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Petrovic, Ivana, Biochemical Society Transactions, 52(6), 2333–2342. https://doi.org/10.1042/BST20240170
, & Isaikina, Polina. (2024). Advances in the molecular understanding of GPCR-arrestin complexes.
Petrovic, Ivana, Biochemical Society Transactions, 52(6), 2333–2342. https://doi.org/10.1042/BST20240170
, & Isaikina, Polina. (2024). Advances in the molecular understanding of GPCR-arrestin complexes.
Petrovic, Ivana, Samit, Desai, Isaikina, Polina, Abiko, Layara Akemi, Spang, Anne, & bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.11.04.621860
. (2024). A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis. In
Petrovic, Ivana, Samit, Desai, Isaikina, Polina, Abiko, Layara Akemi, Spang, Anne, & bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.11.04.621860
. (2024). A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis. In
Abiko, Layara Akemi, Petrovic, Ivana, Tatli, Meltem, Desai, Samit, Stahlberg, Henning, Spang, Anne, & bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.07.19.604263
. (2024). Biased agonism of carvedilol in the beta1-adrenergic receptor is governed by conformational exclusion [Posted-content]. In
Abiko, Layara Akemi, Petrovic, Ivana, Tatli, Meltem, Desai, Samit, Stahlberg, Henning, Spang, Anne, & bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.07.19.604263
. (2024). Biased agonism of carvedilol in the beta1-adrenergic receptor is governed by conformational exclusion [Posted-content]. In
Paladini, Johannes, Maier, Annalena, Habazettl, Judith Maria, Hertel, Ines, Sonti, Rajesh, & eLife, 12(Version of Record). https://doi.org/10.7554/elife.92324.3
. (2024). The molecular basis of Abelson kinase regulation by its αI-helix [Journal-article].
Paladini, Johannes, Maier, Annalena, Habazettl, Judith Maria, Hertel, Ines, Sonti, Rajesh, & eLife, 12(Version of Record). https://doi.org/10.7554/elife.92324.3
. (2024). The molecular basis of Abelson kinase regulation by its αI-helix [Journal-article].
Paladini, Johannes, Maier, Annalena, Habazettl, Judith Maria, Hertel, Ines, Sonti, Rajesh, & eLife. https://doi.org/10.7554/elife.92324
. (2023). The molecular basis of Abelson kinase regulation by its αI-helix [Posted-content].
Paladini, Johannes, Maier, Annalena, Habazettl, Judith Maria, Hertel, Ines, Sonti, Rajesh, & eLife. https://doi.org/10.7554/elife.92324
. (2023). The molecular basis of Abelson kinase regulation by its αI-helix [Posted-content].
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, & Journal of Biological Chemistry, 299(10). https://doi.org/10.1016/j.jbc.2023.105142
. (2023). The key role of glutamine for protein expression and isotopic labeling in insect cells.
Wu, Feng-Jie, Kronenberg, Domenic, Hertel, Ines, & Journal of Biological Chemistry, 299(10). https://doi.org/10.1016/j.jbc.2023.105142
. (2023). The key role of glutamine for protein expression and isotopic labeling in insect cells.
Isaikina, Polina, Petrovic, Ivana, Jakob, Roman P., Sarma, Parishmita, Ranjan, Ashutosh, Baruah, Minakshi, Panwalkar, Vineet, Maier, Timm, Shukla, Arun K., & Molecular cell, 83(12), 2108–2121. https://doi.org/10.1016/j.molcel.2023.05.002
. (2023). A key GPCR phosphorylation motif discovered in arrestin2⋅CCR5 phosphopeptide complexes.
Isaikina, Polina, Petrovic, Ivana, Jakob, Roman P., Sarma, Parishmita, Ranjan, Ashutosh, Baruah, Minakshi, Panwalkar, Vineet, Maier, Timm, Shukla, Arun K., & Molecular cell, 83(12), 2108–2121. https://doi.org/10.1016/j.molcel.2023.05.002
. (2023). A key GPCR phosphorylation motif discovered in arrestin2⋅CCR5 phosphopeptide complexes.
