Publication list

Dong, J., Bai, Y., Wang, Q., Chen, Q., Li, X., Wang, Y., Ji, H., Meng, X., Pijning, T., Svensson, B., Dijkhuizen, L., Abou Hachem, M., & Jin, Z. (2024). Insights into the Structure–Function Relationship of GH70 GtfB α-Glucanotransferases from the Crystal Structure and Molecular Dynamic Simulation of a Newly Characterized Limosilactobacillus reuteri N1 GtfB Enzyme. Journal of Agricultural and Food Chemistry, 5391-5402. Article acs.jafc.4c00104. Advance online publication. https://doi.org/10.1021/acs.jafc.4c00104

Podoliak, E., Lamm, G. H. U., Marin, E., Schellbach, A. V., Fedotov, D. A., Stetsenko, A., Asido, M., Maliar, N., Bourenkov, G., Balandin, T., Baeken, C., Astashkin, R., Schneider, T. R., Bateman, A., Wachtveitl, J., Schapiro, I., Busskamp, V., Guskov, A., Gordeliy, V., ... Kovalev, K. (2024). A subgroup of light-driven sodium pumps with an additional Schiff base counterion. Nature Communications, 15, Article 3119. https://doi.org/10.1038/s41467-024-47469-0

Sauciuc, A., Whittaker, J., Tadema, M., Tych, K., Guskov, A., & Maglia, G. (2024). Unravelled proteins form blobs during translocation across nanopores. Manuscript submitted for publication. https://doi.org/10.1101/2024.01.23.576815

Pijning, T., Vujičić-Žagar, A., Laan, J.-M. V. D., Jong, R. M. D., Ramirez-Palacios, C., Vente, A., Edens, L., & Dijkstra, B. W. (2024). Structural and time-resolved mechanistic investigations of protein hydrolysis by the acidic proline-specific endoprotease from Aspergillus niger. Protein Science, 33(1), Article e4856. https://doi.org/10.1002/pro.4856

Hameleers, L., Pijning, T., Gray, B. B., Fauré, R., & Jurak, E. (2024). Novel β-galactosidase activity and first crystal structure of Glycoside Hydrolase family 154. New Biotechnology, 80, 1-11. Advance online publication. https://doi.org/10.1016/j.nbt.2023.12.011

Marin, E., Kovalev, K., Poelman, T., Veenstra, R., Borshchevskiy, V., & Guskov, A. (2024). Custom Design of a Humidifier Chamber for In Meso Crystallization. Crystal Growth & Design, 24(1), 325-330. Article 3c01034. https://doi.org/10.1021/acs.cgd.3c01034

Marin, E., Kovaleva, M., Kadukova, M., Mustafin, K., Khorn, P., Rogachev, A., Mishin, A., Guskov, A., & Borshchevskiy, V. (2024). Regression-Based Active Learning for Accessible Acceleration of Ultra-Large Library Docking. Journal of chemical information and modeling, 64(7), 2612–2623. Article 3c01661. https://doi.org/10.1021/acs.jcim.3c01661

Partipilo, M., Whittaker, J. J., Pontillo, N., Coenradij, J., Herrmann, A., Guskov, A., & Slotboom, D. J. (2023). Biochemical and structural insight into the chemical resistance and cofactor specificity of the formate dehydrogenase from Starkeya novella. The FEBS Journal, 290(17), 4238-4255. https://doi.org/10.1111/febs.16871

Wiedemann, C., Whittaker, J. J., Carrillo, V. H. P., Goretzki, B., Dajka, M., Tebbe, F., Harder, J.-M., Krajczy, P. R., Joseph, B., Hausch, F., Guskov, A., & Hellmich, U. A. (2023). Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding. International Journal of Biological Macromolecules, 252, Article 126366. https://doi.org/10.1016/j.ijbiomac.2023.126366

Colucci, E., Anshari, Z., Patiño-Ruiz, M., Nemchinova, M., Whittaker, J., Slotboom, D., & Guskov, A. (2023). Mutation in glutamate transporter homologue GltTk provides insights into pathologic mechanism of episodic ataxia 6. Nature Communications, 14, Article 1799. https://doi.org/10.1038/s41467-023-37503-y

Kolosova , O., Zgadzay, Y., Stetsenko, A., Atamas, A., Wu, C.-H., Sachs, M. S., Jenner, L., Guskov, A., & Yusupov, M. (2023). Structural characterization of cephaeline binding to the eukaryotic ribosome using Cryo-Electron Microscopy. Biopolymers and Cell, 39(4), 265-276. https://doi.org/10.7124/bc.000AA4

Atamas, A. A., Guskov, A. I., & Rogachev, A. V. (2023). Structural Study of the Candida auris Ribosome. Moscow University Biological Sciences Bulletin, 78(Suppl 1), S56-S58. https://doi.org/10.3103/S0096392523700220

Bikmullin, A. G., Fatkhullin, B., Stetsenko, A., Gabdulkhakov, A., Garaeva, N., Nurullina, L., Klochkova, E., Golubev, A., Khusainov, I., Trachtmann, N., Blokhin, D., Guskov, A., Validov, S., Usachev, K., & Yusupov, M. (2023). Yet Another Similarity between Mitochondrial and Bacterial Ribosomal Small Subunit Biogenesis Obtained by Structural Characterization of RbfA from S. aureus. International Journal of Molecular Sciences, 24(3), Article 24032118. https://doi.org/10.3390/ijms24032118

Meng, X., Li, X., Pijning, T., Wang, X., van Leeuwen, S. S., Dijkhuizen, L., Chen, G., & Liu, W. (2022). Characterization of the (Engineered) Branching Sucrase GtfZ-CD2 from Apilactobacillus kunkeei for Efficient Glucosylation of Benzenediol Compounds. Applied and environmental microbiology, 88(16), Article e0103122. https://doi.org/10.1128/aem.01031-22

