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Purification of the key enzyme complexes of the anammox pathway from DEMON sludge
Akram, M., Dietl, A., Müller, M., & Barends, T. R. M. (2021). Purification of the key enzyme complexes of the anammox pathway from DEMON sludge. Biopolymers. https://doi.org/10.1002/bip.23428
Biosynthesis of the tricyclic aromatic type II polyketide rishirilide: new potential third ring oxygenation after three cyclization steps
Alali, A., Zhang, L., Li, J., Zuo, C., Wassouf, D., Yan, X., … Bechthold, A. (2021). Biosynthesis of the tricyclic aromatic type II polyketide rishirilide: new potential third ring oxygenation after three cyclization steps. Molecular Biotechnology, 23, 502-514. https://doi.org/10.1007/s12033-021-00314-x
Crystal structure and subsequent ligand design of a nonriboside partial agonist bound to the adenosine A<sub>2A</sub> receptor
Amelia, T., van Veldhoven, J. P. D., Falsini, M., Liu, R., Heitman, L. H., van Westen, G. J. P., … IJzerman, A. P. (2021). Crystal structure and subsequent ligand design of a nonriboside partial agonist bound to the adenosine A2A receptor. Journal of Medicinal Chemistry, 64(7), 3827-3842. https://doi.org/10.1021/acs.jmedchem.0c01856
Ancestral reconstruction of mammalian FMO1 enables structural determination, revealing unique features that explain its catalytic properties
Bailleul, G., Nicoll, C. R., Mascotti, M. L., Mattevi, A., & Fraaije, M. W. (2021). Ancestral reconstruction of mammalian FMO1 enables structural determination, revealing unique features that explain its catalytic properties. Journal of Biological Chemistry, 296, 100221 (13 pp.). https://doi.org/10.1074/jbc.RA120.016297
Mechanisms of regulation and diverse activities of tau-tubulin kinase (TTBK) isoforms
Bao, C., Bajrami, B., Marcotte, D. J., Chodaparambil, J. V., Kerns, H. M., Henderson, J., … Dillon, G. M. (2021). Mechanisms of regulation and diverse activities of tau-tubulin kinase (TTBK) isoforms. Cellular and Molecular Neurobiology, 41, 669-685. https://doi.org/10.1007/s10571-020-00875-6
An antibiotic-resistance conferring mutation in a neisserial porin: Structure, ion flux, and ampicillin binding
Bartsch, A., Ives, C. M., Kattner, C., Pein, F., Diehn, M., Tanabe, M., … Llabrés, S. (2021). An antibiotic-resistance conferring mutation in a neisserial porin: Structure, ion flux, and ampicillin binding. Biochimica et Biophysica Acta: Biomembranes, 1863(6), 183601 (11 pp.). https://doi.org/10.1016/j.bbamem.2021.183601
The crystal structure of the Ca<sup>2+</sup>-ATPase 1 from <em>Listeria monocytogenes </em>reveals a pump primed for dephosphorylation
Basse Hansen, S., Dyla, M., Neumann, C., Quistgaard, E. M. H., Andersen, J. L., Kjaergaard, M., & Nissen, P. (2021). The crystal structure of the Ca2+-ATPase 1 from Listeria monocytogenes reveals a pump primed for dephosphorylation. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2021.167015
Structure-based design of high-affinity macrocyclic FKBP51 inhibitors
Bauder, M., Meyners, C., Purder, P. L., Merz, S., Sugiarto, W. O., Voll, A. M., … Hausch, F. (2021). Structure-based design of high-affinity macrocyclic FKBP51 inhibitors. Journal of Medicinal Chemistry, 64(6), 3320-3349. https://doi.org/10.1021/acs.jmedchem.0c02195
Design of buried charged networks in artificial proteins
Baumgart, M., Röpke, M., Mühlbauer, M. E., Asami, S., Mader, S. L., Fredriksson, K., … Kaila, V. R. I. (2021). Design of buried charged networks in artificial proteins. Nature Communications, 12, 1895 (9 pp.). https://doi.org/10.1038/s41467-021-21909-7
&lt;em&gt;In vitro&lt;/em&gt; reconstitution of a five-step pathway for bacterial ergothioneine catabolism
Beliaeva, M. A., Leisinger, F., & Seebeck, F. P. (2021). In vitro reconstitution of a five-step pathway for bacterial ergothioneine catabolism. ACS Chemical Biology, 16(2), 397-403. https://doi.org/10.1021/acschembio.0c00968