Isaikina, Polina, Petrovic, Ivana, Jakob, Roman P., Sarma, Parishmita, Ranjan, Ashutosh, Baruah, Minakshi, Panwalkar, Vineet, Maier, Timm, Shukla, Arun K., & A key GPCR phosphorylation motif discovered in arrestin2•CCR5 phosphopeptide complexes [Posted-content]. bioRxiv. https://doi.org/10.1101/2022.10.10.511578
. (2022).
Isaikina, Polina, Petrovic, Ivana, Jakob, Roman P., Sarma, Parishmita, Ranjan, Ashutosh, Baruah, Minakshi, Panwalkar, Vineet, Maier, Timm, Shukla, Arun K., & A key GPCR phosphorylation motif discovered in arrestin2•CCR5 phosphopeptide complexes [Posted-content]. bioRxiv. https://doi.org/10.1101/2022.10.10.511578
. (2022).
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
, 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].
Abiko, Layara Akemi, Dias Teixeira, Raphael, Engilberge, Sylvain, Grahl, Anne, Mühlethaler, Tobias, Sharpe, Timothy, & Nature Chemistry, 14(10), 1133–1141. https://doi.org/10.1038/s41557-022-01009-9
. (2022). Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol.
Abiko, Layara Akemi, Dias Teixeira, Raphael, Engilberge, Sylvain, Grahl, Anne, Mühlethaler, Tobias, Sharpe, Timothy, & Nature Chemistry, 14(10), 1133–1141. https://doi.org/10.1038/s41557-022-01009-9
. (2022). Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol.
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
, 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.
Jahnke, Wolfgang, Paladini, Johannes, Habazettl, Judith M., Wiget, Andrea, Loo, Alice, Cowan Jacob, Sandra W., Angewandte Chemie International Edition, 61(46), e202117276. https://doi.org/10.1002/anie.202117276
, & Manley, Paul W. (2022). Correspondence on “Synergy and Antagonism between Allosteric and Active-Site Inhibitors of Abl Tyrosine Kinase”.
Jahnke, Wolfgang, Paladini, Johannes, Habazettl, Judith M., Wiget, Andrea, Loo, Alice, Cowan Jacob, Sandra W., Angewandte Chemie International Edition, 61(46), e202117276. https://doi.org/10.1002/anie.202117276
, & Manley, Paul W. (2022). Correspondence on “Synergy and Antagonism between Allosteric and Active-Site Inhibitors of Abl Tyrosine Kinase”.
Wu, Feng-Jie, Rieder, Pascal S., Abiko, Layara Akemi, Rössler, Philip, Gossert, Alvar D., Häussinger, Daniel, & Journal of the American Chemical Society, 144(47), 21728–21740. https://doi.org/10.1021/jacs.2c09692
. (2022). Nanobody GPS by PCS: An Efficient New NMR Analysis Method for G Protein Coupled Receptors and Other Large Proteins.
Wu, Feng-Jie, Rieder, Pascal S., Abiko, Layara Akemi, Rössler, Philip, Gossert, Alvar D., Häussinger, Daniel, & Journal of the American Chemical Society, 144(47), 21728–21740. https://doi.org/10.1021/jacs.2c09692
. (2022). Nanobody GPS by PCS: An Efficient New NMR Analysis Method for G Protein Coupled Receptors and Other Large Proteins.
Isaikina, Polina, Tsai, Ching-Ju, Petrovic, Ivana, Rogowski, Marco, Dürr, Alexandra Meng, & Biomolecular Interactions Part B (Vol. 169, pp. 115–141). Elsevier. https://doi.org/10.1016/bs.mcb.2022.03.001
. (2022). Preparation of a stable CCL5·CCR5·Gi signaling complex for Cryo-EM analysis. In Shukla, Arun K. (ed.),
Isaikina, Polina, Tsai, Ching-Ju, Petrovic, Ivana, Rogowski, Marco, Dürr, Alexandra Meng, & Biomolecular Interactions Part B (Vol. 169, pp. 115–141). Elsevier. https://doi.org/10.1016/bs.mcb.2022.03.001
. (2022). Preparation of a stable CCL5·CCR5·Gi signaling complex for Cryo-EM analysis. In Shukla, Arun K. (ed.),
Abiko, Layara Akemi, Teixeira, Raphael Dias, Engilberge, Sylvain, Grahl, Anne, & 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
. (2021).
