Publications
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Baumann, Kevin N., Bertosin, Eva, Barth, Anders, Dekker, Cees, & (2025). Elucidating the nanoscopic organization and dynamics of the nuclear pore complex [Journal-article]. Nucleus, 16(1). https://doi.org/10.1080/19491034.2025.2510106
Baumann, Kevin N., Bertosin, Eva, Barth, Anders, Dekker, Cees, & (2025). Elucidating the nanoscopic organization and dynamics of the nuclear pore complex [Journal-article]. Nucleus, 16(1). https://doi.org/10.1080/19491034.2025.2510106
Heuberger, Lukas, Balestri, Arianna, Tarvirdipour, Shabnam, Kapinos, Larisa E., , Lörtscher, Emanuel, Schoenenberger, Cora‐Ann, & Palivan, Cornelia G. (2025). Polymeric Giant Unilamellar Vesicles Support Longevity of Native Nuclei in Protocells [Journal-article]. Small Science, 5(6). https://doi.org/10.1002/smsc.202400622
Heuberger, Lukas, Balestri, Arianna, Tarvirdipour, Shabnam, Kapinos, Larisa E., , Lörtscher, Emanuel, Schoenenberger, Cora‐Ann, & Palivan, Cornelia G. (2025). Polymeric Giant Unilamellar Vesicles Support Longevity of Native Nuclei in Protocells [Journal-article]. Small Science, 5(6). https://doi.org/10.1002/smsc.202400622
Brüderlin, Mitchell, Kolesnikov, Maxim, Röthlin, Florian, , & Basler, Marek. (2025). Pseudomonas aeruginosa assembles H1-T6SS in response to physical and chemical damage of the outer membrane. Science Advances , 11(10). https://doi.org/10.1126/sciadv.adr1713
Brüderlin, Mitchell, Kolesnikov, Maxim, Röthlin, Florian, , & Basler, Marek. (2025). Pseudomonas aeruginosa assembles H1-T6SS in response to physical and chemical damage of the outer membrane. Science Advances , 11(10). https://doi.org/10.1126/sciadv.adr1713
Feng, Qingzhou, Saladin, Martin, Chunxiang , Wu, Cao, Eason, Zheng, Wei, Zhang, Amy, Bhardwaj, Pushpanjali, Li, Xia, Shen, Qi, Kapinos, Larisa E., Kozai, Toshiya, Mariappan, Malaiyalam, Xiong, Yong, Lusk, C. Patrick, , & Lin, Chenxiang. (2024). Channel width modulates the permeability of DNA origami–based nuclear pore mimics. Science Advances , 10(46). https://doi.org/10.1126/sciadv.adq8773
Feng, Qingzhou, Saladin, Martin, Chunxiang , Wu, Cao, Eason, Zheng, Wei, Zhang, Amy, Bhardwaj, Pushpanjali, Li, Xia, Shen, Qi, Kapinos, Larisa E., Kozai, Toshiya, Mariappan, Malaiyalam, Xiong, Yong, Lusk, C. Patrick, , & Lin, Chenxiang. (2024). Channel width modulates the permeability of DNA origami–based nuclear pore mimics. Science Advances , 10(46). https://doi.org/10.1126/sciadv.adq8773
Kapinos, Larisa E., Kalita, Joanna, Kassianidou, Elena, Rencurel, Chantal, & (2024). Mechanism of exportin retention in the cell nucleus [Journal-article]. Journal of Cell Biology, 223(2). https://doi.org/10.1083/jcb.202306094
Kapinos, Larisa E., Kalita, Joanna, Kassianidou, Elena, Rencurel, Chantal, & (2024). Mechanism of exportin retention in the cell nucleus [Journal-article]. Journal of Cell Biology, 223(2). https://doi.org/10.1083/jcb.202306094
Diez, Lisa, Kapinos, Larisa E., , & Wegmann, Susanne. (2023). Analysis of Tau/Nucleoporin Interactions by Surface Plasmon Resonance Spectroscopy. In Cieplak, Andrzej Stanisław (Ed.), Protein Aggregation (pp. 95–109). Springer. https://doi.org/10.1007/978-1-0716-2597-2_8
Diez, Lisa, Kapinos, Larisa E., , & Wegmann, Susanne. (2023). Analysis of Tau/Nucleoporin Interactions by Surface Plasmon Resonance Spectroscopy. In Cieplak, Andrzej Stanisław (Ed.), Protein Aggregation (pp. 95–109). Springer. https://doi.org/10.1007/978-1-0716-2597-2_8
Kapinos, Larisa E., & (2023). Multivalent Interactions with Intrinsically Disordered Proteins Probed by Surface Plasmon Resonance. In Goldberg, Martin W. (Ed.), The Nuclear Pore Complex (Vol. 2502, pp. 311–328). Springer. https://doi.org/10.1007/978-1-0716-2337-4_21
Kapinos, Larisa E., & (2023). Multivalent Interactions with Intrinsically Disordered Proteins Probed by Surface Plasmon Resonance. In Goldberg, Martin W. (Ed.), The Nuclear Pore Complex (Vol. 2502, pp. 311–328). Springer. https://doi.org/10.1007/978-1-0716-2337-4_21
Svirelis, Justas, Adali, Zeynep, Emilsson, Gustav, Medin, Jesper, Andersson, John, Vattikunta, Radhika, Hulander, Mats, Järlebark, Julia, Kolman, Krzysztof, Olsson, Oliver, Sakiyama, Yusuke, , & Dahlin, Andreas. (2023). Stable trapping of multiple proteins at physiological conditions using nanoscale chambers with macromolecular gates [Journal-article]. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-40889-4
Svirelis, Justas, Adali, Zeynep, Emilsson, Gustav, Medin, Jesper, Andersson, John, Vattikunta, Radhika, Hulander, Mats, Järlebark, Julia, Kolman, Krzysztof, Olsson, Oliver, Sakiyama, Yusuke, , & Dahlin, Andreas. (2023). Stable trapping of multiple proteins at physiological conditions using nanoscale chambers with macromolecular gates [Journal-article]. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-40889-4
