Publications Overview

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

Volarić, J., van der Heide, N. J., Mutter, N. L., Samplonius, D. F., Helfrich, W., Maglia, G., Szymanski, W., & Feringa, B. L. (2024). Visible Light Control over the Cytolytic Activity of a Toxic Pore-Forming Protein. ACS chemical biology, 19(2), 451–461. Article 3c00640. https://doi.org/10.1021/acschembio.3c00640

Bonini, A., Sauciuc, A., & Maglia, G. (2024). Engineered nanopores for exopeptidase protein sequencing. Nature Methods, 21, 16-17. https://doi.org/10.1038/s41592-023-02136-y

Lucas, F. L. R., Finol-Urdaneta, R. K., Van Thillo, T., McArthur, J. R., van der Heide, N. J., Maglia, G., Dedecker, P., Strauss, O., & Wloka, C. (2023). Evidence of Cytolysin A nanopore incorporation in mammalian cells assessed by a graphical user interface. Nanoscale, 15(23), 16914–16923. https://doi.org/10.1039/d3nr01977b

Paulo, G., Sun, K., Di Muccio, G., Gubbiotti, A., Morozzo della Rocca, B., Geng, J., Maglia, G., Chinappi, M., & Giacomello, A. (2023). Hydrophobically gated memristive nanopores for neuromorphic applications. Nature Communications, 14(1), Article 8390. https://doi.org/10.1038/s41467-023-44019-y

Straathof, S., Di Muccio, G., Yelleswarapu, M., Alzate Banguero, M., Wloka, C., van der Heide, N. J., Chinappi, M., & Maglia, G. (2023). Protein Sizing with 15 nm Conical Biological Nanopore YaxAB. Acs Nano, 17(14), 13685–13699. https://doi.org/10.1021/acsnano.3c02847

Abraham Versloot, R. C., Arias-Orozco, P., Tadema, M. J., Rudolfus Lucas, F. L., Zhao, X., Marrink, S. J., Kuipers, O. P., & Maglia, G. (2023). Seeing the Invisibles: Detection of Peptide Enantiomers, Diastereomers, and Isobaric Ring Formation in Lanthipeptides Using Nanopores. Journal of the American Chemical Society, 145(33), 18355-18365. Article 4076. https://doi.org/10.1021/jacs.3c04076

Zhang, X., Galenkamp, N. S., van der Heide, N. J., Moreno, J., Maglia, G., & Kjems, J. (2023). Specific Detection of Proteins by a Nanobody-Functionalized Nanopore Sensor. Acs Nano, 17(10), 9167-9177. Article 12733. https://doi.org/10.1021/acsnano.2c12733

Sauciuc, A., Morozzo Della Rocca, B., Tadema, M. J., Chinappi, M., & Maglia, G. (2023). Translocation of linearized full-length proteins through an engineered nanopore under opposing electrophoretic force. Nature Biotechnology, Article 01954-x. Advance online publication. https://doi.org/10.1038/s41587-023-01954-x

Kobauri, P., Galenkamp, N. S., Schulte, A. M., de Vries, J., Simeth, N. A., Maglia, G., Thallmair, S., Kolarski, D., Szymanski, W., & Feringa, B. L. (2022). Hypothesis-Driven, Structure-Based Design in Photopharmacology: The Case of eDHFR Inhibitors. Journal of Medicinal Chemistry, 65(6), 4798-4817. Article 1c01962. https://doi.org/10.1021/acs.jmedchem.1c01962

Ying, Y.-L., Hu, Z.-L., Zhang, S., Qing, Y., Fragasso, A., Maglia, G., Meller, A., Bayley, H., Dekker, C., & Long, Y.-T. (2022). Nanopore-based technologies beyond DNA sequencing. Nature Nanotechnology, 17, 1136-1146. https://doi.org/10.1038/s41565-022-01193-2

