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Prof. Dr. Joachim Seelig

Department Biozentrum
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Seelig, Joachim, & Seelig, Anna. (2023). Protein Unfolding-Thermodynamic Perspectives and Unfolding Models. International journal of molecular sciences, 24(6), 5457. https://doi.org/10.3390/ijms24065457
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Seelig, Joachim, & Seelig, Anna. (2023). Protein Stability─Analysis of Heat and Cold Denaturation without and with Unfolding Models. Journal of Physical Chemistry B, 127(15), 3352–3363. https://doi.org/10.1021/acs.jpcb.3c00882
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Seelig, Joachim, & Seelig, Anna. (2023). Chemical Protein Unfolding - A Simple Cooperative Model. Journal of Physical Chemistry B, 127(39), 8296–8304. https://doi.org/10.1021/acs.jpcb.3c03558
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Seelig, Joachim, & Seelig, Anna. (2021). Molecular Understanding of Calorimetric Protein Unfolding Experiments. Biophysical Reports, 2(1), 100037. https://doi.org/10.1016/j.bpr.2021.100037
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Garidel, Patrick, Eiperle, Andrea, Blech, Michaela, & Seelig, Joachim. (2020). Thermal and Chemical Unfolding of a Monoclonal IgG1 Antibody: Application of the Multistate Zimm-Bragg Theory. Biophysical Journal, 118(5), 1067–1075. https://doi.org/10.1016/j.bpj.2019.12.037
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Li-Blatter, Xiaochun, & Seelig, Joachim. (2019). Thermal and Chemical Unfolding of Lysozyme. Multistate Zimm-Bragg Theory Versus Two-State Model. The Journal of Physical Chemistry. B, 123(48), 10181–10191. https://doi.org/10.1021/acs.jpcb.9b08816
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Eckhardt, D., Li-Blatter, X., Schönfeld, H.-J., Heerklotz, H., & Seelig, J. (2018). Cooperative unfolding of apolipoprotein A-1 induced by chemical denaturation. Biophysical Chemistry, 240, 42–49. https://doi.org/10.1016/j.bpc.2018.05.005
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Seelig, Joachim. (2018). Cooperative protein unfolding. A statistical-mechanical model for the action of denaturants. Biophysical Chemistry, 233, 19–25. https://doi.org/10.1016/j.bpc.2017.12.001
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Assmus, Frauke, Ross, Alfred, Fischer, Holger, Seelig, Joachim, & Seelig, Anna. (2017). (31)P and (1)H NMR Studies of the Molecular Organization of Lipids in the Parallel Artificial Membrane Permeability Assay. Molecular Pharmaceutics, 14(1), 284–295. https://doi.org/10.1021/acs.molpharmaceut.6b00889
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Schönfeld, Hans-Joachim, Roessner, Dierk, & Seelig, Joachim. (2016). Self-Association of Apo A-1 Studied with Dynamic and Static Light Scattering. Journal of Physical Chemistry B, 120(7), 1228–1235. https://doi.org/10.1021/acs.jpcb.5b12397
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Seelig, Joachim, & Schönfeld, Hans-Joachim. (2016). Thermal protein unfolding by differential scanning calorimetry and circular dichroism spectroscopy Two-state model versus sequential unfolding. Quarterly Reviews of Biophysics, 49, e9. https://doi.org/10.1017/s0033583516000044
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Schulthess, Therese, Schönfeld, Hans-Joachim, & Seelig, Joachim. (2015). Thermal unfolding of apolipoprotein a-1 : evaluation of methods and models. Biochemistry, 54(19), 3063–3075. https://doi.org/10.1021/acs.biochem.5b00238
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Voievoda, Nataliia, Schulthess, Therese, Bechinger, Burkhard, & Seelig, Joachim. (2015). Thermodynamic and Biophysical Analysis of the Membrane-Association of a Histidine-Rich Peptide with Efficient Antimicrobial and Transfection Activities. Journal of Physical Chemistry B, 119(30), 9678–9687. https://doi.org/10.1021/acs.jpcb.5b04543
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Schmidt, Annika, Belaaouaj, Azzaq, Bissinger, Rosi, Koller, Garrit, Malleret, Laurette, D’Orazio, Ciro, Facchinelli, Martino, Schulte-Hubbert, Bernhard, Molinaro, Antonio, Holst, Otto, Hammermann, Jutta, Schniederjans, Monika, Meyer, Keith C., Damkiaer, Soeren, Piacentini, Giorgio, Assael, Baroukh, Bruce, Kenneth, Häußler, Susanne, LiPuma, John J., et al. (2014). Neutrophil elastase-mediated increase in airway temperature during inflammation. Journal of Cystic Fibrosis, 13(6), 623–631. https://doi.org/10.1016/j.jcf.2014.03.004
