Publications
210 found
Show per page
Petrovic, Ivana, Desai, Samit, Isaikina, Polina, Abiko, Layara Akemi, Spang, Anne, & . (2025). A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis [Posted-content]. In eLife. eLife Sciences Publications, Ltd. https://doi.org/10.7554/elife.106839.1
Petrovic, Ivana, Desai, Samit, Isaikina, Polina, Abiko, Layara Akemi, Spang, Anne, & . (2025). A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis [Posted-content]. In eLife. eLife Sciences Publications, Ltd. https://doi.org/10.7554/elife.106839.1
Petrovic, Ivana, Tatli, Meltem, Desai, Samit, Grahl, Anne, Ni, Dongchun, Stahlberg, Henning, Spang, Anne, , & Abiko, Layara Akemi. (2025). Arrestin recognizes GPCRs independently of the receptor state [Journal-article]. Proceedings of the National Academy of Sciences, 122(20). https://doi.org/10.1073/pnas.2501487122
Petrovic, Ivana, Tatli, Meltem, Desai, Samit, Grahl, Anne, Ni, Dongchun, Stahlberg, Henning, Spang, Anne, , & Abiko, Layara Akemi. (2025). Arrestin recognizes GPCRs independently of the receptor state [Journal-article]. Proceedings of the National Academy of Sciences, 122(20). https://doi.org/10.1073/pnas.2501487122
Wu, Feng-Jie, Rieder, Pascal S., Abiko, Layara Akemi, Grahl, Anne, Häussinger, Daniel, & . (2025). Activation dynamics traced through a G protein–coupled receptor by 81 1 H- 15 N NMR probes. Science, 388(6748). https://doi.org/10.1126/science.adq9106
Wu, Feng-Jie, Rieder, Pascal S., Abiko, Layara Akemi, Grahl, Anne, Häussinger, Daniel, & . (2025). Activation dynamics traced through a G protein–coupled receptor by 81 1 H- 15 N NMR probes. Science, 388(6748). https://doi.org/10.1126/science.adq9106
Petrovic, Ivana, , & Isaikina, Polina. (2024). Advances in the molecular understanding of GPCR-arrestin complexes. Biochemical Society Transactions, 52(6), 2333–2342. https://doi.org/10.1042/BST20240170
Petrovic, Ivana, , & Isaikina, Polina. (2024). Advances in the molecular understanding of GPCR-arrestin complexes. Biochemical Society Transactions, 52(6), 2333–2342. https://doi.org/10.1042/BST20240170
Petrovic, Ivana, Samit, Desai, Isaikina, Polina, Abiko, Layara Akemi, Spang, Anne, & . (2024). A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis. In bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.11.04.621860
Petrovic, Ivana, Samit, Desai, Isaikina, Polina, Abiko, Layara Akemi, Spang, Anne, & . (2024). A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis. In bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.11.04.621860
Abiko, Layara Akemi, Petrovic, Ivana, Tatli, Meltem, Desai, Samit, Stahlberg, Henning, Spang, Anne, & . (2024). Biased agonism of carvedilol in the beta1-adrenergic receptor is governed by conformational exclusion [Posted-content]. In bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.07.19.604263
Abiko, Layara Akemi, Petrovic, Ivana, Tatli, Meltem, Desai, Samit, Stahlberg, Henning, Spang, Anne, & . (2024). Biased agonism of carvedilol in the beta1-adrenergic receptor is governed by conformational exclusion [Posted-content]. In bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.07.19.604263
Paladini, Johannes, Maier, Annalena, Habazettl, Judith Maria, Hertel, Ines, Sonti, Rajesh, & . (2024). The molecular basis of Abelson kinase regulation by its αI-helix [Journal-article]. eLife, 12(Version of Record). https://doi.org/10.7554/elife.92324.3
Paladini, Johannes, Maier, Annalena, Habazettl, Judith Maria, Hertel, Ines, Sonti, Rajesh, & . (2024). The molecular basis of Abelson kinase regulation by its αI-helix [Journal-article]. eLife, 12(Version of Record). https://doi.org/10.7554/elife.92324.3
Paladini, Johannes, Maier, Annalena, Habazettl, Judith Maria, Hertel, Ines, Sonti, Rajesh, & . (2023). The molecular basis of Abelson kinase regulation by its αI-helix [Posted-content]. eLife. https://doi.org/10.7554/elife.92324
Paladini, Johannes, Maier, Annalena, Habazettl, Judith Maria, Hertel, Ines, Sonti, Rajesh, & . (2023). The molecular basis of Abelson kinase regulation by its αI-helix [Posted-content]. eLife. https://doi.org/10.7554/elife.92324
Paladini, J., Maier, A., Habazettl, J. M., Hertel, I., Sonti, R., & Grzesiek, S. (2023). The molecular basis of Abelson kinase regulation by its αI-helix [Posted-content]. bioRxiv. https://doi.org/10.1101/2023.10.04.560671
Paladini, J., Maier, A., Habazettl, J. M., Hertel, I., Sonti, R., & Grzesiek, S. (2023). The molecular basis of Abelson kinase regulation by its αI-helix [Posted-content]. bioRxiv. https://doi.org/10.1101/2023.10.04.560671
Wu, Feng-Jie, Kronenberg, Domenic, Hertel, Ines, & . (2023). The key role of glutamine for protein expression and isotopic labeling in insect cells. Journal of Biological Chemistry, 299(10). https://doi.org/10.1016/j.jbc.2023.105142
Wu, Feng-Jie, Kronenberg, Domenic, Hertel, Ines, & . (2023). The key role of glutamine for protein expression and isotopic labeling in insect cells. Journal of Biological Chemistry, 299(10). https://doi.org/10.1016/j.jbc.2023.105142
Isaikina, Polina, Petrovic, Ivana, Jakob, Roman P., Sarma, Parishmita, Ranjan, Ashutosh, Baruah, Minakshi, Panwalkar, Vineet, Maier, Timm, Shukla, Arun K., & . (2023). A key GPCR phosphorylation motif discovered in arrestin2⋅CCR5 phosphopeptide complexes. Molecular cell, 83(12), 2108–2121. https://doi.org/10.1016/j.molcel.2023.05.002
Isaikina, Polina, Petrovic, Ivana, Jakob, Roman P., Sarma, Parishmita, Ranjan, Ashutosh, Baruah, Minakshi, Panwalkar, Vineet, Maier, Timm, Shukla, Arun K., & . (2023). A key GPCR phosphorylation motif discovered in arrestin2⋅CCR5 phosphopeptide complexes. Molecular cell, 83(12), 2108–2121. https://doi.org/10.1016/j.molcel.2023.05.002
Isaikina, Polina, Tsai, Ching-Ju, Petrovic, Ivana, Rogowski, Marco, Dürr, Alexandra Meng, & . (2022). Preparation of a stable CCL5·CCR5·Gi signaling complex for Cryo-EM analysis. In Shukla, Arun K. (ed.), Biomolecular Interactions Part B (Vol. 169, pp. 115–141). Elsevier. https://doi.org/10.1016/bs.mcb.2022.03.001
Isaikina, Polina, Tsai, Ching-Ju, Petrovic, Ivana, Rogowski, Marco, Dürr, Alexandra Meng, & . (2022). Preparation of a stable CCL5·CCR5·Gi signaling complex for Cryo-EM analysis. In Shukla, Arun K. (ed.), Biomolecular Interactions Part B (Vol. 169, pp. 115–141). Elsevier. https://doi.org/10.1016/bs.mcb.2022.03.001
Isaikina, Polina, Petrovic, Ivana, Jakob, Roman P., Sarma, Parishmita, Ranjan, Ashutosh, Baruah, Minakshi, Panwalkar, Vineet, Maier, Timm, Shukla, Arun K., & . (2022). A key GPCR phosphorylation motif discovered in arrestin2•CCR5 phosphopeptide complexes [Posted-content]. bioRxiv. https://doi.org/10.1101/2022.10.10.511578
Isaikina, Polina, Petrovic, Ivana, Jakob, Roman P., Sarma, Parishmita, Ranjan, Ashutosh, Baruah, Minakshi, Panwalkar, Vineet, Maier, Timm, Shukla, Arun K., & . (2022). A key GPCR phosphorylation motif discovered in arrestin2•CCR5 phosphopeptide complexes [Posted-content]. bioRxiv. https://doi.org/10.1101/2022.10.10.511578
, Paladini, Johannes, Habazettl, Judith, & Sonti, Rajesh. (2022). Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket [Posted-content]. Magnetic Resonance, 3, 91–99. https://doi.org/10.5194/mr-2022-6