Huang, G., Voorspoels, A., Versloot, R. C. A., Van Der Heide, N. J., Carlon, E., Willems, K., & Maglia, G. (2022). PlyAB Nanopores Detect Single Amino Acid Differences in Folded Haemoglobin from Blood. Angewandte Chemie (International ed. in English), 61(34), Article e202206227. https://doi.org/10.1002/anie.202206227

Versloot, R. C. A., Lucas, F. L. R., Yakovlieva, L., Tadema, M. J., Zhang, Y., Wood, T. M., Martin, N. I., Marrink, S. J., Walvoort, M. T. C., & Maglia, G. (2022). Quantification of Protein Glycosylation Using Nanopores. Nano Letters, 22(13), 5357-5364. Article 2c10338. https://doi.org/10.1021/acs.nanolett.2c01338

Galenkamp, N. S., & Maglia, G. (2022). Single-Molecule Sampling of Dihydrofolate Reductase Shows Kinetic Pauses and an Endosteric Effect Linked to Catalysis. ACS Catalysis, 12(2), 1228-1236. Article 04388. https://doi.org/10.1021/acscatal.1c04388

Lucas, F. L. R., Willems, K., Tadema, M. J., Tych, K. M., Maglia, G., & Wloka, C. (2022). Unbiased Data Analysis for the Parameterization of Fast Translocation Events through Nanopores. ACS Omega, 7, 26040–26046. https://doi.org/10.1021/acsomega.2c00871

Versloot, R. C. A., Straathof, S. A. P., Stouwie, G., Tadema, M. J., & Maglia, G. (2022). β-Barrel Nanopores with an Acidic-Aromatic Sensing Region Identify Proteinogenic Peptides at Low pH. Acs Nano, 16(5), 7258-7268. Article 1c11455. https://doi.org/10.1021/acsnano.1c11455

Lucas, F. L. R., Piso, T. R. C., van der Heide, N. J., Galenkamp, N. S., Hermans, J., Wloka, C., & Maglia, G. (2021). Automated Electrical Quantification of Vitamin B1 in a Bodily Fluid using an Engineered Nanopore-Sensor. Angewandte Chemie (International ed. in English), 60(42), 22849-22855. https://doi.org/10.1002/anie.202107807

Zhang, S., Huang, G., Versloot, R. C. A., Bruininks, B. M. H., de Souza, P. C. T., Marrink, S.-J., & Maglia, G. (2021). Bottom-up fabrication of a proteasome-nanopore that unravels and processes single proteins. Nature Chemistry, 13(12), 1192–1199. https://doi.org/10.1038/s41557-021-00824-w

de Lannoy, C., Lucas, F. L. R., Maglia, G., & de Ridder, D. (2021). In silico assessment of a novel single-molecule protein fingerprinting method employing fragmentation and nanopore detection. Iscience, 24(10), Article 103202. https://doi.org/10.1016/j.isci.2021.103202

Lauxen, A. I., Kobauri, P., Wegener, M., Hansen, M. J., Galenkamp, N. S., Maglia, G., Szymanski, W., Feringa, B. L., & Kuipers, O. P. (2021). Mechanism of Resistance Development in E. coli against TCAT, a Trimethoprim-Based Photoswitchable Antibiotic. Pharmaceuticals, 14(5), Article ph14050392. https://doi.org/10.3390/ph14050392

Lucas, F. L. R., Versloot, R. C. A., Yakovlieva, L., Walvoort, M. T. C., & Maglia, G. (2021). Protein identification by nanopore peptide profiling. Nature Communications, 12, Article 5795. https://doi.org/10.1038/s41467-021-26046-9

Wloka, C., Galenkamp, N. S., van der Heide, N. J., Lucas, F. L. R., & Maglia, G. (2021). Strategies for enzymological studies and measurements of biological molecules with the cytolysin A nanopore. Methods in Enzymology, 649, 567-585. https://doi.org/10.1016/bs.mie.2021.01.007