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Domingues, Tatiana M., Mattei, Bruno, Seelig, Joachim, Perez, Katia R., Miranda, Antonio, & Riske, Karin A. (2013). Interaction of the antimicrobial Peptide gomesin with model membranes : a calorimetric study. Langmuir, 29(27), 8609–8618. https://doi.org/10.1021/la401596s
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Perspicace, Samantha, Rufer, Arne C., Thoma, Ralf, Müller, Francis, Hennig, Michael, Ceccarelli, Simona, Schulz-Gasch, Tanja, & Seelig, Joachim. (2013). Isothermal titration calorimetry with micelles : thermodynamics of inhibitor binding to carnitine palmitoyltransferase 2 membrane protein. FEBS Open Bio, 3, 204–211. https://doi.org/10.1016/j.fob.2013.04.003
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Québatte, Gabriela, Kitas, Eric, & Seelig, Joachim. (2013). riDOM, a Cell-Penetrating Peptide : Interaction with DNA and Heparan Sulfate. Journal of Physical Chemistry B, 117(37), 10807–10817. https://doi.org/10.1021/jp404979y
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Québatte, Gabriela, Kitas, Eric, & Seelig, Joachim. (2013). riDOM, a cell penetrating peptide : interaction with phospholipid bilayers. BBA - Biochimica et Biophysica Acta, 1838(3), 968–977. https://doi.org/10.1016/j.bbamem.2013.10.017
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Zehender, F, Ziegler, A, Schönfeld, H-J, & Seelig, J. (2012). Thermodynamics of protein self-association and unfolding : the case of apolipoprotein a-I. Biochemistry, 51(6), 1269–1280. https://doi.org/10.1021/bi2013799
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Loew, C., Riske, K. A., Lamy, M. T., & Seelig, J. (2011). Thermal Phase Behavior of DMPG as revealed by 2H- and 31P- NMR. Langmuir, 27(16), 10041–10049. https://doi.org/10.1021/la201027p
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Sauder, Reto, Seelig, Joachim, & Ziegler, André. (2011). Thermodynamics of lipid interactions with cell-penetrating peptides. Methods in Molecular Biology, 683, 129–155. https://doi.org/10.1007/978-1-60761-919-2_10
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Ziegler, Andre, & Seelig, Joachim. (2011). Contributions of Glycosaminoglycan Binding and Clustering to the Biological Uptake of the Nonamphipathic Cell-Penetrating Peptide WR(9). Biochemistry, 50(21), 4650–4664. https://doi.org/10.1021/bi1019429
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Beck, A., Li-Blatter, X., Seelig, A., & Seelig, J. (2010). On the Interaction of Ionic Detergents with Lipid Membranes : Thermodynamic Comparison of n-Alkyl-+N(CH3)3 and n-Alkyl-SO4-. Journal of Physical Chemistry B, 114(48), 15862–15871. https://doi.org/10.1021/jp107088d
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Meier, Matthias, & Seelig, Joachim. (2010). Lipid and peptide dynamics in membranes upon insertion of n-alkyl-beta-D-glucopyranosides. Biophysical Journal, 98(8), 1529–1538. https://doi.org/10.1016/j.bpj.2009.12.4286
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Hayley, Michael, Perspicace, Samantha, Schulthess, Therese, & Seelig, Joachim. (2009). Calcium enhances the proteolytic activity of BACE1 : an in vitro biophysical and biochemical characterization of the BACE1-calcium interaction. Biochimica et Biophysica Acta, 1788(9), 1933–1938. https://doi.org/10.1016/j.bbamem.2009.05.015
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Klocek, Gabriela, Schulthess, Therese, Shai, Yechiel, & Seelig, Joachim. (2009). Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation. Biochemistry, 48(12), 2586–2596. https://doi.org/10.1021/bi802127h
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Klocek, Gabriela, & Seelig, Joachim. (2008). Melittin interaction with sulfated cell surface sugars. Biochemistry, 47(9), 2841–2849. https://doi.org/10.1021/bi702258z
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Meier, M., & Seelig, J. (2008). Length dependence of the coil beta-sheet transition in a membrane environment. Journal of the American Chemical Society, 130(3), 1017–1024. https://doi.org/10.1021/ja077231r
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Ziegler, André, & Seelig, Joachim. (2008). Binding and clustering of glycosaminoglycans : a common property of mono- and multivalent cell-penetrating compounds. Biophysical Journal, 94(6), 2142–2149. https://doi.org/10.1529/biophysj.107.113472