Pijning, T., Te Poele, E. M., de Leeuw, T. C., Guskov, A., & Dijkhuizen, L. (2022). Crystal Structure of 4,6-α-Glucanotransferase GtfC-ΔC from Thermophilic Geobacillus 12AMOR1: Starch Transglycosylation in Non-Permuted GH70 Enzymes. Journal of Agricultural and Food Chemistry, 70(48), 15283–15295. Article 2c06394. https://doi.org/10.1021/acs.jafc.2c06394

Xu, W., Ni, D., Hou, X., Pijning, T., Guskov, A., Rao, Y., & Mu, W. (2022). Crystal Structure of Levansucrase from the Gram-Negative Bacterium Brenneria Provides Insights into Its Product Size Specificity. Journal of Agricultural and Food Chemistry, 70(16), 5095-5105. https://doi.org/10.1021/acs.jafc.2c01225

Zgadzay, Y., Kolosova , O., Stetsenko, A., Wu, C., Bruchlen, D., Usachev, K., Validov, S., Jenner, L., Rogachev, A., Yusupova, G., Sachs, M. S., Guskov, A., & Yusupov, M. (2022). E-site drug specificity of the human pathogen Candida albicans ribosome. Science Advances, 8(21), Article eabn1062. https://doi.org/10.1126/sciadv.abn1062

Li, X., Meng, X., de Leeuw, T. C., Te Poele, E. M., Pijning, T., Dijkhuizen, L., & Liu, W. (2023). Enzymatic glucosylation of polyphenols using glucansucrases and branching sucrases of glycoside hydrolase family 70. Critical Reviews in Food Science and Nutrition, 63(21), 5247–5267. Article 2016598. https://doi.org/10.1080/10408398.2021.2016598

Jiang, Y., Li, X., Pijning, T., Bai, Y., & Dijkhuizen, L. (2022). Mutations in Amino Acid Residues of Limosilactobacillus reuteri 121 GtfB 4,6-α-Glucanotransferase that Affect Reaction and Product Specificity. Journal of Agricultural and Food Chemistry, 70(6), 1952-1961. Article 1c07618. https://doi.org/10.1021/acs.jafc.1c07618

Ghauri, K., Pijning, T., Munawar, N., Ali, H., Ghauri, M. A., Anwar, M. A., & Wallis, R. (2021). Crystal structure of an inulosucrase from Halalkalicoccus jeotgali B3T-a halophilic archaeal strain. The FEBS Journal, 288(19), 5723-5736. https://doi.org/10.1111/febs.15843

Pijning, T., Gangoiti, J., Te Poele, E. M., Börner, T., & Dijkhuizen, L. (2021). Insights into Broad-Specificity Starch Modification from the Crystal Structure of Limosilactobacillus Reuteri NCC 2613 4,6-α-Glucanotransferase GtfB. Journal of Agricultural and Food Chemistry, 69(44), 13235-13245. Article 05657. https://doi.org/10.1021/acs.jafc.1c05657

Semchonok, D. A., Mondal, J., Cooper, C. J., Schlum, K., Li, M., Amin, M., Sorzano, C. O. S., Ramírez-Aportela, E., Kastritis, P. L., Boekema, E. J., Guskov, A., & Bruce, B. D. (2022). Cryo-EM structure of a tetrameric photosystem I from Chroococcidiopsis TS-821, a thermophilic, unicellular, non-heterocyst-forming cyanobacterium. Plant Communications, 3(1), Article 100248. https://doi.org/10.1016/j.xplc.2021.100248

Stehantsev, P., Stetsenko, A., Nemchinova, M., Aduri, N. G., Marrink, S., Gati, C., & Guskov, A. (2021). A structural view onto disease-linked mutations in the human neutral amino acid exchanger ASCT1. Computational and Structural Biotechnology Journal, 19, 5246-5254. https://doi.org/10.1016/j.csbj.2021.09.015

Nemchinova, M., Melcr, J., Wassenaar, T., Marrink, S., & Guskov, A. (2021). Asymmetric CorA Gating Mechanism as Observed by Molecular Dynamics Simulations. Journal of chemical information and modeling, 61(5), 2407-2417. https://doi.org/10.1021/acs.jcim.1c00261

Volkova, M., Atamas, A., Tsarenko, A., Rogachev, A., & Guskov, A. (2021). Cation Transporters of Candida albicans—New Targets to Fight Candidiasis? Biomolecules, 11(4), Article 584. https://doi.org/10.3390/biom11040584

Trinco, G., Arkhipova, V., Garaeva, A., Hutter, C. A. J., Seeger, M. A., Guskov, A., & Slotboom, D. (2021). Kinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk. Communications biology, 4, Article 751. https://doi.org/10.1038/s42003-021-02267-y

Stetsenko, A., Stehantsev, P., Dranenko, N. O., Gelfand, M. S., & Guskov, A. (2021). Structural and biochemical characterization of a novel ZntB (CmaX) transporter protein from Pseudomonas aeruginosa. International Journal of Biological Macromolecules, 184, 760-767. https://doi.org/10.1016/j.ijbiomac.2021.06.130

Plötz, E., Schuurman-Wolters, G., Zijlstra, N., Jager, A., Griffith, D., Guskov, A., Gouridis, G., Poolman, B., & Cordes, T. (2021). Structural and biophysical characterization of the tandem substrate-binding domains of the ABC importer GlnPQ. Open Biology, 11(4), Article 200406. https://doi.org/10.1098/rsob.200406