Alfaro, J. A., Bohlander, P., Dai, M., Filius, M., Howard, C. J., van Kooten, X. F., Ohayon, S., Pomorski, A., Schmid, S., Aksimentiev, A., Anslyn, E. V., Bedran, G., Cao, C., Chinappi, M., Coyaud, E., Dekker, C., Dittmar, G., Drachman, N., Eelkema, R., ... Joo, C. (2021). The emerging landscape of single-molecule protein sequencing technologies. Nature Methods, 18(6), 604-617. https://doi.org/10.1038/s41592-021-01143-1

Lucas, F. L. R., Sarthak, K., Lenting, E. M., Coltan, D., van der Heide, N. J., Versloot, R. C. A., Aksimentiev, A., & Maglia, G. (2021). The Manipulation of the Internal Hydrophobicity of FraC Nanopores Augments Peptide Capture and Recognition. Acs Nano, 15(6), 9600-9613. Article acsnano.0c09958. https://doi.org/10.1021/acsnano.0c09958

Bayoumi, M., Nomidis, S. K., Willems, K., Carlon, E., & Maglia, G. (2021). Autonomous and Active Transport Operated by an Entropic DNA Piston. Nano Letters, 21(1), 762-768. Article acs.nanolett.0c04464. https://doi.org/10.1021/acs.nanolett.0c04464

Willems, K., Ruić, D., L R Lucas, F., Barman, U., Verellen, N., Hofkens, J., Maglia, G., & Van Dorpe, P. (2020). Accurate modeling of a biological nanopore with an extended continuum framework. Nanoscale, 12(32), 16775-16795. https://doi.org/10.1039/d0nr03114c

Ciudad, S., Puig, E., Botzanowski, T., Meigooni, M., Arango, A. S., Do, J., Mayzel, M., Bayoumi, M., Chaignepain, S., Maglia, G., Cianferani, S., Orekhov, V., Tajkhorshid, E., Bardiaux, B., & Carulla, N. (2020). Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage. Nature Communications, 11(1), Article 3014. https://doi.org/10.1038/s41467-020-16566-1

Restrepo-Pérez, L., Huang, G., Bohländer, P. R., Worp, N., Eelkema, R., Maglia, G., Joo, C., & Dekker, C. (2020). Correction to Resolving Chemical Modifications to a Single Amino Acid within a Peptide Using a Biological Nanopore. Acs Nano, 14(4), 5148. Article acsnano.0c01699. https://doi.org/10.1021/acsnano.0c01699

Zernia, S., van der Heide, N. J., Galenkamp, N. S., Gouridis, G., & Maglia, G. (2020). Current Blockades of Proteins Inside Nanopores for Real-Time Metabolome Analysis. Acs Nano, 14(2), 2296-2307. Article acsnano.9b09434. https://doi.org/10.1021/acsnano.9b09434

Galenkamp, N. S., Biesemans, A., & Maglia, G. (2020). Directional conformer exchange in dihydrofolate reductase revealed by single-molecule nanopore recordings. Nature Chemistry, 12(5), 481-488. https://doi.org/10.1038/s41557-020-0437-0

Huang, G., Willems, K., Bartelds, M., van Dorpe, P., Soskine, M., & Maglia, G. (2020). Electro-Osmotic Vortices Promote the Capture of Folded Proteins by PlyAB Nanopores. Nano Letters, 20(5), 3819-3827. https://doi.org/10.1021/acs.nanolett.0c00877

Willems, K., Ruic, D., Biesemans, A., Galenkamp, N., Van Dorpe, P., & Maglia, G. (2020). Electrophoretic Trapping of a Single Protein Inside a Nanopore. Biophysical Journal, 118(3), 305A-305A.

