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Mohammed, Inayathulla, Schmitz, Kai A., Schenck, Niko, Balasopoulos, Dimitrios, Topitsch, Annika, Maier, Timm, & Structure, 30(9), 1254–1268. https://doi.org/10.1016/j.str.2022.06.006
. (2022). Catalytic cycling of human mitochondrial Lon protease.
Mohammed, Inayathulla, Schmitz, Kai A., Schenck, Niko, Balasopoulos, Dimitrios, Topitsch, Annika, Maier, Timm, & Structure, 30(9), 1254–1268. https://doi.org/10.1016/j.str.2022.06.006
. (2022). Catalytic cycling of human mitochondrial Lon protease.
Blum, Thorsten B., Housset, Dominique, Clabbers, Max T. B., van Genderen, Eric, Bacia-Verloop, Maria, Zander, Ulrich, McCarthy, Andrew A., Schoehn, Guy, Ling, Wai Li, & Acta Crystallographica Section D: Structural Biology, 77(Pt 1), 75–85. https://doi.org/10.1107/s2059798320014540
. (2021). Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals.
Blum, Thorsten B., Housset, Dominique, Clabbers, Max T. B., van Genderen, Eric, Bacia-Verloop, Maria, Zander, Ulrich, McCarthy, Andrew A., Schoehn, Guy, Ling, Wai Li, & Acta Crystallographica Section D: Structural Biology, 77(Pt 1), 75–85. https://doi.org/10.1107/s2059798320014540
. (2021). Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals.
Blum, Thorsten B., Housset, Dominique, Clabbers, Max T. B., van Genderen, Eric, Bacia-Verloop, Maria, Zander, Ulrich, McCarthy, Andrew A., Schoehn, Guy, Li Ling, Wai, & Statistically correcting dynamical electron scattering improves refinement of protein nanocrystals, including charge refinement of coordinated metals. bioRxiv. https://doi.org/10.1101/2020.07.08.191049
. (2020).
Blum, Thorsten B., Housset, Dominique, Clabbers, Max T. B., van Genderen, Eric, Bacia-Verloop, Maria, Zander, Ulrich, McCarthy, Andrew A., Schoehn, Guy, Li Ling, Wai, & Statistically correcting dynamical electron scattering improves refinement of protein nanocrystals, including charge refinement of coordinated metals. bioRxiv. https://doi.org/10.1101/2020.07.08.191049
. (2020).
Matz, Joachim M., Drepper, Benjamin, Blum, Thorsten B., van Genderen, Eric, Burrell, Alana, Martin, Peer, Stach, Thomas, Collinson, Lucy, bioRxiv. bioRxiv. https://doi.org/10.1101/2020.02.18.954289
, Matuschewski, Kai, & Blackman, Michael J. (2020). A lipocalin mediates unidirectional haem biomineralization in malaria parasites. In
Matz, Joachim M., Drepper, Benjamin, Blum, Thorsten B., van Genderen, Eric, Burrell, Alana, Martin, Peer, Stach, Thomas, Collinson, Lucy, bioRxiv. bioRxiv. https://doi.org/10.1101/2020.02.18.954289
, Matuschewski, Kai, & Blackman, Michael J. (2020). A lipocalin mediates unidirectional haem biomineralization in malaria parasites. In
Matz, Joachim M., Drepper, Benjamin, Blum, Thorsten B., van Genderen, Eric, Burrell, Alana, Martin, Peer, Stach, Thomas, Collinson, Lucy M., Proceedings of the National Academy of Sciences of the United States of America, 117(28), 16546–16556. https://doi.org/10.1073/pnas.2001153117
, Matuschewski, Kai, & Blackman, Michael J. (2020). A lipocalin mediates unidirectional heme biomineralization in malaria parasites.
Matz, Joachim M., Drepper, Benjamin, Blum, Thorsten B., van Genderen, Eric, Burrell, Alana, Martin, Peer, Stach, Thomas, Collinson, Lucy M., Proceedings of the National Academy of Sciences of the United States of America, 117(28), 16546–16556. https://doi.org/10.1073/pnas.2001153117
, Matuschewski, Kai, & Blackman, Michael J. (2020). A lipocalin mediates unidirectional heme biomineralization in malaria parasites.