Arkhipova, V., Fu, H., Hoorens, M., Trinco, G., Lameijer, L., Marin, E., Feringa, B. L., Poelarends, G., Szymanski, W., Slotboom, D., & Guskov, A. (2021). Structural Aspects of Photopharmacology: Insight into the Binding of Photoswitchable and Photocaged Inhibitors to the Glutamate Transporter Homologue. Journal of the American Chemical Society, 143(3), 1513-1520. https://doi.org/10.1021/jacs.0c11336

Guo, C., Ni, Y., Biewenga, L., Pijning, T., Thunnissen, A.-M. W. H., & Poelarends, G. J. (2021). Using Mutability Landscapes To Guide Enzyme Thermostabilization. ChemBioChem, 22(1), 170-175. https://doi.org/10.1002/cbic.202000442

Rempel, S., Gati, C., Nijland, M., Thangaratnarajah, C., Karyolaimos, A., Gier, J.-W. L. D., Guskov, A., & Slotboom, D. (2020). A mycobacterial ABC transporter mediates the uptake of hydrophilic compounds. Nature, 580(7803), 409-412. https://doi.org/10.1038/s41586-020-2072-8

Stetsenko, A., & Guskov, A. (2020). Cation permeability in CorA family of proteins. Scientific Reports, 10(1), Article 840. https://doi.org/10.1038/s41598-020-57869-z

Skitchenko, R. K., Usoltsev, D., Uspenskaya, M., Kajava, A. V., & Guskov, A. (2020). Census of halide-binding sites in protein structures. Bioinformatics (Oxford, England), 36(10), 3064-3071. https://doi.org/10.1093/bioinformatics/btaa079

Setyawati, I., Stanek, W. K., Dosz-Majsnerowska, M., Ziel-Swier, L., Pardon, E., Steyaert, J., Guskov, A., & Slotboom, D. (2020). In vitro reconstitution of dynamically interacting integral membrane subunits of energy-coupling factor transporters. eLife, 9, 1-21. Article e64389. https://doi.org/10.7554/eLife.64389

Faustino, I., Abdizadeh, H., Souza, P. C. T., Jeucken, A., Stanek, W. K., Guskov, A., Slotboom, D., & Marrink, S. (2020). Membrane mediated toppling mechanism of the folate energy coupling factor transporter. Nature Communications, 11(1), Article 1763. https://doi.org/10.1038/s41467-020-15554-9

Stetsenko, A., Singh, R., Jähme, M., Guskov, A., & Slotboom, D. (2020). Structural and Functional Characterization of NadR from Lactococcus lactis. Molecules, 25(8), Article 1940. https://doi.org/10.3390/molecules25081940

Arkhipova, V., Guskov, A., & Slotboom, D. (2020). Structural ensemble of a glutamate transporter homologue in lipid nanodisc environment. Nature Communications, 11(1), Article 998. https://doi.org/10.1038/s41467-020-14834-8

Dubach, V. R. A., & Guskov, A. (2020). The Resolution in X-ray Crystallography and Single-Particle Cryogenic Electron Microscopy. Crystals, 10(7), 1-13. Article 580. https://doi.org/10.3390/cryst10070580

Biewenga, L., Thangavelu, S., Kunzendorf, A., Van Der Meer, J., Pijning, T., Tepper, P., Van Merkerk, R., Charnock, S. J., Thunnissen, A. W. H., & Poelarends, G. J. (2019). Enantioselective Synthesis of Pharmaceutically Active γ-Aminobutyric Acids Using a Tailor-Made Artificial Michaelase in One-Pot Cascade Reactions. ACS Catalysis, 9, 1503-1513. https://doi.org/10.1021/acscatal.8b04299

Zhang, X., Leemhuis, R., Janecek, S., Martinovicova, M., Pijning, T., & van der Maarel, M. (2019). Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity. Applied Microbiology and Biotechnology, 103(15), 6141–6151. https://doi.org/10.1007/s00253-019-09938-1

Leth, M. L., Ejby, M., Madland, E., Kitaoku, Y., Slotboom, D. J., Guskov, A., Aachmann, F. L., & Abou Hachem, M. (2020). Molecular insight into a new low affinity xylan binding module from the xylanolytic gut symbiont Roseburia intestinalis. The FEBS Journal, 287(10), 2105-2117. https://doi.org/10.1111/febs.15117

Garaeva, A. A., Guskov, A., Slotboom, D. J., & Paulino, C. (2019). A one-gate elevator mechanism for the human neutral amino acid transporter ASCT2. Nature Communications, 10, Article 3427. https://doi.org/10.1038/s41467-019-11363-x

Arkhipova, V. I., Trinco, G., Thijs, E., Jensen, S., Slotboom, D., & Guskov, A. (2019). Binding and transport of D-aspartate by the glutamate transporter homologue GltTk. eLife, 8, Article e45286. https://doi.org/10.7554/eLife.45286

Ejby, M., Guskov, A., Pichler, M. J., Zanten, G. C., Schoof, E., Saburi, W., Slotboom, D. J., & Abou Hachem, M. (2019). Two binding proteins of the ABC transporter that confers growth of Bifidobacterium animalis subsp. lactis ATCC27673 on β-mannan possess distinct manno-oligosaccharide binding profiles. Molecular Microbiology, 112(1), 114-130. Article 14257. https://doi.org/10.1111/mmi.14257

Zhang, F., Liu, H., Zhang, T., Pijning, T., Yu, L., Zhang, W., Liu, W., & Meng, X. (2018). Biochemical and genetic characterization of fungal proline hydroxylase in echinocandin biosynthesis. Applied Microbiology and Biotechnology, 102(18), 7877-7890. https://doi.org/10.1007/s00253-018-9179-y

