Jühlen, Ramona et al. (2024) ‘Alteration of actin cytoskeletal organisation in fetal akinesia deformation sequence’, Scientific Reports, 14(1). Available at: https://doi.org/10.1038/s41598-023-50615-1.

Kapinos, Larisa E. et al. (2024) ‘Mechanism of exportin retention in the cell nucleus’, Journal of Cell Biology, 223(2). Available at: https://doi.org/10.1083/jcb.202306094.

Postigo, Alejandro et al. (2024) ‘Assessing the influence of small structural modifications in simple DNA-based nanostructures on their role as drug nanocarriers’, Biomaterials Science, 12(6), pp. 1549–1557. Available at: https://doi.org/10.1039/d3bm01987j.

Svirelis, Justas et al. (2023) ‘Stable trapping of multiple proteins at physiological conditions using nanoscale chambers with macromolecular gates’, Nature Communications, 14(1). Available at: https://doi.org/10.1038/s41467-023-40889-4.

Baumann, K.N. et al. (2023) ‘A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on Aβ42 Aggregation’, ACS Chemical Neuroscience, 14(2), pp. 323–329. Available at: https://doi.org/10.1021/acschemneuro.2c00765.

Jühlen, Ramona and Fahrenkrog, Birthe (2023) ‘From the sideline: Tissue‐specific nucleoporin function in health and disease, an update’, FEBS Letters, 597(22), pp. 2750–2768. Available at: https://doi.org/10.1002/1873-3468.14761.

Diez, Lisa et al. (2023) ‘Analysis of Tau/Nucleoporin Interactions by Surface Plasmon Resonance Spectroscopy’, in Cieplak, Andrzej Stanisław (ed.) Protein Aggregation. New York: Springer (Methods in Molecular Biology), pp. 95–109. Available at: https://doi.org/10.1007/978-1-0716-2597-2_8.

Kapinos, Larisa E. and Lim, Roderick Y. H. (2023) ‘Multivalent Interactions with Intrinsically Disordered Proteins Probed by Surface Plasmon Resonance’, in Goldberg, Martin W. (ed.) The Nuclear Pore Complex. New York: Springer (Methods in Molecular Biology), pp. 311–328. Available at: https://doi.org/10.1007/978-1-0716-2337-4_21.

Diez, Lisa et al. (2022) ‘Phosphorylation but Not Oligomerization Drives the Accumulation of Tau with Nucleoporin Nup98’, International journal of molecular sciences, 23(7), p. 3495. Available at: https://doi.org/10.3390/ijms23073495.

Kalita, Joanna et al. (2022) ‘Karyopherin enrichment and compensation fortifies the nuclear pore complex against nucleocytoplasmic leakage’, Journal of Cell Biology, 221(3), p. e202108107. Available at: https://doi.org/10.1083/jcb.202108107.

Tarvirdipour, Shabnam et al. (2022) ‘A self-assembling peptidic platform to boost the cellular uptake and nuclear delivery of oligonucleotides’, Biomaterials science, 10(15), pp. 4309–4323. Available at: https://doi.org/10.1039/d2bm00826b.

Hoogenboom, Bart W. et al. (2021) ‘Physics of the nuclear pore complex: Theory, modeling and experiment’, Physics reports, 921, pp. 1–53. Available at: https://doi.org/10.1016/j.physrep.2021.03.003.

Kalita, Joanna, Kapinos, Larisa E. and Lim, Roderick Y. H. (2021) ‘On the asymmetric partitioning of nucleocytoplasmic transport - recent insights and open questions’, Journal of cell science, 134(7), p. jcs240382. Available at: https://doi.org/10.1242/jcs.240382.

Sharma, Deepika et al. (2021) ‘Optimization of Nanofluidic Devices for Geometry-Induced Electrostatic Trapping’, Particle & Particle Systems Characterization, 38(2), p. 2170003. Available at: https://doi.org/10.1002/ppsc.202170003.