, Paladini, Johannes, Habazettl, Judith, & Sonti, Rajesh. (2022). Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket [Posted-content]. Magnetic Resonance, 3, 91–99. https://doi.org/10.5194/mr-2022-6
Abiko, Layara Akemi, Dias Teixeira, Raphael, Engilberge, Sylvain, Grahl, Anne, Mühlethaler, Tobias, Sharpe, Timothy, & . (2022). Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol. Nature Chemistry, 14(10), 1133–1141. https://doi.org/10.1038/s41557-022-01009-9
Abiko, Layara Akemi, Dias Teixeira, Raphael, Engilberge, Sylvain, Grahl, Anne, Mühlethaler, Tobias, Sharpe, Timothy, & . (2022). Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol. Nature Chemistry, 14(10), 1133–1141. https://doi.org/10.1038/s41557-022-01009-9
, Paladini, Johannes, Habazettl, Judith, & Sonti, Rajesh. (2022). Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket. Magnetic Resonance, 3, 91–99. https://doi.org/10.5194/mr-3-91-2022
, Paladini, Johannes, Habazettl, Judith, & Sonti, Rajesh. (2022). Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket. Magnetic Resonance, 3, 91–99. https://doi.org/10.5194/mr-3-91-2022
Jahnke, Wolfgang, Paladini, Johannes, Habazettl, Judith M., Wiget, Andrea, Loo, Alice, Cowan Jacob, Sandra W., , & Manley, Paul W. (2022). Correspondence on “Synergy and Antagonism between Allosteric and Active-Site Inhibitors of Abl Tyrosine Kinase”. Angewandte Chemie International Edition, 61(46), e202117276. https://doi.org/10.1002/anie.202117276
Jahnke, Wolfgang, Paladini, Johannes, Habazettl, Judith M., Wiget, Andrea, Loo, Alice, Cowan Jacob, Sandra W., , & Manley, Paul W. (2022). Correspondence on “Synergy and Antagonism between Allosteric and Active-Site Inhibitors of Abl Tyrosine Kinase”. Angewandte Chemie International Edition, 61(46), e202117276. https://doi.org/10.1002/anie.202117276
Wu, Feng-Jie, Rieder, Pascal S., Abiko, Layara Akemi, Rössler, Philip, Gossert, Alvar D., Häussinger, Daniel, & . (2022). Nanobody GPS by PCS: An Efficient New NMR Analysis Method for G Protein Coupled Receptors and Other Large Proteins. Journal of the American Chemical Society, 144(47), 21728–21740. https://doi.org/10.1021/jacs.2c09692
Wu, Feng-Jie, Rieder, Pascal S., Abiko, Layara Akemi, Rössler, Philip, Gossert, Alvar D., Häussinger, Daniel, & . (2022). Nanobody GPS by PCS: An Efficient New NMR Analysis Method for G Protein Coupled Receptors and Other Large Proteins. Journal of the American Chemical Society, 144(47), 21728–21740. https://doi.org/10.1021/jacs.2c09692
Abiko, Layara Akemi, Teixeira, Raphael Dias, Engilberge, Sylvain, Grahl, Anne, & . (2021). Filling of a water-free void explains the allosteric regulation of the β<sub>1</sub>-adrenergic receptor by cholesterol [Posted-content]. bioRxiv. https://doi.org/10.1101/2021.08.30.457941
Abiko, Layara Akemi, Teixeira, Raphael Dias, Engilberge, Sylvain, Grahl, Anne, & . (2021). Filling of a water-free void explains the allosteric regulation of the β<sub>1</sub>-adrenergic receptor by cholesterol [Posted-content]. bioRxiv. https://doi.org/10.1101/2021.08.30.457941
Abiko, Layara Akemi, Rogowski, Marco, Gautier, Antoine, Schertler, Gebhard, & . (2021). Efficient production of a functional G protein-coupled receptor in E. coli for structural studies. Journal of Biomolecular NMR, 75(1), 25–38. https://doi.org/10.1007/s10858-020-00354-6
Abiko, Layara Akemi, Rogowski, Marco, Gautier, Antoine, Schertler, Gebhard, & . (2021). Efficient production of a functional G protein-coupled receptor in E. coli for structural studies. Journal of Biomolecular NMR, 75(1), 25–38. https://doi.org/10.1007/s10858-020-00354-6
Isaikina, Polina, Tsai, Ching-Ju, Dietz, Nikolaus, Pamula, Filip, Grahl, Anne, Goldie, Kenneth N., Guixà-González, Ramon, Branco, Camila, Paolini-Bertrand, Marianne, Calo, Nicolas, Cerini, Fabrice, Schertler, Gebhard F. X., Hartley, Oliver, Stahlberg, Henning, Maier, Timm, Deupi, Xavier, & . (2021). Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist. Science Advances, 7(25), eabg8685. https://doi.org/10.1126/sciadv.abg8685
Isaikina, Polina, Tsai, Ching-Ju, Dietz, Nikolaus, Pamula, Filip, Grahl, Anne, Goldie, Kenneth N., Guixà-González, Ramon, Branco, Camila, Paolini-Bertrand, Marianne, Calo, Nicolas, Cerini, Fabrice, Schertler, Gebhard F. X., Hartley, Oliver, Stahlberg, Henning, Maier, Timm, Deupi, Xavier, & . (2021). Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist. Science Advances, 7(25), eabg8685. https://doi.org/10.1126/sciadv.abg8685
Franke, Bastian, Frigård, Tuomo, , & Isogai, Shin. (2020). Versatile modules enable automated multi-column purifications on the ÄKTA pure chromatography system. Journal of Chromatography A, 1618, 460846. https://doi.org/10.1016/j.chroma.2019.460846
Franke, Bastian, Frigård, Tuomo, , & Isogai, Shin. (2020). Versatile modules enable automated multi-column purifications on the ÄKTA pure chromatography system. Journal of Chromatography A, 1618, 460846. https://doi.org/10.1016/j.chroma.2019.460846
Grahl, Anne, Abiko, Layara Akemi, Isogai, Shin, Sharpe, Timothy, & . (2020). A high-resolution description of β1-adrenergic receptor functional dynamics and allosteric coupling from backbone NMR. Nature communications, 11(1), 2216. https://doi.org/10.1038/s41467-020-15864-y
Grahl, Anne, Abiko, Layara Akemi, Isogai, Shin, Sharpe, Timothy, & . (2020). A high-resolution description of β1-adrenergic receptor functional dynamics and allosteric coupling from backbone NMR. Nature communications, 11(1), 2216. https://doi.org/10.1038/s41467-020-15864-y
Hee, Chee-Seng, Habazettl, Judith, Schmutz, Christoph, Schirmer, Tilman, Jenal, Urs, & . (2020). Intercepting second-messenger signaling by rationally designed peptides sequestering c-di-GMP. Proceedings of the National Academy of Sciences of the United States of America, 117(29), 17211–17220. https://doi.org/10.1073/pnas.2001232117
Hee, Chee-Seng, Habazettl, Judith, Schmutz, Christoph, Schirmer, Tilman, Jenal, Urs, & . (2020). Intercepting second-messenger signaling by rationally designed peptides sequestering c-di-GMP. Proceedings of the National Academy of Sciences of the United States of America, 117(29), 17211–17220. https://doi.org/10.1073/pnas.2001232117
Abiko, Layara Akemi, Grahl, Anne, & . (2019). High Pressure Shifts the β1-Adrenergic Receptor to the Active Conformation in the Absence of G Protein. Journal of the American Chemical Society, 141(42), 16663–16670. https://doi.org/10.1021/jacs.9b06042
Abiko, Layara Akemi, Grahl, Anne, & . (2019). High Pressure Shifts the β1-Adrenergic Receptor to the Active Conformation in the Absence of G Protein. Journal of the American Chemical Society, 141(42), 16663–16670. https://doi.org/10.1021/jacs.9b06042
Opitz, Christian, Ahrné, Erik, Goldie, Kenneth N., Schmidt, Alexander, & . (2019). Deuterium induces a distinctive Escherichia coli proteome that correlates with the reduction in growth rate. Journal of Biological Chemistry, 294(7), 2279–2292. https://doi.org/10.1074/jbc.ra118.006914