Meng, X., Gangoiti, J., Wang, X., Grijpstra, P., van Leeuwen, S. S., Pijning, T., & Dijkhuizen, L. (2018). Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity. Applied Microbiology and Biotechnology, 102(18), 7935-7950. https://doi.org/10.1007/s00253-018-9236-6

Meng, X., Gangoiti, J., de Kok, N., van Leeuwen, S. S., Pijning, T., & Dijkhuizen, L. (2018). Biochemical characterization of two GH70 family 4,6-α-glucanotransferases with distinct product specificity from Lactobacillus aviarius subsp. aviarius DSM 20655. Food Chemistry, 253, 236-246. Article j.foodchem.2018.01.154. https://doi.org/10.1016/j.foodchem.2018.01.154

Pham, H., Pijning, T., Dijkhuizen, L., & van Leeuwen, S. S. (2018). Mutational Analysis of the Role of the Glucansucrase Gtf180-Delta N Active Site Residues in Product and Linkage Specificity with Lactose as Acceptor Substrate. Journal of Agricultural and Food Chemistry, 66(47), 12544-12554. Article acs.jafc.8b04486. https://doi.org/10.1021/acs.jafc.8b04486

Garaeva, A., Oostergetel, G., Gati, C., Guskov, A., Batista Paulino, C., & Slotboom, D. (2018). Cryo-EM structure of the human neutral amino acid transporter ASCT2. Nature Structural & Molecular Biology, 25, 515-521. https://doi.org/10.1038/s41594-018-0076-y

Rempel, S., Colucci, E., Gier, J.-W. D., Guskov, A., & Slotboom, D. (2018). Cysteine-mediated decyanation of vitamin B12 by the predicted membrane transporter BtuM. Nature Communications, 9(1), Article 3038. https://doi.org/10.1038/s41467-018-05441-9

Luís da Silva Santos Guimarães, J. A., Rempel, S., Mous, S. T. M., Tambascia Pereira, C., ter Beek, J., Gier, J.-W. D., Guskov, A., & Slotboom, D. (2018). Functional and structural characterization of an ECF-type ABC transporter for vitamin B12. eLife, 7, Article e35828. https://doi.org/10.7554/eLife.35828

Gangoiti, J., Pijning, T., & Dijkhuizen, L. (2018). Biotechnological potential of novel glycoside hydrolase family 70 enzymes synthesizing α-glucans from starch and sucrose. Biotechnology Advances, 36, 196-207. https://doi.org/10.1016/j.biotechadv.2017.11.001

Gangoiti Muñecas, J., van Leeuwen, S. S., Gerwig, G. J., Duboux, S., Vafiadi, C., Pijning, T., & Dijkhuizen, L. (2017). 4,3-α-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H. Scientific Reports, 7, 1-15. Article 39761. https://doi.org/10.1038/srep39761

Franken, L., Oostergetel, G., Pijning, T., Puri, P., Arkhipova, V. I., Boekema, E., Poolman, B., & Guskov, A. (2017). A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy. Nature Communications, 8, Article 722. https://doi.org/10.1038/s41467-017-00718-x

Sarian, F. D., Janeček, Š., Pijning, T., Ihsanawati, Nurachman, Z., Radjasa, O. K., Dijkhuizen, L., Natalia, D., & van der Maarel, M. J. E. C. (2017). A new group of glycoside hydrolase family 13 α-amylases with an aberrant catalytic triad. Scientific Reports, 7, Article 44230. https://doi.org/10.1038/srep44230

Yin, H., Pijning, T., Meng, X., Dijkhuizen, L., & van Leeuwen, S. S. (2017). Biochemical characterization of the functional roles of residues in the active site of the β-galactosidase from Bacillus circulans ATCC 31382. Biochemistry, 56(24), 3109-3118. https://doi.org/10.1021/acs.biochem.7b00207

Meng, X., Pijning, T., Tietema, M., Dobruchowska, J. M., Yin, H., Gerwig, G. J., Kralj, S., & Dijkhuizen, L. (2017). Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition. Food Chemistry, 217, 81-90. https://doi.org/10.1016/j.foodchem.2016.08.087

Yin, H., Pijning, T., Meng, X., Dijkhuizen, L., & van Leeuwen, S. S. (2017). Engineering of the Bacillus circulans β-galactosidase product specificity. Biochemistry, 56(5), 704-711. https://doi.org/10.1021/acs.biochem.7b00032

Gangoiti, J., van Leeuwen, S. S., Meng, X., Duboux, S., Vafiadi, C., Pijning, T., & Dijkhuizen, L. (2017). Mining novel starch-converting Glycoside Hydrolase 70 enzymes from the Nestlé Culture Collection genome database: The Lactobacillus reuteri NCC 2613 GtfB. Scientific Reports, 7(1), Article 9947. https://doi.org/10.1038/s41598-017-07190-z

Arkhipova, V. I., Guskov, A., & Slotboom, D. (2017). Analysis of the quality of crystallographic data and the limitations of structural models. The Journal of General Physiology, 149(12). https://doi.org/10.1085/jgp.201711852

Stetsenko, A., & Guskov, A. (2017). An Overview of the Top Ten Detergents Used for Membrane Protein Crystallization. Crystals, 7(7), 1-16. Article 197. https://doi.org/10.3390/cryst7070197

Gati, C., Stetsenko, A., Slotboom, D., Scheres, S., & Guskov, A. (2017). The structural basis of proton driven zinc transport by ZntB. Nature Communications, 8, Article 1313. https://doi.org/10.1038/s41467-017-01483-7

Bai, Y., Gangoiti , J., Dijkstra, B. W., Dijkhuizen, L., & Pijning, T. (2017). Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria. Structure, 25(2), 231-242. https://doi.org/10.1016/j.str.2016.11.023