Diez, Lisa, Kapinos, Larisa E., Hochmair, Janine, Huebschmann, Sabrina, Dominguez-Baquero, Alvaro, Vogt, Amelie, Rankovic, Marija, Zweckstetter, Markus, , & Wegmann, Susanne. (2022). Phosphorylation but Not Oligomerization Drives the Accumulation of Tau with Nucleoporin Nup98. International Journal of Molecular Sciences, 23(7), 3495. https://doi.org/10.3390/ijms23073495
Diez, Lisa, Kapinos, Larisa E., Hochmair, Janine, Huebschmann, Sabrina, Dominguez-Baquero, Alvaro, Vogt, Amelie, Rankovic, Marija, Zweckstetter, Markus, , & Wegmann, Susanne. (2022). Phosphorylation but Not Oligomerization Drives the Accumulation of Tau with Nucleoporin Nup98. International Journal of Molecular Sciences, 23(7), 3495. https://doi.org/10.3390/ijms23073495
Kalita, Joanna, Kapinos, Larisa E., Zheng, Tiantian, Rencurel, Chantal, Zilman, Anton, & (2022). Karyopherin enrichment and compensation fortifies the nuclear pore complex against nucleocytoplasmic leakage. Journal of Cell Biology, 221(3), e202108107. https://doi.org/10.1083/jcb.202108107
Kalita, Joanna, Kapinos, Larisa E., Zheng, Tiantian, Rencurel, Chantal, Zilman, Anton, & (2022). Karyopherin enrichment and compensation fortifies the nuclear pore complex against nucleocytoplasmic leakage. Journal of Cell Biology, 221(3), e202108107. https://doi.org/10.1083/jcb.202108107
Tarvirdipour, Shabnam, Skowicki, Michal, Schoenenberger, Cora-Ann, Kapinos, Larisa E., , Benenson, Yaakov, & Palivan, Cornelia G. (2022). A self-assembling peptidic platform to boost the cellular uptake and nuclear delivery of oligonucleotides. Biomaterials Science, 10(15), 4309–4323. https://doi.org/10.1039/d2bm00826b
Tarvirdipour, Shabnam, Skowicki, Michal, Schoenenberger, Cora-Ann, Kapinos, Larisa E., , Benenson, Yaakov, & Palivan, Cornelia G. (2022). A self-assembling peptidic platform to boost the cellular uptake and nuclear delivery of oligonucleotides. Biomaterials Science, 10(15), 4309–4323. https://doi.org/10.1039/d2bm00826b
Hoogenboom, Bart W., Hough, Loren E., Lemke, Edward A., , Onck, Patrick R., & Zilman, Anton. (2021). Physics of the nuclear pore complex: Theory, modeling and experiment. Physics Reports, 921, 1–53. https://doi.org/10.1016/j.physrep.2021.03.003
Hoogenboom, Bart W., Hough, Loren E., Lemke, Edward A., , Onck, Patrick R., & Zilman, Anton. (2021). Physics of the nuclear pore complex: Theory, modeling and experiment. Physics Reports, 921, 1–53. https://doi.org/10.1016/j.physrep.2021.03.003
Kalita, Joanna, Kapinos, Larisa E., & (2021). On the asymmetric partitioning of nucleocytoplasmic transport - recent insights and open questions. Journal of Cell Science, 134(7), jcs240382. https://doi.org/10.1242/jcs.240382
Kalita, Joanna, Kapinos, Larisa E., & (2021). On the asymmetric partitioning of nucleocytoplasmic transport - recent insights and open questions. Journal of Cell Science, 134(7), jcs240382. https://doi.org/10.1242/jcs.240382
Sharma, Deepika, , Pfohl, Thomas, & Ekinci, Yasin. (2021). Optimization of Nanofluidic Devices for Geometry-Induced Electrostatic Trapping. Particle & Particle Systems Characterization, 38(2), 2170003. https://doi.org/10.1002/ppsc.202170003
Sharma, Deepika, , Pfohl, Thomas, & Ekinci, Yasin. (2021). Optimization of Nanofluidic Devices for Geometry-Induced Electrostatic Trapping. Particle & Particle Systems Characterization, 38(2), 2170003. https://doi.org/10.1002/ppsc.202170003
Sharma, Deepika, , Pfohl, Thomas, & Ekinci, Yasin. (2021). Surface-modified elastomeric nanofluidic devices for single nanoparticle trapping. Microsystems & Nanoengineering, 7(1), 46. https://doi.org/10.1038/s41378-021-00273-y
Sharma, Deepika, , Pfohl, Thomas, & Ekinci, Yasin. (2021). Surface-modified elastomeric nanofluidic devices for single nanoparticle trapping. Microsystems & Nanoengineering, 7(1), 46. https://doi.org/10.1038/s41378-021-00273-y
Avsar, Saziye Yorulmaz, Kapinos, Larisa E., Schoenenberger, Cora-Ann, Schertler, Gebhard F. X., Muhle, Jonas, Meger, Benoit, , Ostermaier, Martin K., Lesca, Elena, & Palivan, Cornelia G. (2020). Immobilization of arrestin-3 on different biosensor platforms for evaluating GPCR binding. Physical Chemistry Chemical Physics, 22(41), 24086–24096. https://doi.org/10.1039/d0cp01464h
Avsar, Saziye Yorulmaz, Kapinos, Larisa E., Schoenenberger, Cora-Ann, Schertler, Gebhard F. X., Muhle, Jonas, Meger, Benoit, , Ostermaier, Martin K., Lesca, Elena, & Palivan, Cornelia G. (2020). Immobilization of arrestin-3 on different biosensor platforms for evaluating GPCR binding. Physical Chemistry Chemical Physics, 22(41), 24086–24096. https://doi.org/10.1039/d0cp01464h
Barbato, Suncica, Kapinos, Larisa E., Rencurel, Chantal, & (2020). Karyopherin enrichment at the nuclear pore complex attenuates Ran permeability. Journal of Cell Science, 133(3), aheadofrint. https://doi.org/10.1242/jcs.238121
