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Structure based design of bicyclic Peptide inhibitors of RbAp48
Hart, P. 't., Hommen, P., Noisier, A., Krzyzanowski, A., Schüler, D., Porfetye, A. T., … Waldmann, H. (2021). Structure based design of bicyclic Peptide inhibitors of RbAp48. Angewandte Chemie International Edition, 60(4), 1813-1820. https://doi.org/10.1002/anie.202009749
Structural insights into the interaction of botulinum neurotoxin a with its neuronal receptor SV2C
Li, X., Brunner, C., Wu, Y., Leka, O., Schneider, G., & Kammerer, R. A. (2020). Structural insights into the interaction of botulinum neurotoxin a with its neuronal receptor SV2C. Toxicon, 175, 36-43. https://doi.org/10.1016/j.toxicon.2019.11.010
Combined peptide and small-molecule approach toward nonacidic THIQ inhibitors of the KEAP1/NRF2 interaction
Ontoria, J. M., Biancofiore, I., Fezzardi, P., Ferrigno, F., Torrente, E., Colarusso, S., … Harper, S. (2020). Combined peptide and small-molecule approach toward nonacidic THIQ inhibitors of the KEAP1/NRF2 interaction. ACS Medicinal Chemistry Letters, 11(5), 740-746. https://doi.org/10.1021/acsmedchemlett.9b00594
Targeted synthesis of complex spiro[3<em>H</em>-indole-3,2'-pyrrolidin]-2(1<em>H</em>)-ones by intramolecular cyclization of azomethine ylides: highly potent MDM2-p53 inhibitors
Gollner, A., Weinstabl, H., Fuchs, J. E., Rudolph, D., Garavel, G., Hofbauer, K. S., … McConnell, D. B. (2019). Targeted synthesis of complex spiro[3H-indole-3,2'-pyrrolidin]-2(1H)-ones by intramolecular cyclization of azomethine ylides: highly potent MDM2-p53 inhibitors. ChemMedChem, 14(1), 88-93. https://doi.org/10.1002/cmdc.201800617
Inhibition of 14-3-3/Tau by hybrid small-molecule peptides operating via two different binding modes
Andrei, S. A., Meijer, F. A., Neves, J. F., Brunsveld, L., Landrieu, I., Ottmann, C., & Milroy, L. G. (2018). Inhibition of 14-3-3/Tau by hybrid small-molecule peptides operating via two different binding modes. ACS Chemical Neuroscience, 9(11), 2639-2654. https://doi.org/10.1021/acschemneuro.8b00118
Structures and interactions among globular proteins above the isoelectric point in the presence of divalent ions: a small angle neutron scattering and dynamic light scattering study
Kundu, S., Pandit, S., Abbas, S., Aswal, V. K., & Kohlbrecher, J. (2018). Structures and interactions among globular proteins above the isoelectric point in the presence of divalent ions: a small angle neutron scattering and dynamic light scattering study. Chemical Physics Letters, 693, 176-182. https://doi.org/10.1016/j.cplett.2018.01.022
Structures and interactions among lysozyme proteins below the isoelectric point in presence of divalent ions
Pandit, S., Kundu, S., Abbas, S., Aswal, V. K., & Kohlbrecher, J. (2018). Structures and interactions among lysozyme proteins below the isoelectric point in presence of divalent ions. Chemical Physics Letters, 711, 8-14. https://doi.org/10.1016/j.cplett.2018.09.021
Structural and biochemical analysis of a NOT1 MIF4G-like domain of the CCR4-NOT complex
Raisch, T., Sandmeir, F., Weichenrieder, O., Valkov, E., & Izaurralde, E. (2018). Structural and biochemical analysis of a NOT1 MIF4G-like domain of the CCR4-NOT complex. Journal of Structural Biology, 204(3), 388-395. https://doi.org/10.1016/j.jsb.2018.10.009
Proximity-Triggered Covalent Stabilization of Low-Affinity Protein Complexes In Vitro and In Vivo
Cigler, M., Müller, T. G., Horn-Ghetko, D., von Wrisberg, M. K., Fottner, M., Goody, R. S., … Lang, K. (2017). Proximity-Triggered Covalent Stabilization of Low-Affinity Protein Complexes In Vitro and In Vivo. Angewandte Chemie International Edition, 56(49), 15737-15741. https://doi.org/10.1002/anie.201706927
Effect of ethanol on structures and interactions among globular proteins