Bai, Y., Böger, M., van der Kaaij, R. M., Woortman, A. J. J., Pijning, T., van Leeuwen, S. S., Lammerts van Bueren, A., & Dijkhuizen, L. (2016). Lactobacillus reuteri strains convert starch and maltodextrins into homo-exopolysaccharides using an extracellular and cell-associated 4,6-α-glucanotransferase. Journal of Agricultural and Food Chemistry, 64(14), 2941-2952. https://doi.org/10.1021/acs.jafc.6b00714

Meng, X., Pijning, T., Dobruchowska, J. M., Yin, H., Gerwig, G. J., & Dijkhuizen, L. (2016). Structural determinants of alternating (α1 → 4) and (α1 → 6) linkage specificity in reuteransucrase of Lactobacillus reuteri. Scientific Reports, 6, Article 35261. https://doi.org/10.1038/srep35261

Meng, X., Gangoiti, J., Bai, Y., Pijning, T., Van Leeuwen, S. S., & Dijkhuizen, L. (2016). Structure-function relationships of family GH70 glucansucrase and 4,6-α-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes. Cellular and molecular life sciences, 73(14), 2681-2706. https://doi.org/10.1007/s00018-016-2245-7

Guskov, A., Jensen, S., Faustino, I., Marrink, S. J., & Slotboom, D. J. (2016). Coupled binding mechanism of three sodium ions and aspartate in the glutamate transporter homologue GltTk. Nature Communications, 7, 1-6. Article 13420. https://doi.org/10.1038/ncomms13420

Jähme, M., Guskov, A., & Slotboom, D. J. (2016). Pnu Transporters: Ain't They SWEET? Trends in Biochemical Sciences, 41(2), 117-118. https://doi.org/10.1016/j.tibs.2015.11.013

Swier, L. J. Y. M., Guskov, A., & Slotboom, D. J. (2016). Structural insight in the toppling mechanism of an energy-coupling factor transporter. Nature Communications, 7, 1-11. Article 11072. https://doi.org/10.1038/ncomms11072

Meng, X., Dobruchowska, J. M., Pijning, T., Gerwig, G. J., & Dijkhuizen, L. (2016). Synthesis of New Hyper-Branched α-Glucans from Sucrose by Lactobacillus reuteri 180 Glucansucrase Mutants. Journal of Agricultural and Food Chemistry, 64(2), 433-442. https://doi.org/10.1021/acs.jafc.5b05161

Bai, Y., van der Kaaij, R. M., Leemhuis, H., Pijning, T., van Leeuwen, S. S., Jin, Z., & Dijkhuizen, L. (2015). Biochemical characterization of Lactobacillus reuteri Glycoside Hydrolase family 70 GTFB type of 4,6-α-Glucanotransferase enzymes that synthesize soluble dietary starch fibers. Applied and environmental microbiology, 81(20), 7223-7232. https://doi.org/10.1128/AEM.01860-15

Meng, X., Pijning, T., Dobruchowska, J. M., Gerwig, G. J., & Dijkhuizen, L. (2015). Characterization of the functional roles of amino acid residues in acceptor binding subsite +1 in the active site of the glucansucrase GTF180 enzyme of Lactobacillus reuteri 180. The Journal of Biological Chemistry, 290(50), 30131-30141. https://doi.org/10.1074/jbc.M115.687558

Gangoiti, J., Pijning, T., & Dijkhuizen, L. (2015). The Exiguobacterium sibiricum 255-15 GtfC enzyme representing a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes. Applied and environmental microbiology, 82(2), 756-766. Article AEM.03420-15. https://doi.org/10.1128/AEM.03420-15

Meng, X., Dobruchowska, J. M., Pijning, T., Gerwig, G. J., Kamerling, J. P., & Dijkhuizen, L. (2015). Truncation of domain V of the multidomain glucansucrase GTF180 of Lactobacillus reuteri 180 heavily impairs its polysaccharide-synthesizing ability. Applied Microbiology and Biotechnology, 99(14), 5885-5894. https://doi.org/10.1007/s00253-014-6361-8

Swier, L. J. Y. M., Monjas, L., Guskov, A., de Voogd, A. R., Erkens, G. B., Slotboom, D. J., & Hirsch, A. K. H. (2015). Structure-Based Design of Potent Small-Molecule Binders to the S-Component of the ECF Transporter for Thiamine. ChemBioChem, 16(5), 819-826. https://doi.org/10.1002/cbic.201402673

Jähme, M., Guskov, A., & Slotboom, D. (2015). The twisted relation between Pnu and SWEET transporters. Trends in Biochemical Sciences, 40(4), 183-188. https://doi.org/10.1016/j.tibs.2015.02.002

Pijning, T., Vujicic - Zagar, A., Kralj, S., Dijkhuizen, L., & Dijkstra, B. W. (2014). Flexibility of truncated and full-length glucansucrase GTF180 enzymes from Lactobacillus reuteri 180. Febs Journal, 281(9), 2159-2171. https://doi.org/10.1111/febs.12769

Balci, H., Ozturk, M. T., Pijning, T., Ozturk, S. I., & Gumusel, F. (2014). Improved activity and pH stability of E-coli ATCC 11105 penicillin acylase by error-prone PCR. Applied Microbiology and Biotechnology, 98(10), 4467-4477. https://doi.org/10.1007/s00253-013-5476-7

Meng, X., Dobruchowska, J. M., Pijning, T., Lopez-Bautista, C., Kamerling, J. P., & Dijkhuizen, L. (2014). Residue Leu(940) Has a Crucial Role in the Linkage and Reaction Specificity of the Glucansucrase GTF180 of the Probiotic Bacterium Lactobacillus reuteri 180. The Journal of Biological Chemistry, 289(47), 32773-32782. https://doi.org/10.1074/jbc.M114.602524