Barbato, Suncica, Kapinos, Larisa E., Rencurel, Chantal, & (2020). Karyopherin enrichment at the nuclear pore complex attenuates Ran permeability. Journal of Cell Science, 133(3), aheadofrint. https://doi.org/10.1242/jcs.238121
Santos, José Carlos, Boucher, Dave, Schneider, Larisa Kapinos, Demarco, Benjamin, Dilucca, Marisa, Shkarina, Kateryna, Heilig, Rosalie, Chen, Kaiwen W., , & Broz, Petr. (2020). Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria. Nature Communications, 11(1), 3276. https://doi.org/10.1038/s41467-020-16889-z
Santos, José Carlos, Boucher, Dave, Schneider, Larisa Kapinos, Demarco, Benjamin, Dilucca, Marisa, Shkarina, Kateryna, Heilig, Rosalie, Chen, Kaiwen W., , & Broz, Petr. (2020). Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria. Nature Communications, 11(1), 3276. https://doi.org/10.1038/s41467-020-16889-z
Zelmer, Christina, Zweifel, Ludovit P., Kapinos, Larisa E., Craciun, Ioana, Güven, Zekiye P., Palivan, Cornelia G., & (2020). Organelle-specific targeting of polymersomes into the cell nucleus. Proceedings of the National Academy of Sciences of the United States of America, 117(6), 2770–2778. https://doi.org/10.1073/pnas.1916395117
Zelmer, Christina, Zweifel, Ludovit P., Kapinos, Larisa E., Craciun, Ioana, Güven, Zekiye P., Palivan, Cornelia G., & (2020). Organelle-specific targeting of polymersomes into the cell nucleus. Proceedings of the National Academy of Sciences of the United States of America, 117(6), 2770–2778. https://doi.org/10.1073/pnas.1916395117
Kassianidou, Elena, Kalita, Joanna, & (2019). The role of nucleocytoplasmic transport in mechanotransduction. Experimental Cell Research, 377(1-2), 86–93. https://doi.org/10.1016/j.yexcr.2019.02.009
Kassianidou, Elena, Kalita, Joanna, & (2019). The role of nucleocytoplasmic transport in mechanotransduction. Experimental Cell Research, 377(1-2), 86–93. https://doi.org/10.1016/j.yexcr.2019.02.009
Panatala, Radhakrishnan, Barbato, Suncica, Kozai, Toshiya, Luo, Jinghui, Kapinos, Larisa E., & (2019). Nuclear Pore Membrane Proteins Self-Assemble into Nanopores. Biochemistry, 58(6), 484–488. https://doi.org/10.1021/acs.biochem.8b01179
Panatala, Radhakrishnan, Barbato, Suncica, Kozai, Toshiya, Luo, Jinghui, Kapinos, Larisa E., & (2019). Nuclear Pore Membrane Proteins Self-Assemble into Nanopores. Biochemistry, 58(6), 484–488. https://doi.org/10.1021/acs.biochem.8b01179
Eftekharzadeh, Bahareh, Daigle, J. Gavin, Kapinos, Larisa E., Coyne, Alyssa, Schiantarelli, Julia, Carlomagno, Yari, Cook, Casey, Miller, Sean J., Dujardin, Simon, Amaral, Ana S., Grima, Jonathan C., Bennet, Rachel E., Tepper, Katharina, DeTure, Michael, Vanderburgh, Charles R., Corjuc, Bianca T., Devos, Sarah L., Gonzalez, Jose Antonio, Chew, Jeannie, et al. (2018). Tau Protein Disrupts Nucleocytoplasmic Transport in Alzheimer’s Disease. Neuron, 99(5), 925–940. https://doi.org/10.1016/j.neuron.2018.07.039
Eftekharzadeh, Bahareh, Daigle, J. Gavin, Kapinos, Larisa E., Coyne, Alyssa, Schiantarelli, Julia, Carlomagno, Yari, Cook, Casey, Miller, Sean J., Dujardin, Simon, Amaral, Ana S., Grima, Jonathan C., Bennet, Rachel E., Tepper, Katharina, DeTure, Michael, Vanderburgh, Charles R., Corjuc, Bianca T., Devos, Sarah L., Gonzalez, Jose Antonio, Chew, Jeannie, et al. (2018). Tau Protein Disrupts Nucleocytoplasmic Transport in Alzheimer’s Disease. Neuron, 99(5), 925–940. https://doi.org/10.1016/j.neuron.2018.07.039
Emilsson, Gustav, Sakiyama, Yusuke, Malekian, Bita, Xiong, Kunli, Adali-Kaya, Zeynep, , & Dahlin, Andreas B. (2018). Gating Protein Transport in Solid State Nanopores by Single Molecule Recognition. ACS Central Science, 4(8), 1007–1014. https://doi.org/10.1021/acscentsci.8b00268
Emilsson, Gustav, Sakiyama, Yusuke, Malekian, Bita, Xiong, Kunli, Adali-Kaya, Zeynep, , & Dahlin, Andreas B. (2018). Gating Protein Transport in Solid State Nanopores by Single Molecule Recognition. ACS Central Science, 4(8), 1007–1014. https://doi.org/10.1021/acscentsci.8b00268
Emilsson, Gustav, Xiong, Kunli, Sakiyama, Yusuke, Malekian, Bita, Gagnér, Viktor Ahlberg, Schoch, Rafael L., , & Dahlin, Andreas B. (2018). Polymer brushes in solid-state nanopores form an impenetrable entropic barrier for proteins. Nanoscale, 10(10), 4663–4669. https://doi.org/10.1039/c7nr09432a
Emilsson, Gustav, Xiong, Kunli, Sakiyama, Yusuke, Malekian, Bita, Gagnér, Viktor Ahlberg, Schoch, Rafael L., , & Dahlin, Andreas B. (2018). Polymer brushes in solid-state nanopores form an impenetrable entropic barrier for proteins. Nanoscale, 10(10), 4663–4669. https://doi.org/10.1039/c7nr09432a
Ganier, Olivier, Schnerch, Dominik, Oertle, Philipp, , Plodinec, Marija, & Nigg, Erich A. (2018). Structural centrosome aberrations promote non-cell-autonomous invasiveness. The EMBO journal, e98576. https://doi.org/10.15252/embj.201798576
