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Blum, T. B., Housset, D., Clabbers, M. T. B., van Genderen, E., Bacia-Verloop, M., Zander, U., McCarthy, A. A., Schoehn, G., Ling, W. L. und Abrahams, J. P. (2021) „Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals“, Acta Crystallographica Section D: Structural Biology, 77, S. 75–85. 10.1107/S2059798320014540.   edoc
Thakkar, P., Guzenko, V. A., Lu, P.-H., Dunin-Borkowski, R. E., Abrahams, J. P. und Tsujino, S. (2020) „Fabrication of low aspect ratio three-element Boersch phase shifters for voltage-controlled three electron beam interference“, Journal of Applied Physics, 128(13), S. 134502. 10.1063/5.0020383.   edoc
Merg, A. D., Touponse, G., van Genderen, E., Blum, T. B., Zuo, X., Bazrafshan, A., Siaw, H. M. H., McCanna, A., Dyer, R. B., Salaita, K., Abrahams, J. P. und Conticello, V. P. (2020) „Shape-Shifting Peptide Nanomaterials: Surface Asymmetry Enables pH-Dependent Formation and Interconversion of Collagen Tubes and Sheets“, Journal of the American Chemical Society, 142(47), S. 19956–19968. 10.1021/jacs.0c08174.   edoc
Xiao, X., Elsayed, S. S., Wu, C., van der Heul, H. U., Metsä-Ketelä, M., Du, C., Prota, A. E., Chen, C.-C., Liu, W., Guo, R.-T., Abrahams, J. P. und van Wezel, G. P. (2020) „Functional and Structural Insights into a Novel Promiscuous Ketoreductase of the Lugdunomycin Biosynthetic Pathway“, ACS Chemical Biology, 15(9), S. 2529–2538. 10.1021/acschembio.0c00564.   edoc | Open Access
van Schayck, J. P., van Genderen, E., Maddox, E., Roussel, L., Boulanger, H., Fröjdh, E., Abrahams, J.-P., Peters, P. J. und Ravelli, R. B. G. (2020) „Sub-pixel electron detection using a convolutional neural network“, Ultramicroscopy, 218, S. 113091. 10.1016/j.ultramic.2020.113091.   edoc
Matz, J. M., Drepper, B., Blum, T. B., van Genderen, E., Burrell, A., Martin, P., Stach, T., Collinson, L. M., Abrahams, J. P., Matuschewski, K. und Blackman, M. J. (2020) „A lipocalin mediates unidirectional heme biomineralization in malaria parasites“, Proceedings of the National Academy of Sciences of the United States of America, 117(28), S. 16546–16556. 10.1073/pnas.2001153117.   edoc | Open Access
Zhang, Z., Wen, K., Zhang, C., Laroche, F., Wang, Z., Zhou, Q., Liu, Z., Abrahams, J. P. und Zhou, X. (2020) „Extracellular Nanovesicle Enhanced Gene Transfection Using Polyethyleneimine in HEK293T Cells and Zebrafish Embryos“, Frontiers in Bioengineering and Biotechnology, 8, S. 448. 10.3389/fbioe.2020.00448.   edoc | Open Access
Wallin, C., Hiruma, Y., Warmlander, S., Huvent, I., Jarvet, J., Abrahams, J. P., Graslund, A., Lippens, G. und Luo, J. (2019) „The Neuronal Tau Protein Blocks In Vitro Fibrillation of the Amyloid-beta (A beta) Peptide“, Biophysical Journal. CellPress. 10.1016/j.bpj.2018.11.1657.   edoc
Blum, T. B. und Abrahams, J. P. (2019) „6T17: Cryo-EM structure of the wild-type flagellar filament of the Firmicute Kurthia“, Worldwide Protein Data Bank, S. 6T17. 10.2210/pdb6t17/pdb.   edoc
Gemmi, M., Mugnaioli, E., Gorelik, T. E., Kolb, U., Palatinus, L., Boullay, P., Hovmöller, S. und Abrahams, J. P. (2019) „3D Electron Diffraction: The Nanocrystallography Revolution“, ACS central science, 5(8), S. 1315–1329. 10.1021/acscentsci.9b00394.   edoc
Merg, A. D., Touponse, G., van Genderen, E., Zuo, X., Bazrafshan, A., Blum, T., Hughes, S., Salaita, K., Abrahams, J. P. und Conticello, V. P. (2019) „2D Crystal Engineering of Nanosheets Assembled from Helical Peptide Building Blocks“, Angewandte Chemie (International ed. in English), 58(38), S. 13507–13512. 10.1002/anie.201906214.   edoc
Clabbers, M. T. B., Gruene, T., van Genderen, E. und Abrahams, J. P. (2019) „Reducing dynamical electron scattering reveals hydrogen atoms“, Acta crystallographica. Section A, Foundations and advances, 75(Pt 1), S. 82–93. 10.1107/S2053273318013918.   edoc
Moradi, M., Opara, N. L., Tulli, L. G., Wäckerlin, C., Dalgarno, S. J., Teat, S. J., Baljozovic, M., Popova, O., van Genderen, E., Kleibert, A., Stahlberg, H., Abrahams, J. P., Padeste, C., Corvini, P. F.-X., Jung, T. A. und Shahgaldian, P. (2019) „Supramolecular architectures of molecularly thin yet robust free-standing layers“, Science Advances, 5(2), S. eaav4489. 10.1126/sciadv.aav4489.   edoc
Merg, A. D., van Genderen, E., Bazrafshan, A., Su, H., Zuo, X., Touponse, G., Blum, T. B., Salaita, K., Abrahams, J. P. und Conticello, V. P. (2019) „Seeded Heteroepitaxial Growth of Crystallizable Collagen Triple Helices: Engineering Multifunctional Two-Dimensional Core-Shell Nanostructures“, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 141(51), S. 20107–20117. 10.1021/jacs.9b09335.   edoc
Blum, T. B., Filippidou, S., Fatton, M., Junier, P. und Abrahams, J. P. (2019) „The wild-type flagellar filament of the Firmicute Kurthia at 2.8 Å resolution in vivo“, Scientific reports, 9(1), S. 14948. 10.1038/s41598-019-51440-1.   edoc