Opitz, Christian, Ahrné, Erik, Goldie, Kenneth N., Schmidt, Alexander, & . (2019). Deuterium induces a distinctive Escherichia coli proteome that correlates with the reduction in growth rate. Journal of Biological Chemistry, 294(7), 2279–2292. https://doi.org/10.1074/jbc.ra118.006914
Opitz, Christian, Schade, Grit, Kaufmann, Silvan, Di Berardino, Marco, Ottiger, Marcel, & . (2019). Rapid determination of general cell status, cell viability, and optimal harvest time in eukaryotic cell cultures by impedance flow cytometry. Applied microbiology and biotechnology, 103(20), 8619–8629. https://doi.org/10.1007/s00253-019-10046-3
Opitz, Christian, Schade, Grit, Kaufmann, Silvan, Di Berardino, Marco, Ottiger, Marcel, & . (2019). Rapid determination of general cell status, cell viability, and optimal harvest time in eukaryotic cell cultures by impedance flow cytometry. Applied microbiology and biotechnology, 103(20), 8619–8629. https://doi.org/10.1007/s00253-019-10046-3
Franke, Bastian, Opitz, Christian, Isogai, Shin, Grahl, Anne, Delgado, Leonildo, Gossert, Alvar D., & . (2018). Production of isotope-labeled proteins in insect cells for NMR. Journal of biomolecular NMR, 71(3), 173–184. https://doi.org/10.1007/s10858-018-0172-7
Franke, Bastian, Opitz, Christian, Isogai, Shin, Grahl, Anne, Delgado, Leonildo, Gossert, Alvar D., & . (2018). Production of isotope-labeled proteins in insect cells for NMR. Journal of biomolecular NMR, 71(3), 173–184. https://doi.org/10.1007/s10858-018-0172-7
Sonti, Rajesh, Hertel-Hering, Ines, Lamontanara, Allan Joaquim, Hantschel, Oliver, & . (2018). ATP Site Ligands Determine the Assembly State of the Abelson Kinase Regulatory Core via the Activation Loop Conformation. Journal of the American Chemical Society, 140(5), 1863–1869. https://doi.org/10.1021/jacs.7b12430
Sonti, Rajesh, Hertel-Hering, Ines, Lamontanara, Allan Joaquim, Hantschel, Oliver, & . (2018). ATP Site Ligands Determine the Assembly State of the Abelson Kinase Regulatory Core via the Activation Loop Conformation. Journal of the American Chemical Society, 140(5), 1863–1869. https://doi.org/10.1021/jacs.7b12430
. (2017). Kann man die Biologie vorausberechnen? In Füglister, K. M.; Hicklin, M.; Mäser, P. (Ed.), natura obscura (pp. 73–74). Schwabe AG.
. (2017). Kann man die Biologie vorausberechnen? In Füglister, K. M.; Hicklin, M.; Mäser, P. (Ed.), natura obscura (pp. 73–74). Schwabe AG.
Nesper, Jutta, Hug, Isabelle, Kato, Setsu, Hee, Chee-Seng, Habazettl, Judith Maria, Manfredi, Pablo, , Schirmer, Tilman, Emonet, Thierry, & Jenal, Urs. (2017). Cyclic di-GMP differentially tunes a bacterial flagellar motor through a novel class of CheY-like regulators. eLife, 6, e28842. https://doi.org/10.7554/elife.28842
Nesper, Jutta, Hug, Isabelle, Kato, Setsu, Hee, Chee-Seng, Habazettl, Judith Maria, Manfredi, Pablo, , Schirmer, Tilman, Emonet, Thierry, & Jenal, Urs. (2017). Cyclic di-GMP differentially tunes a bacterial flagellar motor through a novel class of CheY-like regulators. eLife, 6, e28842. https://doi.org/10.7554/elife.28842
Aznauryan, Mikayel, Delgado, Leonildo, Soranno, Andrea, Nettels, Daniel, Huang, Jie-Rong, Labhardt, Alexander M., , & Schuler, Benjamin. (2016). Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS. Proceedings of the National Academy of Sciences, 113(37), E5389–98. https://doi.org/10.1073/pnas.1607193113
Aznauryan, Mikayel, Delgado, Leonildo, Soranno, Andrea, Nettels, Daniel, Huang, Jie-Rong, Labhardt, Alexander M., , & Schuler, Benjamin. (2016). Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS. Proceedings of the National Academy of Sciences, 113(37), E5389–98. https://doi.org/10.1073/pnas.1607193113
Hoi Tik Alvin Leung, Bignucolo, Olivier, Aregger, Regula, Dames, Sonja A., Mazur, Adam, Berneche, Simon, & . (2016). A Rigorous and Efficient Method To Reweight Very Large Conformational Ensembles Using Average Experimental Data and To Determine Their Relative Information Content. Journal of Chemical Theory and Computation, 12(1), 383–394. https://doi.org/10.1021/acs.jctc.5b00759
Hoi Tik Alvin Leung, Bignucolo, Olivier, Aregger, Regula, Dames, Sonja A., Mazur, Adam, Berneche, Simon, & . (2016). A Rigorous and Efficient Method To Reweight Very Large Conformational Ensembles Using Average Experimental Data and To Determine Their Relative Information Content. Journal of Chemical Theory and Computation, 12(1), 383–394. https://doi.org/10.1021/acs.jctc.5b00759
Isogai, Shin, Deupi, Xavier, Opitz, Christian, Heydenreich, Franziska M, Tsai, Ching-Ju, Brueckner, Florian, Schertler, Gebhard F X, Veprintsev, Dmitry B, & . (2016). Backbone NMR reveals allosteric signal transduction networks in the β1-adrenergic receptor. Nature, 530(7589), 41–237. https://doi.org/10.1038/nature16577
Isogai, Shin, Deupi, Xavier, Opitz, Christian, Heydenreich, Franziska M, Tsai, Ching-Ju, Brueckner, Florian, Schertler, Gebhard F X, Veprintsev, Dmitry B, & . (2016). Backbone NMR reveals allosteric signal transduction networks in the β1-adrenergic receptor. Nature, 530(7589), 41–237. https://doi.org/10.1038/nature16577
Bignucolo, Olivier, Leung, Hoi Tik Alvin, , & Bernèche, Simon. (2015). Backbone hydration determines the folding signature of amino acid residues. Journal of the American Chemical Society, 137(13), 3–4300. https://doi.org/10.1021/jacs.5b00660
Bignucolo, Olivier, Leung, Hoi Tik Alvin, , & Bernèche, Simon. (2015). Backbone hydration determines the folding signature of amino acid residues. Journal of the American Chemical Society, 137(13), 3–4300. https://doi.org/10.1021/jacs.5b00660
Lamley, Jonathan M, Lougher, Matthew J, Sass, Hans Juergen, Rogowski, Marco, , & Lewandowski, Józef R. (2015). Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements. Physical Chemistry, Chemical Physics, 17(34), 2008–21997. https://doi.org/10.1039/c5cp03484a
Lamley, Jonathan M, Lougher, Matthew J, Sass, Hans Juergen, Rogowski, Marco, , & Lewandowski, Józef R. (2015). Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements. Physical Chemistry, Chemical Physics, 17(34), 2008–21997. https://doi.org/10.1039/c5cp03484a
Opitz, Christian, Isogai, Shin, & . (2015). An economic approach to efficient isotope labeling in insect cells using homemade 15N-, 13C- and 2H-labeled yeast extracts. Journal of Biomolecular NMR, 62(3), 373–385. https://doi.org/10.1007/s10858-015-9954-3
Opitz, Christian, Isogai, Shin, & . (2015). An economic approach to efficient isotope labeling in insect cells using homemade 15N-, 13C- and 2H-labeled yeast extracts. Journal of Biomolecular NMR, 62(3), 373–385. https://doi.org/10.1007/s10858-015-9954-3
Habazettl, Judith, Allan, Martin, Jensen, Pernille Rose, Sass, Hans-Jürgen, Thompson, Charles J, & . (2014). Structural basis and dynamics of multidrug recognition in a minimal bacterial multidrug resistance system. Proceedings of the National Academy of Sciences of the United States of America, 111(51), E5498–507. https://doi.org/10.1073/pnas.1412070111