Ganier, Olivier, Schnerch, Dominik, Oertle, Philipp, , Plodinec, Marija, & Nigg, Erich A. (2018). Structural centrosome aberrations promote non-cell-autonomous invasiveness. The EMBO journal, e98576. https://doi.org/10.15252/embj.201798576
Malekian, Bita, Schoch, Rafael L., Robson, Timothy, Ferrand-Drake del Castillo, Gustav, Xiong, Kunli, Emilsson, Gustav, Kapinos, Larisa E., , & Dahlin, Andreas B. (2018). Detecting Selective Protein Binding inside Plasmonic Nanopores: Towards a Mimic of the Nuclear Pore Complex. Frontiers in Chemistry, 6, 637. https://doi.org/10.3389/fchem.2018.00637
Malekian, Bita, Schoch, Rafael L., Robson, Timothy, Ferrand-Drake del Castillo, Gustav, Xiong, Kunli, Emilsson, Gustav, Kapinos, Larisa E., , & Dahlin, Andreas B. (2018). Detecting Selective Protein Binding inside Plasmonic Nanopores: Towards a Mimic of the Nuclear Pore Complex. Frontiers in Chemistry, 6, 637. https://doi.org/10.3389/fchem.2018.00637
Zanetti-Dällenbach, Rosanna, Plodinec, Marija, Oertle, Philipp, Redling, Katharina, Obermann, Ellen C., , & Schoenenberger, Cora-Ann. (2018). Length Scale Matters: Real-Time Elastography versus Nanomechanical Profiling by Atomic Force Microscopy for the Diagnosis of Breast Lesions. BioMed Research International, 2018, 3840597. https://doi.org/10.1155/2018/3840597
Zanetti-Dällenbach, Rosanna, Plodinec, Marija, Oertle, Philipp, Redling, Katharina, Obermann, Ellen C., , & Schoenenberger, Cora-Ann. (2018). Length Scale Matters: Real-Time Elastography versus Nanomechanical Profiling by Atomic Force Microscopy for the Diagnosis of Breast Lesions. BioMed Research International, 2018, 3840597. https://doi.org/10.1155/2018/3840597
Benning, Friederike M. C., Sakiyama, Yusuke, Mazur, Adam, Bukhari, Habib S. T., , & Maier, Timm. (2017). High-Speed Atomic Force Microscopy Visualization of the Dynamics of the Multienzyme Fatty Acid Synthase. ACS Nano, 11(11), 10852–10859. https://doi.org/10.1021/acsnano.7b04216
Benning, Friederike M. C., Sakiyama, Yusuke, Mazur, Adam, Bukhari, Habib S. T., , & Maier, Timm. (2017). High-Speed Atomic Force Microscopy Visualization of the Dynamics of the Multienzyme Fatty Acid Synthase. ACS Nano, 11(11), 10852–10859. https://doi.org/10.1021/acsnano.7b04216
Emilsson, Gustav, Schoch, Rafael L., Oertle, Philipp, Xiong, Kunli, , & Dahlin, Andreas B. (2017). Surface plasmon resonance methodology for monitoring polymerization kinetics and morphology changes of brushes - evaluated with poly(N-isopropylacrylamide). Applied Surface Science, 396, 384–392. https://doi.org/10.1016/j.apsusc.2016.10.165
Emilsson, Gustav, Schoch, Rafael L., Oertle, Philipp, Xiong, Kunli, , & Dahlin, Andreas B. (2017). Surface plasmon resonance methodology for monitoring polymerization kinetics and morphology changes of brushes - evaluated with poly(N-isopropylacrylamide). Applied Surface Science, 396, 384–392. https://doi.org/10.1016/j.apsusc.2016.10.165
Kapinos, Larisa E., Huang, Binlu, Rencurel, Chantal, & (2017). Karyopherins regulate nuclear pore complex barrier and transport function. Journal of Cell Biology, 216(11), 3609–3624. https://doi.org/10.1083/jcb.201702092
Kapinos, Larisa E., Huang, Binlu, Rencurel, Chantal, & (2017). Karyopherins regulate nuclear pore complex barrier and transport function. Journal of Cell Biology, 216(11), 3609–3624. https://doi.org/10.1083/jcb.201702092
Luo, Wangxi, Ruba, Andrew, Takao, Daisuke, Zweifel, Ludovit P., , Verhey, Kristen J., & Yang, Weidong. (2017). Axonemal Lumen Dominates Cytosolic Protein Diffusion inside the Primary Cilium. Scientific Reports, 7(1), 15793. https://doi.org/10.1038/s41598-017-16103-z
Luo, Wangxi, Ruba, Andrew, Takao, Daisuke, Zweifel, Ludovit P., , Verhey, Kristen J., & Yang, Weidong. (2017). Axonemal Lumen Dominates Cytosolic Protein Diffusion inside the Primary Cilium. Scientific Reports, 7(1), 15793. https://doi.org/10.1038/s41598-017-16103-z
Sakiyama, Yusuke, Panatala, Radhakrishnan, & (2017). Structural dynamics of the nuclear pore complex. Seminars in Cell and Developmental Biology, 68, 27–33. https://doi.org/10.1016/j.semcdb.2017.05.021
Sakiyama, Yusuke, Panatala, Radhakrishnan, & (2017). Structural dynamics of the nuclear pore complex. Seminars in Cell and Developmental Biology, 68, 27–33. https://doi.org/10.1016/j.semcdb.2017.05.021
Schoch, Rafael L., Emilsson, Gustav, Dahlin, Andreas B., & (2017). Protein exclusion is preserved by temperature sensitive PEG brushes. Polymer, 132, 362–367. https://doi.org/10.1016/j.polymer.2017.10.063
Schoch, Rafael L., Emilsson, Gustav, Dahlin, Andreas B., & (2017). Protein exclusion is preserved by temperature sensitive PEG brushes. Polymer, 132, 362–367. https://doi.org/10.1016/j.polymer.2017.10.063