Latychevskaia, T. und Abrahams, J. P. (2019) „Inelastic scattering and solvent scattering reduce dynamical diffraction in biological crystals“, Acta Crystallographica Section B-Structural Science Crystal Engineering and Materials, 75, S. 523–531. 10.1107/S2052520619009661.   edoc
Clabbers, M., Gruene, T., van Genderen, E. und Abrahams, J. P. (2018) „Experimental and computational reduction of dynamical electron scattering allows visualizing individual hydrogen atoms“, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. 10.1107/S2053273318088770.   edoc
Abrahams, J. P., Clabbers, M., van Genderen, E. und Blum, T. (2018) „Electron tomography of radiation sensitive 3D nano-crystals in imaging and diffraction mode“, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. 10.1107/S205327331809397X.   edoc
Tinti, G., Fröjdh, E., van Genderen, E., Gruene, T., Schmitt, B., de Winter, D. A. M., Weckhuysen, B. M. und Abrahams, J. P. (2018) „Electron crystallography with the EIGER detector“, IUCrJ, 5(Pt 2), S. 190–199. 10.1107/S2052252518000945.   edoc
Wallin, C., Hiruma, Y., Wärmländer, S. K. T. S., Huvent, I., Jarvet, J., Abrahams, J. P., Gräslund, A., Lippens, G. und Luo, J. (2018) „The Neuronal Tau Protein Blocks in Vitro Fibrillation of the Amyloid-β (Aβ) Peptide at the Oligomeric Stage“, Journal of the American Chemical Society, S. 8138–8146. 10.1021/jacs.7b13623.   edoc
Thomas, B., Dubey, R. K., Clabbers, M. T. B., Gupta, K. B. S. S., van Genderen, E., Jager, W. F., Abrahams, J. P., Sudholter, E. J. R. und de Groot, H. J. M. (2018) „A Molecular Level Approach To Elucidate the Supramolecular Packing of Light-Harvesting Antenna Systems“, Chemistry (Weinheim an der Bergstrasse, Germany), 24(56), S. 14989–14993. 10.1002/chem.201802288.   edoc
Clabbers, M. T. B., Gruene, T., Parkhurst, J. M., Abrahams, J. P. und Waterman, D. G. (2018) „Electron diffraction data processing with DIALS“, Acta crystallographica. Section D, Structural biology, 74(Pt 6), S. 506–518. 10.1107/S2059798318007726.   edoc
Clabbers, M. T. B. und Abrahams, J. P. (2018) „Electron diffraction and three-dimensional crystallography for structural biology“, CRYSTALLOGRAPHY REVIEWS, 24(3), S. 176–204. 10.1080/0889311X.2018.1446427.   edoc
Tinti, G., Frojdh, E., Van Genderen, E., Gruene, T., Schmitt, B., De Winter, D. A. M., Weckhuysen, B. M. und Abrahams, J. P. (2018) „CCDC 1817054: Experimental Crystal Structure Determination“, Cambridge Structural Database, S. 1817054. 10.5517/ccdc.csd.cc1yzsnc.   edoc
Matheson, J., Moldovan, G., Kirkland, A., Allinson, N. und Abrahams, J. P. (2017) „Testing and Comparison of Imaging Detectors for Electrons in the Energy Range 10–20 keV“, Journal of Instrumentation, 12(11), S. C11016. 10.1088/1748-0221/12/11/C11016.   edoc
Nederlof, I., van Genderen, E., Clabbers, M. E. und Abrahams, J. P. (2017) „Electron Crystallography of Protein Nano-Crystals “, Acta Crystallographica Section A: Foundations And Advances, A73, S. a297-a298.   edoc
Nikolopoulos, S., Galanis, A. S., Vallcorba, O., Eggeman, A., Das, P. P., Abrahams, J. P., Rauch, E., Midgley, P. und Gemmi, M. (2017) „Random electron diffraction tomography for structure analysis of pharmaceuticals “, Acta Crystallographica A-Foundation And Advances. erausgegeben von International Union of Crystallography, 73, S. c980. erfügbar unter: https://journals.iucr.org/a/issues/2017/a2/00/a56076/a56076.pdf.   edoc
Yin, Q., Liu, Z., Laroche, F., Zhou, X., Shao, N., Lin, B., Wang, R., Yuan, N., Ding, J. und Abrahams, J. P. (2017) „A Novel Capturing Method for Quantification of Extra-Cellular Nanovesicles “, Journal of nanoscience and nanotechnology, 17(2), S. 908–913. 10.1166/jnn.2017.12631.   edoc
Clabbers, M. T. B., van Genderen, E., Wan, W., Wiegers, E. L., Gruene, T. und Abrahams, J. P. (2017) „Protein structure determination by electron diffraction using a single three-dimensional nanocrystal“, Acta crystallographica. Section D, Structural biology, 73(Pt 9), S. 738–748. 10.1107/S2059798317010348.   edoc
Su, J., Wang, H., Wu, K., Liu, Z., Yin, Q., Wang, R., Lv, W., Yin, S., Liu, Z. und Abrahams, J. P. (2017) „Neutravidin-Mediated Extraction of Isolated Small Diameter Single Walled Carbon Nanotubes for Bio-Recognition“, Journal of nanoscience and nanotechnology, 17(5), S. 3588–3596. 10.1166/jnn.2017.12860.   edoc
Wang, R., Boleij, M., Yin, Q., Galjart, N., Lin, B., Yuan, N., Zhou, X., Tan, M., Ding, J., Liu, Z. und Abrahams, J. P. (2017) „Purification of Biotinylated Proteins Using Single Walled Carbon Nanotube-Streptavidin Complexes“, Journal of nanoscience and nanotechnology, 17(2), S. 926–931. 10.1166/jnn.2017.12716.   edoc
Abrahams, J. P. (2016) „Electron nanodiffraction for structural biology“, Acta Crystallographica A-Foundation And Advances, 72(a1), S. s6. 10.1107/S2053273316099903.   edoc
van Genderen, E., Li, Y. W., Nederlof, I. und Abrahams, J. P. (2016) „Lattice filter for processing image data of three-dimensional protein nanocrystals“, Acta crystallographica. Section D, Structural biology, 72(Pt 1), S. 34–39. 10.1107/S205979831502149X.   edoc