Merg, Andrea D., Touponse, Gavin, van Genderen, Eric, Blum, Thorsten B., Zuo, Xiaobing, Bazrafshan, Alisina, Siaw, Hew Ming Helen, McCanna, Arthur, Dyer, R. Brian, Salaita, Khalid, Journal of the American Chemical Society, 142(47), 19956–19968. https://doi.org/10.1021/jacs.0c08174
, & Conticello, Vincent P. (2020). Shape-Shifting Peptide Nanomaterials: Surface Asymmetry Enables pH-Dependent Formation and Interconversion of Collagen Tubes and Sheets.
Merg, Andrea D., Touponse, Gavin, van Genderen, Eric, Blum, Thorsten B., Zuo, Xiaobing, Bazrafshan, Alisina, Siaw, Hew Ming Helen, McCanna, Arthur, Dyer, R. Brian, Salaita, Khalid, Journal of the American Chemical Society, 142(47), 19956–19968. https://doi.org/10.1021/jacs.0c08174
, & Conticello, Vincent P. (2020). Shape-Shifting Peptide Nanomaterials: Surface Asymmetry Enables pH-Dependent Formation and Interconversion of Collagen Tubes and Sheets.
Thakkar, Pooja, Guzenko, Vitaliy A., Lu, Peng-Han, Dunin-Borkowski, Rafal E., Journal of Applied Physics, 128(13), 134502. https://doi.org/10.1063/5.0020383
, & Tsujino, Soichiro. (2020). Fabrication of low aspect ratio three-element Boersch phase shifters for voltage-controlled three electron beam interference.
Thakkar, Pooja, Guzenko, Vitaliy A., Lu, Peng-Han, Dunin-Borkowski, Rafal E., Journal of Applied Physics, 128(13), 134502. https://doi.org/10.1063/5.0020383
, & Tsujino, Soichiro. (2020). Fabrication of low aspect ratio three-element Boersch phase shifters for voltage-controlled three electron beam interference.
van Schayck, J. Paul, van Genderen, Eric, Maddox, Erik, Roussel, Lucas, Boulanger, Hugo, Fröjdh, Erik, Ultramicroscopy, 218, 113091. https://doi.org/10.1016/j.ultramic.2020.113091
, Peters, Peter J., & Ravelli, Raimond B. G. (2020). Sub-pixel electron detection using a convolutional neural network.
van Schayck, J. Paul, van Genderen, Eric, Maddox, Erik, Roussel, Lucas, Boulanger, Hugo, Fröjdh, Erik, Ultramicroscopy, 218, 113091. https://doi.org/10.1016/j.ultramic.2020.113091
, Peters, Peter J., & Ravelli, Raimond B. G. (2020). Sub-pixel electron detection using a convolutional neural network.
Xiao, Xiansha, Elsayed, Somayah S., Wu, Changsheng, van der Heul, Helga U., Metsä-Ketelä, Mikko, Du, Chao, Prota, Andrea E., Chen, Chun-Chi, Liu, Weidong, Guo, Rey-Ting, ACS Chemical Biology, 15(9), 2529–2538. https://doi.org/10.1021/acschembio.0c00564
, & van Wezel, Gilles P. (2020). Functional and Structural Insights into a Novel Promiscuous Ketoreductase of the Lugdunomycin Biosynthetic Pathway.
Xiao, Xiansha, Elsayed, Somayah S., Wu, Changsheng, van der Heul, Helga U., Metsä-Ketelä, Mikko, Du, Chao, Prota, Andrea E., Chen, Chun-Chi, Liu, Weidong, Guo, Rey-Ting, ACS Chemical Biology, 15(9), 2529–2538. https://doi.org/10.1021/acschembio.0c00564
, & van Wezel, Gilles P. (2020). Functional and Structural Insights into a Novel Promiscuous Ketoreductase of the Lugdunomycin Biosynthetic Pathway.
Zhang, Zhenzhen, Wen, Kai, Zhang, Chao, Laroche, Fabrice, Wang, Zhenglong, Zhou, Qiang, Liu, Zunfeng, Frontiers in Bioengineering and Biotechnology, 8, 448. https://doi.org/10.3389/fbioe.2020.00448
, & Zhou, Xiang. (2020). Extracellular Nanovesicle Enhanced Gene Transfection Using Polyethyleneimine in HEK293T Cells and Zebrafish Embryos.
