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International journal of molecular sciences, 24(6), 5457. https://doi.org/10.3390/ijms24065457
, & Seelig, Anna. (2023). Protein Unfolding-Thermodynamic Perspectives and Unfolding Models.
International journal of molecular sciences, 24(6), 5457. https://doi.org/10.3390/ijms24065457
, & Seelig, Anna. (2023). Protein Unfolding-Thermodynamic Perspectives and Unfolding Models.
Journal of Physical Chemistry B, 127(15), 3352–3363. https://doi.org/10.1021/acs.jpcb.3c00882
, & 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
, & Seelig, Anna. (2023). Protein Stability─Analysis of Heat and Cold Denaturation without and with Unfolding Models.
Journal of Physical Chemistry B, 127(39), 8296–8304. https://doi.org/10.1021/acs.jpcb.3c03558
, & 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
, & Seelig, Anna. (2023). Chemical Protein Unfolding - A Simple Cooperative Model.
Protein unfolding. Thermodynamic perspectives and unfolding models. bioRxiv. https://doi.org/10.1101/2022.11.08.515403
, & Seelig, Anna. (2022).
Protein unfolding. Thermodynamic perspectives and unfolding models. bioRxiv. https://doi.org/10.1101/2022.11.08.515403
, & Seelig, Anna. (2022).
Biophysical Reports, 2(1), 100037. https://doi.org/10.1016/j.bpr.2021.100037
, & Seelig, Anna. (2021). Molecular Understanding of Calorimetric Protein Unfolding Experiments.
Biophysical Reports, 2(1), 100037. https://doi.org/10.1016/j.bpr.2021.100037
, & Seelig, Anna. (2021). Molecular Understanding of Calorimetric Protein Unfolding Experiments.
Garidel, Patrick, Eiperle, Andrea, Blech, Michaela, & Biophysical Journal, 118(5), 1067–1075. https://doi.org/10.1016/j.bpj.2019.12.037
. (2020). Thermal and Chemical Unfolding of a Monoclonal IgG1 Antibody: Application of the Multistate Zimm-Bragg Theory.
Garidel, Patrick, Eiperle, Andrea, Blech, Michaela, & Biophysical Journal, 118(5), 1067–1075. https://doi.org/10.1016/j.bpj.2019.12.037
. (2020). Thermal and Chemical Unfolding of a Monoclonal IgG1 Antibody: Application of the Multistate Zimm-Bragg Theory.
Li-Blatter, Xiaochun, & The Journal of Physical Chemistry. B, 123(48), 10181–10191. https://doi.org/10.1021/acs.jpcb.9b08816
. (2019). Thermal and Chemical Unfolding of Lysozyme. Multistate Zimm-Bragg Theory Versus Two-State Model.
Li-Blatter, Xiaochun, & The Journal of Physical Chemistry. B, 123(48), 10181–10191. https://doi.org/10.1021/acs.jpcb.9b08816
. (2019). Thermal and Chemical Unfolding of Lysozyme. Multistate Zimm-Bragg Theory Versus Two-State Model.
Eckhardt, D., Li-Blatter, X., Schönfeld, H.-J., Heerklotz, H., & Biophysical Chemistry, 240, 42–49. https://doi.org/10.1016/j.bpc.2018.05.005
(2018). Cooperative unfolding of apolipoprotein A-1 induced by chemical denaturation.
Eckhardt, D., Li-Blatter, X., Schönfeld, H.-J., Heerklotz, H., & Biophysical Chemistry, 240, 42–49. https://doi.org/10.1016/j.bpc.2018.05.005
(2018). Cooperative unfolding of apolipoprotein A-1 induced by chemical denaturation.
Biophysical Chemistry, 233, 19–25. https://doi.org/10.1016/j.bpc.2017.12.001
. (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
. (2018). Cooperative protein unfolding. A statistical-mechanical model for the action of denaturants.
Enthalpy and Internal Energy. Liquids, Solutions and Vapours (pp. 299–314). Royal Society of Chemistry. https://doi.org/10.1039/9781788010214
. (2018). Titration Calorimetry and Differential Scanning Calorimetry of Lipid-Protein Interactions. In Wilhelm, Emmerich; Letcher, Trevor M. (Ed.),
Enthalpy and Internal Energy. Liquids, Solutions and Vapours (pp. 299–314). Royal Society of Chemistry. https://doi.org/10.1039/9781788010214
. (2018). Titration Calorimetry and Differential Scanning Calorimetry of Lipid-Protein Interactions. In Wilhelm, Emmerich; Letcher, Trevor M. (Ed.),
Assmus, Frauke, Ross, Alfred, Fischer, Holger, Molecular Pharmaceutics, 14(1), 284–295. https://doi.org/10.1021/acs.molpharmaceut.6b00889
, & Seelig, Anna. (2017). (31)P and (1)H NMR Studies of the Molecular Organization of Lipids in the Parallel Artificial Membrane Permeability Assay.