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Brockhaus, M., Ganz, P., Huber, W., Bohrmann, B., Loetscher, H. -R., & Seelig, J. (2007). Thermodynamic studies on the interaction of antibodies with beta-amyloid peptide. Journal of Physical Chemistry B, 111(5), 1238–1243. https://doi.org/10.1021/jp0664059
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Heerklotz, H., & Seelig, J. (2007). Leakage and lysis of lipid membranes induced by the lipopeptide surfactin. European Biophysics Journal, 36(4-5), 305–314. https://doi.org/10.1007/s00249-006-0091-5
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Kohler, G., Rost, F., & Seelig, J. (2007). Simultaneous separation of intracellular and extracellular lactate NMR signals of human erythrocytes. Magnetic Resonance in Medicine, 58(2), 213–217. https://doi.org/10.1002/mrm.21309
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Meier, Matthias, & Seelig, Joachim. (2007). Thermodynamics of the coil beta-sheet transition in a membrane environment. Journal of Molecular Biology, 369(1), 277–289. https://doi.org/10.1016/j.jmb.2007.02.082
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Ziegler, André, & Seelig, Joachim. (2007). High affinity of the cell-penetrating peptide HIV-1 Tat-PTD for DNA. Biochemistry, 46(27), 8138–8145. https://doi.org/10.1021/bi700416h
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Gonçalves, Elisabete, Kitas, Eric, & Seelig, Joachim. (2006). Structural and thermodynamic aspects of the interaction between heparan sulfate and analogues of melittin. Biochemistry, 45(9), 3086–3094. https://doi.org/10.1021/bi052221t
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Honnappa, Srinivas, Jahnke, Wolfgang, Seelig, Joachim, & Steinmetz, Michel O. (2006). Control of intrinsically disordered stathmin by multisite phosphorylation. Journal of Biological Chemistry, 281(23), 16078–16083. https://doi.org/10.1074/jbc.m513524200
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Meier, M, Blatter, X Li, Seelig, A, & Seelig, J. (2006). Interaction of verapamil with lipid membranes and P-glycoprotein : connecting thermodynamics and membrane structure with functional activity. Biophysical Journal, 91(8), 2943–2955. https://doi.org/10.1529/biophysj.106.089581
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Gonçalves, Elisabete, Kitas, Eric, & Seelig, Joachim. (2005). Binding of oligoarginine to membrane lipids and heparan sulfate : structural and thermodynamic characterization of a cell-penetrating peptide. Biochemistry, 44(7), 2692–2702. https://doi.org/10.1021/bi048046i
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Ziegler, André, Nervi, Pierluigi, Dürrenberger, Markus, & Seelig, Joachim. (2005). The cationic cell-penetrating peptide CPP(TAT) derived from the HIV-1 protein TAT is rapidly transported into living fibroblast : optical, biophysical, and metabolic evidence. Biochemistry, 44(1), 138–148. https://doi.org/10.1021/bi0491604
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Anderson, Thomas G, Tan, Anmin, Ganz, Peter, & Seelig, Joachim. (2004). Calorimetric measurement of phospholipid interaction with methyl-beta-cyclodextrin. Biochemistry, 43(8), 2251–2261. https://doi.org/10.1021/bi0358869
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Heerklotz, Heiko, Wieprecht, Torsten, & Seelig, Joachim. (2004). Membrane perturbation by the lipopeptide surfactin and detergents as studied by deuterium NMR. Journal of Physical Chemistry B, 108(15), 4909–4915. https://doi.org/10.1021/jp0371938
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Schwarz, R., Seelig, J., & Kunnecke, B. (2004). Structural properties of perfluorinated linear alkanes : a 19F and 13C NMR study of perfluorononane. Magnetic Resonance in Chemistry, 42(6), 512–517. https://doi.org/10.1002/mrc.1380
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Seelig, J. (2004). Thermodynamics of lipid-peptide interactions. Biochimica et Biophysica Acta, 1666(1-2), 40–50. https://doi.org/10.1016/j.bbamem.2004.08.004
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Ziegler, André, & Seelig, Joachim. (2004). Interaction of the protein transduction domain of HIV-1 TAT with heparan sulfate : binding mechanism and thermodynamic parameters. Biophysical Journal, 86(1 Pt 1), 254–263. https://doi.org/10.1016/s0006-3495(04)74101-6