Sharma, Deepika, Gerspach, Michael Adrian, Pfohl, Thomas, , & Ekinci, Yasin. (2017). Single positively charged particle trapping in nanofluidic systems. Microelectronic Engineering, 175, 43–49. https://doi.org/10.1016/j.mee.2017.01.001
Sharma, Deepika, Gerspach, Michael Adrian, Pfohl, Thomas, , & Ekinci, Yasin. (2017). Single positively charged particle trapping in nanofluidic systems. Microelectronic Engineering, 175, 43–49. https://doi.org/10.1016/j.mee.2017.01.001
Sakiyama, Yusuke, Mazur, Adam, Kapinos, Larisa E., & (2016). Spatiotemporal dynamics of the nuclear pore complex transport barrier resolved by high-speed atomic force microscopy. Nature Nanotechnology, 11(8), 23–719. https://doi.org/10.1038/nnano.2016.62
Sakiyama, Yusuke, Mazur, Adam, Kapinos, Larisa E., & (2016). Spatiotemporal dynamics of the nuclear pore complex transport barrier resolved by high-speed atomic force microscopy. Nature Nanotechnology, 11(8), 23–719. https://doi.org/10.1038/nnano.2016.62
Vovk, Andrei, Gu, Chad, Opferman, Michael G, Kapinos, Larisa E, , Coalson, Rob D, Jasnow, David, & Zilman, Anton. (2016). Simple biophysics underpins collective conformations of the intrinsically disordered proteins of the Nuclear Pore Complex. eLife, 5, e10785. https://doi.org/10.7554/elife.10785.001
Vovk, Andrei, Gu, Chad, Opferman, Michael G, Kapinos, Larisa E, , Coalson, Rob D, Jasnow, David, & Zilman, Anton. (2016). Simple biophysics underpins collective conformations of the intrinsically disordered proteins of the Nuclear Pore Complex. eLife, 5, e10785. https://doi.org/10.7554/elife.10785.001
Vujica, Suncica, Zelmer, Christina, Panatala, Radhakrishnan, & . (2016). Nucleocytoplasmic Transport: A Paradigm for Molecular Logistics in Artificial Systems. Chimia, 70(6), 7–413. https://doi.org/10.2533/chimia.2016.413
Vujica, Suncica, Zelmer, Christina, Panatala, Radhakrishnan, & . (2016). Nucleocytoplasmic Transport: A Paradigm for Molecular Logistics in Artificial Systems. Chimia, 70(6), 7–413. https://doi.org/10.2533/chimia.2016.413
Zweifel, Ludovit P., Shorubalko, Ivan, & (2016). Helium scanning transmission ion microscopy and electrical characterization of glass nanocapillaries with reproducible tip geometries. ACS nano, 10(2), 25–1918. https://doi.org/10.1021/acsnano.5b05754
Zweifel, Ludovit P., Shorubalko, Ivan, & (2016). Helium scanning transmission ion microscopy and electrical characterization of glass nanocapillaries with reproducible tip geometries. ACS nano, 10(2), 25–1918. https://doi.org/10.1021/acsnano.5b05754
Emilsson, Gustav, Schoch, Rafael L, Feuz, Laurent, Höök, Fredrik, , & Dahlin, Andreas B. (2015). Strongly Stretched Protein Resistant Poly(ethylene glycol) Brushes Prepared by Grafting-To. ACS Applied Materials & Interfaces, 7(14), 15–7505. https://doi.org/10.1021/acsami.5b01590
Emilsson, Gustav, Schoch, Rafael L, Feuz, Laurent, Höök, Fredrik, , & Dahlin, Andreas B. (2015). Strongly Stretched Protein Resistant Poly(ethylene glycol) Brushes Prepared by Grafting-To. ACS Applied Materials & Interfaces, 7(14), 15–7505. https://doi.org/10.1021/acsami.5b01590
, Huang, Binlu, & Kapinos, Larisa E. (2015). How to operate a nuclear pore complex by Kap-centric control. Nucleus (Austin, Tex.), 6(5), 366–372. https://doi.org/10.1080/19491034.2015.1090061
, Huang, Binlu, & Kapinos, Larisa E. (2015). How to operate a nuclear pore complex by Kap-centric control. Nucleus (Austin, Tex.), 6(5), 366–372. https://doi.org/10.1080/19491034.2015.1090061
Plodinec, Marija, & (2015). Nanomechanical characterization of living mammary tissues by atomic force microscopy. Methods in Molecular Biology, 1293, 46–231. https://doi.org/10.1007/978-1-4939-2519-3_14
Plodinec, Marija, & (2015). Nanomechanical characterization of living mammary tissues by atomic force microscopy. Methods in Molecular Biology, 1293, 46–231. https://doi.org/10.1007/978-1-4939-2519-3_14
Wagner, Raphael S., Kapinos, Larisa E., Marshall, Neil J., Stewart, Murray, & (2015). Promiscuous Binding of Karyopherinβ1 Modulates FG Nucleoporin Barrier Function and Expedites NTF2 Transport Kinetics. Biophysical Journal, 108(4), 27–918. https://doi.org/10.1016/j.bpj.2014.12.041
Wagner, Raphael S., Kapinos, Larisa E., Marshall, Neil J., Stewart, Murray, & (2015). Promiscuous Binding of Karyopherinβ1 Modulates FG Nucleoporin Barrier Function and Expedites NTF2 Transport Kinetics. Biophysical Journal, 108(4), 27–918. https://doi.org/10.1016/j.bpj.2014.12.041
Fuxreiter, Monika, Toth-Petroczy, Agnes, Kraut, Daniel A., Matouschek, Andreas T., , Xue, Bin, Kurgan, Lukasz, & Uversky, Vladimir N. (2014). Disordered Proteinaceous Machines. Chemical Reviews, 114(13), 6806–6843. https://doi.org/10.1021/cr4007329
Fuxreiter, Monika, Toth-Petroczy, Agnes, Kraut, Daniel A., Matouschek, Andreas T., , Xue, Bin, Kurgan, Lukasz, & Uversky, Vladimir N. (2014). Disordered Proteinaceous Machines. Chemical Reviews, 114(13), 6806–6843. https://doi.org/10.1021/cr4007329