Maglia, G., & Browne, W. (2019). Editorial overview: Reprogramming biology: from biopolymers to complex systems. Current Opinion in Biotechnology, 58, v-vi. https://doi.org/10.1016/j.copbio.2019.08.002

Zhao, S., Restrepo-Pérez, L., Soskine, M., Maglia, G., Joo, C., Dekker, C., & Aksimentiev, A. (2019). Electro-Mechanical Conductance Modulation of a Nanopore Using a Removable Gate. Acs Nano, 13(2), 2398-2409. https://doi.org/10.1021/acsnano.8b09266

Willems, K., Ruić, D., Biesemans, A., Galenkamp, N. S., Van Dorpe, P., & Maglia, G. (2019). Engineering and Modeling the Electrophoretic Trapping of a Single Protein Inside a Nanopore. Acs Nano, 13(9), 9980-9992. https://doi.org/10.1021/acsnano.8b09137

Huang, G., Voet, A., & Maglia, G. (2019). FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution. Nature Communications, 10, Article 835. https://doi.org/10.1038/s41467-019-08761-6

Restrepo-Pérez, L., Wong, C. H., Maglia, G., Dekker, C., & Joo, C. (2019). Label-Free Detection of Post-translational Modifications with a Nanopore. Nano Letters, 19(11), 7957-7964. https://doi.org/10.1021/acs.nanolett.9b03134

Restrepo-Pérez, L., Huang, G., Bohländer, P. R., Worp, N., Eelkema, R., Maglia, G., Joo, C., & Dekker, C. (2019). Resolving Chemical Modifications to a Single Amino Acid within a Peptide Using a Biological Nanopore. Acs Nano, 13(12), 13668-13676. https://doi.org/10.1021/acsnano.9b05156

Mutter, N. L., Volarić, J., Szymanski, W., Feringa, B. L., & Maglia, G. (2019). Reversible Photocontrolled Nanopore Assembly. Journal of the American Chemical Society, 141(36), 14356-14363. https://doi.org/10.1021/jacs.9b06998

Galenkamp, N. S., Soskine, M., Hermans, J., Wloka, C., & Maglia, G. (2018). Direct electrical quantification of glucose and asparagine from bodily fluids using nanopores. Nature Communications, 9(1), Article 4085. https://doi.org/10.1038/s41467-018-06534-1

Nomidis, S. K., Hooyberghs, J., Maglia, G., & Carlon, E. (2018). DNA capture into the ClyA nanopore: Diffusion-limited versus reaction-limited processes. Journal of Physics-Condensed Matter, 30(30), Article 304001. https://doi.org/10.1088/1361-648X/aacc01

Mutter, N. L., Soskine, M., Huang, G., Albuquerque, I. S., Bernardes, G. J. L., & Maglia, G. (2018). Modular pore-forming immunotoxins with caged cytotoxicity tailored by directed evolution. ACS chemical biology, 13(11), 3153–3160. Article 8b00720. https://doi.org/10.1021/acschembio.8b00720

Wilmaerts, D., Bayoumi, M., Dewachter, L., Knapen, W., Mika, J. T., Hofkens, J., Dedecker, P., Maglia, G., Verstraeten, N., & Michiels, J. (2018). The Persistence-Inducing Toxin HokB Forms Dynamic Pores That Cause ATP Leakage. mBio, 9(4), Article ARTN e00744-18. https://doi.org/10.1128/mBio.00744-18

Huang, G., Willems, K., Soskine, M., Wloka, C., & Maglia, G. (2017). Electro-osmotic capture and ionic discrimination of peptide and protein biomarkers with FraC nanopores. Nature Communications, 8, 1-11. Article 935. https://doi.org/10.1038/s41467-017-01006-4

Aminipour, Z., Khorshid, M., Bayoumi, M., Losada-Perez, P., Thoelen, R., Bonakdar, S., Keshvari, H., Maglia, G., Wagner, P., & Van der Bruggen, B. (2017). Formation and electrical characterization of black lipid membranes in porous filter materials. Physica Status Solidi A-Applications and materials science, 214(9), Article 1700104. https://doi.org/10.1002/pssa.201700104