Habazettl, Judith, Allan, Martin, Jensen, Pernille Rose, Sass, Hans-Jürgen, Thompson, Charles J, & . (2014). Structural basis and dynamics of multidrug recognition in a minimal bacterial multidrug resistance system. Proceedings of the National Academy of Sciences of the United States of America, 111(51), E5498–507. https://doi.org/10.1073/pnas.1412070111
Lamley, Jonathan M, Iuga, Dinu, Öster, Carl, Sass, Hans-Juergen, Rogowski, Marco, Oss, Andres, Past, Jaan, Reinhold, Andres, , Samoson, Ago, & Lewandowski, Józef R. (2014). Solid-state NMR of a protein in a precipitated complex with a full-length antibody. Journal of the American Chemical Society, 136(48), 6–16800. https://doi.org/10.1021/ja5069992
Lamley, Jonathan M, Iuga, Dinu, Öster, Carl, Sass, Hans-Juergen, Rogowski, Marco, Oss, Andres, Past, Jaan, Reinhold, Andres, , Samoson, Ago, & Lewandowski, Józef R. (2014). Solid-state NMR of a protein in a precipitated complex with a full-length antibody. Journal of the American Chemical Society, 136(48), 6–16800. https://doi.org/10.1021/ja5069992
Bignucolo, Olivier, , & Bernèche, Simon. (2013). Aromatic Amino Acids Confer Folding Propensities to a Nine-Residue Peptide [Journal-article]. Biophysical Journal, 104(2), 400a. https://doi.org/10.1016/j.bpj.2012.11.2231
Bignucolo, Olivier, , & Bernèche, Simon. (2013). Aromatic Amino Acids Confer Folding Propensities to a Nine-Residue Peptide [Journal-article]. Biophysical Journal, 104(2), 400a. https://doi.org/10.1016/j.bpj.2012.11.2231
Nielsen, Gerd, Jonker, Hendrik R A, Vajpai, Navratna, , & Schwalbe, Harald. (2013). Kinase in Motion : Insights into the Dynamic Nature of p38α by High-Pressure NMR Spectroscopic Studies. ChemBioChem, 14(14), 806–1799. https://doi.org/10.1002/cbic.201300170
Nielsen, Gerd, Jonker, Hendrik R A, Vajpai, Navratna, , & Schwalbe, Harald. (2013). Kinase in Motion : Insights into the Dynamic Nature of p38α by High-Pressure NMR Spectroscopic Studies. ChemBioChem, 14(14), 806–1799. https://doi.org/10.1002/cbic.201300170
Ramón-García, Santiago, Ng, Carol, Jensen, Pernille R, Dosanjh, Manisha, Burian, Jan, Morris, Rowan P, Folcher, Marc, Eltis, Lindsay D, , Nguyen, Liem, & Thompson, Charles J. (2013). WhiB7, an Fe-S-dependent Transcription Factor That Activates Species-specific Repertoires of Drug Resistance Determinants in Actinobacteria. Journal of Biological Chemistry, 288(48), 28–34514. https://doi.org/10.1074/jbc.m113.516385
Ramón-García, Santiago, Ng, Carol, Jensen, Pernille R, Dosanjh, Manisha, Burian, Jan, Morris, Rowan P, Folcher, Marc, Eltis, Lindsay D, , Nguyen, Liem, & Thompson, Charles J. (2013). WhiB7, an Fe-S-dependent Transcription Factor That Activates Species-specific Repertoires of Drug Resistance Determinants in Actinobacteria. Journal of Biological Chemistry, 288(48), 28–34514. https://doi.org/10.1074/jbc.m113.516385
Skora, Lukasz, Mestan, Jürgen, Fabbro, Doriano, Jahnke, Wolfgang, & . (2013). NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors. Proceedings of the National Academy of Sciences of the United States of America, 110(47), E4437–45. https://doi.org/10.1073/pnas.1314712110
Skora, Lukasz, Mestan, Jürgen, Fabbro, Doriano, Jahnke, Wolfgang, & . (2013). NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors. Proceedings of the National Academy of Sciences of the United States of America, 110(47), E4437–45. https://doi.org/10.1073/pnas.1314712110
Vajpai, Navratna, Nisius, Lydia, Wiktor, Maciej, & . (2013). High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin. Proceedings of the National Academy of Sciences of the United States of America, 110(5), E368–76. https://doi.org/10.1073/pnas.1212222110
Vajpai, Navratna, Nisius, Lydia, Wiktor, Maciej, & . (2013). High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin. Proceedings of the National Academy of Sciences of the United States of America, 110(5), E368–76. https://doi.org/10.1073/pnas.1212222110
Wiktor, Maciej, Hartley, Oliver, & . (2013). Characterization of Structure, Dynamics, and Detergent Interactions of the Anti-HIV Chemokine Variant 5P12-RANTES. Biophysical Journal, 105(11), 97–2586. https://doi.org/10.1016/j.bpj.2013.10.025
Wiktor, Maciej, Hartley, Oliver, & . (2013). Characterization of Structure, Dynamics, and Detergent Interactions of the Anti-HIV Chemokine Variant 5P12-RANTES. Biophysical Journal, 105(11), 97–2586. https://doi.org/10.1016/j.bpj.2013.10.025
Wiktor, Maciej, Morin, Sébastien, Sass, Hans-Jürgen, Kebbel, Fabian, & . (2013). Biophysical and structural investigation of bacterially expressed and engineered CCR5, a G protein-coupled receptor. Journal of Biomolecular NMR, 55(1), 79–95. https://doi.org/10.1007/s10858-012-9688-4
Wiktor, Maciej, Morin, Sébastien, Sass, Hans-Jürgen, Kebbel, Fabian, & . (2013). Biophysical and structural investigation of bacterially expressed and engineered CCR5, a G protein-coupled receptor. Journal of Biomolecular NMR, 55(1), 79–95. https://doi.org/10.1007/s10858-012-9688-4
Bax, Ad, & . (2012). ChemInform Abstract: ROESY [Journal-article]. ChemInform, 43(36). https://doi.org/10.1002/chin.201236274
Bax, Ad, & . (2012). ChemInform Abstract: ROESY [Journal-article]. ChemInform, 43(36). https://doi.org/10.1002/chin.201236274
Gentner, Martin, Allan, Martin G, Zaehringer, Franziska, Schirmer, Tilman, & . (2012). Oligomer formation of the bacterial second messenger c-di-GMP : reaction rates and equilibrium constants indicate a monomeric state at physiological concentrations. The journal of the American Chemical Society, 134(2), 29–1019. https://doi.org/10.1021/ja207742q
Gentner, Martin, Allan, Martin G, Zaehringer, Franziska, Schirmer, Tilman, & . (2012). Oligomer formation of the bacterial second messenger c-di-GMP : reaction rates and equilibrium constants indicate a monomeric state at physiological concentrations. The journal of the American Chemical Society, 134(2), 29–1019. https://doi.org/10.1021/ja207742q
Huang, Jie-rong, Gabel, Frank, Jensen, Malene Ringkjøbing, , & Blackledge, Martin. (2012). Sequence-Specific Mapping of the Interaction between Urea and Unfolded Ubiquitin from Ensemble Analysis of NMR and Small Angle Scattering Data. Journal of the American Chemical Society, 134(9), 36–4429. https://doi.org/10.1021/ja2118688
Huang, Jie-rong, Gabel, Frank, Jensen, Malene Ringkjøbing, , & Blackledge, Martin. (2012). Sequence-Specific Mapping of the Interaction between Urea and Unfolded Ubiquitin from Ensemble Analysis of NMR and Small Angle Scattering Data. Journal of the American Chemical Society, 134(9), 36–4429. https://doi.org/10.1021/ja2118688
Huang, Jie-rong, Gentner, Martin, Vajpai, Navratna, , & Blackledge, Martin. (2012). Residual dipolar couplings measured in unfolded proteins are sensitive to amino-acid-specific geometries as well as local conformational sampling. Biochemical Society Transactions, 40(5), 94–989. https://doi.org/10.1042/bst20120187
Huang, Jie-rong, Gentner, Martin, Vajpai, Navratna, , & Blackledge, Martin. (2012). Residual dipolar couplings measured in unfolded proteins are sensitive to amino-acid-specific geometries as well as local conformational sampling. Biochemical Society Transactions, 40(5), 94–989. https://doi.org/10.1042/bst20120187