Assmus, Frauke, Ross, Alfred, Fischer, Holger, Molecular Pharmaceutics, 14(1), 284–295. https://doi.org/10.1021/acs.molpharmaceut.6b00889
, & Seelig, Anna. (2017). (31)P and (1)H NMR Studies of the Molecular Organization of Lipids in the Parallel Artificial Membrane Permeability Assay.
Schönfeld, Hans-Joachim, Roessner, Dierk, & Journal of Physical Chemistry B, 120(7), 1228–1235. https://doi.org/10.1021/acs.jpcb.5b12397
. (2016). Self-Association of Apo A-1 Studied with Dynamic and Static Light Scattering.
Schönfeld, Hans-Joachim, Roessner, Dierk, & Journal of Physical Chemistry B, 120(7), 1228–1235. https://doi.org/10.1021/acs.jpcb.5b12397
. (2016). Self-Association of Apo A-1 Studied with Dynamic and Static Light Scattering.
Quarterly Reviews of Biophysics, 49, e9. https://doi.org/10.1017/s0033583516000044
, & 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
, & Schönfeld, Hans-Joachim. (2016). Thermal protein unfolding by differential scanning calorimetry and circular dichroism spectroscopy Two-state model versus sequential unfolding.
Schulthess, Therese, Schönfeld, Hans-Joachim, & Biochemistry, 54(19), 3063–3075. https://doi.org/10.1021/acs.biochem.5b00238
. (2015). Thermal unfolding of apolipoprotein a-1 : evaluation of methods and models.
Schulthess, Therese, Schönfeld, Hans-Joachim, & Biochemistry, 54(19), 3063–3075. https://doi.org/10.1021/acs.biochem.5b00238
. (2015). Thermal unfolding of apolipoprotein a-1 : evaluation of methods and models.
Voievoda, Nataliia, Schulthess, Therese, Bechinger, Burkhard, & Journal of Physical Chemistry B, 119(30), 9678–9687. https://doi.org/10.1021/acs.jpcb.5b04543
. (2015). Thermodynamic and Biophysical Analysis of the Membrane-Association of a Histidine-Rich Peptide with Efficient Antimicrobial and Transfection Activities.
Voievoda, Nataliia, Schulthess, Therese, Bechinger, Burkhard, & Journal of Physical Chemistry B, 119(30), 9678–9687. https://doi.org/10.1021/acs.jpcb.5b04543
. (2015). Thermodynamic and Biophysical Analysis of the Membrane-Association of a Histidine-Rich Peptide with Efficient Antimicrobial and Transfection Activities.
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
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
Domingues, Tatiana M., Mattei, Bruno, Langmuir, 29(27), 8609–8618. https://doi.org/10.1021/la401596s
, Perez, Katia R., Miranda, Antonio, & Riske, Karin A. (2013). Interaction of the antimicrobial Peptide gomesin with model membranes : a calorimetric study.
Domingues, Tatiana M., Mattei, Bruno, Langmuir, 29(27), 8609–8618. https://doi.org/10.1021/la401596s
, Perez, Katia R., Miranda, Antonio, & Riske, Karin A. (2013). Interaction of the antimicrobial Peptide gomesin with model membranes : a calorimetric study.
Perspicace, Samantha, Rufer, Arne C., Thoma, Ralf, Müller, Francis, Hennig, Michael, Ceccarelli, Simona, Schulz-Gasch, Tanja, & FEBS Open Bio, 3, 204–211. https://doi.org/10.1016/j.fob.2013.04.003
. (2013). Isothermal titration calorimetry with micelles : thermodynamics of inhibitor binding to carnitine palmitoyltransferase 2 membrane protein.