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Heerklotz, Heiko, Szadkowska, Halina, Anderson, Thomas, & Seelig, Joachim. (2003). The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton. Journal of Molecular Biology, 329(4), 793–799. https://doi.org/10.1016/s0022-8236(03)00504-7
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Honnappa, S, Cutting, B, Jahnke, W, Seelig, J, & Steinmetz, MO. (2003). Thermodynamics of the Op18/stathmin-tubulin interaction. Journal of Biological Chemistry, 278(40), 38926–38934. https://doi.org/10.1074/jbc.m305546200
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Karelson, G., Ziegler, A., Kunnecke, B., & Seelig, J. (2003). Feeding versus infusion : a novel approach to study the NAA metabolism in rat brain. NMR in Biomedicine, 16(6-7), 413–423. https://doi.org/10.1002/nbm.845
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Machaidze, Gia, & Seelig, Joachim. (2003). Specific binding of cinnamycin (Ro 09-0198) to phosphatidylethanolamine : Comparison between micellar and membrane environments. Biochemistry, 42(43), 12570–12576. https://doi.org/10.1021/bi035225b
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Ziegler, André, Blatter, Xiaochun Li, Seelig, Anna, & Seelig, Joachim. (2003). Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles : binding mechanism and thermodynamic analysis. Biochemistry, 42(30), 9185–9194. https://doi.org/10.1021/bi0346805
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Heerklotz, Heiko, & Seelig, Joachim. (2002). Application of pressure perturbation calorimetry to lipid bilayers. Biophysical Journal, 82(3), 1445–1452. https://doi.org/10.1016/s0006-3495(02)75498-2
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Machaidze, Gia, Ziegler, André, & Seelig, Joachim. (2002). Specific binding of Ro 09-0198 (cinnamycin) to phosphatidylethanolamine : a thermodynamic analysis. Biochemistry, 41(6), 1965–1971. https://doi.org/10.1021/bi015841c
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Schote, Uwe, Ganz, Peter, Fahr, Alfred, & Seelig, Joachim. (2002). Interactions of cyclosporines with lipid membranes as studied by solid-state nuclear magnetic resonance spectroscopy and high-sensitivity titration calorimetry. Journal of Pharmaceutical Sciences, 91(3), 856–867. https://doi.org/10.1002/jps.10071
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Schwarz, R., Kaspar, A., Seelig, J., & Kunnecke, B. (2002). Gastrointestinal transit times in mice and humans measured with 27Al and 19F nuclear magnetic resonance. Magnetic Resonance in Medicine, 48(2), 255–261. https://doi.org/10.1002/mrm.10207
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Tan, Anmin, Ziegler, André, Steinbauer, Bernhard, & Seelig, Joachim. (2002). Thermodynamics of sodium dodecyl sulfate partitioning into lipid membranes. Biophysical Journal, 83(3), 1547–1556. https://doi.org/10.1016/s0006-3495(02)73924-6
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Wieprecht, T., Beyermann, M., & Seelig, J. (2002). Thermodynamics of the coil-alpha-helix transition of amphipathic peptides in a membrane environment : the role of vesicle curvature. Biophysical Chemistry, 96(2-3), 191–201. https://doi.org/10.1016/s0301-4622(02)00025-x
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Fahr, A., & Seelig, J. (2001). Liposomal formulations of Cyclosporin A : a biophysical approach to pharmacokinetics and pharmacodynamics. Critical Reviews in Therapeutic Drug Carrier Systems, 18(2), 141–172. https://doi.org/10.1023/a:1016220211925
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Heerklotz, H, & Seelig, J. (2001). Detergent-like action of the antibiotic peptide surfactin on lipid membranes. Biophysical Journal, 81(3), 1547–1554. https://doi.org/10.1016/s0006-3495(01)75808-0
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Breukink, E, Ganz, P, de Kruijff, B, & Seelig, J. (2000). Binding of Nisin Z to bilayer vesicles as determined with isothermal titration calorimetry. Biochemistry, 39(33), 10247–10254. https://doi.org/10.1021/bi000915q
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Haselhorst, R., Kappos, L., Bilecen, D., Scheffler, K., Mori, D., Radu, E. W., & Seelig, J. (2000). Dynamic susceptibility contrast MR imaging of plaque development in multiple sclerosis : application of an extended blood-brain barrier leakage correction. Journal of Magnetic Resonance Imaging, 11(5), 495–505. https://doi.org/10.1002/(sici)1522-2586(200005)11:53.0.co;2-s