Sharma, Deepika et al. (2021) ‘Surface-modified elastomeric nanofluidic devices for single nanoparticle trapping’, Microsystems & Nanoengineering, 7(1), p. 46. Available at: https://doi.org/10.1038/s41378-021-00273-y.

Avsar, Saziye Yorulmaz et al. (2020) ‘Immobilization of arrestin-3 on different biosensor platforms for evaluating GPCR binding’, Physical Chemistry Chemical Physics, 22(41), pp. 24086–24096. Available at: https://doi.org/10.1039/d0cp01464h.

Barbato, Suncica et al. (2020) ‘Karyopherin enrichment at the nuclear pore complex attenuates Ran permeability’, Journal of Cell Science, 133(3), p. aheadofrint. Available at: https://doi.org/10.1242/jcs.238121.

Santos, José Carlos et al. (2020) ‘Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria’, Nature Communications, 11(1), p. 3276. Available at: https://doi.org/10.1038/s41467-020-16889-z.

Zelmer, Christina et al. (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), pp. 2770–2778. Available at: https://doi.org/10.1073/pnas.1916395117.

Eftekharzadeh, B. et al. (2019) ‘Erratum: Tau Protein Disrupts Nucleocytoplasmic Transport in Alzheimer’s Disease (Neuron (2018) 99(5) (925–940.e7), (S0896627318306378) (10.1016/j.neuron.2018.07.039))’, Neuron, 101(2). Available at: https://doi.org/10.1016/j.neuron.2018.12.031.

Kassianidou, Elena, Kalita, Joanna and Lim, Roderick Y. H. (2019) ‘The role of nucleocytoplasmic transport in mechanotransduction’, Experimental cell research, 377(1-2), pp. 86–93. Available at: https://doi.org/10.1016/j.yexcr.2019.02.009.

Panatala, Radhakrishnan et al. (2019) ‘Nuclear Pore Membrane Proteins Self-Assemble into Nanopores’, Biochemistry, 58(6), pp. 484–488. Available at: https://doi.org/10.1021/acs.biochem.8b01179.

Kapinos, L.E. et al. (2018) ‘Erratum: Karyopherin-Centric Control of Nuclear Pores Based on Molecular Occupancy and Kinetic Analysis of Multivalent Binding with FG Nucleoporins (Biophysical Journal (2014) 106(8) (1751–1762)(S0006349514002276)(10.1016/j.bpj.2014.02.021))’, Biophysical Journal, 115(12). Available at: https://doi.org/10.1016/j.bpj.2018.11.3125.

Eftekharzadeh, Bahareh et al. (2018) ‘Tau Protein Disrupts Nucleocytoplasmic Transport in Alzheimer’s Disease’, Neuron, 99(5), pp. 925–940.e7. Available at: https://doi.org/10.1016/j.neuron.2018.07.039.

Emilsson, Gustav et al. (2018) ‘Gating Protein Transport in Solid State Nanopores by Single Molecule Recognition’, ACS Central Science, 4(8), pp. 1007–1014. Available at: https://doi.org/10.1021/acscentsci.8b00268.

Emilsson, Gustav et al. (2018) ‘Polymer brushes in solid-state nanopores form an impenetrable entropic barrier for proteins’, Nanoscale, 10(10), pp. 4663–4669. Available at: https://doi.org/10.1039/c7nr09432a.

Ganier, Olivier et al. (2018) ‘Structural centrosome aberrations promote non-cell-autonomous invasiveness’, The EMBO journal, p. e98576. Available at: https://doi.org/10.15252/embj.201798576.

Malekian, Bita et al. (2018) ‘Detecting Selective Protein Binding inside Plasmonic Nanopores: Towards a Mimic of the Nuclear Pore Complex’, Frontiers in Chemistry, 6, p. 637. Available at: https://doi.org/10.3389/fchem.2018.00637.