Wloka, C., Van Meervelt, V., van Gelder, D., Danda, N., Jager, N., Williams, C. P., & Maglia, G. (2017). Label-Free and Real-Time Detection of Protein Ubiquitination with a Biological Nanopore. Acs Nano, 11(5), 4387-4394. Article acsnano.6b07760. https://doi.org/10.1021/acsnano.6b07760

Bayoumi, M., Bayley, H., Maglia, G., & Sapra, K. T. (2017). Multi-compartment encapsulation of communicating droplets and droplet networks in hydrogel as a model for artificial cells. Scientific Reports, 7, 1-11. Article 45167. https://doi.org/10.1038/srep45167

Van Meervelt, V., Soskine, M., Singh, S., Schuurman-Wolters, G., Wijma, H. J., Poolman, B., & Maglia, G. (2017). Real-time conformational changes and controlled orientation of native proteins inside a protein nanoreactor. Journal of the American Chemical Society, 139(51), 18640-18646. Article jacs.7b10106. https://doi.org/10.1021/jacs.7b10106

Loveridge, E. J., Hroch, L., Hughes, R. L., Williams, T., Davies, R. L., Angelastro, A., Luk, L. Y. P., Maglia, G., & Allemann, R. K. (2017). Reduction of Folate by Dihydrofolate Reductase from Thermotoga maritima. Biochemistry, 56(13), 1879-1886. Article acs.biochem.6b01268. https://doi.org/10.1021/acs.biochem.6b01268

Willems, K., Van Meervelt, V., Wloka, C., & Maglia, G. (2017). Single-molecule nanopore enzymology. Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 372(1726), Article 20160230. https://doi.org/10.1098/rstb.2016.0230

Wloka, C., Mutter, N. L., Soskine, M., & Maglia, G. (2016). Alpha-Helical Fragaceatoxin C Nanopore Engineered for Double-Stranded and Single-Stranded Nucleic Acid Analysis. Angewandte Chemie - International Edition, 55(40), 12494-12498. https://doi.org/10.1002/anie.201606742

Serra-Batiste, M., Ninot-Pedrosa, M., Bayoumi, M., Gairí, M., Maglia, G., & Carulla, N. (2016). Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments. Proceedings of the National Academy of Sciences of the United States of America, 113(39), 10866-10871. https://doi.org/10.1073/pnas.1605104113

Biesemans, A., Soskine, M., & Maglia, G. (2016). Controlling the Nanoscopic Confinement of Enzymes Inside ClyA Nanopores for Single-Protein Studies. Biophysical Journal, 110(3, Supplement 1), 518A-518A. https://doi.org/10.1016/j.bpj.2015.11.2769

Maglia, G. (2016). Design and Engineering of Nanopores with Emergent Functions. Biophysical Journal, 110(3), 536A-536A. https://doi.org/10.1016/j.bpj.2015.11.2871

Franceschini, L., Brouns, T., Willems, K., Carlon, E., & Maglia, G. (2016). DNA Translocation through Nanopores at Physiological Ionic Strengths Requires Precise Nanoscale Engineering. Acs Nano, 10(9), 8394-8402. https://doi.org/10.1021/acsnano.6b03159

Vega, M., Perez, M. S., Granell, P., Golmar, F., Wloka, C., Maglia, G., Dieguez, M. J., Del Valle, E. M., Lasorsa, C., & Lerner, B. (2016). Effect of butanol and salt concentration on solid-state nanopores resistance. Cogent chemistry, 2, Article 1225345. https://doi.org/10.1080/23312009.2016.1225345

McGinn, S., Bauer, D., Brefort, T., Dong, L., El-Sagheer, A., Elsharawy, A., Evans, G., Falk-Sörqvist, E., Forster, M., Fredriksson, S., Freeman, P., Freitag, C., Fritzsche, J., Gibson, S., Gullberg, M., Gut, M., Heath, S., Heath-Brun, I., Heron, A. J., ... Gut, I. G. (2016). New Technologies for DNA analysis-A review of the READNA Project. New Biotechnology, 33(3), 311-330. https://doi.org/10.1016/j.nbt.2015.10.003

