Single-molecule protein sensing in a nanopore: a tutorial

Characterization of individual polynucleotide molecules using a membrane channel

Kasianowicz, J. J., Brandin, E., Branton, D., & Deamer, D. W. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13770 · Cited by 3,362

Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore

Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., & Gouaux, J. E. (1996) · Science · doi:10.1126/science.274.5294.1859 · Cited by 2,377

Nanopore sequencing and assembly of a human genome with ultra-long reads

Jain, M., Koren, S., Miga, K. H., Quick, J., Rand, A. C., Sasani, T. A., Tyson, J. R., Beggs, A. D., Dilthey, A. T., Fiddes, I. T., et al. (2018) · Nature Biotechnology · doi:10.1038/nbt.4060 · Cited by 1,892

Ion-beam sculpting at nanometre length scales

Li, J., Stein, D., McMullan, C., Branton, D., Aziz, M. J., & Golovchenko, J. A. (2001) · Nature · doi:10.1038/35084037 · Cited by 1,677

Graphene as a subnanometre trans-electrode membrane

Garaj, S., Hubbard, W., Reina, A., Kong, J., Branton, D., & Golovchenko, J. A. (2010) · Nature · doi:10.1038/nature09379 · Cited by 1,439

Fabrication of solid-state nanopores with single-nanometre precision

Storm, A. J., Chen, J. H., Ling, X. S., Zandbergen, H. W., & Dekker, C. (2003) · Nature Materials · doi:10.1038/nmat941 · Cited by 1,364

Electrostatic focusing of unlabelled DNA into nanoscale pores using a salt gradient

Wanunu, M., Morrison, W., Rabin, Y., Grosberg, A. Y., & Meller, A. (2010) · Nature Nanotechnology · doi:10.1038/nnano.2009.379 · Cited by 745

Controlling protein translocation through nanopores with bio-inspired fluid walls

Yusko, E. C., Johnson, J. M., Majd, S., Prangkio, P., Rollings, R. C., Li, J., Yang, J., & Mayer, M. (2011) · Nature Nanotechnology · doi:10.1038/nnano.2011.12 · Cited by 660

Identification of single nucleotides in MoS2 nanopores

Feng, J., Liu, K., Bulushev, R. D., Khlybov, S., Dumcenco, D., Kis, A., & Radenovic, A. (2015) · Nature Nanotechnology · doi:10.1038/nnano.2015.219 · Cited by 512

DNA Translocation Governed by Interactions with Solid-State Nanopores

Wanunu, M., Sutin, J. D. B., McNally, B., Chow, A., & Meller, A. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.140475 · Cited by 504

Single molecule sensing with solid-state nanopores: novel materials, methods, and applications

Miles, B. N., Ivanov, A. P., Wilson, K. A., Doğan, F., Japrung, D., & Edel, J. B. (2013) · Chem. Soc. Rev. · doi:10.1039/c2cs35286a · Cited by 499

Real-time shape approximation and fingerprinting of single proteins using a nanopore

Yusko, E. C., Bruhn, B. R., Eggenberger, O. M., Houghtaling, J., Rollings, R. C., Walsh, N. C., Nandivada, S., Pindrus, M., Hall, A. R., Sept, D., et al. (2017) · Nature Nanotechnology · doi:10.1038/nnano.2016.267 · Cited by 473

Single-Molecule Protein Unfolding in Solid State Nanopores

Talaga, D. S., & Li, J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja901088b · Cited by 413

Fast Translocation of Proteins through Solid State Nanopores

Plesa, C., Kowalczyk, S. W., Zinsmeester, R., Grosberg, A. Y., Rabin, Y., & Dekker, C. (2013) · Nano Letters · doi:10.1021/nl3042678 · Cited by 381

Unfoldase-mediated protein translocation through an α-hemolysin nanopore

Nivala, J., Marks, D. B., & Akeson, M. (2013) · Nature Biotechnology · doi:10.1038/nbt.2503 · Cited by 361

Single‐Molecule Sensors: Challenges and Opportunities for Quantitative Analysis

Gooding, J. J., & Gaus, K. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201600495 · Cited by 340

Single-molecule analysis of DNA-protein complexes using nanopores

Hornblower, B., Coombs, A., Whitaker, R. D., et al. (2007) · Nature Methods · doi:10.1038/nmeth1021 · Cited by 309

Multistep protein unfolding during nanopore translocation

Rodriguez-Larrea, D., & Bayley, H. (2013) · Nature Nanotechnology · doi:10.1038/nnano.2013.22 · Cited by 305

Electro-osmotic capture and ionic discrimination of peptide and protein biomarkers with FraC nanopores

Huang, G., Willems, K., Soskine, M., Wloka, C., & Maglia, G. (2017) · Nature Communications · doi:10.1038/s41467-017-01006-4 · Cited by 278

Single-molecule site-specific detection of protein phosphorylation with a nanopore

Rosen, C. B., Rodriguez-Larrea, D., & Bayley, H. (2014) · Nature Biotechnology · doi:10.1038/nbt.2799 · Cited by 270

Nanopore-Based Measurements of Protein Size, Fluctuations, and Conformational Changes

Waduge, P., Hu, R., Bandarkar, P., Yamazaki, H., Cressiot, B., Zhao, Q., Whitford, P. C., & Wanunu, M. (2017) · ACS Nano · doi:10.1021/acsnano.7b01212 · Cited by 270