Zhang, Zhenzhen, Wen, Kai, Zhang, Chao, Laroche, Fabrice, Wang, Zhenglong, Zhou, Qiang, Liu, Zunfeng, Frontiers in Bioengineering and Biotechnology, 8, 448. https://doi.org/10.3389/fbioe.2020.00448
, & Zhou, Xiang. (2020). Extracellular Nanovesicle Enhanced Gene Transfection Using Polyethyleneimine in HEK293T Cells and Zebrafish Embryos.
Blum, T. B., & Worldwide Protein Data Bank, 6T17. https://doi.org/10.2210/pdb6t17/pdb
(2019). 6T17: Cryo-EM structure of the wild-type flagellar filament of the Firmicute Kurthia.
Blum, T. B., & Worldwide Protein Data Bank, 6T17. https://doi.org/10.2210/pdb6t17/pdb
(2019). 6T17: Cryo-EM structure of the wild-type flagellar filament of the Firmicute Kurthia.
Blum, Thorsten B., Filippidou, Sevasti, Fatton, Mathilda, Junier, Pilar, & Scientific Reports, 9(1), 14948. https://doi.org/10.1038/s41598-019-51440-1
. (2019). The wild-type flagellar filament of the Firmicute Kurthia at 2.8 Å resolution in vivo.
Blum, Thorsten B., Filippidou, Sevasti, Fatton, Mathilda, Junier, Pilar, & Scientific Reports, 9(1), 14948. https://doi.org/10.1038/s41598-019-51440-1
. (2019). The wild-type flagellar filament of the Firmicute Kurthia at 2.8 Å resolution in vivo.
Clabbers, Max T. B., Gruene, Tim, van Genderen, Eric, & Acta Crystallographica. Section A, Foundations and Advances, 75(Pt 1), 82–93. https://doi.org/10.1107/s2053273318013918
. (2019). Reducing dynamical electron scattering reveals hydrogen atoms.
Clabbers, Max T. B., Gruene, Tim, van Genderen, Eric, & Acta Crystallographica. Section A, Foundations and Advances, 75(Pt 1), 82–93. https://doi.org/10.1107/s2053273318013918
. (2019). Reducing dynamical electron scattering reveals hydrogen atoms.
Gemmi, Mauro, Mugnaioli, Enrico, Gorelik, Tatiana E., Kolb, Ute, Palatinus, Lukas, Boullay, Philippe, Hovmöller, Sven, & ACS Central Science, 5(8), 1315–1329. https://doi.org/10.1021/acscentsci.9b00394
. (2019). 3D Electron Diffraction: The Nanocrystallography Revolution.
Gemmi, Mauro, Mugnaioli, Enrico, Gorelik, Tatiana E., Kolb, Ute, Palatinus, Lukas, Boullay, Philippe, Hovmöller, Sven, & ACS Central Science, 5(8), 1315–1329. https://doi.org/10.1021/acscentsci.9b00394
. (2019). 3D Electron Diffraction: The Nanocrystallography Revolution.
Latychevskaia, Tatiana, & Acta Crystallographica Section B-Structural Science Crystal Engineering and Materials, 75, 523–531. https://doi.org/10.1107/s2052520619009661
. (2019). Inelastic scattering and solvent scattering reduce dynamical diffraction in biological crystals.
Latychevskaia, Tatiana, & Acta Crystallographica Section B-Structural Science Crystal Engineering and Materials, 75, 523–531. https://doi.org/10.1107/s2052520619009661
. (2019). Inelastic scattering and solvent scattering reduce dynamical diffraction in biological crystals.
Merg, Andrea D., Touponse, Gavin, van Genderen, Eric, Zuo, Xiaobing, Bazrafshan, Alisina, Blum, Thorsten, Hughes, Spencer, Salaita, Khalid, Angewandte Chemie (International Ed. In English), 58(38), 13507–13512. https://doi.org/10.1002/anie.201906214
, & Conticello, Vincent P. (2019). 2D Crystal Engineering of Nanosheets Assembled from Helical Peptide Building Blocks.