Perspicace, Samantha, Rufer, Arne C., Thoma, Ralf, Müller, Francis, Hennig, Michael, Ceccarelli, Simona, Schulz-Gasch, Tanja, & FEBS Open Bio, 3, 204–211. https://doi.org/10.1016/j.fob.2013.04.003
. (2013). Isothermal titration calorimetry with micelles : thermodynamics of inhibitor binding to carnitine palmitoyltransferase 2 membrane protein.
Québatte, Gabriela, Kitas, Eric, & Journal of Physical Chemistry B, 117(37), 10807–10817. https://doi.org/10.1021/jp404979y
. (2013). riDOM, a Cell-Penetrating Peptide : Interaction with DNA and Heparan Sulfate.
Québatte, Gabriela, Kitas, Eric, & Journal of Physical Chemistry B, 117(37), 10807–10817. https://doi.org/10.1021/jp404979y
. (2013). riDOM, a Cell-Penetrating Peptide : Interaction with DNA and Heparan Sulfate.
Québatte, Gabriela, Kitas, Eric, & BBA - Biochimica et Biophysica Acta, 1838(3), 968–977. https://doi.org/10.1016/j.bbamem.2013.10.017
. (2013). riDOM, a cell penetrating peptide : interaction with phospholipid bilayers.
Québatte, Gabriela, Kitas, Eric, & BBA - Biochimica et Biophysica Acta, 1838(3), 968–977. https://doi.org/10.1016/j.bbamem.2013.10.017
. (2013). riDOM, a cell penetrating peptide : interaction with phospholipid bilayers.
Zehender, F, Ziegler, A, Schönfeld, H-J, & Biochemistry, 51(6), 1269–1280. https://doi.org/10.1021/bi2013799
. (2012). Thermodynamics of protein self-association and unfolding : the case of apolipoprotein a-I.
Zehender, F, Ziegler, A, Schönfeld, H-J, & Biochemistry, 51(6), 1269–1280. https://doi.org/10.1021/bi2013799
. (2012). Thermodynamics of protein self-association and unfolding : the case of apolipoprotein a-I.
Loew, C., Riske, K. A., Lamy, M. T., & Langmuir, 27(16), 10041–10049. https://doi.org/10.1021/la201027p
(2011). Thermal Phase Behavior of DMPG as revealed by 2H- and 31P- NMR.
Loew, C., Riske, K. A., Lamy, M. T., & Langmuir, 27(16), 10041–10049. https://doi.org/10.1021/la201027p
(2011). Thermal Phase Behavior of DMPG as revealed by 2H- and 31P- NMR.
Sauder, Reto, Methods in Molecular Biology, 683, 129–155. https://doi.org/10.1007/978-1-60761-919-2_10
, & Ziegler, André. (2011). Thermodynamics of lipid interactions with cell-penetrating peptides.
Sauder, Reto, Methods in Molecular Biology, 683, 129–155. https://doi.org/10.1007/978-1-60761-919-2_10
, & Ziegler, André. (2011). Thermodynamics of lipid interactions with cell-penetrating peptides.
Ziegler, Andre, & Biochemistry, 50(21), 4650–4664. https://doi.org/10.1021/bi1019429
. (2011). Contributions of Glycosaminoglycan Binding and Clustering to the Biological Uptake of the Nonamphipathic Cell-Penetrating Peptide WR(9).
Ziegler, Andre, & Biochemistry, 50(21), 4650–4664. https://doi.org/10.1021/bi1019429
. (2011). Contributions of Glycosaminoglycan Binding and Clustering to the Biological Uptake of the Nonamphipathic Cell-Penetrating Peptide WR(9).
Beck, A., Li-Blatter, X., Seelig, A., & Journal of Physical Chemistry B, 114(48), 15862–15871. https://doi.org/10.1021/jp107088d
(2010). On the Interaction of Ionic Detergents with Lipid Membranes : Thermodynamic Comparison of n-Alkyl-+N(CH3)3 and n-Alkyl-SO4-.
Beck, A., Li-Blatter, X., Seelig, A., & Journal of Physical Chemistry B, 114(48), 15862–15871. https://doi.org/10.1021/jp107088d
(2010). On the Interaction of Ionic Detergents with Lipid Membranes : Thermodynamic Comparison of n-Alkyl-+N(CH3)3 and n-Alkyl-SO4-.
Meier, Matthias, & Biophysical Journal, 98(8), 1529–1538. https://doi.org/10.1016/j.bpj.2009.12.4286
. (2010). Lipid and peptide dynamics in membranes upon insertion of n-alkyl-beta-D-glucopyranosides.