Zanetti-Dällenbach, Rosanna et al. (2018) ‘Length Scale Matters: Real-Time Elastography versus Nanomechanical Profiling by Atomic Force Microscopy for the Diagnosis of Breast Lesions’, BioMed research international, 2018, p. 3840597. Available at: https://doi.org/10.1155/2018/3840597.

Benning, Friederike M. C. et al. (2017) ‘High-Speed Atomic Force Microscopy Visualization of the Dynamics of the Multienzyme Fatty Acid Synthase’, ACS Nano, 11(11), pp. 10852–10859. Available at: https://doi.org/10.1021/acsnano.7b04216.

Emilsson, Gustav et al. (2017) ‘Surface plasmon resonance methodology for monitoring polymerization kinetics and morphology changes of brushes - evaluated with poly(N-isopropylacrylamide)’, Applied Surface Science, 396, pp. 384–392. Available at: https://doi.org/10.1016/j.apsusc.2016.10.165.

Kapinos, Larisa E. et al. (2017) ‘Karyopherins regulate nuclear pore complex barrier and transport function’, Journal of Cell Biology, 216(11), pp. 3609–3624. Available at: https://doi.org/10.1083/jcb.201702092.

Luo, Wangxi et al. (2017) ‘Axonemal Lumen Dominates Cytosolic Protein Diffusion inside the Primary Cilium’, Scientific Reports, 7(1), p. 15793. Available at: https://doi.org/10.1038/s41598-017-16103-z.

Sakiyama, Yusuke, Panatala, Radhakrishnan and Lim, Roderick Y. H. (2017) ‘Structural dynamics of the nuclear pore complex’, Seminars in Cell and Developmental Biology, 68, pp. 27–33. Available at: https://doi.org/10.1016/j.semcdb.2017.05.021.

Schoch, Rafael L. et al. (2017) ‘Protein exclusion is preserved by temperature sensitive PEG brushes’, Polymer, 132, pp. 362–367. Available at: https://doi.org/10.1016/j.polymer.2017.10.063.

Sharma, Deepika et al. (2017) ‘Single positively charged particle trapping in nanofluidic systems’, Microelectronic Engineering, 175, pp. 43–49. Available at: https://doi.org/10.1016/j.mee.2017.01.001.

Reyes Lua, Magaly et al. (2016) ‘Superior Rim Stability of the Lens Capsule Following Manual Over Femtosecond Laser Capsulotomy’, Investigative Ophthalmology & Visual Science, 57(6), pp. 2839–49. Available at: https://doi.org/10.1167/iovs.15-18355.

Sakiyama, Yusuke et al. (2016) ‘Spatiotemporal dynamics of the nuclear pore complex transport barrier resolved by high-speed atomic force microscopy’, Nature Nanotechnology, 11(8), pp. 719–23. Available at: https://doi.org/10.1038/nnano.2016.62.

Vovk, Andrei et al. (2016) ‘Simple biophysics underpins collective conformations of the intrinsically disordered proteins of the Nuclear Pore Complex’, eLife, 5, p. e10785. Available at: https://doi.org/10.7554/elife.10785.001.

Vujica, Suncica et al. (2016) ‘Nucleocytoplasmic Transport: A Paradigm for Molecular Logistics in Artificial Systems’, Chimia, 70(6), pp. 413–7. Available at: https://doi.org/10.2533/chimia.2016.413.

Zweifel, Ludovit P., Shorubalko, Ivan and Lim, Roderick Y. H. (2016) ‘Helium scanning transmission ion microscopy and electrical characterization of glass nanocapillaries with reproducible tip geometries’, ACS nano, 10(2), pp. 1918–25. Available at: https://doi.org/10.1021/acsnano.5b05754.

