, 0104 chemical sciences, Histone-like nucleoid-structuring protein, Solid-state nuclear magnetic resonance, chemistry, Oligomers, Fimbriae Proteins, Proteïnes
Abstract

Members of the histone-like nucleoid structuring protein (H-NS) family play roles both as architectural proteins and as modulators of gene expression in Gram-negative bacteria. The H-NS protein participates in modulatory processes that respond to environmental changes in osmolarity, pH, or temperature. H-NS oligomerization is essential for its activity. Structural models of different truncated forms are available. However, high-resolution structural details of full-length H-NS and its DNA-bound state have largely remained elusive. We report on progress in characterizing the biologically active H-NS oligomers with solid-state NMR. We compared uniformly (13C,15N)-labeled ssNMR preparations of the isolated N-terminal region (H-NS 1–47) and full-length H-NS (H-NS 1–137). In both cases, we obtained ssNMR spectra of good quality and characteristic of well-folded proteins. Analysis of the results of 2D and 3D 13C–13C and 15N–13C correlation experiments conducted at high magnetic field led to assignments of residues located in different topological regions of the free full-length H-NS. These findings confirm that the structure of the N-terminal dimerization domain is conserved in the oligomeric full-length protein. Small changes in the dimerization interface suggested by localized chemical shift variations between solution and solid-state spectra may be relevant for DNA recoginition. Database Structural data are available in the BioMagResBank database (BMRB; http://www.bmrb.wisc.edu) under accession number 18814. Structured digital abstract H-NS and H-NS bind by nuclear magnetic resonance (View interaction)

Published
2013

44. Characterization of a cyclic nucleotide-activated K(+) channel and its lipid environment by using solid-state NMR spectroscopy

Author

Cukkemane, A.A., Baldus, M., NMR Spectroscopy, and Sub NMR Spectroscopy

Subjects
Potassium Channels, Mutant, Lipid Bilayers, 010402 general chemistry, 01 natural sciences, Biochemistry, 03 medical and health sciences, Cyclic nucleotide, chemistry.chemical_compound, Lipid bilayer, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular, Ion channel, 030304 developmental biology, 0303 health sciences, Carbon Isotopes, Binding Sites, Nitrogen Isotopes, Nucleotides, Organic Chemistry, Recombinant Proteins, 0104 chemical sciences, Protein Structure, Tertiary, Crystallography, Membrane, Solid-state nuclear magnetic resonance, Membrane protein, chemistry, 13. Climate action, Cyclic nucleotide-binding domain, Biophysics, Molecular Medicine
Abstract

Voltage-gated ion channels are large tetrameric multidomain membrane proteins that play crucial roles in various cellular transduction pathways. Because of their large size and domain-related mobility, structural characterization has proved challenging. We analyzed high-resolution solid-state NMR data on different isotope-labeled protein constructs of a bacterial cyclic nucleotide-activated K(+) channel (MlCNG) in lipid bilayers. We could identify the different subdomains of the 4×355 residue protein, such as the voltage-sensing domain and the cyclic nucleotide binding domain. Comparison to ssNMR data obtained on isotope-labeled cell membranes suggests a tight association of negatively charged lipids to the channel. We detected spectroscopic polymorphism that extends beyond the ligand binding site, and the corresponding protein segments have been associated with mutant channel types in eukaryotic systems. These findings illustrate the potential of ssNMR for structural investigations on large membrane-embedded proteins, even in the presence of local disorder.

Published
2013

45. Structural determinants of specific lipid binding to potassium channels

Author

Weingarth, M.H., Prokofyev, A., van der Cruijsen, E.A.W., Nand, D., Bonvin, A.M.J.J., Pongs, O., Baldus, M., NMR Spectroscopy, and Sub NMR Spectroscopy

Subjects
Models, Molecular, Binding Sites, Kv1.3 Potassium Channel, Potassium Channels, Molecular Structure, Chemistry, KcsA potassium channel, General Chemistry, Biochemistry, Lipids, Catalysis, Potassium channel, Colloid and Surface Chemistry, Bacterial Proteins, Lipid binding, Taverne, Molecule, Binding site, Nuclear Magnetic Resonance, Biomolecular
Abstract

We have investigated specific lipid binding to the pore domain of potassium channels KcsA and chimeric KcsA-Kv1.3 on the structural and functional level using extensive coarse-grained and atomistic molecular dynamics simulations, solid-state NMR, and single channel measurements. We show that, while KcsA activity is critically modulated by the specific and cooperative binding of anionic nonannular lipids close to the channel's selectivity filter, the influence of nonannular lipid binding on KcsA-Kv1.3 is much reduced. The diminished impact of specific lipid binding on KcsA-Kv1.3 results from a point-mutation at the corresponding nonannular lipid binding site leading to a salt-bridge between adjacent KcsA-Kv1.3 subunits, which is conserved in many voltage-gated potassium channels and prevents strong nonannular lipid binding to the pore domain. Our findings elucidate how protein-lipid and protein-protein interactions modulate K(+) channel activity. The combination of MD, NMR, and functional studies as shown here may help to dissect the structural and dynamical processes that are critical for the functioning of larger membrane proteins, including Kv channels in a membrane setting.