Wallin, C., Kulkarni, Y. S., Abelein, A., Jarvet, J., Liao, Q., Strodel, B., Olsson, L., Luo, J., Abrahams, J. P., Sholts, S. B., Roos, P. M., Kamerlin, S. C. L., Gräslund, A. und Wärmländer, S. K. T. S. (2016) „Characterization of Mn(II) ion binding to the amyloid-β peptide in Alzheimer’s disease“, Journal of Trace Elements in Medicine and Biology, 38, S. 183–193. 10.1016/j.jtemb.2016.03.009.   edoc
Luo, J., Wärmländer, S. K. T. S., Gräslund, A. und Abrahams, J. P. (2016) „Reciprocal Molecular Interactions between the Aβ Peptide Linked to Alzheimer’s Disease and Insulin Linked to Diabetes Mellitus Type II“, ACS Chemical Neuroscience , 7(3), S. 269–274. 10.1021/acschemneuro.5b00325.   edoc
Luo, J., Wärmländer, S. K. T. S., Gräslund, A. und Abrahams, J. P. (2016) „Cross-interactions between the Alzheimer Disease Amyloid-β Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis“, Journal of Biological Chemistry, 291(32), S. 16485–16493. 10.1074/jbc.R116.714576.   edoc
van Genderen, E., Clabbers, M. T. B., Das, P. P., Stewart, A., Nederlof, I., Barentsen, K. C., Portillo, Q., Pannu, N. S., Nicolopoulos, S., Gruene, T. und Abrahams, J. P. (2016) „Ab initio structure determination of nanocrystals of organic pharmaceutical compounds by electron diffraction at room temperature using a Timepix quantum area direct electron detector“, Acta Crystallographica Section A : Foundations and Advances, 72(2), S. 236–242. 10.1107/S2053273315022500.   edoc
Tiiman, A., Luo, J., Wallin, C., Olsson, L., Lindgren, J., Jarvet, J., Per, R., Sholts, S. B., Rahimipour, S., Abrahams, J. P., Karlström, A. E., Gräslund, A. und Wärmländer, S. K. T. S. (2016) „Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species“, Journal of Alzheimer’s Disease, 54(3), S. 971–982. 10.3233/JAD-160427.   edoc
Afanasyev, P., Ravelli, R. B. G., Matadeen, R., De Carlo, S., van Duinen, G., Alewijnse, B., Peters, P. J., Abrahams, J.-P., Portugal, R. V., Schatz, M. und van Heel, M. (2015) „A posteriori correction of camera characteristics from large image data sets“, Scientific Reports, 5, S. 10317. 10.1038/srep10317.   edoc
Clabbers, M. T. B., van Genderen, E., Nederlof, I., Li, Y.-W. und Abrahams, J. P. (2015) „Electron crystallography of 3D nano-crystals“, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. 10.1107/S2053273315093985.   edoc
Abrahams, J. P., van Genderent, E., Nederlof, I., Clabbers, M. und Li, Y. (2015) „Electron diffraction and imaging of 3D nanocrystals of pharmaceuticals, peptides and proteins“, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. 10.1107/S2053273315098496.   edoc
Luo, J. und Abrahams, J. P. (2014) „Cyclic Peptides as Inhibitors of Amyloid Fibrillation “, Chemistry - A European Journal, 20(9), S. 2410–2419. 10.1002/chem.201304253.   edoc
Luo, J., Wärmländer, S. K. T. S., Chien-Hung, Y., Muhammad, K., Gräslund, A. und Abrahams, J. P. (2014) „The Aβ peptide forms non-amyloid fibrils in the presence of carbon nanotubes“, Nanoscale, 6(12), S. 6720–6726. 10.1039/c4nr00291a.   edoc
Luo, J., Wärmländer, S. K. T. S., Gräslund, A. und Abrahams, J. P. (2014) „Alzheimer Peptides Aggregate into Transient Nanoglobules That Nucleate Fibrils“, Biochemistry, 53(40), S. 6302–6308. 10.1021/bi5003579.   edoc
Luo, J., Wärmländer, S. K. T. S., Gräslund, A. und Abrahams, J. P. (2014) „Non-chaperone Proteins Can Inhibit Aggregation and Cytotoxicity of Alzheimer Amyloid beta Peptide“, Journal of Biological Chemistry, 289(40), S. 27766–27775. 10.1074/jbc.M114.574947.   edoc
Abelein, A., Abrahams, J. P., Danielsson, J., Graslund, A., Jarvet, J., Luo, J., Tiiman, A. und Warmlander, S. K. T. S. (2014) „The hairpin conformation of the amyloid beta peptide is an important structural motif along the aggregation pathway “, Journal of Biological Inorganic Chemistry, 19(4-5), S. 623–634. 10.1007/s00775-014-1131-8.   edoc
Luo, J., Mohammed, I., Warmlander, S. K. T. S., Hiruma, Y., Graslund, A. und Abrahams, J. P. (2014) „Endogenous Polyamines Reduce the Toxicity of Soluble A beta Peptide Aggregates Associated with Alzheimer’s Disease“, Biomacromolecules, 15(6), S. 1985–1991. 10.1021/bm401874j.   edoc
Liu, Z., Voskamp, P., Zhang, Y., Chu, F. und Abrahams, J. P. (2013) „Capture of unstable protein complex on the streptavidin-coated single-walled carbon nanotubes “, Journal of Nanoparticle Research, 15(4), S. A 1582. 10.1007/s11051-013-1582-9.   edoc
Luo, J., Yu, C.-H., Yu, H., Borstnar, R., Kamerlin, S. C. L., Gräslund, A., Abrahams, J. P. und Wärmländer, S. K. T. S. (2013) „Cellular Polyamines Promote Amyloid-Beta Peptide Fibrillation and Modulate the Aggregation Pathways“, Biophysical Journal. Cell Press. 10.1016/j.bpj.2012.11.2170.   edoc
Nederlof, I., Li, Y. W., van Heel, M. und Abrahams, J. P. (2013) „Imaging protein three-dimensional nanocrystals with cryo-EM“, Acta Crystallographica. Section D, Biological Crystallography, 69, S. 852–859. 10.1107/S0907444913002734.   edoc