Emilsson, Gustav et al. (2015) ‘Strongly Stretched Protein Resistant Poly(ethylene glycol) Brushes Prepared by Grafting-To’, ACS applied materials & interfaces, 7(14), pp. 7505–15. Available at: https://doi.org/10.1021/acsami.5b01590.

Lim, Roderick Y. H., Huang, Binlu and Kapinos, Larisa E. (2015) ‘How to operate a nuclear pore complex by Kap-centric control’, Nucleus (Austin, Tex.), 6(5), pp. 366–372. Available at: https://doi.org/10.1080/19491034.2015.1090061.

Plodinec, Marija and Lim, Roderick Y. H. (2015) ‘Nanomechanical characterization of living mammary tissues by atomic force microscopy’, Methods in Molecular Biology, 1293, pp. 231–46. Available at: https://doi.org/10.1007/978-1-4939-2519-3_14.

Wagner, Raphael S. et al. (2015) ‘Promiscuous Binding of Karyopherinβ1 Modulates FG Nucleoporin Barrier Function and Expedites NTF2 Transport Kinetics’, Biophysical journal, 108(4), pp. 918–27. Available at: https://doi.org/10.1016/j.bpj.2014.12.041.

Fuxreiter, Monika et al. (2014) ‘Disordered Proteinaceous Machines’, Chemical reviews, 114(13), pp. 6806–6843. Available at: https://doi.org/10.1021/cr4007329.

Kapinos, Larisa E. et al. (2014) ‘Karyopherin-centric control of nuclear pores based on molecular occupancy and kinetic analysis of multivalent binding with FG nucleoporins’, Biophysical journal, 106(8), pp. 1751–62. Available at: https://doi.org/10.1016/j.bpj.2014.02.021.

Schleicher, Kai D et al. (2014) ‘Selective transport control on molecular velcro made from intrinsically disordered proteins’, Nature nanotechnology, 9(7), pp. 525–30. Available at: https://doi.org/10.1038/nnano.2014.103.

Halfter, Willi et al. (2013) ‘The Bi-Functional Organization of Human Basement Membranes’, PLoS ONE, 8(7), p. e67660. Available at: https://doi.org/10.1371/journal.pone.0067660.

Schoch, Rafael L and Lim, Roderick Y H (2013) ‘Non-interacting molecules as innate structural probes in surface plasmon resonance’, Langmuir, 29(12), pp. 4068–76. Available at: https://doi.org/10.1021/la3049289.

Yang, Liu et al. (2013) ‘Mutations in LMNA Modulate the Lamin A - Nesprin-2 Interaction and Cause LINC Complex Alterations’, PLoS ONE, 8(8), p. e71850. Available at: https://doi.org/10.1371/journal.pone.0071850.

Henrich, Paul B. et al. (2012) ‘Nanoscale topographic and biomechanical studies of the human internal limiting membrane’, Investigative ophthalmology & visual science, 53(6), pp. 2561–70. Available at: https://doi.org/10.1167/iovs.11-8502.

Lim, Roderick Y H and 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), pp. 1–2. Available at: https://doi.org/10.1016/j.jsb.2011.12.011.

Plodinec, Marija et al. (2012) ‘The nanomechanical signature of breast cancer.’, Nature nanotechnology, 7(11), pp. 757–65. Available at: https://doi.org/10.1038/nnano.2012.167.

Schoch, Rafael L., Kapinos, Larisa E. and Lim, Roderick Y. H. (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), pp. 16911–6. Available at: https://doi.org/10.1073/pnas.1208440109.

Hyotyla, J. T. and Lim, R. Y. H. (2012) ‘Atomic force microscopy’, in Supramolecular chemistry. From molecules to nanomaterials. Oxford: Wiley-Blackwell (Supramolecular chemistry. From molecules to nanomaterials), pp. 659–668. Available at: https://doi.org/10.1002/9780470661345.smc043.