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Heerklotz, H, & Seelig, J. (2000). Titration calorimetry of surfactant-membrane partitioning and membrane solubilization. Biochimica et Biophysica Acta, 1508(1-2), 69–85. https://doi.org/10.1016/s0304-4157(00)00009-5
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Kunnecke, B., Kustermann, E., & Seelig, J. (2000). Simultaneous in vivo monitoring of hepatic glucose and glucose-6-phosphate by (13)C-NMR spectroscopy. Magnetic Resonance in Medicine, 44(4), 556–562. https://doi.org/10.1002/1522-2594(200010)44:43.0.co;2-3
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Mader, I., Roser, W., Kappos, L., Hagberg, G., Seelig, J., Radue, E. W., & Steinbrich, W. (2000). Serial proton MR spectroscopy of contrast-enhancing multiple sclerosis plaques : absolute metabolic values over 2 years during a clinical pharmacological study. American Journal of Neuroradiology, 21(7), 1220–1227. http://www.ajnr.org/content/21/7/1220
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Seelig, J. (2000). Correlation of membrane / water partition coefficients of detergents with the critical micelle concentration. Biophysical Journal, 78(5), 2435–2440. https://doi.org/10.1016/s0006-3495(00)76787-7
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Wieprecht, T, Apostolov, O, Beyermann, M, & Seelig, J. (2000). Membrane binding and pore formation of the antibacterial peptide PGLa : thermodynamic and mechanistic aspects. Biochemistry, 39(2), 442–452. https://doi.org/10.1021/bi992146k
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Wieprecht, T, Apostolov, O, Beyermann, M, & Seelig, J. (2000). Interaction of a mitochondrial presequence with lipid membranes : role of helix formation for membrane binding and perturbation. Biochemistry, 39(50), 15297–15305. https://doi.org/10.1021/bi001774v
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Wieprecht, T., Apostolov, O., & Seelig, J. (2000). Binding of the antibacterial peptide magainin 2 amide to small and large unilamellar vesicles. Biophysical Chemistry, 85(2-3), 187–198. https://doi.org/10.1016/s0301-4622(00)00120-4
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Fischer, H., Seelig, A., Beier, N., Raddatz, P., & Seelig, J. (1999). New drugs for the Na+/H+ exchanger : Influence of Na+ concentration and determination of inhibition constants with a microphysiometer. The Journal of Membrane Biology, 168(1), 39–45. https://doi.org/10.1007/s002329900496
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Pellaud, J, Schote, U, Arvinte, T, & Seelig, J. (1999). Conformation and self-association of human recombinant transforming growth factor-beta3 in aqueous solutions. Journal of Biological Chemistry, 274(12), 7699–7704. https://doi.org/10.1074/jbc.274.12.7699
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Roser, W., Bubl, R., Buergin, D., Seelig, J., Radue, E. W., & Rost, B. (1999). Metabolic changes in the brain of patients with anorexia and bulimia nervosa as detected by proton magnetic resonance spectroscopy. International Journal of Eating Disorders, 26(2), 119–136. https://doi.org/10.1002/(sici)1098-108x(199909)26:23.0.co;2-m
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Schwarz, R., Schuurmans, M., Seelig, J., & Kunnecke, B. (1999). 19F-MRI of perfluorononane as a novel contrast modality for gastrointestinal imaging. Magnetic Resonance in Medicine, 41(1), 80–86. https://doi.org/10.1002/(sici)1522-2594(199901)41:13.0.co;2-6
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Wieprecht, T, Apostolov, O, Beyermann, M, & Seelig, J. (1999). Thermodynamics of the alpha-helix-coil transition of amphipathic peptides in a membrane environment : implications for the peptide-membrane binding equilibrium. Journal of Molecular Biology, 294(3), 785–794. https://doi.org/10.1006/jmbi.1999.3268
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Wieprecht, T, Beyermann, M, & Seelig, J. (1999). Binding of antibacterial magainin peptides to electrically neutral membranes : thermodynamics and structure. Biochemistry, 38(32), 10377–10387. https://doi.org/10.1021/bi990913+
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Küstermann, E, Seelig, J, & Künnecke, B. (1998). Ascorbic acid, a vitamin, is observed by in vivo 13C nuclear magnetic resonance spectroscopy of rat liver. American Journal of Physiology. Endocrinology and Metabolism, 274(1 Pt 1), E65–71.