Jähme, M., Guskov, A., & Slotboom, D. J. (2014). Crystal structure of the vitamin B3 transporter PnuC, a full-length SWEET homolog. Nature Structural & Molecular Biology, 21(11), 1013-1015. https://doi.org/10.1038/nsmb.2909

ter Beek, J., Guskov, A., & Slotboom, D. J. (2014). Structural diversity of ABC transporters. Journal of general physiology, 143(4), 419-435. https://doi.org/10.1085/jgp.201411164

Leemhuis, H., Dijkman, W. P., Dobruchowska, J. M., Pijning, T., Grijpstra, P., Kralj, S., Kamerling, J. P., Dijkhuizen, L., & Gerwig, G. J. (2013). 4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily. Applied Microbiology and Biotechnology, 97(1), 181-193. https://doi.org/10.1007/s00253-012-3943-1

Leemhuis, H., Pijning, T., Dobruchowska, J. M., van Leeuwen, S. S., Kralj, S., Dijkstra, B. W., & Dijkhuizen, L. (2013). Glucansucrases: Three-dimensional structures, reactions, mechanism, alpha-glucan analysis and their implications in biotechnology and food applications. Journal of Biotechnology, 163(2), 250-272. https://doi.org/10.1016/j.jbiotec.2012.06.037

Akbulut, N., Ozturk, M. T., Pijning, T., Ozturk, S. I., & Gumusel, F. (2013). Improved activity and thermostability of Bacillus pumilus lipase by directed evolution. Journal of Biotechnology, 164(1), 123-129. https://doi.org/10.1016/j.jbiotec.2012.12.016

How, J., Zhang, A., Phillips, M., Reynaud, A., Lu, S. Y., Pan, L. X., Ho, H. T., Yau, Y. H., Guskov, A., Pervushin, K., Shochat, S. G., & Eshaghi, S. (2013). Comprehensive analysis and identification of the human STIM1 domains for structural and functional studies. PLoS ONE, 8(1), Article e53979. https://doi.org/10.1371/journal.pone.0053979

Jensen, S., Guskov, A., Rempel, S., Hänelt, I., & Slotboom, D. J. (2013). Crystal structure of a substrate-free aspartate transporter. Nature Structural & Molecular Biology, 20(10), 1224-1226. https://doi.org/10.1038/nsmb.2663

Nordin, N., Guskov, A., Phua, T., Sahaf, N., Xia, Y., Lu, S., Eshaghi, H., & Eshaghi, S. (2013). Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport. Biochemical Journal, 451(3), 365-374. https://doi.org/10.1042/BJ20121745

Fulyani, F., Schuurman-Wolters, G. K., Vujicic - Zagar, A., Guskov, A., Slotboom, D.-J., & Poolman, B. (2013). Functional Diversity of Tandem Substrate-Binding Domains in ABC Transporters from Pathogenic Bacteria. Structure, 21(10), 1879-1888. https://doi.org/10.1016/j.str.2013.07.020

Kesters, D., Thompson, A. J., Brams, M., van Elk, R., Spurny, R., Geitmann, M., Villalgordo, J. M., Guskov, A., Danielson, U. H., Lummis, S. C. R., Smit, A. B., & Ulens, C. (2013). Structural basis of ligand recognition in 5-HT3 receptors. Embo Reports, 14(1), 49-56. https://doi.org/10.1038/embor.2012.189

Kemelbekov, U., Saipov, A., Abdildanova, A., Ospanov, I., Luo, Y., Guskov, A., Saenger, W., Imachova, S., Nasyrova, S., & Pichkhadze, G. (2013). Structure and pharmacological studies of the anaesthetic 1-(3-n-butoxypropyl)-4-benzoyloxypiperidin hydrochloride and its complex with beta-cyclodextrin in solution. NMR and IR-spectroscopy data. Journal of inclusion phenomena and macrocyclic chemistry, 77(1-4), 249-257. https://doi.org/10.1007/s10847-012-0239-0

Augustyniak, W., Brzezinska, A. A., Pijning, T., Wienk, H., Boelens, R., Dijkstra, B. W., & Reetz, M. T. (2012). Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: Factors contributing to increased activity retention. Protein Science, 21(4), 487-497. https://doi.org/10.1002/pro.2031

Brison, Y., Pijning, T., Malbert, Y., Fabre, E., Mourey, L., Morel, S., Potocki-Veronese, G., Monsan, P., Tranier, S., Remaud-Simeon, M., & Dijkstra, B. W. (2012). Functional and Structural Characterization of alpha-(1 -> 2) Branching Sucrase Derived from DSR-E Glucansucrase. The Journal of Biological Chemistry, 287(11), 7915-7924. https://doi.org/10.1074/jbc.M111.305078

Leemhuis, H., Pijning, T., Dobruchowska, J. M., Dijkstra, B. W., & Dijkhuizen, L. (2012). Glycosidic bond specificity of glucansucrases: on the role of acceptor substrate binding residues. Biocatalysis and Biotransformation, 30(3), 366-376. https://doi.org/10.3109/10242422.2012.676301

Pijning, T., Vujicic-Zagar, A., Kralj, S., Dijkhuizen, L., & Dijkstra, B. W. (2012). Structure of the alpha-1,6/alpha-1,4-specific glucansucrase GTFA from Lactobacillus reuteri 121. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68(12), 1448-1454. https://doi.org/10.1107/S1744309112044168

Anwar, M. A., Leemhuis, H., Pijning, T., Kralj, S., Dijkstra, B. W., & Dijkhuizen, L. (2012). The role of conserved inulosucrase residues in the reaction and product specificity of Lactobacillus reuteri inulosucrase. Febs Journal, 279(19), 3612-3621. https://doi.org/10.1111/j.1742-4658.2012.08721.x