Meier, Matthias, & Biophysical Journal, 98(8), 1529–1538. https://doi.org/10.1016/j.bpj.2009.12.4286
. (2010). Lipid and peptide dynamics in membranes upon insertion of n-alkyl-beta-D-glucopyranosides.
Hayley, Michael, Perspicace, Samantha, Schulthess, Therese, & Biochimica et Biophysica Acta, 1788(9), 1933–1938. https://doi.org/10.1016/j.bbamem.2009.05.015
. (2009). Calcium enhances the proteolytic activity of BACE1 : an in vitro biophysical and biochemical characterization of the BACE1-calcium interaction.
Hayley, Michael, Perspicace, Samantha, Schulthess, Therese, & Biochimica et Biophysica Acta, 1788(9), 1933–1938. https://doi.org/10.1016/j.bbamem.2009.05.015
. (2009). Calcium enhances the proteolytic activity of BACE1 : an in vitro biophysical and biochemical characterization of the BACE1-calcium interaction.
Klocek, Gabriela, Schulthess, Therese, Shai, Yechiel, & Biochemistry, 48(12), 2586–2596. https://doi.org/10.1021/bi802127h
. (2009). Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.
Klocek, Gabriela, Schulthess, Therese, Shai, Yechiel, & Biochemistry, 48(12), 2586–2596. https://doi.org/10.1021/bi802127h
. (2009). Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.
Klocek, Gabriela, & Biochemistry, 47(9), 2841–2849. https://doi.org/10.1021/bi702258z
. (2008). Melittin interaction with sulfated cell surface sugars.
Klocek, Gabriela, & Biochemistry, 47(9), 2841–2849. https://doi.org/10.1021/bi702258z
. (2008). Melittin interaction with sulfated cell surface sugars.
Meier, M., & Journal of the American Chemical Society, 130(3), 1017–1024. https://doi.org/10.1021/ja077231r
(2008). Length dependence of the coil beta-sheet transition in a membrane environment.
Meier, M., & Journal of the American Chemical Society, 130(3), 1017–1024. https://doi.org/10.1021/ja077231r
(2008). Length dependence of the coil beta-sheet transition in a membrane environment.
Ziegler, André, & Biophysical Journal, 94(6), 2142–2149. https://doi.org/10.1529/biophysj.107.113472
. (2008). Binding and clustering of glycosaminoglycans : a common property of mono- and multivalent cell-penetrating compounds.
Ziegler, André, & Biophysical Journal, 94(6), 2142–2149. https://doi.org/10.1529/biophysj.107.113472
. (2008). Binding and clustering of glycosaminoglycans : a common property of mono- and multivalent cell-penetrating compounds.
Brockhaus, M., Ganz, P., Huber, W., Bohrmann, B., Loetscher, H. -R., & Journal of Physical Chemistry B, 111(5), 1238–1243. https://doi.org/10.1021/jp0664059
(2007). Thermodynamic studies on the interaction of antibodies with beta-amyloid peptide.
Brockhaus, M., Ganz, P., Huber, W., Bohrmann, B., Loetscher, H. -R., & Journal of Physical Chemistry B, 111(5), 1238–1243. https://doi.org/10.1021/jp0664059
(2007). Thermodynamic studies on the interaction of antibodies with beta-amyloid peptide.
Heerklotz, H., & European Biophysics Journal, 36(4-5), 305–314. https://doi.org/10.1007/s00249-006-0091-5
(2007). Leakage and lysis of lipid membranes induced by the lipopeptide surfactin.
Heerklotz, H., & European Biophysics Journal, 36(4-5), 305–314. https://doi.org/10.1007/s00249-006-0091-5
(2007). Leakage and lysis of lipid membranes induced by the lipopeptide surfactin.
Kohler, G., Rost, F., & Magnetic Resonance in Medicine, 58(2), 213–217. https://doi.org/10.1002/mrm.21309
(2007). Simultaneous separation of intracellular and extracellular lactate NMR signals of human erythrocytes.
Kohler, G., Rost, F., & Magnetic Resonance in Medicine, 58(2), 213–217. https://doi.org/10.1002/mrm.21309
(2007). Simultaneous separation of intracellular and extracellular lactate NMR signals of human erythrocytes.
Meier, Matthias, & Journal of Molecular Biology, 369(1), 277–289. https://doi.org/10.1016/j.jmb.2007.02.082
. (2007). Thermodynamics of the coil beta-sheet transition in a membrane environment.