Luo, J., Yu, C.-H., Yu, H., Borstnar, R., Kamerlin, S. C. L., Gräslund, A., Abrahams, J. P. und Wärmländer, S. K. T. S. (2013) „Cellular Polyamines Promote Amyloid-Beta (A beta) Peptide Fibrillation and Modulate the Aggregation Pathways“, ACS Chemical Neuroscience , 4(3), S. 454–462. 10.1021/cn300170x.   edoc
Nederlof, I., van Genderen, E., Li, Y.-W. und Abrahams, J. P. (2013) „A Medipix quantum area detector allows rotation electron diffraction data collection from submicrometre three-dimensional protein crystals“, Acta Crystallographica. Section D, Biological Crystallography, 69, S. 1223–1230. 10.1107/S0907444913009700.   edoc
Luo, J., Zwier, R. und Abrahams, J. P. (2013) „An efficient nanolitre-volume multi-channel device for highly viscous materials used in membrane protein crystallization“, Journal of applied crystallography, 46, S. 829–831. 10.1107/S0021889813006742.   edoc
Luo, J., Wärmländer, S. K. T. S., Gräslund, A. und Abrahams, J. P. (2013) „Human lysozyme inhibits the in vitro aggregation of Aβ peptides, which in vivo are associated with Alzheimer’s disease“, Chemical Communications , 49(58), S. 6507–6509. 10.1039/c3cc42325e.   edoc
Luo, J., Otero, J. M., Yu, C.-H., Wärmländer, S. K. T. S., Gräslund, A., Overhand, M. und Abrahams, J. P. (2013) „Inhibiting and Reversing Amyloid‐β Peptide (1–40) Fibril Formation with Gramicidin S and Engineered Analogues “, Chemistry - A European Journal, 19(51), S. 17338–17348. 10.1002/chem.201301535.   edoc
ten Bruggencate, F., Laroche, F., Zhang, Y., Song, G., Yin, S., Abrahams, J. P. und Liu, Z. (2013) „Visualizing the localization of transfection complexes during graphene nanoparticle-based transfection“, Journal of Materials Chemistry B, 1(46), S. 6353–6358. 10.1039/c3tb21349h.   edoc
Meulenbroek, E. M., Thomassen, E. A. J., Pouvreau, L., Abrahams, J. P., Gruppen, H. und Pannu, N. S. (2012) „Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serine protease inhibitor from potato“, Acta Crystallographica. Section D, Biological Crystallography, 68(Pt 7), S. 794–799. 10.1107/S090744491201222X.   edoc
Liu, Z., Galli, F., Waterreus, W.-J., Meulenbroek, E., Koning, R. I., Lamers, G. E. M., Olsthoorn, R. C. L., Pannu, N., Oosterkamp, T. H., Koster, A. J., Dame, R. T. und Abrahams, J. P. (2012) „Single-walled carbon nanotubes as scaffolds to concentrate DNA for the study of DNA-protein interactions“, ChemPhysChem, 13(6), S. 1569–1575. 10.1002/cphc.201100896.   edoc
Nederlof, I., Georgieva, D. und Abrahams, J. P. (2011) „Electron diffraction of submicron 3D protein crystals“, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. 10.1107/S010876731109430X.   edoc
Nicolopoulos, S., Rauch, E., Georgieva, D. und Abrahams, J. P. (2011) „Low resolution electron crystallography challenges in organic and inorganic crystals with transmission electron microscope (TEM)“, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. 10.1107/S0108767311095304.   edoc
Waterreus, W.-J., Skubák, P., Sikharulidze, I., Abrahams, J. P., de Graaff, R. A. G. und Pannu, N. S. (2011) „Advances in the CRANK software suite for automated crystal structure solution“, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. 10.1107/S0108767311083346.   edoc
Abrahams, J.-P., Apweiler, R., Balling, R., Bertero, M. G., Bujnicki, J. M., Chayen, N. E., Chène, P., Corthals, G. L., Dyląg, T., Förster, F., Heck, A. J. R., Henderson, P. J. F., Herwig, R., Jehenson, P., Kokalj, S. J., Laue, E., Legrain, P., Martens, L., Migliorini, C., Musacchio, A., Podobnik, M., Schertler, G. F. X., Schreiber, G., Sixma, T. K., Smit, A. B., Stuart, D., Svergun, D. I. und Taussig, M. J. (2011) „‚4D Biology for health and disease‘ workshop report“, New biotechnology, 28(4), S. 291–293. 10.1016/j.nbt.2010.10.003.   edoc
Jiang, L., Georgieva, D., Nederlof, I., Liu, Z. und Abrahams, J. P. (2011) „Image processing and lattice determination for three-dimensional nanocrystals“, Microscopy and Microanalysis, 17(6), S. 879–885. 10.1017/S1431927611012244.   edoc
Pannu, N. S., Waterreus, W. J., Skubák, P., Sikharulidze, I., Abrahams, J. P. und de Graaff, R. A. G. (2011) „Recent advances in the CRANK software suite for experimental phasing“, Acta Crystallographica. Section D, Biological Crystallography, 67(Pt 4), S. 331–337. 10.1107/S0907444910052224.   edoc
Sikharulidze, I., Van Gastel, R., Schramm, S., Abrahams, J. P., Poelsema, B., Trom, R. M. und Van der Molen, S. J. (2010) „Improved Imaging in low Energy Electron Microscopy and Photo Emission Electron Microscopy Using Medipix2 Pixel Detector“, in Leroy, C., Rancoita, P.-G., Barone, M., Gaddi, A., Price, L., und Ruchti, R. (Hrsg.) Astroparticle, Particle and Space Physics, Detectors and Medical Physics Applications. Proceedings of the 11th Conference, Villa Olmo, Como, Italy, 5-9 October 2009. Singapore: World Scientific (Astroparticle, Particle, Space Physics, Radiation Interaction, Detectors and Medical Physics Applications), S. 133–139. 10.1142/9789814307529_0023.   edoc