Guskov, A., Nordin, N., Reynaud, A., Engman, H., Lundbäck, A.-K., Jong, A. J. O., Cornvik, T., Phua, T., & Eshaghi, S. (2012). Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA. Proceedings of the National Academy of Sciences of the United States of America, 109(45), 18459-18464. https://doi.org/10.1073/pnas.1210076109

Guskov, A., & Eshaghi, S. (2012). The mechanisms of Mg2+ and Co2+ transport by the CorA family of divalent cation transporters. Current topics in membranes, 69, 393-414. https://doi.org/10.1016/B978-0-12-394390-3.00014-8

Pijning, T., Anwar, M. A., Boger, M., Dobruchowska, J. M., Leemhuis, H., Kralj, S., Dijkhuizen, L., & Dijkstra, B. W. (2011). Crystal Structure of Inulosucrase from Lactobacillus: Insights into the Substrate Specificity and Product Specificity of GH68 Fructansucrases. Journal of Molecular Biology, 412(1), 80-93. https://doi.org/10.1016/j.jmb.2011.07.031

Palomo, M., Pijning, T., Booiman, T., Dobruchowska, J. M., Vlist, J. V. D., Kralj, S., Planas, A., Loos, K., Kamerling, J. P., Dijkstra, B. W., Maarel, M. J. E. C. V. D., Dijkhuizen, L., & Leemhuis, H. (2011). Thermus thermophilus Glycoside Hydrolase Family 57 Branching Enzyme: Crystal Structure, Mechanism of Action, and Products Formed. The Journal of Biological Chemistry, 286(5), 3520-3530. https://doi.org/10.1074/jbc.M110.179515

Brams, M., Gay, E. A., Sáez, J. C., Guskov, A., van Elk, R., van der Schors, R. C., Peigneur, S., Tytgat, J., Strelkov, S. V., Smit, A. B., Yakel, J. L., & Ulens, C. (2011). Crystal structures of a cysteine-modified mutant in loop D of acetylcholine-binding protein. The Journal of Biological Chemistry, 286(6), 4420-4428. https://doi.org/10.1074/jbc.M110.188730

Kern, J., & Guskov, A. (2011). Lipids in photosystem II: Multifunctional cofactors. Journal of Photochemistry and Photobiology B: Biology, 104(1-2), 19-34. https://doi.org/10.1016/j.jphotobiol.2011.02.025

Broser, M., Glöckner, C., Gabdulkhakov, A., Guskov, A., Buchta, J., Kern, J., Müh, F., Dau, H., Saenger, W., & Zouni, A. (2011). Structural basis of cyanobacterial photosystem II Inhibition by the herbicide terbutryn. The Journal of Biological Chemistry, 286(18), 15964-15972. https://doi.org/10.1074/jbc.M110.215970

Vujičić-Žagar, A., Pijning, T., Kralj, S., López, C. A., Eeuwema, W., Dijkhuizen, L., & Dijkstra, B. W. (2010). Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes. Proceedings of the National Academy of Sciences of the United States of America, 107(50), 21406-21411. https://doi.org/10.1073/pnas.1007531107

Kale, A., Pijning, T., Sonke, T., Dijkstra, B. W., & Thunnissen, A.-M. W. H. (2010). Crystal Structure of the Leucine Aminopeptidase from Pseudomonas putida Reveals the Molecular Basis for its Enantioselectivity and Broad Substrate Specificity. Journal of Molecular Biology, 398(5), 703-714. https://doi.org/10.1016/j.jmb.2010.03.042

Broser, M., Gabdulkhakov, A., Kern, J., Guskov, A., Müh, F., Saenger, W., & Zouni, A. (2010). Crystal structure of monomeric photosystem II from Thermosynechococcus elongatus at 3.6-a resolution. The Journal of Biological Chemistry, 285(34), 26255-26262. https://doi.org/10.1074/jbc.M110.127589

Kemelbekov, U. S., Hagenbach, A., Lentz, D., Imachova, S. O., Pichkhadze, G. M., Rustembekov, Z. I., Beketov, K. M., Praliev, K. D., Gabdulkhakov, A., Guskov, A., & Saenger, W. (2010). Pharmacology and structures of the free base of the anaesthetic kazcaine and its complex with beta-cyclodextrin. Journal of inclusion phenomena and macrocyclic chemistry, 68(3-4), 323-330. https://doi.org/10.1007/s10847-010-9791-7

Guskov, A., Gabdulkhakov, A., Broser, M., Glöckner, C., Hellmich, J., Kern, J., Frank, J., Müh, F., Saenger, W., & Zouni, A. (2010). Recent progress in the crystallographic studies of photosystem II. Chemphyschem, 11(6), 1160-1171. https://doi.org/10.1002/cphc.200900901

Pijning, T., van Pouderoyen, G., Kluskens, L., van der Oost, J., & Dijkstra, B. W. (2009). The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer. FEBS Letters, 583(22), 3665-3670. https://doi.org/10.1016/j.febslet.2009.10.047

Guskov, A., Kern, J., Gabdulkhakov, A., Broser, M., Zouni, A., & Saenger, W. (2009). Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride. Nature Structural & Molecular Biology, 16(3), 334-342. https://doi.org/10.1038/nsmb.1559

Gabdulkhakov, A., Guskov, A., Broser, M., Kern, J., Müh, F., Saenger, W., & Zouni, A. (2009). Probing the accessibility of the Mn(4)Ca cluster in photosystem II: Channels calculation, noble gas derivatization, and cocrystallization with DMSO. Structure, 17(9), 1223-1234. https://doi.org/10.1016/j.str.2009.07.010