Meier, Matthias, & Journal of Molecular Biology, 369(1), 277–289. https://doi.org/10.1016/j.jmb.2007.02.082
. (2007). Thermodynamics of the coil beta-sheet transition in a membrane environment.
Ziegler, André, & Biochemistry, 46(27), 8138–8145. https://doi.org/10.1021/bi700416h
. (2007). High affinity of the cell-penetrating peptide HIV-1 Tat-PTD for DNA.
Ziegler, André, & Biochemistry, 46(27), 8138–8145. https://doi.org/10.1021/bi700416h
. (2007). High affinity of the cell-penetrating peptide HIV-1 Tat-PTD for DNA.
Gonçalves, Elisabete, Kitas, Eric, & Biochemistry, 45(9), 3086–3094. https://doi.org/10.1021/bi052221t
. (2006). Structural and thermodynamic aspects of the interaction between heparan sulfate and analogues of melittin.
Gonçalves, Elisabete, Kitas, Eric, & Biochemistry, 45(9), 3086–3094. https://doi.org/10.1021/bi052221t
. (2006). Structural and thermodynamic aspects of the interaction between heparan sulfate and analogues of melittin.
Honnappa, Srinivas, Jahnke, Wolfgang, Journal of Biological Chemistry, 281(23), 16078–16083. https://doi.org/10.1074/jbc.m513524200
, & Steinmetz, Michel O. (2006). Control of intrinsically disordered stathmin by multisite phosphorylation.
Honnappa, Srinivas, Jahnke, Wolfgang, Journal of Biological Chemistry, 281(23), 16078–16083. https://doi.org/10.1074/jbc.m513524200
, & Steinmetz, Michel O. (2006). Control of intrinsically disordered stathmin by multisite phosphorylation.
Meier, M, Blatter, X Li, Seelig, A, & Biophysical Journal, 91(8), 2943–2955. https://doi.org/10.1529/biophysj.106.089581
. (2006). Interaction of verapamil with lipid membranes and P-glycoprotein : connecting thermodynamics and membrane structure with functional activity.
Meier, M, Blatter, X Li, Seelig, A, & Biophysical Journal, 91(8), 2943–2955. https://doi.org/10.1529/biophysj.106.089581
. (2006). Interaction of verapamil with lipid membranes and P-glycoprotein : connecting thermodynamics and membrane structure with functional activity.
Gonçalves, Elisabete, Kitas, Eric, & Biochemistry, 44(7), 2692–2702. https://doi.org/10.1021/bi048046i
. (2005). Binding of oligoarginine to membrane lipids and heparan sulfate : structural and thermodynamic characterization of a cell-penetrating peptide.
Gonçalves, Elisabete, Kitas, Eric, & Biochemistry, 44(7), 2692–2702. https://doi.org/10.1021/bi048046i
. (2005). Binding of oligoarginine to membrane lipids and heparan sulfate : structural and thermodynamic characterization of a cell-penetrating peptide.
Ziegler, André, Nervi, Pierluigi, Dürrenberger, Markus, & Biochemistry, 44(1), 138–148. https://doi.org/10.1021/bi0491604
. (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.
Ziegler, André, Nervi, Pierluigi, Dürrenberger, Markus, & Biochemistry, 44(1), 138–148. https://doi.org/10.1021/bi0491604
. (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.
Anderson, Thomas G, Tan, Anmin, Ganz, Peter, & Biochemistry, 43(8), 2251–2261. https://doi.org/10.1021/bi0358869
. (2004). Calorimetric measurement of phospholipid interaction with methyl-beta-cyclodextrin.
Anderson, Thomas G, Tan, Anmin, Ganz, Peter, & Biochemistry, 43(8), 2251–2261. https://doi.org/10.1021/bi0358869
. (2004). Calorimetric measurement of phospholipid interaction with methyl-beta-cyclodextrin.
Heerklotz, Heiko, Wieprecht, Torsten, & Journal of Physical Chemistry B, 108(15), 4909–4915. https://doi.org/10.1021/jp0371938
. (2004). Membrane perturbation by the lipopeptide surfactin and detergents as studied by deuterium NMR.
Heerklotz, Heiko, Wieprecht, Torsten, & Journal of Physical Chemistry B, 108(15), 4909–4915. https://doi.org/10.1021/jp0371938
. (2004). Membrane perturbation by the lipopeptide surfactin and detergents as studied by deuterium NMR.