Kapinos, Larisa E., Schoch, Rafael L., Wagner, Raphael S., Schleicher, Kai D., & (2014). Karyopherin-centric control of nuclear pores based on molecular occupancy and kinetic analysis of multivalent binding with FG nucleoporins. Biophysical Journal, 106(8), 62–1751. https://doi.org/10.1016/j.bpj.2014.02.021
Kapinos, Larisa E., Schoch, Rafael L., Wagner, Raphael S., Schleicher, Kai D., & (2014). Karyopherin-centric control of nuclear pores based on molecular occupancy and kinetic analysis of multivalent binding with FG nucleoporins. Biophysical Journal, 106(8), 62–1751. https://doi.org/10.1016/j.bpj.2014.02.021
Schleicher, Kai D, Dettmer, Simon L, Kapinos, Larisa E, Pagliara, Stefano, Keyser, Ulrich F, Jeney, Sylvia, & . (2014). Selective transport control on molecular velcro made from intrinsically disordered proteins. Nature Nanotechnology, 9(7), 30–525. https://doi.org/10.1038/nnano.2014.103
Schleicher, Kai D, Dettmer, Simon L, Kapinos, Larisa E, Pagliara, Stefano, Keyser, Ulrich F, Jeney, Sylvia, & . (2014). Selective transport control on molecular velcro made from intrinsically disordered proteins. Nature Nanotechnology, 9(7), 30–525. https://doi.org/10.1038/nnano.2014.103
Halfter, Willi, Monnier, Christophe, Müller, David, Oertle, Philipp, Uechi, Guy, Balasubramani, Manimalha, Safi, Farhad, , Loparic, Marko, & Henrich, Paul Bernhard. (2013). The Bi-Functional Organization of Human Basement Membranes. PLoS ONE, 8(7), e67660. https://doi.org/10.1371/journal.pone.0067660
Halfter, Willi, Monnier, Christophe, Müller, David, Oertle, Philipp, Uechi, Guy, Balasubramani, Manimalha, Safi, Farhad, , Loparic, Marko, & Henrich, Paul Bernhard. (2013). The Bi-Functional Organization of Human Basement Membranes. PLoS ONE, 8(7), e67660. https://doi.org/10.1371/journal.pone.0067660
Schoch, Rafael L, & . (2013). Non-interacting molecules as innate structural probes in surface plasmon resonance. Langmuir, 29(12), 76–4068. https://doi.org/10.1021/la3049289
Schoch, Rafael L, & . (2013). Non-interacting molecules as innate structural probes in surface plasmon resonance. Langmuir, 29(12), 76–4068. https://doi.org/10.1021/la3049289
Hyotyla, J. T., & (2012). Atomic force microscopy. In Supramolecular chemistry. From molecules to nanomaterials: Vol. Vol. 2: Techniques (pp. 659–668). Wiley-Blackwell. https://doi.org/10.1002/9780470661345.smc043
Hyotyla, J. T., & (2012). Atomic force microscopy. In Supramolecular chemistry. From molecules to nanomaterials: Vol. Vol. 2: Techniques (pp. 659–668). Wiley-Blackwell. https://doi.org/10.1002/9780470661345.smc043
Henrich, Paul B., Monnier, Christophe A., Halfter, Willi, Haritoglou, Christos, Strauss, Rupert W., , & Loparic, Marko. (2012). Nanoscale topographic and biomechanical studies of the human internal limiting membrane. Investigative ophthalmology & visual science, 53(6), 70–2561. https://doi.org/10.1167/iovs.11-8502
Henrich, Paul B., Monnier, Christophe A., Halfter, Willi, Haritoglou, Christos, Strauss, Rupert W., , & Loparic, Marko. (2012). Nanoscale topographic and biomechanical studies of the human internal limiting membrane. Investigative ophthalmology & visual science, 53(6), 70–2561. https://doi.org/10.1167/iovs.11-8502
, & Herrmann, Harald. (2012). From structural architecture to cellular organization : celebrating the scientific contributions of Ueli Aebi on the occasion of his retirement. Journal of Structural Biology, 177(1), 1–2. https://doi.org/10.1016/j.jsb.2011.12.011
, & Herrmann, Harald. (2012). From structural architecture to cellular organization : celebrating the scientific contributions of Ueli Aebi on the occasion of his retirement. Journal of Structural Biology, 177(1), 1–2. https://doi.org/10.1016/j.jsb.2011.12.011
Plodinec, Marija, Loparic, Marko, Monnier, Christophe A, Obermann, Ellen C, Zanetti-Dallenbach, Rosanna, Oertle, Philipp, Hyotyla, Janne T, Aebi, Ueli, Bentires-Alj, Mohamed, , & Schoenenberger, Cora-Ann. (2012). The nanomechanical signature of breast cancer. Nature Nanotechnology, 7(11), 65–757. https://doi.org/10.1038/nnano.2012.167
Plodinec, Marija, Loparic, Marko, Monnier, Christophe A, Obermann, Ellen C, Zanetti-Dallenbach, Rosanna, Oertle, Philipp, Hyotyla, Janne T, Aebi, Ueli, Bentires-Alj, Mohamed, , & Schoenenberger, Cora-Ann. (2012). The nanomechanical signature of breast cancer. Nature Nanotechnology, 7(11), 65–757. https://doi.org/10.1038/nnano.2012.167
Schoch, Rafael L., Kapinos, Larisa E., & (2012). Nuclear transport receptor binding avidity triggers a self-healing collapse transition in FG-nucleoporin molecular brushes. Proceedings of the National Academy of Sciences of the United States of America, 109(42), 6–16911. https://doi.org/10.1073/pnas.1208440109