Published
2013

46. Development of a 4,4’-biphenyl/phosphine-based COF for the heterogeneous Pd-catalysed telomerisation of 1,3-butadiene

Author

Hausoul, P.J.C., Eggenhuisen, T.M., Nand, D., Baldus, M., Weckhuysen, B.M., Klein Gebbink, R.J.M., Bruijnincx, P.C.A., Inorganic Chemistry and Catalysis, NMR Spectroscopy, Sub Inorganic Chemistry and Catalysis, Sub NMR Spectroscopy, and Sub Chem Biol & Organic Chem begr 1-6-12

Abstract

The improved synthesis, characterisation and application of a microporous 4,40-biphenyl/phosphine-based covalent organic framework (COF) for the heterogeneous Pd-catalysed telomerisation of 1,3-butadiene with phenol and glycerol are presented. The solid polyphosphine is amorphous, microporous and an excellent support for Pd(acac)2. Solid-state NMR and DRIFT analysis of materials of varying Pd-loading show that bis-phosphine complexes of palladium are preferably formed. Under solvent- and base-free conditions, high conversions and selectivities are obtained for this catalyst material with both phenol and glycerol as substrates. The product selectivity, with both butenylation and telomerisation activity observed with phenol, can be tuned by variation of the metal loading. For glycerol it is shown that the selectivity to the undesired tri telomer is low under all applied conditions and, remarkably, that the heterogeneous catalyst outperforms its homogeneous PPh3-based counterpart.

Published
2013

47. Systematic analysis of barrier-forming FG hydrogels from Xenopus nuclear pore complexes

Author

Labokha, A.A., Gradmann, S.H.E., Frey, S., Hülsmann, B.B., Urlaub, H., Baldus, M., Görlich, D., NMR Spectroscopy, Sub NMR Spectroscopy, NMR Spectroscopy, and Sub NMR Spectroscopy

Subjects
Repetitive Sequences, Amino Acid, Have You Seen...?, Phenylalanine, Xenopus, Molecular Sequence Data, Active Transport, Cell Nucleus, Glycine, Saccharomyces cerevisiae, macromolecular substances, Importin, Permeability, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, Membrane Microdomains, 0302 clinical medicine, Animals, Amino Acid Sequence, Nuclear pore, Molecular Biology, 030304 developmental biology, Cell Nucleus, 0303 health sciences, General Immunology and Microbiology, biology, General Neuroscience, Hydrogels, Nuclear magnetic resonance spectroscopy, beta Karyopherins, biology.organism_classification, Nuclear Pore Complex Proteins, Biochemistry, Cytoplasm, Self-healing hydrogels, Nuclear Pore, Biophysics, Nucleoporin, Nuclear transport, 030217 neurology & neurosurgery
Abstract

Nuclear pore complexes (NPCs) control the traffic between cell nucleus and cytoplasm. While facilitating translocation of nuclear transport receptors (NTRs) and NTR·cargo complexes, they suppress passive passage of macromolecules greater than or equal to30 kDa. Previously, we reconstituted the NPC barrier as hydrogels comprising S. cerevisiae FG domains. We now studied FG domains from 10 Xenopus nucleoporins and found that all of them form hydrogels. Related domains with low FG motif density also substantially contribute to the NPC’s hydrogel mass. We characterized all these hydrogels and observed the strictest sieving effect for the Nup98-derived hydrogel. It fully blocks entry of GFP-sized inert objects, permits facilitated entry of the small NTR NTF2, but arrests importin β-type NTRs at its surface. O-GlcNAc modification of the Nup98 FG domain prevented this arrest and allowed also large NTR·cargo complexes to enter. Solid-state NMR spectroscopy revealed that the O-GlcNAc-modified Nup98 gel lacks amyloid-like β-structures that dominate the rigid regions in the S. cerevisiae Nsp1 FG hydrogel. This suggests that FG hydrogels can assemble through different structural principles and yet acquire the same NPC-like permeability.

Published
2013

48. The importance of the lipid-pore loop interface for potassium channel structure and function

Author

van der Cruijsen, E.A.W., Nand, D., Weingarth, M.H., Prokofyev, A., Hornig, S., Cukkemane, A.A., Bonvin, A.M.J.J., Becker, S., Hulse, R.E., Perozo, E., Pongs, O., Baldus, M., NMR Spectroscopy, and Sub NMR Spectroscopy