Boersma, Y. L., Droge, M. J., van der Sloot, A. M., Pijning, T., Cool, R. H., Dijkstra, B. W., Quax, W. J., & Dröge, M. J. (2008). A novel genetic selection system for improved enantioselectivity of Bacillus subtilis lipase A. ChemBioChem, 9(7), 1110-1115. https://doi.org/10.1002/cbic.200700754

Pijning, T., Vujicic-Zagar, A., Kralj, S., Eeuwema, W., Dijkhuizen, L., & Dijkstra, B. W. (2008). Biochemical and crystallographic characterization of a glucansucrase from Lactobacillus reuteri 180. Biocatalysis and Biotransformation, 26(1-2), 12-17. https://doi.org/10.1080/10242420701789163

Boersma, Y. L., Pijning, T., Bosma, M., van der Sloot, A. M., da Silva Godinho, L., Dröge, M., Winter, R. T., van Pouderoyen, G., Dijkstra, B. W., & Quax, W. (2008). Loop grafting of Bacillus subtilis lipase A: Inversion of enantioselectivity. Chemistry & Biology, 15(8), 782-789. https://doi.org/10.1016/j.chembiol.2008.06.009

Alagaratnam, S., van Pouderoyen, G., Pijning, T., Dijkstra, B. W., Cavazzini, D., Rossi, G. L., Van Dongen, W. M. A. M., Van Mierlo, C. P. M., Canters, G. W., & Van Berkel, WJH. (2005). A crystallographic study of Cys69Ala flavodoxin II from Azotobacter vinelandii: Structural determinants of redox potential: Structural determinants of redox potential. Protein Science, 14(9), 2284 - 2295. https://doi.org/10.1110/ps.051582605

Fusetti, F., Pijning, T., Kalk, KH., Bos, E., Dijkstra, BW., & Dijkstra, B. W. (2003). Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39. The Journal of Biological Chemistry, 278(39), 37753-37760. https://doi.org/10.1074/jbc.M303137200

Fusetti, F., Schröter, K. H., Steiner, R. A., Noort, P. I. V., Pijning, T., Rozeboom, H. J., Kalk, K. H., Egmond, M. R., & Dijkstra, B. W. (2002). Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus. Structure, 10(2), 259-268. https://doi.org/10.1016/S0969-2126(02)00704-9

van Montfort, R., Pijning, T., Kalk, K. H., Hangyi, I., Kouwijzer, M., Robillard, G. T., & Dijkstra, B. W. (1998). The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site. Structure, 6(3), 377 - 388. https://doi.org/10.1016/S0969-2126(98)00039-2

Bordo, D., Monfort, R. L. M. V., Pijning, T., Kalk, K. H., Reizer, J., Saier Jr., M. H., & Dijkstra, B. W. (1998). The three-dimensional structure of the nitrogen regulatory protein IIA(Ntr) from Escherichia coli. Journal of Molecular Biology, 279(1), 245-255. https://doi.org/10.1006/jmbi.1998.1753

van Montfort, R. L. M., Pijning, T., Kalk, K. H., Reizer, J., Saier Jr., M. H., Thunnissen, M. M. G. M., Robillard, G. T., & Dijkstra, B. W. (1997). The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases. Structure, 5(2), 217-225. https://doi.org/10.1016/S0969-2126(97)00180-9

van Montfort, R., Pijning, T., Kalk, K., Schuurman-Wolters, G. K., Reizer, J., Safer Jr., M. H., Robillard, G., & Dijkstra, B. W. (1994). Crystallization of Enzyme IIB of the Cellobiose-specific Phosphotransferase System of Escherichia coli. Journal of Molecular Biology, 239(4), 588-590. https://doi.org/10.1006/jmbi.1994.1399

Nijssen, HMJ., Pijning, T., Proost, JH., Meijer, DKF., & Groothuis, GMM. (1994). The sinusoidal efflux of dibromosulfophthalein from rat liver is stimulated by albumin, ligandin and fatty acid binding protein but not by other dibromosulfophthalein binding proteins. Journal of Hepatology, 21(1), 29-36. https://doi.org/10.1016/S0168-8278(94)80133-9

NIJSSEN, HMJ., PIJNING, T., MEIJER, DKF., & GROOTHUIS, GMM. (1992). INFLUENCE OF ALBUMIN ON THE NET SINUSOIDAL EFFLUX OF THE ORGANIC ANION DIBROMOSULFOPHTHALEIN FROM RAT-LIVER. Hepatology, 15(2), 302-309.

VERLINDE, CLMJ., WITMANS, CJ., PIJNING, T., KALK, KH., HOL, WGJ., CALLENS, M., & OPPERDOES, FR. (1992). STRUCTURE OF THE COMPLEX BETWEEN TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE AND N-HYDROXY-4-PHOSPHONO-BUTANAMIDE - BINDING AT THE ACTIVE-SITE DESPITE AN OPEN FLEXIBLE LOOP CONFORMATION. Protein Science, 1(12), 1578-1584.

Nijssen, H. M. J., Pijning, T., Meijer, D. K. F., & Groothuis, G. M. M. (1991). Mechanistic aspects of uptake and sinusoidal efflux of dibromosulfophthalein in the isolated perfused rat liver. Biochemical Pharmacology, 42(10), 1997-2002. https://doi.org/10.1016/0006-2952(91)90600-A

Braakman, I., Pijning, T., Verest, O., Weert, B., Meijer, D. K. F., & Groothuis, G. M. M. (1989). Vesicular uptake system for the cation lucigenin in the rat hepatocyte. Molecular Pharmacology, 36(4), 537-542.

Braakman, I., Verest, O., Pijning, T., Meijer, D. K. F., & Groothuis, G. M. M. (1989). Zonal distribution of the cation lucigenin in rat liver: Influence of taurocholate. Molecular Pharmacology, 36(4), 532-536.