Abrahams, J. P. (2010) „The strong phase object approximation may allow extending crystallographic phases of dynamical electron diffraction patterns of 3D protein nano-crystals“, Zeitschrift für Kristallographie - Crystalline Materials, 225(2-3), S. 67–76. 10.1524/zkri.2010.1216.   edoc
Liu, Z., Galli, F., Janssen, K. G. H., Jiang, L., van der Linden, H. J., de Geus, D. C., Voskamp, P., Kuil, M. E., Olsthoorn, R. C. L., Oosterkamp, T. H., Hankemeier, T. und Abrahams, J. P. (2010) „Stable Single-Walled Carbon Nanotube-Streptavidin Complex for Biorecognition“, Journal of Physical Chemistry C, 114(10), S. 4345–4352. 10.1021/jp911441d.   edoc
Liu, Z., Jiang, L., Galli, F., Nederlof, I., Olsthoorn, R. C. L., Lamers, G. E. M., Oosterkamp, T. H. und Abrahams, J. P. (2010) „A Graphene Oxide center dot Streptavidin Complex for Biorecognition - Towards Affinity Purification“, Advanced Functional Materials, 20(17), S. 2857–2865. 10.1002/adfm.201000761; 10.1002/adfm.201000761.   edoc
Jiang, L., Liu, Z., Georgieva, D., Kuil, M. E. und Abrahams, J. P. (2010) „A novel approximation method of CTF amplitude correction for 3D single particle reconstruction“, Ultramicroscopy, 110(4), S. 350–358. 10.1016/j.ultramic.2010.01.011.   edoc
De Geus, D. C., Van Roon, A. M. M., Thomassen, E. A. J., Hokke, C. H., Deelder, A. M. und Abrahams, J. P. (2009) „2VQ1: Anti Trimeric Lewis X Fab54-5C10-A“, Worldwide Protein Data Bank, S. 2VQ1. 10.2210/pdb2vq1/pdb.   edoc
De Geus, D. C., Thomassen, E. A. J., Hagedoorn, P. L., Pannu, N. S. und Abrahams, J. P. (2009) „2VXH: The Crystal Structure Of Chlorite Dismutase: A Detox Enzyme Producing Molecular Oxygen“, Worldwide Protein Data Bank, S. 2VXH. 10.2210/pdb2vxh/pdb.   edoc
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Jiang, L., Schaffitzel, C., Bingel-Erlenmeyer, R., Ban, N., Korber, P., Koning, R. I., Plaisier, J. R. und Abrahams, J. P. (2008) „EMD-1455: Recycling of Aborted Ribosomal 50S Subunit-Nascent Chain-tRNA Complexes by the Heat Shock Protein Hsp15“, Journal of Molecular Biology, ‏ 386(5), S. –. 10.1016/j.jmb.2008.10.079 .   edoc
Jiang, L., Schaffitzel, C., Bingel-Erlenmeyer, R., Ban, N., Korber, P., Koning, R. I., Plaisier, J. R. und Abrahams, J. P. (2008) „EMD-1456.map“, Electron Microscopy Data Bank, S. EMD–1456.map.   edoc
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Zovko, S., Abrahams, J. P., Koster, A. J., Galjart, N. und Mommaas, A. M. (2008) „Microtubule plus-end conformations and dynamics in the periphery of interphase mouse fibroblasts“, Molecular Biology of the Cell, 19(7), S. 3138–3146. 10.1091/mbc.E07-07-0681.   edoc
de Geus, D. C., Thomassen, E. A. J., van der Feltz, C. L. und Abrahams, J. P. (2008) „Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of chlorite dismutase: a detoxifying enzyme producing molecular oxygen“, Acta Crystallographica Section F, 64, S. 730–732. 10.1107/S1744309108020551.   edoc
Paspaleva, K., Thomassen, E., Pannu, N. S., Iwai, S., Moolenaar, G. F., Goosen, N. und Abrahams, J. P. (2007) „Crystal structure of the DNA repair enzyme ultraviolet damage endonuclease“, Structure, 15(10), S. 1316–1324. 10.1016/j.str.2007.05.010.   edoc
Georgieva, D. G., Kuil, M. E., Oosterkamp, T. H., Zandbergen, H. W. und Abrahams, J. P. (2007) „Heterogeneous nucleation of three-dimensional protein nanocrystals“, Acta Crystallographica. Section D, Biological Crystallography, 63, S. 564–570. 10.1107/S0907444907007810.   edoc
Plaisier, J. R., Jiang, L. und Abrahams, J. P. (2007) „Cyclops: New modular software suite for cryo-EM“, Journal of structural biology, 157(1), S. 19–27. 10.1016/j.jsb.2006.07.002.   edoc
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I. und Ban, N. (2007) „Erratum: Structure of the E-coli signal recognition particle bound to a translating ribosome (vol 444, pg 503, 2006)“, Nature, 448(7157), S. 1076. 10.1038/nature06169.   edoc
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I. und Ban, N. (2006) „2IY3“, Nucleic Acid Database, S. 2iy3. 10.2210/pdb2iy3/pdb.   edoc
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I. und Ban, N. (2006) „2IY3: Structure of the E. Coli Signal Regognition Particle“, Worldwide Protein Data Bank, S. 2IY3. 10.2210/pdb2iy3/pdb.   edoc
Thomassen, E. A. J., Dekking, E. H. A., Thompson, A., Franken, K. L., Sanal, Ö., Abrahams, J. P., van Tol, M. J. D. und Koning, F. (2006) „The Impact of Single Amino Acid Substitutions in CD3γ on the CD3ϵγ Interaction and T-Cell Receptor–CD3 Complex Formation“, Human immunology, 67(8), S. 579–588. 10.1016/j.humimm.2006.04.015.   edoc
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I. und Ban, N. (2006) „Structure of the E. coli signal recognition particle bound to a translating ribosome“, Nature, 444(7118), S. 503–506. 10.1038/nature05182.   edoc
Kuil, M. E., Abrahams, J. P. und Marijnissen, J. C. M. (2006) „Nano-dispensing by electrospray for biotechnology“, Biotechnology journal, 1(9), S. 969–975. 10.1002/biot.200600062.   edoc