Hyotyla, Janne T, Deng, Jie and Lim, Roderick Y H (2011) ‘Synthetic Protein Targeting by the Intrinsic Biorecognition Functionality of Poly(ethylene glycol) Using PEG Antibodies as Biohybrid Molecular Adaptors’, ACS nano, 5(6), pp. 5180–7. Available at: https://doi.org/10.1021/nn201327y.

Kowalczyk, Stefan W et al. (2011) ‘Single-molecule transport across an individual biomimetic nuclear pore complex’, Nature Nanotechnology, 6(7), pp. 433–8. Available at: https://doi.org/10.1038/nnano.2011.88.

Backmann, Natalija et al. (2010) ‘Sensing surface PEGylation with microcantilevers’, Beilstein Journal of Nanotechnology, 1, pp. 3–13. Available at: https://doi.org/10.3762/bjnano.1.2.

Peleg, O. and Lim, R. Y. H. (2010) ‘Converging on the function of intrinsically disordered nucleoporins in the nuclear pore complex’, Biological Chemistry, 391(7), pp. 719–30. Available at: https://doi.org/10.1515/bc.2010.092.

Elad, Nadav et al. (2009) ‘Structural analysis of the nuclear pore complex by integrated approaches’, Current Opinion in Structural Biology, 19(2), pp. 226–32. Available at: https://doi.org/10.1016/j.sbi.2009.02.009.

Lim, Roderick Y H and Deng, Jie (2009) ‘Interaction forces and reversible collapse of a polymer brush-gated nanopore’, ACS nano, 3(10), pp. 2911–8. Available at: https://doi.org/10.1021/nn900152m.

Staple, Douglas B. et al. (2009) ‘Stretching, unfolding, and deforming protein filaments adsorbed at solid-liquid interfaces using the tip of an atomic-force microscope’, Physical Review Letters, 102(12), p. 128302. Available at: https://doi.org/10.1103/physrevlett.102.128302.

Lim, Roderick Y. H., Aebi, Ueli and Fahrenkrog, Birthe (2008) ‘Towards reconciling structure and function in the nuclear pore complex’, Histochemistry and cell biology, 129(2), pp. 105–16. Available at: https://doi.org/10.1007/s00418-007-0371-x.

Lim, Roderick Y H (2007) ‘Gate-crashing the nuclear pore complex’, Structure: with folding and design, 15(8), pp. 889–91. Available at: https://doi.org/10.1016/j.str.2007.07.005.

Lim, Roderick Y H et al. (2007) ‘Nanomechanical basis of selective gating by the nuclear pore complex’, Science, 318(5850), pp. 640–3. Available at: https://doi.org/10.1126/science.1145980.

Lim, Roderick Y H et al. (2007) ‘Nanomechanical interactions of phenylalanine-glycine nucleoporins studied by single molecule force-volume spectroscopy’, Journal of Structural Biology, 159(2), pp. 277–89. Available at: https://doi.org/10.1016/j.jsb.2007.01.018.

Lim, Roderick Y H, Aebi, Ueli and Stoffler, Daniel (2006) ‘From the trap to the basket : getting to the bottom of the nuclear pore complex’, Chromosoma, 115(1), pp. 15–26. Available at: https://doi.org/10.1007/s00412-005-0037-1.

Lim, Roderick Y. H. and Fahrenkrog, Birthe (2006) ‘The nuclear pore complex up close’, Current opinion in cell biology, 18(3), pp. 342–347. Available at: https://doi.org/10.1016/j.ceb.2006.03.006.

Lim, Roderick Y. H. et al. (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), pp. 9512–7. Available at: https://doi.org/10.1073/pnas.0603521103.

Lim, Roderick Y H and Aebi, Ueli (2005) ‘In silico access to the nuclear pore complex’, Structure: with folding and design, 13(12), pp. 1741–3. Available at: https://doi.org/10.1016/j.str.2005.11.002.