Abiko, Layara Akemi, Teixeira, Raphael Dias, Engilberge, Sylvain, Grahl, Anne, & 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
. (2021).
Abiko, Layara Akemi, Rogowski, Marco, Gautier, Antoine, Schertler, Gebhard, & Journal of Biomolecular NMR, 75(1), 25–38. https://doi.org/10.1007/s10858-020-00354-6
. (2021). Efficient production of a functional G protein-coupled receptor in E. coli for structural studies.
Abiko, Layara Akemi, Rogowski, Marco, Gautier, Antoine, Schertler, Gebhard, & Journal of Biomolecular NMR, 75(1), 25–38. https://doi.org/10.1007/s10858-020-00354-6
. (2021). Efficient production of a functional G protein-coupled receptor in E. coli for structural studies.
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, & Science Advances, 7(25), eabg8685. https://doi.org/10.1126/sciadv.abg8685
. (2021). Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist.
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, & Science Advances, 7(25), eabg8685. https://doi.org/10.1126/sciadv.abg8685
. (2021). Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist.
Franke, Bastian, Frigård, Tuomo, Journal of Chromatography A, 1618, 460846. https://doi.org/10.1016/j.chroma.2019.460846
, & Isogai, Shin. (2020). Versatile modules enable automated multi-column purifications on the ÄKTA pure chromatography system.
Franke, Bastian, Frigård, Tuomo, Journal of Chromatography A, 1618, 460846. https://doi.org/10.1016/j.chroma.2019.460846
, & Isogai, Shin. (2020). Versatile modules enable automated multi-column purifications on the ÄKTA pure chromatography system.
Grahl, Anne, Abiko, Layara Akemi, Isogai, Shin, Sharpe, Timothy, & Nature communications, 11(1), 2216. https://doi.org/10.1038/s41467-020-15864-y
. (2020). A high-resolution description of β1-adrenergic receptor functional dynamics and allosteric coupling from backbone NMR.
Grahl, Anne, Abiko, Layara Akemi, Isogai, Shin, Sharpe, Timothy, & Nature communications, 11(1), 2216. https://doi.org/10.1038/s41467-020-15864-y
. (2020). A high-resolution description of β1-adrenergic receptor functional dynamics and allosteric coupling from backbone NMR.
Hee, Chee-Seng, Habazettl, Judith, Schmutz, Christoph, Schirmer, Tilman, Jenal, Urs, & Proceedings of the National Academy of Sciences of the United States of America, 117(29), 17211–17220. https://doi.org/10.1073/pnas.2001232117
. (2020). Intercepting second-messenger signaling by rationally designed peptides sequestering c-di-GMP.
Hee, Chee-Seng, Habazettl, Judith, Schmutz, Christoph, Schirmer, Tilman, Jenal, Urs, & Proceedings of the National Academy of Sciences of the United States of America, 117(29), 17211–17220. https://doi.org/10.1073/pnas.2001232117
. (2020). Intercepting second-messenger signaling by rationally designed peptides sequestering c-di-GMP.
Abiko, Layara Akemi, Grahl, Anne, & Journal of the American Chemical Society, 141(42), 16663–16670. https://doi.org/10.1021/jacs.9b06042
. (2019). High Pressure Shifts the β1-Adrenergic Receptor to the Active Conformation in the Absence of G Protein.
Abiko, Layara Akemi, Grahl, Anne, & Journal of the American Chemical Society, 141(42), 16663–16670. https://doi.org/10.1021/jacs.9b06042
. (2019). High Pressure Shifts the β1-Adrenergic Receptor to the Active Conformation in the Absence of G Protein.