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Schote, U, & Seelig, J. (1998). Interaction of the neuronal marker dye FM1-43 with lipid membranes : thermodynamics and lipid ordering. Biochimica et Biophysica Acta, 1415(1), 135–146. https://doi.org/10.1016/s0005-2736(98)00188-6
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Wenk, M R, & Seelig, J. (1998). Magainin 2 amide interaction with lipid membranes : calorimetric detection of peptide binding and pore formation. Biochemistry, 37(11), 3909–3916. https://doi.org/10.1021/bi972615n
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Wenk, M R, & Seelig, J. (1998). Proton induced vesicle fusion and the isothermal lalpha--. Biochimica et Biophysica Acta, 1372(2), 227–236. https://doi.org/10.1016/s0005-2736(98)00059-5
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Hertel, C, Terzi, E, Hauser, N, Jakob-Rotne, R, Seelig, J, & Kemp, J A. (1997). Inhibition of the electrostatic interaction between beta-amyloid peptide and membranes prevents beta-amyloid-induced toxicity. Proceedings of the National Academy of Sciences of the United States of America, 94(17), 9412–9416. https://doi.org/10.1073/pnas.94.17.9412
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Nebel, S, Ganz, P, & Seelig, J. (1997). Heat changes in lipid membranes under sudden osmotic stress. Biochemistry, 36(10), 2853–2859. https://doi.org/10.1021/bi961839n
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Seelig, J. (1997). Titration calorimetry of lipid-peptide interactions. Biochimica et Biophysica Acta, 1331(1), 103–116. https://doi.org/10.1016/s0304-4157(97)00002-6
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Terzi, E, Hölzemann, G, & Seelig, J. (1997). Interaction of Alzheimer beta-amyloid peptide(1-40) with lipid membranes. Biochemistry, 36(48), 14845–14852. https://doi.org/10.1021/bi971843e
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Wenk, Markus R., & Seelig, Joachim. (1997). Vesicle-micelle transformation of phosphatidylcholine / octyl-beta-D-glucopyranoside mixtures as detected with titration calorimetry. Journal of Physical Chemistry B, 101(26), 5224–5231. https://doi.org/10.1021/jp9707955
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Wenk, M. R., Alt, T., Seelig, A., & Seelig, J. (1997). Octyl-beta-D-glucopyranoside partitioning into lipid bilayers: thermodynamics of binding and structural changes of the bilayer. Biophysical Journal, 72(4), 1719–1731. https://doi.org/10.1016/s0006-3495(97)78818-0
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Wenk, M R, & Seelig, J. (1997). Interaction of octyl-beta-thioglucopyranoside with lipid membranes. Biophysical Journal, 73(5), 2565–2574. https://doi.org/10.1016/s0006-3495(97)78285-7
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Fried, R, Beckmann, N, Keller, U, Ninnis, R, Stalder, G, & Seelig, J. (1996). Early glycogenolysis and late glycogenesis in human liver after intravenous administration of galactose. American Journal of Physiology. Gastrointestinal and Liver Physiology, 270(1 Pt 1), G14–9.
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Roser, W., Beckmann, N., Wiesmann, U., & Seelig, J. (1996). Absolute quantification of the hepatic glycogen content in a patient with glycogen storage disease by 13C magnetic resonance spectroscopy. Magnetic Resonance Imaging, 14(10), 1217–1220. https://doi.org/10.1016/s0730-725x(96)00243-3
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Seelig, A, & Seelig, J. (1996). Interaction of drugs and peptides with the lipid membrane (T. Schwartz,; S.A. Hjorth,; J. Sandholm, Ed.; Vol. 39). Munksgaard.