Lim, Roderick Y. H. and O’Shea, S. J. (2004) ‘Discrete solvation layering in confined binary liquids’, Langmuir, 20(12), pp. 4916–9. Available at: https://doi.org/10.1021/la036200g.

Lim, R., Li, S. F. Y. and O’Shea, S. J. (2002) ‘Solvation forces using sample-modulation atomic force microscopy’, Langmuir, 18(16), pp. 6116–6124. Available at: https://doi.org/10.1021/la011789+.

Lim, R. and O’Shea, S. J. (2002) ‘Solvation forces in branched molecular liquids’, Physical Review Letters, 88(24), p. 246101. Available at: https://doi.org/10.1103/physrevlett.88.246101.

Loh, K. P. et al. (2002) ‘Surface oxygenation studies on (100)-oriented diamond using an atom beam source and local anodic oxidation’, Surface Science, 505(1-3), pp. 93–114. Available at: https://doi.org/10.1016/s0039-6028(02)01103-2.

Tripathy, S. et al. (2002) ‘Electronic and vibronic properties of Mg-doped GaN: The influence of etching and annealing’, Journal of Applied Physics, 91(5), pp. 3398–3407. Available at: https://doi.org/10.1063/1.1446236.

Xie, X. N. et al. (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), pp. 1218–1223. Available at: https://doi.org/10.1016/s0925-9635(00)00398-8.

Lim, R. et al. (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), pp. 7023–7030. Available at: https://doi.org/10.1021/la000083x.

Kornilova, S. et al. (1998) ‘DNA interaction with biologically active metal ions. Cooperativity of metal ion binding and compacting of DNA’, Acta Biochimica Polonica, 45(1), pp. 107–17. Available at: https://doi.org/10.18388/abp.2017_1496.

Andrushchenko, VV et al. (1997) ‘IR-spectroscopic studies of divalent metal ion effects on DNA hydration’, Journal of molecular structure, 408, pp. 225–228. Available at: https://doi.org/10.1016/s0022-2860(96)09672-x.

Hackl, E. V. et al. (1997) ‘Study of Ca2+, Mn2+and Cu2+ binding to DNA in solution by means of IR spectroscopy’, Journal of Molecular Structure, 408, pp. 229–232. Available at: https://doi.org/10.1016/s0022-2860(96)09534-8.

Kornilova, S. V. et al. (1997) ‘Kalorimetricheskoe issledovanie vliianiia ionov Ca2+ i Mn2+ na perekhodspiral”-klubok v DNK’, Biofizika, 42(3), pp. 599–606.

Kornilova, S. V. et al. (1997) ‘Vibrational spectroscopic studies of the divalent metal ion effect on DNA structural transitions’, Journal of Molecular Structure, 408, pp. 219–223. Available at: https://doi.org/10.1016/s0022-2860(96)09671-8.

Kornilova, S. V., Kapinos Schneider, Larisa E. E and Blagoĭ, Iu. P. (1995) ‘Izuchenie vzaimodeĭstviia DNK s ionami kal’tsiia metodom kolebatel’noĭ spektroskopii’, Molekulyarnaya Biologiya, 29(3), pp. 574–84.

Blagoĭ, Iu P. et al. (1994) ‘Strukturnye i fiziko-khimicheskie kharakteristiki DNK iz tkaneǐ zhivotnykh, podvergavshikhsia dlitel’nomu khronicheskomu oblucheniiu v zone chernobylia’, Biofizika, 39(4), pp. 637–45.

Kornilova, S. V. et al. (1994) ‘Izuchenie metodami IK- i Ramanovskoǐ spektroskopii vzaimodeǐstviia DNK s ionami medi’, Biofizika, 39(3), pp. 423–36.

Kornilova, S. A., Kapinos, L. E. and Blagoĭ, Iu. P. (1993) ‘Studies on DNA interaction with manganese ions by IR spectroscopy’, Molekulyarnaya Biologiya, 27(6), pp. 1276–86.