Merg, Andrea D., Touponse, Gavin, van Genderen, Eric, Zuo, Xiaobing, Bazrafshan, Alisina, Blum, Thorsten, Hughes, Spencer, Salaita, Khalid, Angewandte Chemie (International Ed. In English), 58(38), 13507–13512. https://doi.org/10.1002/anie.201906214
, & Conticello, Vincent P. (2019). 2D Crystal Engineering of Nanosheets Assembled from Helical Peptide Building Blocks.
Merg, Andrea D., van Genderen, Eric, Bazrafshan, Alisina, Su, Hanquan, Zuo, Xiaobing, Touponse, Gavin, Blum, Thorsten B., Salaita, Khalid, Journal of the American Chemical Society, 141(51), 20107–20117. https://doi.org/10.1021/jacs.9b09335
, & Conticello, Vincent P. (2019). Seeded Heteroepitaxial Growth of Crystallizable Collagen Triple Helices: Engineering Multifunctional Two-Dimensional Core-Shell Nanostructures.
Merg, Andrea D., van Genderen, Eric, Bazrafshan, Alisina, Su, Hanquan, Zuo, Xiaobing, Touponse, Gavin, Blum, Thorsten B., Salaita, Khalid, Journal of the American Chemical Society, 141(51), 20107–20117. https://doi.org/10.1021/jacs.9b09335
, & Conticello, Vincent P. (2019). Seeded Heteroepitaxial Growth of Crystallizable Collagen Triple Helices: Engineering Multifunctional Two-Dimensional Core-Shell Nanostructures.
Moradi, Mina, Opara, Nadia L., Tulli, Ludovico G., Wäckerlin, Christian, Dalgarno, Scott J., Teat, Simon J., Baljozovic, Milos, Popova, Olha, van Genderen, Eric, Kleibert, Armin, Stahlberg, Henning, Science Advances, 5(2), eaav4489. https://doi.org/10.1126/sciadv.aav4489
, Padeste, Celestino, Corvini, Philippe F.-X., Jung, Thomas A., & Shahgaldian, Patrick. (2019). Supramolecular architectures of molecularly thin yet robust free-standing layers.
Moradi, Mina, Opara, Nadia L., Tulli, Ludovico G., Wäckerlin, Christian, Dalgarno, Scott J., Teat, Simon J., Baljozovic, Milos, Popova, Olha, van Genderen, Eric, Kleibert, Armin, Stahlberg, Henning, Science Advances, 5(2), eaav4489. https://doi.org/10.1126/sciadv.aav4489
, Padeste, Celestino, Corvini, Philippe F.-X., Jung, Thomas A., & Shahgaldian, Patrick. (2019). Supramolecular architectures of molecularly thin yet robust free-standing layers.
Wallin, Cecilia, Hiruma, Yoshitaka, Warmlander, Sebastian, Huvent, Isabelle, Jarvet, Juri, Biophysical Journal, 116(3, Supplement 1), Article 3, Supplement 1. https://doi.org/10.1016/j.bpj.2018.11.1657
, Graslund, Astrid, Lippens, Guy, & Luo, Jinghui. (2019). The Neuronal Tau Protein Blocks In Vitro Fibrillation of the Amyloid-beta (A beta) Peptide (Patent No. 3, Supplement 1).
Wallin, Cecilia, Hiruma, Yoshitaka, Warmlander, Sebastian, Huvent, Isabelle, Jarvet, Juri, Biophysical Journal, 116(3, Supplement 1), Article 3, Supplement 1. https://doi.org/10.1016/j.bpj.2018.11.1657
, Graslund, Astrid, Lippens, Guy, & Luo, Jinghui. (2019). The Neuronal Tau Protein Blocks In Vitro Fibrillation of the Amyloid-beta (A beta) Peptide (Patent No. 3, Supplement 1).
Acta Crystallographica A-Foundation and Advances, 74, E83. https://doi.org/10.1107/s205327331809397x
, Clabbers, Max, van Genderen, Eric, & Blum, Thorsten. (2018). Electron tomography of radiation sensitive 3D nano-crystals in imaging and diffraction mode [International Union of Crystallography].
Acta Crystallographica A-Foundation and Advances, 74, E83. https://doi.org/10.1107/s205327331809397x
, Clabbers, Max, van Genderen, Eric, & Blum, Thorsten. (2018). Electron tomography of radiation sensitive 3D nano-crystals in imaging and diffraction mode [International Union of Crystallography].