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Wenk, M R, Fahr, A, Reszka, R, & Seelig, J. (1996). Paclitaxel partitioning into lipid bilayers. Journal of Pharmaceutical Sciences, 85(2), 228–231. https://doi.org/10.1021/js950120i
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Seelig, J., Lehrmann, R., & Terzi, E. (1995). Domain formation induced by lipid-ion and lipid-peptide interactions. Molecular Membrane Biology, 12(1), 51–57. https://doi.org/10.3109/09687689509038495
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Terzi, E, Hölzemann, G, & Seelig, J. (1995). Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes. Journal of Molecular Biology, 252(5), 633–642. https://doi.org/10.1006/jmbi.1995.0525
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Burlina, A. P., Corazza, A., Ferrari, V., Erhard, P., Kunnecke, B., Seelig, J., & Burlina, A. B. (1994). Detection of increased urinary N-acetylaspartylglutamate in Canavan disease. European Journal of Pediatrics, 153(7), 538–539. https://doi.org/10.1007/bf01957015
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Lehrmann, R, & Seelig, J. (1994). Adsorption of Ca2+ and La3+ to bilayer membranes : measurement of the adsorption enthalpy and binding constant with titration calorimetry. Biochimica et Biophysica Acta, 1189(1), 89–95. https://doi.org/10.1016/0005-2736(94)90284-4
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Moldes, M., Cerdan, S., Erhard, P., & Seelig, J. (1994). 1H-2H exchange in the perfused rat liver metabolizing [3-13C]alanine and 2H2O as detected by multinuclear NMR spectroscopy. NMR in Biomedicine, 7(6), 249–262. https://doi.org/10.1002/nbm.1940070602
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Spuhler, P, Anantharamaiah, G M, Segrest, J P, & Seelig, J. (1994). Binding of apolipoprotein A-I model peptides to lipid bilayers : measurement of binding isotherms and peptide-lipid headgroup interactions. Journal of Biological Chemistry, 269(39), 23904–23910.
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Terzi, E, Hölzemann, G, & Seelig, J. (1994). Reversible random coil-beta-sheet transition of the Alzheimer beta-amyloid fragment (25-35). Biochemistry, 33(6), 1345–1350. https://doi.org/10.1021/bi00172a009
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Terzi, E, Hölzemann, G, & Seelig, J. (1994). Alzheimer beta-amyloid peptide 25-35 : electrostatic interactions with phospholipid membranes. Biochemistry, 33(23), 7434–7441. https://doi.org/10.1021/bi00189a051
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Kunnecke, B., Cerdan, S., & Seelig, J. (1993). Cerebral metabolism of [1,2-13C2]glucose and [U-13C4]3-hydroxybutyrate in rat brain as detected by 13C NMR spectroscopy. NMR in Biomedicine, 6(4), 264–277. https://doi.org/10.1002/nbm.1940060406
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Montich, G, Scarlata, S, McLaughlin, S, Lehrmann, R, & Seelig, J. (1993). Thermodynamic characterization of the association of small basic peptides with membranes containing acidic lipids. Biochimica et Biophysica Acta, 1146(1), 17–24. https://doi.org/10.1016/0005-2736(93)90333-u
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SEELIG, J, NEBEL, S, GANZ, P, & BRUNS, C. (1993). Electrostatic and nonpolar peptide-membrane interactions : lipid binding and functional properties of somatostatin analogues of charge z = +1 to z = +3. Biochemistry, 32(37), 9714–9721. https://doi.org/10.1021/bi00088a025
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Thomas, P. G., & Seelig, J. (1993). Binding of the calcium antagonist flunarizine to phosphatidylcholine bilayers : charge effects and thermodynamics. Biochemical Journal, 291 ( Pt 2)(2), 397–402. https://doi.org/10.1042/bj2910397
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Beschiaschvili, G, & Seelig, J. (1992). Peptide binding to lipid bilayers : nonclassical hydrophobic effect and membrane-induced pK shifts. Biochemistry, 31(41), 10044–10053. https://doi.org/10.1021/bi00156a026
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