Schoch, Rafael L., Kapinos, Larisa E., & (2012). Nuclear transport receptor binding avidity triggers a self-healing collapse transition in FG-nucleoporin molecular brushes. Proceedings of the National Academy of Sciences of the United States of America, 109(42), 6–16911. https://doi.org/10.1073/pnas.1208440109
Hyotyla, Janne T, Deng, Jie, & . (2011). Synthetic Protein Targeting by the Intrinsic Biorecognition Functionality of Poly(ethylene glycol) Using PEG Antibodies as Biohybrid Molecular Adaptors. ACS Nano, 5(6), 7–5180. https://doi.org/10.1021/nn201327y
Hyotyla, Janne T, Deng, Jie, & . (2011). Synthetic Protein Targeting by the Intrinsic Biorecognition Functionality of Poly(ethylene glycol) Using PEG Antibodies as Biohybrid Molecular Adaptors. ACS Nano, 5(6), 7–5180. https://doi.org/10.1021/nn201327y
Kowalczyk, Stefan W, Kapinos, Larisa, Blosser, Timothy R, Magalhães, Tomás, van Nies, Pauline, , & Dekker, Cees. (2011). Single-molecule transport across an individual biomimetic nuclear pore complex. Nature Nanotechnology, 6(7), 8–433. https://doi.org/10.1038/nnano.2011.88
Kowalczyk, Stefan W, Kapinos, Larisa, Blosser, Timothy R, Magalhães, Tomás, van Nies, Pauline, , & Dekker, Cees. (2011). Single-molecule transport across an individual biomimetic nuclear pore complex. Nature Nanotechnology, 6(7), 8–433. https://doi.org/10.1038/nnano.2011.88
Backmann, Natalija, Kappeler, Natascha, Braun, Thomas, Huber, François, Lang, Hans-Peter, Gerber, Christoph, & (2010). Sensing surface PEGylation with microcantilevers. Beilstein Journal of Nanotechnology, 1, 3–13. https://doi.org/10.3762/bjnano.1.2
Backmann, Natalija, Kappeler, Natascha, Braun, Thomas, Huber, François, Lang, Hans-Peter, Gerber, Christoph, & (2010). Sensing surface PEGylation with microcantilevers. Beilstein Journal of Nanotechnology, 1, 3–13. https://doi.org/10.3762/bjnano.1.2
Peleg, O., & (2010). Converging on the function of intrinsically disordered nucleoporins in the nuclear pore complex. Biological Chemistry, 391(7), 30–719. https://doi.org/10.1515/bc.2010.092
Peleg, O., & (2010). Converging on the function of intrinsically disordered nucleoporins in the nuclear pore complex. Biological Chemistry, 391(7), 30–719. https://doi.org/10.1515/bc.2010.092
Elad, Nadav, Maimon, Tal, Frenkiel-Krispin, Daphna, , & Medalia, Ohad. (2009). Structural analysis of the nuclear pore complex by integrated approaches. Current Opinion in Structural Biology, 19(2), 32–226. https://doi.org/10.1016/j.sbi.2009.02.009
Elad, Nadav, Maimon, Tal, Frenkiel-Krispin, Daphna, , & Medalia, Ohad. (2009). Structural analysis of the nuclear pore complex by integrated approaches. Current Opinion in Structural Biology, 19(2), 32–226. https://doi.org/10.1016/j.sbi.2009.02.009
, & Deng, Jie. (2009). Interaction forces and reversible collapse of a polymer brush-gated nanopore. ACS Nano, 3(10), 8–2911. https://doi.org/10.1021/nn900152m
, & Deng, Jie. (2009). Interaction forces and reversible collapse of a polymer brush-gated nanopore. ACS Nano, 3(10), 8–2911. https://doi.org/10.1021/nn900152m
, Aebi, Ueli, & Fahrenkrog, Birthe. (2008). Towards reconciling structure and function in the nuclear pore complex. Histochemistry and Cell Biology, 129(2), 16–105. https://doi.org/10.1007/s00418-007-0371-x
, Aebi, Ueli, & Fahrenkrog, Birthe. (2008). Towards reconciling structure and function in the nuclear pore complex. Histochemistry and Cell Biology, 129(2), 16–105. https://doi.org/10.1007/s00418-007-0371-x
. (2007). Gate-crashing the nuclear pore complex. Structure: With Folding and Design, 15(8), 91–889. https://doi.org/10.1016/j.str.2007.07.005
. (2007). Gate-crashing the nuclear pore complex. Structure: With Folding and Design, 15(8), 91–889. https://doi.org/10.1016/j.str.2007.07.005
, Fahrenkrog, Birthe, Köser, Joachim, Schwarz-Herion, Kyrill, Deng, Jie, & Aebi, Ueli. (2007). Nanomechanical basis of selective gating by the nuclear pore complex. Science, 318(5850), 3–640. https://doi.org/10.1126/science.1145980
, Fahrenkrog, Birthe, Köser, Joachim, Schwarz-Herion, Kyrill, Deng, Jie, & Aebi, Ueli. (2007). Nanomechanical basis of selective gating by the nuclear pore complex. Science, 318(5850), 3–640. https://doi.org/10.1126/science.1145980
, Köser, Joachim, Huang, Ning-Ping, Schwarz-Herion, Kyrill, & Aebi, Ueli. (2007). Nanomechanical interactions of phenylalanine-glycine nucleoporins studied by single molecule force-volume spectroscopy. Journal of Structural Biology, 159(2), 89–277. https://doi.org/10.1016/j.jsb.2007.01.018
, Köser, Joachim, Huang, Ning-Ping, Schwarz-Herion, Kyrill, & Aebi, Ueli. (2007). Nanomechanical interactions of phenylalanine-glycine nucleoporins studied by single molecule force-volume spectroscopy. Journal of Structural Biology, 159(2), 89–277. https://doi.org/10.1016/j.jsb.2007.01.018