Opitz, Christian, Ahrné, Erik, Goldie, Kenneth N., Schmidt, Alexander, & Journal of Biological Chemistry, 294(7), 2279–2292. https://doi.org/10.1074/jbc.ra118.006914
. (2019). Deuterium induces a distinctive Escherichia coli proteome that correlates with the reduction in growth rate.
Opitz, Christian, Ahrné, Erik, Goldie, Kenneth N., Schmidt, Alexander, & Journal of Biological Chemistry, 294(7), 2279–2292. https://doi.org/10.1074/jbc.ra118.006914
. (2019). Deuterium induces a distinctive Escherichia coli proteome that correlates with the reduction in growth rate.
Opitz, Christian, Schade, Grit, Kaufmann, Silvan, Di Berardino, Marco, Ottiger, Marcel, & Applied microbiology and biotechnology, 103(20), 8619–8629. https://doi.org/10.1007/s00253-019-10046-3
. (2019). Rapid determination of general cell status, cell viability, and optimal harvest time in eukaryotic cell cultures by impedance flow cytometry.
Opitz, Christian, Schade, Grit, Kaufmann, Silvan, Di Berardino, Marco, Ottiger, Marcel, & Applied microbiology and biotechnology, 103(20), 8619–8629. https://doi.org/10.1007/s00253-019-10046-3
. (2019). Rapid determination of general cell status, cell viability, and optimal harvest time in eukaryotic cell cultures by impedance flow cytometry.
Franke, Bastian, Opitz, Christian, Isogai, Shin, Grahl, Anne, Delgado, Leonildo, Gossert, Alvar D., & Journal of biomolecular NMR, 71(3), 173–184. https://doi.org/10.1007/s10858-018-0172-7
. (2018). Production of isotope-labeled proteins in insect cells for NMR.
Franke, Bastian, Opitz, Christian, Isogai, Shin, Grahl, Anne, Delgado, Leonildo, Gossert, Alvar D., & Journal of biomolecular NMR, 71(3), 173–184. https://doi.org/10.1007/s10858-018-0172-7
. (2018). Production of isotope-labeled proteins in insect cells for NMR.
Sonti, Rajesh, Hertel-Hering, Ines, Lamontanara, Allan Joaquim, Hantschel, Oliver, & Journal of the American Chemical Society, 140(5), 1863–1869. https://doi.org/10.1021/jacs.7b12430
. (2018). ATP Site Ligands Determine the Assembly State of the Abelson Kinase Regulatory Core via the Activation Loop Conformation.
Sonti, Rajesh, Hertel-Hering, Ines, Lamontanara, Allan Joaquim, Hantschel, Oliver, & Journal of the American Chemical Society, 140(5), 1863–1869. https://doi.org/10.1021/jacs.7b12430
. (2018). ATP Site Ligands Determine the Assembly State of the Abelson Kinase Regulatory Core via the Activation Loop Conformation.
Nesper, Jutta, Hug, Isabelle, Kato, Setsu, Hee, Chee-Seng, Habazettl, Judith Maria, Manfredi, Pablo, eLife, 6, e28842. https://doi.org/10.7554/elife.28842
, Schirmer, Tilman, Emonet, Thierry, & Jenal, Urs. (2017). Cyclic di-GMP differentially tunes a bacterial flagellar motor through a novel class of CheY-like regulators.
Nesper, Jutta, Hug, Isabelle, Kato, Setsu, Hee, Chee-Seng, Habazettl, Judith Maria, Manfredi, Pablo, eLife, 6, e28842. https://doi.org/10.7554/elife.28842
, Schirmer, Tilman, Emonet, Thierry, & Jenal, Urs. (2017). Cyclic di-GMP differentially tunes a bacterial flagellar motor through a novel class of CheY-like regulators.
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Aznauryan, Mikayel, Delgado, Leonildo, Soranno, Andrea, Nettels, Daniel, Huang, Jie-Rong, Labhardt, Alexander M., Proceedings of the National Academy of Sciences, 113(37), E5389–98. https://doi.org/10.1073/pnas.1607193113
, & Schuler, Benjamin. (2016). Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.
