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Crystal structures of FNIP/FGxxFN motif-containing leucine-rich repeat proteins
Huyton, T., Jaiswal, M., Taxer, W., Fischer, M., & Görlich, D. (2022). Crystal structures of FNIP/FGxxFN motif-containing leucine-rich repeat proteins. Scientific Reports, 12(1), 16430 (12 pp.). https://doi.org/10.1038/s41598-022-20758-8
Alternative catalytic residues in the active site of Esco acetyltransferases
Ajam, T., De, I., Petkau, N., Whelan, G., Pena, V., & Eichele, G. (2020). Alternative catalytic residues in the active site of Esco acetyltransferases. Scientific Reports, 10(1), 9828 (13 pp.). https://doi.org/10.1038/s41598-020-66795-z
A new perspective on the interaction between the Vg/VGLL1-3 proteins and the TEAD transcription factors
Mesrouze, Y., Aguilar, G., Bokhovchuk, F., Martin, T., Delaunay, C., Villard, F., … Chène, P. (2020). A new perspective on the interaction between the Vg/VGLL1-3 proteins and the TEAD transcription factors. Scientific Reports, 10, 17442 (12 pp.). https://doi.org/10.1038/s41598-020-74584-x
Conformational changes in apolipoprotein N-acyltransferase (Lnt)
Wiseman, B., & Högbom, M. (2020). Conformational changes in apolipoprotein N-acyltransferase (Lnt). Scientific Reports, 10(1), 639 (11 pp.). https://doi.org/10.1038/s41598-020-57419-7
Structural consequences of BMPR2 kinase domain mutations causing pulmonary arterial hypertension
Chaikuad, A., Thangaratnarajah, C., von Delft, F., & Bullock, A. N. (2019). Structural consequences of BMPR2 kinase domain mutations causing pulmonary arterial hypertension. Scientific Reports, 9(1), 18351 (10 pp.). https://doi.org/10.1038/s41598-019-54830-7
Rigid fusions of designed helical repeat binding proteins efficiently protect a binding surface from crystal contacts
Ernst, P., Honegger, A., van der Valk, F., Ewald, C., Mittl, P. R. E., & Plückthun, A. (2019). Rigid fusions of designed helical repeat binding proteins efficiently protect a binding surface from crystal contacts. Scientific Reports, 9(1), 16162 (10 pp.). https://doi.org/10.1038/s41598-019-52121-9
Structural determinants of specificity and regulation of activity in the allosteric loop network of human KLK8/neuropsin
Debela, M., Magdolen, V., Skala, W., Elsässer, B., Schneider, E. L., Craik, C. S., … Goettig, P. (2018). Structural determinants of specificity and regulation of activity in the allosteric loop network of human KLK8/neuropsin. Scientific Reports, 8(1), 10705 (15 pp.). https://doi.org/10.1038/s41598-018-29058-6
Acylated-acyl carrier protein stabilizes the <em>Pseudomonas aeruginosa</em> WaaP lipopolysaccharide heptose kinase
Kreamer, N. N. K., Chopra, R., Caughlan, R. E., Fabbro, D., Fang, E., Gee, P., … Uehara, T. (2018). Acylated-acyl carrier protein stabilizes the Pseudomonas aeruginosa WaaP lipopolysaccharide heptose kinase. Scientific Reports, 8(1), 14124 (12 pp.). https://doi.org/10.1038/s41598-018-32379-1
The human IL-17A/F heterodimer: a two-faced cytokine with unique receptor recognition properties
Goepfert, A., Lehmann, S., Wirth, E., & Rondeau, J. M. (2017). The human IL-17A/F heterodimer: a two-faced cytokine with unique receptor recognition properties. Scientific Reports, 7(1), 8906 (13 pp.). https://doi.org/10.1038/s41598-017-08360-9
Stepwise evolution improves identification of diverse peptides binding to a protein target
Lyamichev, V. I., Goodrich, L. E., Sullivan, E. H., Bannen, R. M., Benz, J., Albert, T. J., & Patel, J. J. (2017). Stepwise evolution improves identification of diverse peptides binding to a protein target. Scientific Reports, 7(1), 12116 (10 pp.). https://doi.org/10.1038/s41598-017-12440-1
Feasibility and physiological relevance of designing highly potent aminopeptidase-sparing leukotriene A4 hydrolase inhibitors
Numao, S., Hasler, F., Laguerre, C., Srinivas, H., Wack, N., Jäger, P., … Röhn, T. A. (2017). Feasibility and physiological relevance of designing highly potent aminopeptidase-sparing leukotriene A4 hydrolase inhibitors. Scientific Reports, 7(1), 13591 (19 pp.). https://doi.org/10.1038/s41598-017-13490-1
Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6
Russo, L., Giller, K., Pfitzner, E., Griesinger, C., & Becker, S. (2017). Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6. Scientific Reports, 7(1), 16845 (12 pp.). https://doi.org/10.1038/s41598-017-17088-5
Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection
Santiago, C., Mudgal, G., Reguera, J., Recacha, R., Albrecht, S., Enjuanes, L., & Casasnovas, J. M. (2017). Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection. Scientific Reports, 7, 46045 (14 pp.). https://doi.org/10.1038/srep46045
Structure of the acetophenone carboxylase core complex: prototype of a new class of ATP-dependent carboxylases/hydrolases
Weidenweber, S., Schühle, K., Demmer, U., Warkentin, E., Ermler, U., & Heider, J. (2017). Structure of the acetophenone carboxylase core complex: prototype of a new class of ATP-dependent carboxylases/hydrolases. Scientific Reports, 7, 39674 (10 pp.). https://doi.org/10.1038/srep39674
Structural and functional analysis of DDX41: a bispecific immune receptor for DNA and cyclic dinucleotide
Omura, H., Oikawa, D., Nakane, T., Kato, M., Ishii, R., Ishitani, R., … Nureki, O. (2016). Structural and functional analysis of DDX41: a bispecific immune receptor for DNA and cyclic dinucleotide. Scientific Reports, 6, 34756 (11 pp.). https://doi.org/10.1038/srep34756
Structure of neprilysin in complex with the active metabolite of sacubitril
Schiering, N., D'Arcy, A., Villard, F., Ramage, P., Logel, C., Cumin, F., … Mogi, M. (2016). Structure of neprilysin in complex with the active metabolite of sacubitril. Scientific Reports, 6, 27909 (5 pp.). https://doi.org/10.1038/srep27909
MtrA of the sodium ion pumping methyltransferase binds cobalamin in a unique mode
Wagner, T., Ermler, U., & Shima, S. (2016). MtrA of the sodium ion pumping methyltransferase binds cobalamin in a unique mode. Scientific Reports, 6, 28226 (10 pp.). https://doi.org/10.1038/srep28226
Small molecules antagonise the MIA-fibronectin interaction in malignant melanoma
Yip, K. T., Zhong, X. Y., Seibel, N., Pütz, S., Autzen, J., Gasper, R., … Stoll, R. (2016). Small molecules antagonise the MIA-fibronectin interaction in malignant melanoma. Scientific Reports, 6, 25119 (12 pp.). https://doi.org/10.1038/srep25119
Renaturing membrane proteins in the lipid cubic phase, a nanoporous membrane mimetic
Li, D., & Caffrey, M. (2014). Renaturing membrane proteins in the lipid cubic phase, a nanoporous membrane mimetic. Scientific Reports, 4, 5806 (5 pp.). https://doi.org/10.1038/srep05806