Clabbers, Max, Gruene, Tim, van Genderen, Eric, & Acta Crystallographica A-Foundation and Advances, 74, E426. https://doi.org/10.1107/s2053273318088770
. (2018). Experimental and computational reduction of dynamical electron scattering allows visualizing individual hydrogen atoms [International Union of Crystallography].
Clabbers, Max, Gruene, Tim, van Genderen, Eric, & Acta Crystallographica A-Foundation and Advances, 74, E426. https://doi.org/10.1107/s2053273318088770
. (2018). Experimental and computational reduction of dynamical electron scattering allows visualizing individual hydrogen atoms [International Union of Crystallography].
Clabbers, Max T. B., & Crystallography Reviews, 24(3), 176–204. https://doi.org/10.1080/0889311x.2018.1446427
. (2018). Electron diffraction and three-dimensional crystallography for structural biology.
Clabbers, Max T. B., & Crystallography Reviews, 24(3), 176–204. https://doi.org/10.1080/0889311x.2018.1446427
. (2018). Electron diffraction and three-dimensional crystallography for structural biology.
Clabbers, Max T. B., Gruene, Tim, Parkhurst, James M., Acta Crystallographica. Section D, Structural Biology, 74(Pt 6), 506–518. https://doi.org/10.1107/s2059798318007726
, & Waterman, David G. (2018). Electron diffraction data processing with DIALS.
Clabbers, Max T. B., Gruene, Tim, Parkhurst, James M., Acta Crystallographica. Section D, Structural Biology, 74(Pt 6), 506–518. https://doi.org/10.1107/s2059798318007726
, & Waterman, David G. (2018). Electron diffraction data processing with DIALS.
Thomas, Brijith, Dubey, Rajeev K., Clabbers, Max T. B., Gupta, Karthick Babu Sai Sankar, van Genderen, Eric, Jager, Wolter F., Chemistry (Weinheim an Der Bergstrasse, Germany), 24(56), 14989–14993. https://doi.org/10.1002/chem.201802288
, Sudholter, Ernst J. R., & de Groot, Huub J. M. (2018). A Molecular Level Approach To Elucidate the Supramolecular Packing of Light-Harvesting Antenna Systems.
Thomas, Brijith, Dubey, Rajeev K., Clabbers, Max T. B., Gupta, Karthick Babu Sai Sankar, van Genderen, Eric, Jager, Wolter F., Chemistry (Weinheim an Der Bergstrasse, Germany), 24(56), 14989–14993. https://doi.org/10.1002/chem.201802288
, Sudholter, Ernst J. R., & de Groot, Huub J. M. (2018). A Molecular Level Approach To Elucidate the Supramolecular Packing of Light-Harvesting Antenna Systems.
Tinti, Gemma, Fröjdh, Erik, van Genderen, Eric, Gruene, Tim, Schmitt, Bernd, de Winter, D. A. Matthijs, Weckhuysen, Bert M., & IUCrJ, 5(Pt 2), 190–199. https://doi.org/10.1107/s2052252518000945
. (2018). Electron crystallography with the EIGER detector.
Tinti, Gemma, Fröjdh, Erik, van Genderen, Eric, Gruene, Tim, Schmitt, Bernd, de Winter, D. A. Matthijs, Weckhuysen, Bert M., & IUCrJ, 5(Pt 2), 190–199. https://doi.org/10.1107/s2052252518000945
. (2018). Electron crystallography with the EIGER detector.
Tinti, G., Frojdh, E., Van Genderen, E., Gruene, T., Schmitt, B., De Winter, D. A. M., Weckhuysen, B. M., & Cambridge Structural Database, 1817054. https://doi.org/10.5517/ccdc.csd.cc1yzsnc
(2018). CCDC 1817054: Experimental Crystal Structure Determination.
Tinti, G., Frojdh, E., Van Genderen, E., Gruene, T., Schmitt, B., De Winter, D. A. M., Weckhuysen, B. M., & Cambridge Structural Database, 1817054. https://doi.org/10.5517/ccdc.csd.cc1yzsnc
(2018). CCDC 1817054: Experimental Crystal Structure Determination.