Aznauryan, Mikayel, Delgado, Leonildo, Soranno, Andrea, Nettels, Daniel, Huang, Jie-Rong, Labhardt, Alexander M., Proceedings of the National Academy of Sciences, 113(37), E5389–98. https://doi.org/10.1073/pnas.1607193113
, & Schuler, Benjamin. (2016). Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.
Hoi Tik Alvin Leung, Bignucolo, Olivier, Aregger, Regula, Dames, Sonja A., Mazur, Adam, Berneche, Simon, & Journal of Chemical Theory and Computation, 12(1), 383–394. https://doi.org/10.1021/acs.jctc.5b00759
. (2016). A Rigorous and Efficient Method To Reweight Very Large Conformational Ensembles Using Average Experimental Data and To Determine Their Relative Information Content.
Hoi Tik Alvin Leung, Bignucolo, Olivier, Aregger, Regula, Dames, Sonja A., Mazur, Adam, Berneche, Simon, & Journal of Chemical Theory and Computation, 12(1), 383–394. https://doi.org/10.1021/acs.jctc.5b00759
. (2016). A Rigorous and Efficient Method To Reweight Very Large Conformational Ensembles Using Average Experimental Data and To Determine Their Relative Information Content.
Isogai, Shin, Deupi, Xavier, Opitz, Christian, Heydenreich, Franziska M, Tsai, Ching-Ju, Brueckner, Florian, Schertler, Gebhard F X, Veprintsev, Dmitry B, & Nature, 530(7589), 237–241. https://doi.org/10.1038/nature16577
. (2016). Backbone NMR reveals allosteric signal transduction networks in the β1-adrenergic receptor.
Isogai, Shin, Deupi, Xavier, Opitz, Christian, Heydenreich, Franziska M, Tsai, Ching-Ju, Brueckner, Florian, Schertler, Gebhard F X, Veprintsev, Dmitry B, & Nature, 530(7589), 237–241. https://doi.org/10.1038/nature16577
. (2016). Backbone NMR reveals allosteric signal transduction networks in the β1-adrenergic receptor.
Bignucolo, Olivier, Leung, Hoi Tik Alvin, Journal of the American Chemical Society, 137(13), 4300–4303. https://doi.org/10.1021/jacs.5b00660
, & Bernèche, Simon. (2015). Backbone hydration determines the folding signature of amino acid residues.
Bignucolo, Olivier, Leung, Hoi Tik Alvin, Journal of the American Chemical Society, 137(13), 4300–4303. https://doi.org/10.1021/jacs.5b00660
, & Bernèche, Simon. (2015). Backbone hydration determines the folding signature of amino acid residues.
Lamley, Jonathan M, Lougher, Matthew J, Sass, Hans Juergen, Rogowski, Marco, Physical Chemistry, Chemical Physics, 17(34), 21997–22008. https://doi.org/10.1039/c5cp03484a
, & Lewandowski, Józef R. (2015). Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.
Lamley, Jonathan M, Lougher, Matthew J, Sass, Hans Juergen, Rogowski, Marco, Physical Chemistry, Chemical Physics, 17(34), 21997–22008. https://doi.org/10.1039/c5cp03484a
, & Lewandowski, Józef R. (2015). Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.
Opitz, Christian, Isogai, Shin, & Journal of Biomolecular NMR, 62(3), 373–385. https://doi.org/10.1007/s10858-015-9954-3
. (2015). An economic approach to efficient isotope labeling in insect cells using homemade 15N-, 13C- and 2H-labeled yeast extracts.
Opitz, Christian, Isogai, Shin, & Journal of Biomolecular NMR, 62(3), 373–385. https://doi.org/10.1007/s10858-015-9954-3
. (2015). An economic approach to efficient isotope labeling in insect cells using homemade 15N-, 13C- and 2H-labeled yeast extracts.
Habazettl, Judith, Allan, Martin, Jensen, Pernille Rose, Sass, Hans-Jürgen, Thompson, Charles J, & Proceedings of the National Academy of Sciences of the United States of America, 111(51), E5498–507. https://doi.org/10.1073/pnas.1412070111
. (2014). Structural basis and dynamics of multidrug recognition in a minimal bacterial multidrug resistance system.