Schmauder, R., van Rijn, R., Abrahams, J. P., Kuil, M. E. und Schmidt, T. (2005) „FCS in non-ideal solutions“, Biophysical Journal. Biophysical Society.   edoc
Thomassen, E. A. J., van Veen, H. A., van Berkel, P. H. C., Nuijens, J. H. und Abrahams, J. P. (2005) „The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin“, Transgenic Research, 14(4), S. 397–405. 10.1007/s11248-005-3233-0.   edoc
Van Roon, A. M. M., Pannu, N. S., De Vrind, J. P. M., Hokke, C. H., Deelder, A. M., Van Der Marel, G. A., Van Boom, J. H. und Abrahams, J. P. (2004) „1UZ6: Anti-Lewis X Fab Fragment Uncomplexed“, Worldwide Protein Data Bank, S. 1UZ6. 10.2210/pdb1uz6/pdb.   edoc
Van Roon, A. M. M., Pannu, N. S., De Vrind, J. P. M., Hokke, C. H., Deelder, A. M., Van Der Marel, G. A., Van Boom, J. H. und Abrahams, J. P. (2004) „1UZ8: Anti-Lewis X Fab Fragment In Complex With Lewis X“, Worldwide Protein Data Bank, S. 1UZ8. 10.2210/pdb1uz8/pdb.   edoc
Van Roon, A. M. M., Bink, H. H. J., Plaisier, J. R., Pleij, C. W. A., Abrahams, J. P. und Pannu, N. S. (2004) „1W39: Crystal Structure Of An Artificial Top Component Of Turnip Yellow Mosaic Virus“, Worldwide Protein Data Bank, S. 1W39. 10.2210/pdb1w39/pdb.   edoc
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Leliveld, S. R., Dame, R. T., Rohn, J. L., Noteborn, M. H. M. und Abrahams, J. P. (2004) „Apoptin’s functional N- and C-termini independently bind DNA“, FEBS Letters, 557(1-3), S. 155–158. 10.1016/S0014-5793(03)01465-0.   edoc
Thomassen, E. A. J., Pouvreau, L., Gruppen, H. und Abrahams, J. P. (2004) „Crystallization and preliminary X-ray crystallographic studies on a Kunitz-type potato serine protease inhibitor“, Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 8), S. 1464–1466. 10.1107/S0907444904013484.   edoc
van Roon, A.-M. M., Bink, H. H. J., Plaisier, J. R., Pleij, C. W. A., Abrahams, J. P. und Pannu, N. S. (2004) „Crystal structure of an empty capsid of turnip yellow mosaic virus“, Journal of Molecular Biology, 341(5), S. 1205–1214. 10.1016/j.jmb.2004.06.085.   edoc
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Plaisier, J. R., Koning, R. I., Koerten, H. K., van Heel, M. und Abrahams, J. P. (2004) „TYSON: robust searching, sorting, and selecting of single particles in electron micrographs“, Journal of Structural Biology, 145(1-2), S. 76–83. 10.1016/j.jsb.2003.09.030.   edoc
van Roon, A.-M. M., Pannu, N. S., de Vrind, J. P. M., van der Marel, G. A., van Boom, J. H., Hokke, C. H., Deelder, A. M. und Abrahams, J. P. (2004) „Structure of an anti-Lewis X Fab fragment in complex with its Lewis X antigen“, Structure, 12(7), S. 1227–1236. 10.1016/j.str.2004.05.008.   edoc
Bos, I. G. A., Lubbers, Y. T. P., Eldering, E., Abrahams, J. P. und Hack, C. E. (2004) „Effect of reactive site loop elongation on the inhibitory activity of C1-inhibitor“, Biochimica et Biophysica Acta - Proteins and Proteomics, 1699(1-2), S. 139–144. 10.1016/j.bbapap.2004.02.006.   edoc
Hilge, M., Siegal, G., Vuister, G. W., Guentert, P., Gloor, S. M. und Abrahams, J. P. (2003) „1MO8: ATPase“, Worldwide Protein Data Bank, S. 1MO8. 10.2210/pdb1mo8/pdb.   edoc
Hilge, M., Siegal, G., Vuister, G. W., Guentert, P., Gloor, S. M. und Abrahams, J. P. (2003) „1MO7: ATPase“, Worldwide Protein Data Bank, S. 1MO7. 10.2210/pdb1mo7/pdb.   edoc
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Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. und Abrahams, J. P. (2003) „ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase“, Nature Structural Biology, 10(6), S. 468–474. 10.1038/nsb924.   edoc
Zhang, Y.-H., Leliveld, S. R., Kooistra, K., Molenaar, C., Rohn, J. L., Tanke, H. J., Abrahams, J. P. und Noteborn, M. H. M. (2003) „Recombinant Apoptin multimers kill tumor cells but are nontoxic and epitope-shielded in a normal-cell-specific fashion“, Experimental Cell Research, 289(1), S. 36–46. 10.1016/S0014-4827(03)00188-5.   edoc
Abrahams, J. P. und Thomassen, E. A. J. (2003) „Mechanism of thrombin’s enigmatic sodium switch revealed“, Structure, 11(4), S. 363–364. 10.1016/S0969-2126(03)00056-X.   edoc
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Koning, R., van den Worm, S., Plaisier, J. R., van Duin, J., Abrahams, J. P. und Koerten, H. (2003) „Visualization by cryo-electron microscopy of genomic RNA that binds to the protein capsid inside bacteriophage MS2“, Journal of Molecular Biology, 332(2), S. 415–422. 10.1016/S0022-2836(03)00846-5.   edoc
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McCoy, A. J., Pei, X. Y., Skinner, R., Abrahams, J.-P. und Carrell, R. W. (2003) „Structure of beta-antithrombin and the effect of glycosylation on antithrombin’s heparin affinity and activity“, Journal of Molecular Biology, 326(3), S. 823–833. 10.1016/S0022-2836(02)01382-7.   edoc