Impact of 3-deazapurine nucleobases on RNA properties
Bereiter, R., Himmelstoß, M., Renard, E., Mairhofer, E., Egger, M., Breuker, K., … Micura, R. (2021). Impact of 3-deazapurine nucleobases on RNA properties. Nucleic Acids Research, 49(8), 4281-4293. https://doi.org/10.1093/nar/gkab256
Structure-kinetic relationship reveals the mechanism of selectivity of FAK inhibitors over PYK2
Berger, B. T., Amaral, M., Kokh, D. B., Nunes-Alves, A., Musil, D., Heinrich, T., … Knapp, S. (2021). Structure-kinetic relationship reveals the mechanism of selectivity of FAK inhibitors over PYK2. Cell Chemical Biology, 28(5), 686-698. https://doi.org/10.1016/j.chembiol.2021.01.003
CYP154C5 regioselectivity in steroid hydroxylation explored by substrate modifications and protein engineering
Bracco, P., Wijma, H. J., Nicolai, B., Rodriguez Buitrago, J. A., Klünemann, T., Vila, A., … Schallmey, A. (2021). CYP154C5 regioselectivity in steroid hydroxylation explored by substrate modifications and protein engineering. ChemBioChem, 22(6), 1099-1110. https://doi.org/10.1002/cbic.202000735
Nonsteroidal ecdysone receptor agonists use a water channel for binding to the ecdysone receptor complex EcR/USP
Browning, C., McEwen, A. G., Mori, K., Yokoi, T., Moras, D., Nakagawa, Y., & Billas, I. M. L. (2021). Nonsteroidal ecdysone receptor agonists use a water channel for binding to the ecdysone receptor complex EcR/USP. Journal of Pesticide Science, 46(1), 88-100. https://doi.org/10.1584/jpestics.D20-095
The dynamic mechanism of 4E-BP1 recognition and phosphorylation by mTORC1
Böhm, R., Imseng, S., Jakob, R. P., Hall, M. N., Maier, T., & Hiller, S. (2021). The dynamic mechanism of 4E-BP1 recognition and phosphorylation by mTORC1. Molecular Cell. https://doi.org/10.1016/j.molcel.2021.03.031
Structural basis for targeting the folded P-loop conformation of c-MET
Collie, G. W., Michaelides, I. N., Embrey, K., Stubbs, C. J., Börjesson, U., Dale, I. L., … Storer, R. I. (2021). Structural basis for targeting the folded P-loop conformation of c-MET. ACS Medicinal Chemistry Letters, 12(1), 162-167. https://doi.org/10.1021/acsmedchemlett.0c00392
Mechanistic insights into the synergistic activation of the RXR–PXR heterodimer by endocrine disruptor mixtures
Delfosse, V., Huet, T., Harrus, D., Granell, M., Bourguet, M., Gardia-Parège, C., … Bourguet, W. (2021). Mechanistic insights into the synergistic activation of the RXR–PXR heterodimer by endocrine disruptor mixtures. Proceedings of the National Academy of Sciences of the United States of America PNAS, 118(1), e2020551118 (10 pp.). https://doi.org/10.1073/PNAS.2020551118
Complexes of the neurotensin receptor 1 with small-molecule ligands reveal structural determinants of full, partial, and inverse agonism
Deluigi, M., Klipp, A., Klenk, C., Merklinger, L., Eberle, S. A., Morstein, L., … Plückthun, A. (2021). Complexes of the neurotensin receptor 1 with small-molecule ligands reveal structural determinants of full, partial, and inverse agonism. Science Advances, 7(5), eabe5504 (15 pp.). https://doi.org/10.1126/sciadv.abe5504
Crystal structure of glutamate dehydrogenase 2, a positively selected novel human enzyme involved in brain biology and cancer pathophysiology
Dimovasili, C., Fadouloglou, V. E., Kefala, A., Providaki, M., Kotsifaki, D., Kanavouras, K., … Kokkinidis, M. (2021). Crystal structure of glutamate dehydrogenase 2, a positively selected novel human enzyme involved in brain biology and cancer pathophysiology. Journal of Neurochemistry. https://doi.org/10.1111/jnc.15296
Marriage of high throughput synthesis and high throughput protein crystallography
Doemling, A., Sutanto, F., Shaabani, S., Oerlemans, R., Deniz, E., Patil, P., … Groves, M. R. (2021). Marriage of high throughput synthesis and high throughput protein crystallography. Angewandte Chemie International Edition. https://doi.org/10.1002/anie.202105584
 

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