Morin, Sébastien, Nisius, Lydia, Wiktor, Maciej, Kebbel, Fabian, Stahlberg, Henning, Jürgen Sass, Hans, & . (2012). Interactions of CCR5, the Main HIV Coreceptor, with Rantes and Other Ligands [Journal-article]. 56th Annual Meeting of the Biophysical-Society, 102, 239a–240a. https://doi.org/10.1016/j.bpj.2011.11.1319
Morin, Sébastien, Nisius, Lydia, Wiktor, Maciej, Kebbel, Fabian, Stahlberg, Henning, Jürgen Sass, Hans, & . (2012). Interactions of CCR5, the Main HIV Coreceptor, with Rantes and Other Ligands [Journal-article]. 56th Annual Meeting of the Biophysical-Society, 102, 239a–240a. https://doi.org/10.1016/j.bpj.2011.11.1319
Nisius, Lydia, & . (2012). Key stabilizing elements of protein structure identified through pressure and temperature perturbation of its hydrogen bond network. Nature Chemistry, 4(9), 7–711. https://doi.org/10.1038/nchem.1396
Nisius, Lydia, & . (2012). Key stabilizing elements of protein structure identified through pressure and temperature perturbation of its hydrogen bond network. Nature Chemistry, 4(9), 7–711. https://doi.org/10.1038/nchem.1396
Secchi, Massimiliano, Longhi, Renato, Vassena, Lia, Sironi, Francesca, , Lusso, Paolo, & Vangelista, Luca. (2012). Enhancement of Anti-HIV-1 Activity by Hot Spot Evolution of RANTES-Derived Peptides. Chemistry & Biology, 19(12), 88–1579. https://doi.org/10.1016/j.chembiol.2012.10.007
Secchi, Massimiliano, Longhi, Renato, Vassena, Lia, Sironi, Francesca, , Lusso, Paolo, & Vangelista, Luca. (2012). Enhancement of Anti-HIV-1 Activity by Hot Spot Evolution of RANTES-Derived Peptides. Chemistry & Biology, 19(12), 88–1579. https://doi.org/10.1016/j.chembiol.2012.10.007
Van den Bergh, Rafael, Morin, Sébastien, Sass, Hans Jürgen, , Vekemans, Marc, Florence, Eric, Thanh Thi Tran, Huyen, Imiru, Rosina Gabriel, Heyndrickx, Leo, Vanham, Guido, De Baetselier, Patrick, & Raes, Geert. (2012). Monocytes Contribute to Differential Immune Pressure on R5 versus X4 HIV through the Adipocytokine Visfatin/NAMPT. PLoS ONE, 7(4), e35074. https://doi.org/10.1371/journal.pone.0035074
Van den Bergh, Rafael, Morin, Sébastien, Sass, Hans Jürgen, , Vekemans, Marc, Florence, Eric, Thanh Thi Tran, Huyen, Imiru, Rosina Gabriel, Heyndrickx, Leo, Vanham, Guido, De Baetselier, Patrick, & Raes, Geert. (2012). Monocytes Contribute to Differential Immune Pressure on R5 versus X4 HIV through the Adipocytokine Visfatin/NAMPT. PLoS ONE, 7(4), e35074. https://doi.org/10.1371/journal.pone.0035074
, & Becker, Edwin D. (2011). Hydrogen bonding. In Harris, Robin K.; Wasylishen, Roderick E. (Ed.), Encyclopedia of NMR (Vol. 4, pp. 1929–1935). John Wiley. https://doi.org/10.1002/9780470034590.emrstm0216.pub2
, & Becker, Edwin D. (2011). Hydrogen bonding. In Harris, Robin K.; Wasylishen, Roderick E. (Ed.), Encyclopedia of NMR (Vol. 4, pp. 1929–1935). John Wiley. https://doi.org/10.1002/9780470034590.emrstm0216.pub2
Vuister, Geerten W., Tjandra, Nico, Shen, Yang, Grishaev, Alex, & . (2011). Measurement of structural restraints in “A guide to protein NMR spectroscopy”. In Lian, Lu-Yun; Roberts, Gordon (Ed.), Protein NMR spectroscopy : principal techniques and applications (p. S. 351). John Wiley & Sons.
Vuister, Geerten W., Tjandra, Nico, Shen, Yang, Grishaev, Alex, & . (2011). Measurement of structural restraints in “A guide to protein NMR spectroscopy”. In Lian, Lu-Yun; Roberts, Gordon (Ed.), Protein NMR spectroscopy : principal techniques and applications (p. S. 351). John Wiley & Sons.
Vuister, G. W., Tjandra, N., Shen, Y., Grishaev, A., & Grzesiek, S. (2011). Measurement of Structural Restraints. In Protein NMR Spectroscopy: Practical Techniques and Applications (pp. 83–157). John Wiley and Sons. https://doi.org/10.1002/9781119972006.ch4
Vuister, G. W., Tjandra, N., Shen, Y., Grishaev, A., & Grzesiek, S. (2011). Measurement of Structural Restraints. In Protein NMR Spectroscopy: Practical Techniques and Applications (pp. 83–157). John Wiley and Sons. https://doi.org/10.1002/9781119972006.ch4
Bigalke, Janna M., Dames, Sonja A., Blankenfeldt, Wulf, , & Geyer, Matthias. (2011). Structure and Dynamics of a Stabilized Coiled-Coil Domain in the P-TEFb Regulator Hexim1. Journal of Molecular Biology, 414(5), 53–639. https://doi.org/10.1016/j.jmb.2011.10.022
Bigalke, Janna M., Dames, Sonja A., Blankenfeldt, Wulf, , & Geyer, Matthias. (2011). Structure and Dynamics of a Stabilized Coiled-Coil Domain in the P-TEFb Regulator Hexim1. Journal of Molecular Biology, 414(5), 53–639. https://doi.org/10.1016/j.jmb.2011.10.022
Dames, Sonja A., Junemann, Alexander, Sass, Hans J., Schönichen, André, Stopschinski, Barbara E., , Faix, Jan, & Geyer, Matthias. (2011). Structure, dynamics, lipid binding, and physiological relevance of the putative GTPase-binding domain of Dictyostelium formin C. Journal of Biological Chemistry, 286(42), 20–36907. https://doi.org/10.1074/jbc.m111.225052
Dames, Sonja A., Junemann, Alexander, Sass, Hans J., Schönichen, André, Stopschinski, Barbara E., , Faix, Jan, & Geyer, Matthias. (2011). Structure, dynamics, lipid binding, and physiological relevance of the putative GTPase-binding domain of Dictyostelium formin C. Journal of Biological Chemistry, 286(42), 20–36907. https://doi.org/10.1074/jbc.m111.225052
Habazettl, Judith, Allan, Martin G, Jenal, Urs, & . (2011). Solution structure of the PilZ domain protein PA4608 complex with cyclic di-GMP identifies charge clustering as molecular readout. Journal of Biological Chemistry, 286(16), 14–14304. https://doi.org/10.1074/jbc.m110.209007
Habazettl, Judith, Allan, Martin G, Jenal, Urs, & . (2011). Solution structure of the PilZ domain protein PA4608 complex with cyclic di-GMP identifies charge clustering as molecular readout. Journal of Biological Chemistry, 286(16), 14–14304. https://doi.org/10.1074/jbc.m110.209007
Lewandowski, Józef R., Sass, Hans Jürgen, , Blackledge, Martin, & Emsley, Lyndon. (2011). Site-specific measurement of slow motions in proteins. Journal of the American Chemical Society, 133(42), 5–16762. https://doi.org/10.1021/ja206815h
Lewandowski, Józef R., Sass, Hans Jürgen, , Blackledge, Martin, & Emsley, Lyndon. (2011). Site-specific measurement of slow motions in proteins. Journal of the American Chemical Society, 133(42), 5–16762. https://doi.org/10.1021/ja206815h
Huang, Jie-rong, & . (2010). Ensemble calculations of unstructured proteins constrained by RDC and PRE data : a case study of urea-denatured ubiquitin. Journal of the American Chemical Society, 132(2), 694–705. https://doi.org/10.1021/ja907974m
Huang, Jie-rong, & . (2010). Ensemble calculations of unstructured proteins constrained by RDC and PRE data : a case study of urea-denatured ubiquitin. Journal of the American Chemical Society, 132(2), 694–705. https://doi.org/10.1021/ja907974m
Lewandowski, Józef R, Sein, Julien, Sass, Hans Jürgen, , Blackledge, Martin, & Emsley, Lyndon. (2010). Measurement of site-specific 13C spin-lattice relaxation in a crystalline protein. Journal of the American Chemical Society, 132(24), 4–8252. https://doi.org/10.1021/ja102744b