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Hoedemaeker, F. J., Siegal, G., Roe, S. M., Driscoll, P. C. und Abrahams, J. P. (1999) „Crystal structure of the C-terminal SH2 domain of the p85 alpha regulatory subunit of phosphoinositide 3-kinase: An SH2 domain mimicking its own substrate (vol 292, pg 763, 1999)“, Journal of Molecular Biology, 294(3), S. 825. 10.1006/jmbi.1999.3337.   edoc
Leslie, A. G. W., Abrahams, J. P., Braig, K., Lutter, R., Menz, R. I., Orriss, G. L., van Raaij, M. J. und Walker, J. E. (1999) „The structure of bovine mitochondrial F-1-ATPase: an example of rotary catalysis“, Biochemical Society Transactions, 27(2), S. 37–42. 10.1042/bst0270037.   edoc
Shirakihara, Y., Leslie, A. G. W., Abrahams, J. P., Walker, J. E., Ueda, T., Sekimoto, Y., Kambara, M., Saika, K., Kagawa, Y. und Yoshida, M. (1998) „1SKY: Crystal Structure Of The Nucleotide Free Alpha3beta3 Sub-Complex Of F1-Atpase From The Thermophilic Bacillus Ps3“, Worldwide Protein Data Bank, S. 1SKY. 10.2210/pdb1sky/pdb.   edoc
Skinner, R., Chang, W. S. W., Jin, L., Pei, X. Y., Huntington, J. A., Abrahams, J. P., Carrell, R. W. und Lomas, D. A. (1998) „1BR8: Implications For Function And Therapy Of A 2.9A Structure Of Binary-Complexed Antithrombin“, Worldwide Protein Data Bank, S. 1BR8. 10.2210/pdb1br8/pdb.   edoc
Abrahams, J. P. und De Graaff, R. A. G. (1998) „New developments in phase refinement“, Current Opinion in Structural Biology, 8(5), S. 601–605. 10.1016/S0959-440X(98)80151-6.   edoc
Elliott, P. R., Abrahams, J.-P. und Lomas, D. A. (1998) „Wild-type alpha(1)-antitrypsin is in the canonical inhibitory conformation“, Journal of Molecular Biology, 275(3), S. 419–425. 10.1006/jmbi.1997.1458.   edoc
Skinner, R., Chang, W.-S. W., Jin, L., Pei, X., Huntington, J. A., Abrahams, J.-P., Carrell, R. W. und Lomas, D. A. (1998) „Implications for function and therapy of a 2.9 å structure of binary-complexed antithrombin“, Journal of Molecular Biology, 283(1), S. 9–14. 10.1006/jmbi.1998.2083.   edoc
Abrahams, J. P., Buchanan, S. K., Van Raaij, M. J., Fearnley, I. M., Leslie, A. G. W. und Walker, J. E. (1997) „1EFR: Bovine Mitochondrial F1-Atpase Complexed With The Peptide Antibiotic Efrapeptin“, Worldwide Protein Data Bank, S. 1EFR. 10.2210/pdb1efr/pdb.   edoc
Skinner, R., Abrahams, J.-P., Whisstock, J. C., Lesk, A. M., Carrell, R. W. und Wardell, M. R. (1997) „2ANT: The 2.6 A Structure Of Antithrombin Indicates A Conformational Change At The Heparin Binding Site“, Worldwide Protein Data Bank, S. 2ANT. 10.2210/pdb2ant/pdb.   edoc
Abrahams, J. P. (1997) „Bias reduction in phase refinement by modified interference functions: Introducing the gamma correction“, Acta Crystallographica. Section D, Biological Crystallography, 53, S. 371–376. 10.1107/S0907444996015272.   edoc
Skinner, R., Abrahams, J.-P., Whisstock, J. C., Lesk, A. M., Carrell, R. W. und Wardell, M. R. (1997) „The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site“, Journal of Molecular Biology, 266(3), S. 601–609. 10.1006/jmbi.1996.0798.   edoc
Jin, L., Abrahams, J. P., Skinner, R., Petitou, M., Pike, R. N. und Carrell, R. W. (1997) „The anticoagulant activation of antithrombin by heparin“, Proceedings of the National Academy of Sciences of the United States of America, 94(26), S. 14683–14688. 10.1073/pnas.94.26.14683.   edoc
Shirakihara, Y., Leslie, A. G. W., Abrahams, J. P., Walker, J. E., Ueda, T., Sekimoto, Y., Kambara, M., Saika, K., Kagawa, Y. und Yoshida, M. (1997) „The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F-1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer“, Structure, 5(6), S. 825–836. 10.1016/S0969-2126(97)00236-0.   edoc
Wardell, M. R., Skinner, R., Carter, D. C., Twigg, P. D. und Abrahams, J. P. (1997) „Improved diffraction of antithrombin crystals grown in microgravity“, Acta Crystallographica. Section D, Biological Crystallography, 53, S. 622–625. 10.1107/S0907444997003302.   edoc
Carrell, R., Skinner, R., Jin, L. und Abrahams, J. P. (1997) „Structural mobility of antithrombin and its modulation by heparin“, Thrombosis and Haemostasis, 78(1), S. 516–519.   edoc
Abrahams, J. P., Leslie, A. G. W., Lutter, R. und Walker, J. E. (1996) „1BMF: Bovine Mitochondrial F1-Atpase“, Worldwide Protein Data Bank, S. 1BMF. 10.2210/pdb1bmf/pdb.   edoc
Van Raaij, M., Abrahams, J. P., Leslie, A. G. W. und Walker, J. E. (1996) „1COW: Bovine Mitochondrial F1-Atpase Complexed With Aurovertin B“, Worldwide Protein Data Bank, S. 1COW. 10.2210/pdb1cow/pdb.   edoc
Abrahams, J. P., Elliott, P. R., Lomas, D. A. und Carrell, R. W. (1996) „1PSI: Intact recombined alpha1-antitrypsin mutant PHE 51 to LEU“, Worldwide Protein Data Bank, S. 1PSI. 10.2210/pdb1psi/pdb.   edoc
Abrahams, J. P., Leslie, A. G. W., Lutter, R. und Walker, J. E. (1996) „The structure of bovine mitochondrial F1-ATPase - An insight into ATP synthesis“, Biophysical Journal. Cell Press.   edoc
Leslie, A. G. W., Abrahams, J. P., van Raaij, M., Lutter, R. und Walker, J. E. (1996) „The structure of bovine mitochondrial F1-ATPase - an example of rotational catalysis?“, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. 10.1107/S010876739609890X.   edoc