Habazettl, Judith, Allan, Martin, Jensen, Pernille Rose, Sass, Hans-Jürgen, Thompson, Charles J, & Proceedings of the National Academy of Sciences of the United States of America, 111(51), E5498–507. https://doi.org/10.1073/pnas.1412070111
. (2014). Structural basis and dynamics of multidrug recognition in a minimal bacterial multidrug resistance system.
Lamley, Jonathan M, Iuga, Dinu, Öster, Carl, Sass, Hans-Juergen, Rogowski, Marco, Oss, Andres, Past, Jaan, Reinhold, Andres, Journal of the American Chemical Society, 136(48), 16800–16806. https://doi.org/10.1021/ja5069992
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Lamley, Jonathan M, Iuga, Dinu, Öster, Carl, Sass, Hans-Juergen, Rogowski, Marco, Oss, Andres, Past, Jaan, Reinhold, Andres, Journal of the American Chemical Society, 136(48), 16800–16806. https://doi.org/10.1021/ja5069992
, Samoson, Ago, & Lewandowski, Józef R. (2014). Solid-state NMR of a protein in a precipitated complex with a full-length antibody.
Bignucolo, Olivier, Biophysical Journal, 104(2), 400a. https://doi.org/10.1016/j.bpj.2012.11.2231
, & Bernèche, Simon. (2013). Aromatic Amino Acids Confer Folding Propensities to a Nine-Residue Peptide [Journal-article].
Bignucolo, Olivier, Biophysical Journal, 104(2), 400a. https://doi.org/10.1016/j.bpj.2012.11.2231
, & Bernèche, Simon. (2013). Aromatic Amino Acids Confer Folding Propensities to a Nine-Residue Peptide [Journal-article].
Nielsen, Gerd, Jonker, Hendrik R A, Vajpai, Navratna, ChemBioChem, 14(14), 1799–1806. https://doi.org/10.1002/cbic.201300170
, & Schwalbe, Harald. (2013). Kinase in Motion : Insights into the Dynamic Nature of p38α by High-Pressure NMR Spectroscopic Studies.
Nielsen, Gerd, Jonker, Hendrik R A, Vajpai, Navratna, ChemBioChem, 14(14), 1799–1806. https://doi.org/10.1002/cbic.201300170
, & Schwalbe, Harald. (2013). Kinase in Motion : Insights into the Dynamic Nature of p38α by High-Pressure NMR Spectroscopic Studies.
Ramón-García, Santiago, Ng, Carol, Jensen, Pernille R, Dosanjh, Manisha, Burian, Jan, Morris, Rowan P, Folcher, Marc, Eltis, Lindsay D, Journal of Biological Chemistry, 288(48), 34514–34528. https://doi.org/10.1074/jbc.m113.516385
, Nguyen, Liem, & Thompson, Charles J. (2013). WhiB7, an Fe-S-dependent Transcription Factor That Activates Species-specific Repertoires of Drug Resistance Determinants in Actinobacteria.
Ramón-García, Santiago, Ng, Carol, Jensen, Pernille R, Dosanjh, Manisha, Burian, Jan, Morris, Rowan P, Folcher, Marc, Eltis, Lindsay D, Journal of Biological Chemistry, 288(48), 34514–34528. https://doi.org/10.1074/jbc.m113.516385
, Nguyen, Liem, & Thompson, Charles J. (2013). WhiB7, an Fe-S-dependent Transcription Factor That Activates Species-specific Repertoires of Drug Resistance Determinants in Actinobacteria.
Skora, Lukasz, Mestan, Jürgen, Fabbro, Doriano, Jahnke, Wolfgang, & Proceedings of the National Academy of Sciences of the United States of America, 110(47), E4437–45. https://doi.org/10.1073/pnas.1314712110
. (2013). NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.
Skora, Lukasz, Mestan, Jürgen, Fabbro, Doriano, Jahnke, Wolfgang, & Proceedings of the National Academy of Sciences of the United States of America, 110(47), E4437–45. https://doi.org/10.1073/pnas.1314712110
. (2013). NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.
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