, Aebi, Ueli, & Stoffler, Daniel. (2006). From the trap to the basket : getting to the bottom of the nuclear pore complex. Chromosoma, 115(1), 15–26. https://doi.org/10.1007/s00412-005-0037-1
, Aebi, Ueli, & Stoffler, Daniel. (2006). From the trap to the basket : getting to the bottom of the nuclear pore complex. Chromosoma, 115(1), 15–26. https://doi.org/10.1007/s00412-005-0037-1
, & Fahrenkrog, Birthe. (2006). The nuclear pore complex up close. Current Opinion in Cell Biology, 18(3), 342–347. https://doi.org/10.1016/j.ceb.2006.03.006
, & Fahrenkrog, Birthe. (2006). The nuclear pore complex up close. Current Opinion in Cell Biology, 18(3), 342–347. https://doi.org/10.1016/j.ceb.2006.03.006
, Huang, Ning-Ping, Köser, Joachim, Deng, Jie, Lau, K. H. Aaron, Schwarz-Herion, Kyrill, Fahrenkrog, Birthe, & Aebi, Ueli. (2006). Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport. Proceedings of the National Academy of Sciences of the United States of America, 103(25), 7–9512. https://doi.org/10.1073/pnas.0603521103
, Huang, Ning-Ping, Köser, Joachim, Deng, Jie, Lau, K. H. Aaron, Schwarz-Herion, Kyrill, Fahrenkrog, Birthe, & Aebi, Ueli. (2006). Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport. Proceedings of the National Academy of Sciences of the United States of America, 103(25), 7–9512. https://doi.org/10.1073/pnas.0603521103
, & Aebi, Ueli. (2005). In silico access to the nuclear pore complex. Structure: With Folding and Design, 13(12), 3–1741. https://doi.org/10.1016/j.str.2005.11.002
, & Aebi, Ueli. (2005). In silico access to the nuclear pore complex. Structure: With Folding and Design, 13(12), 3–1741. https://doi.org/10.1016/j.str.2005.11.002
, & O’Shea, S. J. (2004). Discrete solvation layering in confined binary liquids. Langmuir, 20(12), 9–4916. https://doi.org/10.1021/la036200g
, & O’Shea, S. J. (2004). Discrete solvation layering in confined binary liquids. Langmuir, 20(12), 9–4916. https://doi.org/10.1021/la036200g
, Li, S. F. Y., & O’Shea, S. J. (2002). Solvation forces using sample-modulation atomic force microscopy. Langmuir, 18(16), 6116–6124. https://doi.org/10.1021/la011789+
, Li, S. F. Y., & O’Shea, S. J. (2002). Solvation forces using sample-modulation atomic force microscopy. Langmuir, 18(16), 6116–6124. https://doi.org/10.1021/la011789+
, & O’Shea, S. J. (2002). Solvation forces in branched molecular liquids. Physical Review Letters, 88(24), 246101. https://doi.org/10.1103/physrevlett.88.246101
, & O’Shea, S. J. (2002). Solvation forces in branched molecular liquids. Physical Review Letters, 88(24), 246101. https://doi.org/10.1103/physrevlett.88.246101
Loh, K. P., Xie, X. N., , Teo, E. J., Zheng, J. C., & Ando, T. (2002). Surface oxygenation studies on (100)-oriented diamond using an atom beam source and local anodic oxidation. Surface Science, 505(1-3), 93–114. https://doi.org/10.1016/s0039-6028(02)01103-2
Loh, K. P., Xie, X. N., , Teo, E. J., Zheng, J. C., & Ando, T. (2002). Surface oxygenation studies on (100)-oriented diamond using an atom beam source and local anodic oxidation. Surface Science, 505(1-3), 93–114. https://doi.org/10.1016/s0039-6028(02)01103-2
Tripathy, S., Chua, S. J., Ramam, A., Sia, E. K., Pan, J. S., , Yu, G., & Shen, Z. X. (2002). Electronic and vibronic properties of Mg-doped GaN: The influence of etching and annealing. Journal of Applied Physics, 91(5), 3398–3407. https://doi.org/10.1063/1.1446236
Tripathy, S., Chua, S. J., Ramam, A., Sia, E. K., Pan, J. S., , Yu, G., & Shen, Z. X. (2002). Electronic and vibronic properties of Mg-doped GaN: The influence of etching and annealing. Journal of Applied Physics, 91(5), 3398–3407. https://doi.org/10.1063/1.1446236
Xie, X. N., , Li, J., Li, S. F. Y., & Loh, K. P. (2001). Atomic hydrogen beam etching of carbon superstructures on 6H-SiC(0001) studied by reflection high-energy electron diffraction. Diamond and Related Materials, 10(3-7), 1218–1223. https://doi.org/10.1016/s0925-9635(00)00398-8
Xie, X. N., , Li, J., Li, S. F. Y., & Loh, K. P. (2001). Atomic hydrogen beam etching of carbon superstructures on 6H-SiC(0001) studied by reflection high-energy electron diffraction. Diamond and Related Materials, 10(3-7), 1218–1223. https://doi.org/10.1016/s0925-9635(00)00398-8
, Li, J., Li, S. F. Y., Feng, Z., & Valiyaveettil, S. (2000). The formation of two-dimensional supramolecular chiral lamellae by diamide molecules at the solution/graphite interface: A scanning tunneling microscopy study. Langmuir, 16(17), 7023–7030. https://doi.org/10.1021/la000083x
, Li, J., Li, S. F. Y., Feng, Z., & Valiyaveettil, S. (2000). The formation of two-dimensional supramolecular chiral lamellae by diamide molecules at the solution/graphite interface: A scanning tunneling microscopy study. Langmuir, 16(17), 7023–7030. https://doi.org/10.1021/la000083x