Lewandowski, Józef R, Sein, Julien, Sass, Hans Jürgen, , Blackledge, Martin, & Emsley, Lyndon. (2010). Measurement of site-specific 13C spin-lattice relaxation in a crystalline protein. Journal of the American Chemical Society, 132(24), 4–8252. https://doi.org/10.1021/ja102744b
Schönichen, André, Bigalke, Janna M, Urbanke, Claus, , Dames, Sonja A, & Geyer, Matthias. (2010). A flexible bipartite coiled coil structure is required for the interaction of Hexim1 with the P-TEFB subunit cyclin T1. Biochemistry, 49(14), 91–3083. https://doi.org/10.1021/bi902072f
Schönichen, André, Bigalke, Janna M, Urbanke, Claus, , Dames, Sonja A, & Geyer, Matthias. (2010). A flexible bipartite coiled coil structure is required for the interaction of Hexim1 with the P-TEFB subunit cyclin T1. Biochemistry, 49(14), 91–3083. https://doi.org/10.1021/bi902072f
Vajpai, Navratna, Gentner, Martin, Huang, Jie-Rong, Blackledge, Martin, & . (2010). Side-chain chi(1) conformations in urea-denatured ubiquitin and protein G from (3)J coupling constants and residual dipolar couplings. Journal of the American Chemical Society, 132(9), 203–3196. https://doi.org/10.1021/ja910331t
Vajpai, Navratna, Gentner, Martin, Huang, Jie-Rong, Blackledge, Martin, & . (2010). Side-chain chi(1) conformations in urea-denatured ubiquitin and protein G from (3)J coupling constants and residual dipolar couplings. Journal of the American Chemical Society, 132(9), 203–3196. https://doi.org/10.1021/ja910331t
Zhang, Jianming, Adrián, Francisco J, Jahnke, Wolfgang, Cowan-Jacob, Sandra W, Li, Allen G, Iacob, Roxana E, Sim, Taebo, Powers, John, Dierks, Christine, Sun, Fangxian, Guo, Gui-Rong, Ding, Qiang, Okram, Barun, Choi, Yongmun, Wojciechowski, Amy, Deng, Xianming, Liu, Guoxun, Fendrich, Gabriele, Strauss, André, et al. (2010). Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors. Nature, 463(7280), 6–501. https://doi.org/10.1038/nature08675
Zhang, Jianming, Adrián, Francisco J, Jahnke, Wolfgang, Cowan-Jacob, Sandra W, Li, Allen G, Iacob, Roxana E, Sim, Taebo, Powers, John, Dierks, Christine, Sun, Fangxian, Guo, Gui-Rong, Ding, Qiang, Okram, Barun, Choi, Yongmun, Wojciechowski, Amy, Deng, Xianming, Liu, Guoxun, Fendrich, Gabriele, Strauss, André, et al. (2010). Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors. Nature, 463(7280), 6–501. https://doi.org/10.1038/nature08675
, & Sass, H. J. (2009). From biomolecular structure to functional understanding : new NMR developments narrow the gap. Current Opinion in Structural Biology, 19(5), 585–595. https://doi.org/10.1016/j.sbi.2009.07.015
, & Sass, H. J. (2009). From biomolecular structure to functional understanding : new NMR developments narrow the gap. Current Opinion in Structural Biology, 19(5), 585–595. https://doi.org/10.1016/j.sbi.2009.07.015
Häussinger, Daniel, Huang, Jie-rong, & . (2009). DOTA-M8 : an extremely rigid, high-affinity lanthanide chelating tag for PCS NMR spectroscopy. Journal of the American Chemical Society, 131(41), 7–14761. https://doi.org/10.1021/ja903233w
Häussinger, Daniel, Huang, Jie-rong, & . (2009). DOTA-M8 : an extremely rigid, high-affinity lanthanide chelating tag for PCS NMR spectroscopy. Journal of the American Chemical Society, 131(41), 7–14761. https://doi.org/10.1021/ja903233w
Jensen, M. R., Markwick, P. R. L., Meier, S., Griesinger, C., Zweckstetter, M., , Bernado, P., & Blackledge, M. (2009). Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings. Structure, 17(9), 85–1169. https://doi.org/10.1016/j.str.2009.08.001
Jensen, M. R., Markwick, P. R. L., Meier, S., Griesinger, C., Zweckstetter, M., , Bernado, P., & Blackledge, M. (2009). Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings. Structure, 17(9), 85–1169. https://doi.org/10.1016/j.str.2009.08.001
Laage, S., Marchetti, A., Sein, J., Pierattelli, R., Sass, H. J., Grzesiek, S., Lesage, A., Pintacuda, G., & Emsley, L. (2008). Band-selective1H-13C cross-polarization in fast magic angle spinning solid-state NMR spectroscopy. Journal of the American Chemical Society, 130(51), 17216–17217. https://doi.org/10.1021/ja805926d
Laage, S., Marchetti, A., Sein, J., Pierattelli, R., Sass, H. J., Grzesiek, S., Lesage, A., Pintacuda, G., & Emsley, L. (2008). Band-selective1H-13C cross-polarization in fast magic angle spinning solid-state NMR spectroscopy. Journal of the American Chemical Society, 130(51), 17216–17217. https://doi.org/10.1021/ja805926d
Wang, Wei, Sass, Hans Jürgen, Zähringer, Ulrich, & . (2008). Structure and Dynamics of <sup>13</sup>C,<sup>15</sup>N‐Labeled Lipopolysaccharides in a Membrane Mimetic [Journal-article]. Angewandte Chemie, 120(51), 10018–10022. https://doi.org/10.1002/ange.200803474
Wang, Wei, Sass, Hans Jürgen, Zähringer, Ulrich, & . (2008). Structure and Dynamics of <sup>13</sup>C,<sup>15</sup>N‐Labeled Lipopolysaccharides in a Membrane Mimetic [Journal-article]. Angewandte Chemie, 120(51), 10018–10022. https://doi.org/10.1002/ange.200803474
Dingley, Andrew J, Nisius, Lydia, Cordier, Florence, & . (2008). Direct detection of N−H⋯N hydrogen bonds in biomolecules by NMR spectroscopy [Journal-article]. Nature Protocols, 3(2), 242–248. https://doi.org/10.1038/nprot.2007.497
Dingley, Andrew J, Nisius, Lydia, Cordier, Florence, & . (2008). Direct detection of N−H⋯N hydrogen bonds in biomolecules by NMR spectroscopy [Journal-article]. Nature Protocols, 3(2), 242–248. https://doi.org/10.1038/nprot.2007.497
Adamczyk, Patrizia, Meier, Sebastian, Gross, Thomas, Hobmayer, Bert, , Bächinger, Hans Peter, Holstein, Thomas W, & Ozbek, Suat. (2008). Minicollagen-15, a novel minicollagen isolated from Hydra, forms tubule structures in nematocysts. Journal of Molecular Biology, 376(4), 20–1008. https://doi.org/10.1016/j.jmb.2007.10.090
Adamczyk, Patrizia, Meier, Sebastian, Gross, Thomas, Hobmayer, Bert, , Bächinger, Hans Peter, Holstein, Thomas W, & Ozbek, Suat. (2008). Minicollagen-15, a novel minicollagen isolated from Hydra, forms tubule structures in nematocysts. Journal of Molecular Biology, 376(4), 20–1008. https://doi.org/10.1016/j.jmb.2007.10.090
Cordier, Florence, Nisius, Lydia, Dingley, Andrew J., & . (2008). Direct detection of N-H[...]O=C hydrogen bonds in biomolecules by NMR spectroscopy. Nature Protocols, 3(2), 41–235. https://doi.org/10.1038/nprot.2007.498
Cordier, Florence, Nisius, Lydia, Dingley, Andrew J., & . (2008). Direct detection of N-H[...]O=C hydrogen bonds in biomolecules by NMR spectroscopy. Nature Protocols, 3(2), 41–235. https://doi.org/10.1038/nprot.2007.498
Dames, Sonja A, Bang, Eunjung, Haüssinger, Daniel, Ahrens, Thomas, Engel, Jürgen, & . (2008). Insights into the low adhesive capacity of human T-cadherin from the NMR structure of Its N-terminal extracellular domain. Journal of Biological Chemistry, 283(34), 95–23485. https://doi.org/10.1074/jbc.m708335200
Dames, Sonja A, Bang, Eunjung, Haüssinger, Daniel, Ahrens, Thomas, Engel, Jürgen, & . (2008). Insights into the low adhesive capacity of human T-cadherin from the NMR structure of Its N-terminal extracellular domain. Journal of Biological Chemistry, 283(34), 95–23485. https://doi.org/10.1074/jbc.m708335200