van Raaij, M. J., Abrahams, J. P., Leslie, A. G. W. und Walker, J. E. (1996) „The structure of bovine F-1-ATPase complexed with the antibiotic inhibitor aurovertin B“, Proceedings of the National Academy of Sciences of the United States of America, 93(14), S. 6913–6917. 10.1073/pnas.93.14.6913.   edoc
Abrahams, J. P. und Leslie, A. G. W. (1996) „Methods used in the structure determination of bovine mitochondrial F-1 ATPase“, Acta Crystallographica. Section D, Biological Crystallography, 52, S. 30–42. 10.1107/S0907444995008754.   edoc
Abrahams, J. P., Buchanan, S. K., van Raaij, M. J., Fearnley, I. M., Leslie, A. G. W. und Walker, J. E. (1996) „The structure of bovine F-1-ATPase complexed with the peptide antibiotic efrapeptin“, Proceedings of the National Academy of Sciences of the United States of America, 93(18), S. 9420–9424. 10.1073/pnas.93.18.9420.   edoc
Elliott, P. R., Lomas, D. A., Carrell, R. W. und Abrahams, J. P. (1996) „Inhibitory conformation of the reactive loop of alpha(1)-antitrypsin“, Nature Structural biology, 3(8), S. 676–681. 10.1038/nsb0896-676.   edoc
Abrahams, J. P., Leslie, A. G. W., Lutter, R. und Walker, J. E. (1994) „Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria“, Nature, 370(6491), S. 621–628. 10.1038/370621a0.   edoc
Abrahams, J. P., Lutter, R., Todd, R. J., Van Raaij, M. J., Leslie, A. G. W. und Walker, J. E. (1993) „Inherent asymmetry of the structure of F1‐ATPase from bovine heart mitochondria at 6.5 A resolution“, The EMBO journal, 12(5), S. 1775–1780. 10.1002/j.1460-2075.1993.tb05825.x.   edoc
Wardell, M. R., Abrahams, J.-P., Bruce, D., Skinner, R. und Leslie, A. G. W. (1993) „Crystallization and Preliminary X-ray Diffraction Analysis of Two Conformations of Intact Human Antithrombin“, Journal of Molecular Biology, 234(4), S. 1253–1258. 10.1006/jmbi.1993.1676.   edoc
Lutter, R., Abrahams, J. P., Van Raaij, M. J., Todd, R. J., Lundqvist, T., Buchanan, S. K., Leslie, A. G. W. und Walker, J. E. (1993) „Crystallization of F1-ATPase from Bovine Heart Mitochondria“, Journal of Molecular Biology, 229(3), S. 787–790. 10.1006/jmbi.1993.1081.   edoc
Abrahams, J. P., Bosch, L., Kraal, B., De Groot, H. J. M., Raap, J. und Lugtenburg, J. (1992) „Magic angle spinning carbon-13 NMR analysis of the complex of elongation factor Tu, GTP and (1-carbon-13) phenylalanyl-tRNA-Phe“, Spectroscopy (Amsterdam), 10(1-6), S. 1–8.   edoc
Abrahams, J. P., Acampo, J. J. C., Kraal, B. und Bosch, L. (1991) „The influence of tRNA located at the P-site on the turnover of EF-Tu·GTP on ribosomes “, Biochimie, 73(7-8), S. 1089–1092. 10.1016/0300-9084(91)90150-Y.   edoc
Abrahams, J. P., Kraal, B., Clark, B. F. C. und Bosch, L. (1991) „Isolation and stability of ternary complexes of elongation factor Tu, GTP and aminoacyl-tRNA “, Nucleic Acids Research, 19(3), S. 553–556. 10.1093/nar/19.3.553.   edoc
Abrahams, J. P., Van Raaij, M. J., Ott, G., Kraal, B. und Bosch, L. (1991) „Kirromycin drastically reduces the affinity of Escherichia coli elongation factor Tu for aminoacyl-tRNA“, Biochemistry, 30(27), S. 6705–6710. 10.1021/bi00241a010.   edoc
Abrahams, J. P., Acampo, J. J. C., Ott, G., Sprinzl, M., Degraaf, J. M., Talens, A. und Kraal, B. (1990) „THE INTERACTION BETWEEN AMINOACYL-TRANSFER RNA AND THE MUTANT ELONGATION FACTOR-TUAR AND FACTOR-TUBO“, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1050(1-3), S. 226–229. 10.1016/0167-4781(90)90171-W.   edoc
Abrahams, J. P., Vandenberg, M., Van Batenburg, E. und Pleij, C. (1990) „Prediction of RNA secondary structure, including pseudoknotting, by computer simulation“, Nucleic Acids Research, 18(10), S. 3035–3044. 10.1093/nar/18.10.3035.   edoc
Kraal, B., Abrahams, J. P. und Bosch, L. (1989) „Effects Of Kirromycin On The Elongation Factor-Ef-Tu And Its Interactions With Gdp Or Gtp And Transfer-Rna - The Application Of Zone-Interference Gel-Electrophoresis, A New Method For The Analysis Of Weak Complexes“, in Bosch, L., Kraal, B., und Parmeggiani, A. (Hrsg.) The guanine-nucleotide binding proteins. Common structural and functional properties. New York: Plenum Press (NATO ASI series. Series A, Life sciences, 165), S. 121–129.   edoc
Abrahams, J. P., Kraal, B. und Bosch, L. (1988) „Zone-interference gel electrophoresis: a new method for studying weak protein-nucleic acid complexes under native equilibrium conditions“, Nucleic Acids Research, 16(21), S. 10099–10108. 10.1093/nar/16.21.10099.   edoc
Pleij, C. W. A., Abrahams, J. P., Van Belkum, A., Rietveld, K. und Bosch, L. (1986) „The Spatial Folding Of The 3’ Noncoding Region Of Aminoacylatable Plant Viral RNAs“, Journal of Cellular Biochemistry. Wiley.   edoc
Van Belkum, A., Abrahams, J. P., Pleij, C. W. A. und Bosch, L. (1985) „Five pseudoknots are present at the 204 nucleotides long 3’ noncoding region of tobacco mosak virus RNA“, Nucleic Acids Research, 13(21), S. 7673–7686. 10.1093/nar/13.21.7673.   edoc