Biesemans, A., Soskine, M., & Maglia, G. (2015). A Protein Rotaxane Controls the Translocation of Proteins Across a ClyA Nanopore. Nano Letters, 15(9), 6076-6081. https://doi.org/10.1021/acs.nanolett.5b02309

Stoddart, D., Franceschini, L., Heron, A., Bayley, H., & Maglia, G. (2015). DNA stretching and optimization of nucleobase recognition in enzymatic nanopore sequencing. Nanotechnology, 26(8), Article 084002. https://doi.org/10.1088/0957-4484/26/8/084002

Ho, C.-W., Meervelt, V., Tsai, K.-C., De Temmerman, P.-J., Mast, J., & Maglia, G. (2015). Engineering a nanopore with co-chaperonin function. Science Advances, 1(11), Article e1500905. https://doi.org/10.1126/sciadv.1500905

Soskine, M., Biesemans, A., & Maglia, G. (2015). Single-Molecule Analyte Recognition with ClyA Nanopores Equipped with Internal Protein Adaptors. Journal of the American Chemical Society, 137(17), 5793-7. https://doi.org/10.1021/jacs.5b01520

Van Meervelt, V., Soskine, M., & Maglia, G. (2014). Detection of Two Isomeric Binding Configurations in a Protein-Aptamer Complex with a Biological Nanopore. Acs Nano, 8(12), 12826-12835. https://doi.org/10.1021/nn506077e

Stoddart, D., Ayub, M., Hoefler, L., Raychaudhuri, P., Klingelhoefer, J. W., Maglia, G., Heron, A., & Bayley, H. (2014). Functional truncated membrane pores. Proceedings of the National Academy of Science of the United States of America, 111(7), 2425-2430. https://doi.org/10.1073/pnas.1312976111

Franceschini, L., Soskine, M., Biesemans, A., & Maglia, G. (2013). A nanopore machine promotes the vectorial transport of DNA across membranes. Nature Communications, 4, 1-8. Article 2415. https://doi.org/10.1038/ncomms3415

Soskine, M., Biesemans, A., De Maeyer, M., & Maglia, G. (2013). Tuning the size and properties of ClyA nanopores assisted by directed evolution. Journal of the American Chemical Society, 135(36), 13456-13463. https://doi.org/10.1021/ja4053398

Soskine, M., Biesemans, A., Moeyaert, B., Cheley, S., Bayley, H., & Maglia, G. (2012). An engineered ClyA nanopore detects folded target proteins by selective external association and pore entry. Nano Letters, 12(9), 4895-4900. https://doi.org/10.1021/nl3024438

Fransceschini, L., Mikhailova, E., Bayley, H., & Maglia, G. (2012). Nucleobase recognition at alkaline pH and apparent pK(a) of single DNA bases immobilised within a biological nanopore. Chemical Communications, 48(10), 1520-1522. https://doi.org/10.1039/c1cc16124e

Rincon-Restrepo, M., Milthallova, E., Bayley, H., & Maglia, G. (2011). Controlled Translocation of Individual DNA Molecules through Protein Nanopores with Engineered Molecular Brakes. Nano Letters, 11(2), 746-750. https://doi.org/10.1021/nl1038874

Maglia, G., Heron, AJ., Stoddart, D., Japrung, D., & Bayley, H. (2010). ANALYSIS OF SINGLE NUCLEIC ACID MOLECULES WITH PROTEIN NANOPORES. Methods in Enzymology, 475, 591-623.

Wallace, E. VB., Stoddart, D., Heron, A., Mikhailova, E., Maglia, G., Donohoe, T. J., & Bayley, H. (2010). Identification of epigenetic DNA modifications with a protein nanopore. Chemical Communications, 46(43), 8195-8197.