Laage, Segolene, Marchetti, Alessandro, Sein, Julien, Pierattelli, Roberta, Sass, Hans Juergen, , Lesage, Anne, Pintacuda, Guido, & Emsley, Lyndon. (2008). Band-selective ¹H-¹³C cross-polarization in fast magic angle spinning solid-state NMR spectroscopy. Journal of the American Chemical Society, 130(51), 17216–+. https://doi.org/10.1021/ja805926d
Laage, Segolene, Marchetti, Alessandro, Sein, Julien, Pierattelli, Roberta, Sass, Hans Juergen, , Lesage, Anne, Pintacuda, Guido, & Emsley, Lyndon. (2008). Band-selective ¹H-¹³C cross-polarization in fast magic angle spinning solid-state NMR spectroscopy. Journal of the American Chemical Society, 130(51), 17216–+. https://doi.org/10.1021/ja805926d
Meier, Sebastian, Blackledge, Martin, & . (2008). Conformational distributions of unfolded polypeptides from novel NMR techniques. Journal of Chemical Physics, 128(5), 52204. https://doi.org/10.1063/1.2838167
Meier, Sebastian, Blackledge, Martin, & . (2008). Conformational distributions of unfolded polypeptides from novel NMR techniques. Journal of Chemical Physics, 128(5), 52204. https://doi.org/10.1063/1.2838167
Mrosek, Michael, Meier, Sebastian, Ucurum-Fotiadis, Zöhre, von Castelmur, Eleonore, Hedbom, Erik, Lustig, Ariel, , Labeit, Dietmar, Labeit, Siegfried, & Mayans, Olga. (2008). Structural analysis of B-Box 2 from MuRF1 : identification of a novel self-association pattern in a RING-like fold. Biochemistry, 47(40), 30–10722. https://doi.org/10.1021/bi800733z
Mrosek, Michael, Meier, Sebastian, Ucurum-Fotiadis, Zöhre, von Castelmur, Eleonore, Hedbom, Erik, Lustig, Ariel, , Labeit, Dietmar, Labeit, Siegfried, & Mayans, Olga. (2008). Structural analysis of B-Box 2 from MuRF1 : identification of a novel self-association pattern in a RING-like fold. Biochemistry, 47(40), 30–10722. https://doi.org/10.1021/bi800733z
Nisius, Lydia, Rogowski, Marco, Vangelista, Luca, & . (2008). Large-scale expression and purification of the major HIV-1 coreceptor CCR5 and characterization of its interaction with RANTES. Protein Expression and Purification, 61(2), 62–155. https://doi.org/10.1016/j.pep.2008.06.001
Nisius, Lydia, Rogowski, Marco, Vangelista, Luca, & . (2008). Large-scale expression and purification of the major HIV-1 coreceptor CCR5 and characterization of its interaction with RANTES. Protein Expression and Purification, 61(2), 62–155. https://doi.org/10.1016/j.pep.2008.06.001
Vajpai, Navratna, Strauss, André, Fendrich, Gabriele, Cowan-Jacob, Sandra W., Manley, Paul W., , & Jahnke, Wolfgang. (2008). Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib. Journal of Biological Chemistry, 283(26), 302–18292. https://doi.org/10.1074/jbc.m801337200
Vajpai, Navratna, Strauss, André, Fendrich, Gabriele, Cowan-Jacob, Sandra W., Manley, Paul W., , & Jahnke, Wolfgang. (2008). Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib. Journal of Biological Chemistry, 283(26), 302–18292. https://doi.org/10.1074/jbc.m801337200
Vajpai, Navratna, Strauss, André, Fendrich, Gabriele, Cowan-Jacob, Sandra W., Manley, Paul W., Jahnke, Wolfgang, & . (2008). Backbone NMR resonance assignment of the Abelson kinase domain in complex with imatinib. Biomolecular NMR Assignments, 2(1), 2–41. https://doi.org/10.1007/s12104-008-9079-7
Vajpai, Navratna, Strauss, André, Fendrich, Gabriele, Cowan-Jacob, Sandra W., Manley, Paul W., Jahnke, Wolfgang, & . (2008). Backbone NMR resonance assignment of the Abelson kinase domain in complex with imatinib. Biomolecular NMR Assignments, 2(1), 2–41. https://doi.org/10.1007/s12104-008-9079-7
Wang, W., Sass, H.J., Zahringer, U., & (2008). Structure and dynamics of 13C,15N-labeled lipopolysaccharides in a membrane mimetic. Angewandte Chemie. International Edition in English, 47(51), 9870–9874. https://doi.org/10.1002/anie.200803474
Wang, W., Sass, H.J., Zahringer, U., & (2008). Structure and dynamics of 13C,15N-labeled lipopolysaccharides in a membrane mimetic. Angewandte Chemie. International Edition in English, 47(51), 9870–9874. https://doi.org/10.1002/anie.200803474
Bax, Ad, & . (2007). Rotating frame Overhauser enhancement spectroscopy. In Grant, David M.; Harris, R. K. (Ed.), Encyclopedia of Nuclear Magnetic Resonance (pp. 245–257). John Wiley. https://doi.org/10.1002/9780470034590.emrstm0473
Bax, Ad, & . (2007). Rotating frame Overhauser enhancement spectroscopy. In Grant, David M.; Harris, R. K. (Ed.), Encyclopedia of Nuclear Magnetic Resonance (pp. 245–257). John Wiley. https://doi.org/10.1002/9780470034590.emrstm0473
Bang, Eunjung, Häussinger, Daniel, Stetefeld, Jörg, Ahrens, Thomas, , & Dames, Sonja A. (2007). ¹H, ¹³C, and ¹⁵N chemical shift assignments for the N-terminal extracellular domain of T-cadherin [Review of ¹H, ¹³C, and ¹⁵N chemical shift assignments for the N-terminal extracellular domain of T-cadherin]. Journal of Biomolecular NMR, 38, Article 2. https://doi.org/10.1007/s10858-006-9106-x
Bang, Eunjung, Häussinger, Daniel, Stetefeld, Jörg, Ahrens, Thomas, , & Dames, Sonja A. (2007). ¹H, ¹³C, and ¹⁵N chemical shift assignments for the N-terminal extracellular domain of T-cadherin [Review of ¹H, ¹³C, and ¹⁵N chemical shift assignments for the N-terminal extracellular domain of T-cadherin]. Journal of Biomolecular NMR, 38, Article 2. https://doi.org/10.1007/s10858-006-9106-x
Christen, Matthias, Christen, Beat, Allan, Martin G, Folcher, Marc, Jenö, Paul, , & Jenal, Urs. (2007). DgrA is a member of a new family of cyclic diguanosine monophosphate receptors and controls flagellar motor function in Caulobacter crescentus. Proceedings of the National Academy of Sciences of the United States of America, 104(10), 7–4112. https://doi.org/10.1073/pnas.0607738104
Christen, Matthias, Christen, Beat, Allan, Martin G, Folcher, Marc, Jenö, Paul, , & Jenal, Urs. (2007). DgrA is a member of a new family of cyclic diguanosine monophosphate receptors and controls flagellar motor function in Caulobacter crescentus. Proceedings of the National Academy of Sciences of the United States of America, 104(10), 7–4112. https://doi.org/10.1073/pnas.0607738104
Dames, Sonja A, Schönichen, André, Schulte, Antje, Barboric, Matjaz, Peterlin, B Matija, , & Geyer, Matthias. (2007). Structure of the Cyclin T binding domain of Hexim1 and molecular basis for its recognition of P-TEFb. Proceedings of the National Academy of Sciences of the United States of America, 104(36), 7–14312. https://doi.org/10.1073/pnas.0701848104
Dames, Sonja A, Schönichen, André, Schulte, Antje, Barboric, Matjaz, Peterlin, B Matija, , & Geyer, Matthias. (2007). Structure of the Cyclin T binding domain of Hexim1 and molecular basis for its recognition of P-TEFb. Proceedings of the National Academy of Sciences of the United States of America, 104(36), 7–14312. https://doi.org/10.1073/pnas.0701848104
Duma, Luminita, Häussinger, Daniel, Rogowski, Marco, Lusso, Paolo, & . (2007). Recognition of RANTES by extracellular parts of the CCR5 receptor. Journal of Molecular Biology, 365(4), 75–1063. https://doi.org/10.1016/j.jmb.2006.10.040
Duma, Luminita, Häussinger, Daniel, Rogowski, Marco, Lusso, Paolo, & . (2007). Recognition of RANTES by extracellular parts of the CCR5 receptor. Journal of Molecular Biology, 365(4), 75–1063. https://doi.org/10.1016/j.jmb.2006.10.040