Wallin, Cecilia, Hiruma, Yoshitaka, Wärmländer, Sebastian K. T. S., Huvent, Isabelle, Jarvet, Jüri, Journal of the American Chemical Society, 8138–8146. https://doi.org/10.1021/jacs.7b13623
, Gräslund, Astrid, Lippens, Guy, & Luo, Jinghui. (2018). The Neuronal Tau Protein Blocks in Vitro Fibrillation of the Amyloid-β (Aβ) Peptide at the Oligomeric Stage.
Wallin, Cecilia, Hiruma, Yoshitaka, Wärmländer, Sebastian K. T. S., Huvent, Isabelle, Jarvet, Jüri, Journal of the American Chemical Society, 8138–8146. https://doi.org/10.1021/jacs.7b13623
, Gräslund, Astrid, Lippens, Guy, & Luo, Jinghui. (2018). The Neuronal Tau Protein Blocks in Vitro Fibrillation of the Amyloid-β (Aβ) Peptide at the Oligomeric Stage.
Clabbers, Max T. B., van Genderen, Eric, Wan, Wei, Wiegers, Emiel L., Gruene, Tim, & Acta Crystallographica. Section D, Structural Biology, 73(Pt 9), 738–748. https://doi.org/10.1107/s2059798317010348
. (2017). Protein structure determination by electron diffraction using a single three-dimensional nanocrystal.
Clabbers, Max T. B., van Genderen, Eric, Wan, Wei, Wiegers, Emiel L., Gruene, Tim, & Acta Crystallographica. Section D, Structural Biology, 73(Pt 9), 738–748. https://doi.org/10.1107/s2059798317010348
. (2017). Protein structure determination by electron diffraction using a single three-dimensional nanocrystal.
Matheson, John, Moldovan, G., Kirkland, Angus, Allinson, Nigel, & Journal of Instrumentation, 12(11), C11016. https://doi.org/10.1088/1748-0221/12/11/c11016
. (2017). Testing and Comparison of Imaging Detectors for Electrons in the Energy Range 10-20 keV.
Matheson, John, Moldovan, G., Kirkland, Angus, Allinson, Nigel, & Journal of Instrumentation, 12(11), C11016. https://doi.org/10.1088/1748-0221/12/11/c11016
. (2017). Testing and Comparison of Imaging Detectors for Electrons in the Energy Range 10-20 keV.
Nederlof, Igor, van Genderen, Eric, Clabbers, Maddox E., & Acta Crystallographica Section A: Foundations and Advances, A73, a297–a298. https://doi.org/10.1107/s0108767317097082
. (2017). Electron Crystallography of Protein Nano-Crystals.
Nederlof, Igor, van Genderen, Eric, Clabbers, Maddox E., & Acta Crystallographica Section A: Foundations and Advances, A73, a297–a298. https://doi.org/10.1107/s0108767317097082
. (2017). Electron Crystallography of Protein Nano-Crystals.
Nikolopoulos, Stavros, Galanis, Athanasios S., Vallcorba, Oriol, Eggeman, Alex, Das, Partha Pratim, Acta Crystallographica A-Foundation and Advances, 73, C980–C980. https://doi.org/10.1107/s2053273317085941
, Rauch, Edgar, Midgley, Paul, & Gemmi, Mauro. (2017). Random electron diffraction tomography for structure analysis of pharmaceuticals.
Nikolopoulos, Stavros, Galanis, Athanasios S., Vallcorba, Oriol, Eggeman, Alex, Das, Partha Pratim, Acta Crystallographica A-Foundation and Advances, 73, C980–C980. https://doi.org/10.1107/s2053273317085941
, Rauch, Edgar, Midgley, Paul, & Gemmi, Mauro. (2017). Random electron diffraction tomography for structure analysis of pharmaceuticals.
Su, Jian, Wang, Hongyan, Wu, Kunkun, Liu, Zhongsheng, Yin, Qu, Wang, Run, Lv, Wei, Yin, Shougen, Liu, Zunfeng, & Journal of Nanoscience and Nanotechnology, 17(5), 3588–3596. https://doi.org/10.1166/jnn.2017.12860
. (2017). Neutravidin-Mediated Extraction of Isolated Small Diameter Single Walled Carbon Nanotubes for Bio-Recognition.