Subjects
Taverne
Abstract

Potassium (i.e., K+) channels allow for the controlled and selective passage of potassium ions across the plasma membrane via a conserved pore domain. In voltage-gated K+ channels, gating is the result of the coordinated action of two coupled gates: an activation gate at the intracellular entrance of the pore and an inactivation gate at the selectivity filter. By using solid-state NMR structural studies, in combination with electrophysiological experiments and molecular dynamics simulations, we show that the turret region connecting the outer transmembrane helix (transmembrane helix 1) and the pore helix behind the selectivity filter contributes to K+ channel inactivation and exhibits a remarkable structural plasticity that correlates to K+ channel inactivation. The transmembrane helix 1 unwinds when the K+ channel enters the inactivated state and rewinds during the transition to the closed state. In addition to well-characterized changes at the K+ ion coordination sites, this process is accompanied by conformational changes within the turret region and the pore helix. Further spectroscopic and computational results show that the same channel domain is critically involved in establishing functional contacts between pore domain and the cellular membrane. Taken together, our results suggest that the interaction between the K+ channel turret region and the lipid bilayer exerts an important influence on the selective passage of potassium ions via the K+ channel pore.

Published
2013

49. Π−Π Stacking increases the stability and loading capacity of thermosensitive polymeric micelles for chemotherapeutic drugs

Author

Shi, Y., van Steenbergen, M.J., Teunissen, E.A., Novo, L., Gradmann, S., Baldus, M., van Nostrum, C.F., Hennink, W.E., NMR Spectroscopy, Pharmaceutics, Sub General Pharmaceutics, Sub Drug targeting, and Sub NMR Spectroscopy

Abstract

Thermosensitive amphiphilic block copolymers self-assemble into micelles above their lower critical solution temperature in water, however, the micelles generally display mediocre physical stability. To stabilize such micelles and increase their loading capacity for chemotherapeutic drugs, block copolymers with novel aromatic monomers were synthesized by free radical polymerization of N-(2-benzoyloxypropyl methacrylamide (HPMAm-Bz) or the corresponding naphthoyl analogue (HPMAm-Nt), with N-(2-hydroxypropyl) methacrylamide monolactate, using a polyethylene glycol based macroinitiator. The critical micelle temperatures and critical micelle concentrations decreased with increasing the HPMAm-Bz/Nt content. The micelles of 30-50 nm were prepared by heating the polymer aqueous solutions from 0 to 50 degrees C and were colloidally stable for at least 48 h at pH 7.4 and 37 degrees C. Paclitaxel and docetaxel encapsulation was performed by mixing drug solutions in ethanol with polymer aqueous solutions and heating from 0 to 50 degrees C. The micelles had a drug loading capacity up to 34 wt % for docetaxel, which is among the highest loadings reported for polymeric micelles, with loaded micelle sizes ranging from 60 to 80 nm. The micelles without aromatic groups almost completely released loaded paclitaxel in 10 days, whereas the HPMAm-Bz/Nt containing micelles released 50% of the paclitaxel at the same time, which showed a better retention for the drug of the latter micelles. (1)H solid-state NMR spectroscopy data are compatible with pi-pi stacking between aromatic groups. The empty micelles demonstrated good cytocompatibility, and paclitaxel-loaded micelles showed high cytotoxicity to tumor cells. In conclusion, the pi-pi stacking effect introduced by aromatic groups increases the stability and loading capacity of polymeric micelles.

Published
2013

50. Cellular solid-state nuclear magnetic resonance spectroscopy

Author

Renault, M.A.M., Tommassen-van Boxtel, H.A.M., Bos, M.P., Post, J.A., Tommassen, J.P.M., Baldus, M., Biomolecular Imaging, Molecular Microbiology, NMR Spectroscopy, Sub NMR Spectroscopy, Dep Biologie, Sub Molecular Microbiology, and Sub Biomolecular Imaging

Subjects
Lipopolysaccharides, Materials science, Magnetic Resonance Spectroscopy, Protein Conformation, Lipoproteins, Proteolipids, Molecular Sequence Data, Context (language use), Peptidoglycan, 010402 general chemistry, 01 natural sciences, 03 medical and health sciences, Protein structure, Commentaries, Escherichia coli, Amino Acid Sequence, Spectroscopy, Integral membrane protein, Cellular compartment, 030304 developmental biology, 0303 health sciences, Multidisciplinary, Escherichia coli Proteins, Cell Membrane, Nuclear magnetic resonance spectroscopy, Biological Sciences, Molecular machine, 0104 chemical sciences, Crystallography, Solid-state nuclear magnetic resonance, Biological system, Bacterial Outer Membrane Proteins
Abstract

Decrypting the structure, function, and molecular interactions of complex molecular machines in their cellular context and at atomic resolution is of prime importance for understanding fundamental physiological processes. Nuclear magnetic resonance is a well-established imaging method that can visualize cellular entities at the micrometer scale and can be used to obtain 3D atomic structures under in vitro conditions. Here, we introduce a solid-state NMR approach that provides atomic level insights into cell-associated molecular components. By combining dedicated protein production and labeling schemes with tailored solid-state NMR pulse methods, we obtained structural information of a recombinant integral membrane protein and the major endogenous molecular components in a bacterial environment. Our approach permits studying entire cellular compartments as well as cell-associated proteins at the same time and at atomic resolution.

Published
2012

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