Meier, Sebastian, , & Blackledge, Martin. (2007). Mapping the conformational landscape of urea-denatured ubiquitin using residual dipolar couplings. Journal of the American Chemical Society, 129(31), 807–9799. https://doi.org/10.1021/ja0724339
Meier, Sebastian, , & Blackledge, Martin. (2007). Mapping the conformational landscape of urea-denatured ubiquitin using residual dipolar couplings. Journal of the American Chemical Society, 129(31), 807–9799. https://doi.org/10.1021/ja0724339
Meier, Sebastian, Jensen, Pernille Rose, Adamczyk, Patrizia, Bächinger, Hans Peter, Holstein, Thomas W, Engel, Jürgen, Ozbek, Suat, & . (2007). Sequence-structure and structure-function analysis in cysteine-rich domains forming the ultrastable nematocyst wall. Journal of Molecular Biology, 368(3), 28–718. https://doi.org/10.1016/j.jmb.2007.02.026
Meier, Sebastian, Jensen, Pernille Rose, Adamczyk, Patrizia, Bächinger, Hans Peter, Holstein, Thomas W, Engel, Jürgen, Ozbek, Suat, & . (2007). Sequence-structure and structure-function analysis in cysteine-rich domains forming the ultrastable nematocyst wall. Journal of Molecular Biology, 368(3), 28–718. https://doi.org/10.1016/j.jmb.2007.02.026
Meier, Sebastian, Strohmeier, Mark, Blackledge, Martin, & . (2007). Direct observation of dipolar couplings and hydrogen bonds across a beta-hairpin in 8 M urea. Journal of the American Chemical Society, 129(4), 5–754. https://doi.org/10.1021/ja067522k
Meier, Sebastian, Strohmeier, Mark, Blackledge, Martin, & . (2007). Direct observation of dipolar couplings and hydrogen bonds across a beta-hairpin in 8 M urea. Journal of the American Chemical Society, 129(4), 5–754. https://doi.org/10.1021/ja067522k
Meier, S., Jensen, P. R., David, C. N., Chapman, J., Holstein, T. W., , & Ozbek, S. (2007). Continuous molecular evolution of protein-domain structures by single amino acid changes. Current Biology, 17(2), 8–173. https://doi.org/10.1016/j.cub.2006.10.063
Meier, S., Jensen, P. R., David, C. N., Chapman, J., Holstein, T. W., , & Ozbek, S. (2007). Continuous molecular evolution of protein-domain structures by single amino acid changes. Current Biology, 17(2), 8–173. https://doi.org/10.1016/j.cub.2006.10.063
Sass, Hans-Jürgen, Schmid, Franziska Fang-Fang, & . (2007). Correlation of protein structure and dynamics to scalar couplings across hydrogen bonds. Journal of the American Chemical Society, 129(18), 903–5898. https://doi.org/10.1021/ja068336h
Sass, Hans-Jürgen, Schmid, Franziska Fang-Fang, & . (2007). Correlation of protein structure and dynamics to scalar couplings across hydrogen bonds. Journal of the American Chemical Society, 129(18), 903–5898. https://doi.org/10.1021/ja068336h
Bouvignies, Guillaume, Meier, Sebastian, , & Blackledge, Martin. (2006). Ultrahigh‐Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media [Journal-article]. Angewandte Chemie, 118(48), 8346–8349. https://doi.org/10.1002/ange.200603627
Bouvignies, Guillaume, Meier, Sebastian, , & Blackledge, Martin. (2006). Ultrahigh‐Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media [Journal-article]. Angewandte Chemie, 118(48), 8346–8349. https://doi.org/10.1002/ange.200603627
Bouvignies, Guillaume, Meier, Sebastian, , & Blackledge, Martin. (2006). Ultrahigh-resolution backbone structure of perdeuterated protein GB1 using residual dipolar couplings from two alignment media. Angewandte Chemie. International Edition in English, 45(48), 9–8166. https://doi.org/10.1002/anie.200603627
Bouvignies, Guillaume, Meier, Sebastian, , & Blackledge, Martin. (2006). Ultrahigh-resolution backbone structure of perdeuterated protein GB1 using residual dipolar couplings from two alignment media. Angewandte Chemie. International Edition in English, 45(48), 9–8166. https://doi.org/10.1002/anie.200603627
Cordier, Florence, Hartmann, Britta, Rogowski, Marco, Affolter, Markus, & . (2006). DNA recognition by the brinker repressor - an extreme case of coupling between binding and folding. Journal of Molecular Biology, 361(4), 72–659. https://doi.org/10.1016/j.jmb.2006.06.045
Cordier, Florence, Hartmann, Britta, Rogowski, Marco, Affolter, Markus, & . (2006). DNA recognition by the brinker repressor - an extreme case of coupling between binding and folding. Journal of Molecular Biology, 361(4), 72–659. https://doi.org/10.1016/j.jmb.2006.06.045
Dames, S. A., Schonichen, A., , & Geyer, M. (2006). NMR assignment of the Cyclin T-binding domain of human Hexim1. Journal of Biomolecular NMR, 36 Suppl 1(Supplement 1), 39. https://doi.org/10.1007/s10858-006-9010-4
Dames, S. A., Schonichen, A., , & Geyer, M. (2006). NMR assignment of the Cyclin T-binding domain of human Hexim1. Journal of Biomolecular NMR, 36 Suppl 1(Supplement 1), 39. https://doi.org/10.1007/s10858-006-9010-4
Dames, Sonja Alexandra, Aregger, Regula, Vajpai, Navratna, Bernado, Pau, Blackledge, Martin, & . (2006). Residual dipolar couplings in short peptides reveal systematic conformational preferences of individual amino acids. Journal of the American Chemical Society, 128(41), 14–13508. https://doi.org/10.1021/ja063606h
Dames, Sonja Alexandra, Aregger, Regula, Vajpai, Navratna, Bernado, Pau, Blackledge, Martin, & . (2006). Residual dipolar couplings in short peptides reveal systematic conformational preferences of individual amino acids. Journal of the American Chemical Society, 128(41), 14–13508. https://doi.org/10.1021/ja063606h
, Allan, M., Cordier, F., Häussinger, D., Jensen, P., Kahmann, J., Meier, S., & Sass, H.J. (2005). Nuclear magnetic resonance as a quantitative tool to study interactions in biomacromolecules. Pure and Applied Chemistry, 77, 1409–1424. https://doi.org/10.1351/pac200577081409
, Allan, M., Cordier, F., Häussinger, D., Jensen, P., Kahmann, J., Meier, S., & Sass, H.J. (2005). Nuclear magnetic resonance as a quantitative tool to study interactions in biomacromolecules. Pure and Applied Chemistry, 77, 1409–1424. https://doi.org/10.1351/pac200577081409
Bouvignies, Guillaume, Bernadó, Pau, Meier, Sebastian, Cho, Kyuil, , Brüschweiler, Rafael, & Blackledge, Martin. (2005). Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings. Proceedings of the National Academy of Sciences of the United States of America, 102(39), 90–13885. https://doi.org/10.1073/pnas.0505129102
Bouvignies, Guillaume, Bernadó, Pau, Meier, Sebastian, Cho, Kyuil, , Brüschweiler, Rafael, & Blackledge, Martin. (2005). Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings. Proceedings of the National Academy of Sciences of the United States of America, 102(39), 90–13885. https://doi.org/10.1073/pnas.0505129102
Dames, S. A., Mulet, J. M., Rathgeb-Szabo, K., Hall, M. N., & (2005). The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability. Journal of Biological Chemistry, 280(21), 20558–20564. https://doi.org/10.1074/jbc.m501116200
Dames, S. A., Mulet, J. M., Rathgeb-Szabo, K., Hall, M. N., & (2005). The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability. Journal of Biological Chemistry, 280(21), 20558–20564. https://doi.org/10.1074/jbc.m501116200