Schwarz, R., Magnetic Resonance in Chemistry, 42(6), 512–517. https://doi.org/10.1002/mrc.1380
, & Kunnecke, B. (2004). Structural properties of perfluorinated linear alkanes : a 19F and 13C NMR study of perfluorononane.
Schwarz, R., Magnetic Resonance in Chemistry, 42(6), 512–517. https://doi.org/10.1002/mrc.1380
, & Kunnecke, B. (2004). Structural properties of perfluorinated linear alkanes : a 19F and 13C NMR study of perfluorononane.
Biochimica et Biophysica Acta, 1666(1-2), 40–50. https://doi.org/10.1016/j.bbamem.2004.08.004
. (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
. (2004). Thermodynamics of lipid-peptide interactions.
Ziegler, André, & Biophysical Journal, 86(1 Pt 1), 254–263. https://doi.org/10.1016/s0006-3495(04)74101-6
. (2004). Interaction of the protein transduction domain of HIV-1 TAT with heparan sulfate : binding mechanism and thermodynamic parameters.
Ziegler, André, & Biophysical Journal, 86(1 Pt 1), 254–263. https://doi.org/10.1016/s0006-3495(04)74101-6
. (2004). Interaction of the protein transduction domain of HIV-1 TAT with heparan sulfate : binding mechanism and thermodynamic parameters.
Bilecen, D., Schulte, A. -C., Kaspar, A., Kustermann, E., NMR in Biomedicine, 16(3), 144–151. https://doi.org/10.1002/nbm.820
, Elverfeldt, D., & Scheffler, K. (2003). Detection of the non-steroidal anti-inflammatory drug niflumic acid in humans : a combined 19F-MRS in vivo and in vitro study.
Bilecen, D., Schulte, A. -C., Kaspar, A., Kustermann, E., NMR in Biomedicine, 16(3), 144–151. https://doi.org/10.1002/nbm.820
, Elverfeldt, D., & Scheffler, K. (2003). Detection of the non-steroidal anti-inflammatory drug niflumic acid in humans : a combined 19F-MRS in vivo and in vitro study.
Heerklotz, Heiko, Szadkowska, Halina, Anderson, Thomas, & Journal of Molecular Biology, 329(4), 793–799. https://doi.org/10.1016/s0022-8236(03)00504-7
. (2003). The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton.
Heerklotz, Heiko, Szadkowska, Halina, Anderson, Thomas, & Journal of Molecular Biology, 329(4), 793–799. https://doi.org/10.1016/s0022-8236(03)00504-7
. (2003). The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton.
Honnappa, S, Cutting, B, Jahnke, W, Journal of Biological Chemistry, 278(40), 38926–38934. https://doi.org/10.1074/jbc.m305546200
, & Steinmetz, MO. (2003). Thermodynamics of the Op18/stathmin-tubulin interaction.
Honnappa, S, Cutting, B, Jahnke, W, Journal of Biological Chemistry, 278(40), 38926–38934. https://doi.org/10.1074/jbc.m305546200
, & Steinmetz, MO. (2003). Thermodynamics of the Op18/stathmin-tubulin interaction.
Karelson, G., Ziegler, A., Kunnecke, B., & NMR in Biomedicine, 16(6-7), 413–423. https://doi.org/10.1002/nbm.845
(2003). Feeding versus infusion : a novel approach to study the NAA metabolism in rat brain.
Karelson, G., Ziegler, A., Kunnecke, B., & NMR in Biomedicine, 16(6-7), 413–423. https://doi.org/10.1002/nbm.845
(2003). Feeding versus infusion : a novel approach to study the NAA metabolism in rat brain.
Machaidze, Gia, & Biochemistry, 42(43), 12570–12576. https://doi.org/10.1021/bi035225b
. (2003). Specific binding of cinnamycin (Ro 09-0198) to phosphatidylethanolamine : Comparison between micellar and membrane environments.
Machaidze, Gia, & Biochemistry, 42(43), 12570–12576. https://doi.org/10.1021/bi035225b
. (2003). Specific binding of cinnamycin (Ro 09-0198) to phosphatidylethanolamine : Comparison between micellar and membrane environments.
Ziegler, André, Blatter, Xiaochun Li, Seelig, Anna, & Biochemistry, 42(30), 9185–9194. https://doi.org/10.1021/bi0346805
. (2003). Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles : binding mechanism and thermodynamic analysis.
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