Kundu, S., Aswal, V. K., & Kohlbrecher, J. (2017). Effect of ethanol on structures and interactions among globular proteins. Chemical Physics Letters, 670, 71-76. https://doi.org/10.1016/j.cplett.2016.12.067
Effect of the acylation of TEAD4 on its interaction with co-activators YAP and TAZ
Mesrouze, Y., Meyerhofer, M., Bokhovchuk, F., Fontana, P., Zimmermann, C., Martin, T., … Chène, P. (2017). Effect of the acylation of TEAD4 on its interaction with co-activators YAP and TAZ. Protein Science, 26(12), 2399-2409. https://doi.org/10.1002/pro.3312
Small-Molecule Stabilization of the 14-3-3/Gab2 Protein-Protein Interaction (PPI) Interface
Bier, D., Bartel, M., Sies, K., Halbach, S., Higuchi, Y., Haranosono, Y., … Ottmann, C. (2016). Small-Molecule Stabilization of the 14-3-3/Gab2 Protein-Protein Interaction (PPI) Interface. ChemMedChem, 11(8), 911-918. https://doi.org/10.1002/cmdc.201500484
Synergistic effect of temperature, protein and salt concentration on structures and interactions among lysozyme proteins
Kundu, S., Aswal, V. K., & Kohlbrecher, J. (2016). Synergistic effect of temperature, protein and salt concentration on structures and interactions among lysozyme proteins. Chemical Physics Letters, 657, 90-94. https://doi.org/10.1016/j.cplett.2016.05.066
Stabilizer-Guided Inhibition of Protein-Protein Interactions
Milroy, L. G., Bartel, M., Henen, M. A., Leysen, S., Adriaans, J. M. C., Brunsveld, L., … Ottmann, C. (2015). Stabilizer-Guided Inhibition of Protein-Protein Interactions. Angewandte Chemie International Edition, 54(52), 15720-15724. https://doi.org/10.1002/anie.201507976
InVitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery
Fromm, S. A., Kamenz, J., Nöldeke, E. R., Neu, A., Zocher, G., & Sprangers, R. (2014). InVitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery. Angewandte Chemie International Edition, 53(28), 7354-7359. https://doi.org/10.1002/anie.201402885
Constrained peptides with target-adapted cross-links as inhibitors of a pathogenic protein-protein interaction
Glas, A., Bier, D., Hahne, G., Rademacher, C., Ottmann, C., & Grossmann, T. N. (2014). Constrained peptides with target-adapted cross-links as inhibitors of a pathogenic protein-protein interaction. Angewandte Chemie International Edition, 53(9), 2489-2493. https://doi.org/10.1002/anie.201310082
The structure of a transient complex of a nonribosomal peptide synthetase and a cytochromep450 monooxygenase
Haslinger, K., Brieke, C., Uhlmann, S., Sieverling, L., Süssmuth, R. D., & Cryle, M. J. (2014). The structure of a transient complex of a nonribosomal peptide synthetase and a cytochromep450 monooxygenase. Angewandte Chemie International Edition, 53(32), 8518-8522. https://doi.org/10.1002/anie.201404977
A designed conformational shift to control protein binding specificity
Michielssens, S., Peters, J. Henning, Ban, D., Pratihar, S., Seeliger, D., Sharma, M., … de Groot, B. L. (2014). A designed conformational shift to control protein binding specificity. Angewandte Chemie International Edition, 53(39), 10367-10371. https://doi.org/10.1002/anie.201403102
A natural-product switch for a dynamic protein interface
Scheepstra, M., Nieto, L., Hirsch, A. K. H., Fuchs, S., Leysen, S., Lam, C. V., … Brunsveld, L. (2014). A natural-product switch for a dynamic protein interface. Angewandte Chemie International Edition, 53(25), 6443-6448. https://doi.org/10.1002/anie.201403773
Using a fragment-based approach to target protein-protein interactions
Scott, D. E., Ehebauer, M. T., Pukala, T., Marsh, M., Blundell, T. L., Venkitaraman, A. R., … Hyvönen, M. (2013). Using a fragment-based approach to target protein-protein interactions. ChemBioChem, 14(3), 332-342. https://doi.org/10.1002/cbic.201200521