Su, Jian, Wang, Hongyan, Wu, Kunkun, Liu, Zhongsheng, Yin, Qu, Wang, Run, Lv, Wei, Yin, Shougen, Liu, Zunfeng, & Journal of Nanoscience and Nanotechnology, 17(5), 3588–3596. https://doi.org/10.1166/jnn.2017.12860
. (2017). Neutravidin-Mediated Extraction of Isolated Small Diameter Single Walled Carbon Nanotubes for Bio-Recognition.
Wang, Run, Boleij, Marissa, Yin, Qu, Galjart, Niels, Lin, Bencai, Yuan, Ningyi, Zhou, Xiang, Tan, Ming, Ding, Jianning, Liu, Zunfeng, & Journal of Nanoscience and Nanotechnology, 17(2), 926–931. https://doi.org/10.1166/jnn.2017.12716
. (2017). Purification of Biotinylated Proteins Using Single Walled Carbon Nanotube-Streptavidin Complexes.
Wang, Run, Boleij, Marissa, Yin, Qu, Galjart, Niels, Lin, Bencai, Yuan, Ningyi, Zhou, Xiang, Tan, Ming, Ding, Jianning, Liu, Zunfeng, & Journal of Nanoscience and Nanotechnology, 17(2), 926–931. https://doi.org/10.1166/jnn.2017.12716
. (2017). Purification of Biotinylated Proteins Using Single Walled Carbon Nanotube-Streptavidin Complexes.
Yin, Qu, Liu, Zunfeng, Laroche, Fabrice, Zhou, Xiang, Shao, Ningning, Lin, Bencai, Wang, Run, Yuan, Ningyi, Ding, Jianning, & Journal of Nanoscience and Nanotechnology, 17(2), 908–913. https://doi.org/10.1166/jnn.2017.12631
. (2017). A Novel Capturing Method for Quantification of Extra-Cellular Nanovesicles.
Yin, Qu, Liu, Zunfeng, Laroche, Fabrice, Zhou, Xiang, Shao, Ningning, Lin, Bencai, Wang, Run, Yuan, Ningyi, Ding, Jianning, & Journal of Nanoscience and Nanotechnology, 17(2), 908–913. https://doi.org/10.1166/jnn.2017.12631
. (2017). A Novel Capturing Method for Quantification of Extra-Cellular Nanovesicles.
Acta Crystallographica A-Foundation and Advances, 72(a1), S6–S6. https://doi.org/10.1107/s2053273316099903
. (2016). Electron nanodiffraction for structural biology.
Acta Crystallographica A-Foundation and Advances, 72(a1), S6–S6. https://doi.org/10.1107/s2053273316099903
. (2016). Electron nanodiffraction for structural biology.
Luo, Jinghui, Wärmländer, Sebastian K. T. S., Gräslund, Astrid, & ACS Chemical Neuroscience, 7(3), 269–274. https://doi.org/10.1021/acschemneuro.5b00325
. (2016). Reciprocal Molecular Interactions between the Aβ Peptide Linked to Alzheimer’s Disease and Insulin Linked to Diabetes Mellitus Type II.
Luo, Jinghui, Wärmländer, Sebastian K. T. S., Gräslund, Astrid, & ACS Chemical Neuroscience, 7(3), 269–274. https://doi.org/10.1021/acschemneuro.5b00325
. (2016). Reciprocal Molecular Interactions between the Aβ Peptide Linked to Alzheimer’s Disease and Insulin Linked to Diabetes Mellitus Type II.
Luo, Jinghui, Wärmländer, Sebastian K. T. S., Gräslund, Astrid, & Journal of Biological Chemistry, 292(5), 2046. https://doi.org/10.1074/jbc.r116.714576
. (2016). Cross-interactions between the Alzheimer Disease Amyloid-β Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis.
Luo, Jinghui, Wärmländer, Sebastian K. T. S., Gräslund, Astrid, & Journal of Biological Chemistry, 292(5), 2046. https://doi.org/10.1074/jbc.r116.714576
. (2016). Cross-interactions between the Alzheimer Disease Amyloid-β Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis.
Tiiman, Ann, Luo, Jinghui, Wallin, Cecilia, Olsson, Lisa, Lindgren, Joel, Jarvet, Jϋri, Per, Roos, Sholts, Sabrina B., Rahimipour, Shai, Journal of Alzheimer’s Disease, 54(3), 971–982. https://doi.org/10.3233/jad-160427
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