Stoddart, D., Maglia, G., Mikhailova, E., Heron, A., & Bayley, H. (2010). Multiple Base-Recognition Sites in a Biological Nanopore: Two Heads are Better than One. Angewandte Chemie - International Edition, 49(3), 556-559.

Stoddart, D., Heron, A., Klingelhoefer, J., Mikhailova, E., Maglia, G., & Bayley, H. (2010). Nucleobase Recognition in ssDNA at the Central Constriction of the alpha-Hemolysin Pore. Nano Letters, 10(9), 3633-3637.

Japrung, D., Henricus, M., Li, QH., Maglia, G., & Bayley, H. (2010). Urea Facilitates the Translocation of Single-Stranded DNA and RNA Through the alpha-Hemolysin Nanopore. Biophysical Journal, 98(9), 1856-1863.

Maglia, G., Henricus, M., Wyss, R., Li, QH., Cheley, S., & Bayley, H. (2009). DNA Strands from Denatured Duplexes are Translocated through Engineered Protein Nanopores at Alkaline pH. Nano Letters, 9(11), 3831-3836.

Maglia, G., Heron, AJ., Hwang, WL., Holden, MA., Mikhailova, E., Li, QH., Cheley, S., & Bayley, H. (2009). Droplet networks with incorporated protein diodes show collective properties. Nature Nanotechnology, 4(7), 437-440.

Stoddart, D., Heron, AJ., Mikhailova, E., Maglia, G., & Bayley, H. (2009). Single-nucleotide discrimination in immobilized DNA oligonucleotides with a biological nanopore. Proceedings of the National Academy of Science of the United States of America, 106(19), 7702-7707.

Loveridge, EJ., Maglia, G., & Allemann, RK. (2009). The Role of Arginine 28 in Catalysis by Dihydrofolate Reductase from the Hyperthermophile Thermotoga maritima. ChemBioChem, 10(16), 2624-2627. https://doi.org/10.1002/cbic.200900465

Maglia, G., Jonkheer, A., De Maeyer, M., Frere, JM., & Engelborghs, Y. (2008). An unusual red-edge excitation and time-dependent Stokes shift in the single tryptophan mutant protein DD-carboxypeptidase from Streptomyces: The role of dynamics and tryptophan rotamers. Protein Science, 17(2), 352-361.

Maglia, G., Restrepo, MR., Mikhailova, E., & Bayley, H. (2008). Enhanced translocation of single DNA molecules through alpha-hemolysin nanopores by manipulation of internal charge. Proceedings of the National Academy of Science of the United States of America, 105(50), 19720-19725.

WU, HC., Astier, Y., Maglia, G., Mikhailova, E., & Bayley, H. (2007). Protein nanopores with covalently attached molecular adapters. Journal of the American Chemical Society, 129(51), 16142-16148.

Swanwick, RS., Maglia, G., Tey, LH., & Allemann, RK. (2006). Coupling of protein motions and hydrogen transfer during catalysis by Escherichia coli dihydrofolate reductase. Biochemical Journal, 394, 259-265.

Allemann, RK., Evans, RM., Tey, LH., Maglia, G., Pang, JY., Rodriguez, R., Shrimpton, PJ., & Swanwick, RS. (2006). Protein motions during catalysis by dihydrofolate reductases. Philosophical Transactions of the Royal Society B: Biological Sciences, 361(1472), 1317-1321.

Maglia, G., & Allemanm, RK. (2003). Evidence for environmentally coupled hydrogen tunneling during dihydrofolate reductase catalysis. Journal of the American Chemical Society, 125(44), 13372-13373.

Maglia, G., Javed, MH., & Allemanm, RK. (2003). Hydride transfer during catalysis by dihydrifolate reductase from Thermotoga maritima. Biochemical Journal, 374, 529-535.