Identification of single amino acid differences in uniformly charged homopolymeric peptides with aerolysin nanopore

Piguet, F., Ouldali, H., Pastoriza-Gallego, M., Manivet, P., Pelta, J., & Oukhaled, A. (2018) · Nature Communications · doi:10.1038/s41467-018-03418-2 · Cited by 268

Decoding DNA, RNA and peptides with quantum tunnelling

Di Ventra, M., & Taniguchi, M. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2015.320 · Cited by 242

Structure of Peptides Investigated by Nanopore Analysis

Sutherland, T. C., Long, Y., Stefureac, R. I., Bediako-Amoa, I., Kraatz, H., & Lee, J. S. (2004) · Nano Letters · doi:10.1021/nl049413e · Cited by 229

Specific Protein Detection Using Designed DNA Carriers and Nanopores

Bell, N. A. W., & Keyser, U. F. (2015) · Journal of the American Chemical Society · doi:10.1021/ja512521w · Cited by 202

Electroosmotic Trap Against the Electrophoretic Force Near a Protein Nanopore Reveals Peptide Dynamics During Capture and Translocation

Asandei, A., Schiopu, I., Chinappi, M., Seo, C. H., Park, Y., & Luchian, T. (2016) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b03697 · Cited by 166

Nanopore Sensing of Protein Folding

Si, W., & Aksimentiev, A. (2017) · ACS Nano · doi:10.1021/acsnano.7b02718 · Cited by 159

Thermal Unfolding of Proteins Probed at the Single Molecule Level Using Nanopores

Payet, L., Martinho, M., Pastoriza‐Gallego, M., Betton, J., Auvray, L., Pelta, J., & Mathé, J. (2012) · Analytical Chemistry · doi:10.1021/ac300129e · Cited by 153

Label-Free and Real-Time Detection of Protein Ubiquitination with a Biological Nanopore

Wloka, C., Meervelt, V. V., van Gelder, D., Danda, N., Jager, N., Williams, C., & Maglia, G. (2017) · ACS Nano · doi:10.1021/acsnano.6b07760 · Cited by 134

Slowing down single-molecule trafficking through a protein nanopore reveals intermediates for peptide translocation

Mereuta, L., Roy, M., Asandei, A., Lee, J. K., Park, Y., Andricioaei, I., & Luchian, T. (2014) · Scientific Reports · doi:10.1038/srep03885 · Cited by 126

Real-Time Conformational Changes and Controlled Orientation of Native Proteins Inside a Protein Nanoreactor

Meervelt, V. V., Soskine, M., Singh, S., Schuurman‐Wolters, G. K., Wijma, H. J., Poolman, B., & Maglia, G. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b10106 · Cited by 113

Simultaneous Quantification of Multiple Cancer Biomarkers in Blood Samples through DNA‐Assisted Nanopore Sensing

Liu, L., Li, T., Zhang, S., Peng, S., Guo, B., Zhao, Y., & Wu, H. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201803324 · Cited by 103

Optical sensing and analyte manipulation in solid-state nanopores

Gilboa, T., & Meller, A. (2015) · The Analyst · doi:10.1039/c4an02388a · Cited by 91

Direct Sensing and Discrimination among Ubiquitin and Ubiquitin Chains Using Solid-State Nanopores

Nir, I., Huttner, D., & Meller, A. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.03.025 · Cited by 87

SDS-assisted protein transport through solid-state nanopores

Restrepo-Pérez, L., John, S., Aksimentiev, A., et al. (2017) · Nanoscale · doi:10.1039/c7nr02450a · Cited by 84

Sampling a Biomarker of the Human Immunodeficiency Virus across a Synthetic Nanopore

Niedzwiecki, D. J., Iyer, R., Borer, P. N., & Movileanu, L. (2013) · ACS Nano · doi:10.1021/nn400125c · Cited by 81

Protein sequencing via nanopore based devices: a nanofluidics perspective

Chinappi, M., & Cecconi, F. (2018) · Journal of Physics Condensed Matter · doi:10.1088/1361-648x/aababe · Cited by 78

Pulling Peptides across Nanochannels: Resolving Peptide Binding and Translocation through the Hetero-oligomeric Channel from Nocardia farcinica

Singh, P. R., Bárcena‐Uribarri, I., Modi, N., Kleinekathöfer, U., Benz, R., Winterhalter, M., & Mahendran, K. R. (2012) · ACS Nano · doi:10.1021/nn303900y · Cited by 73

Nanopore sensing of individual transcription factors bound to DNA

Squires, A. H., Atas, E., & Meller, A. (2015) · Scientific Reports · doi:10.1038/srep11643 · Cited by 71

Communication: Charge, diffusion, and mobility of proteins through nanopores

Muthukumar, M. (2014) · The Journal of Chemical Physics · doi:10.1063/1.4894401 · Cited by 63

Sensing Native Protein Solution Structures Using a Solid-state Nanopore: Unraveling the States of VEGF

Varongchayakul, N., Huttner, D., Grinstaff, M. W., & Meller, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-19332-y · Cited by 53

Observing Changes in the Structure and Oligomerization State of a Helical Protein Dimer Using Solid-State Nanopores

Niedzwiecki, D. J., Lanci, C. J., Shemer, G., et al. (2015) · ACS Nano · doi:10.1021/acsnano.5b02714 · Cited by 38

Optical Monitoring of In Situ Iron Loading into Single, Native Ferritin Proteins

Yousefi, A., Ying, C., Parmenter, C. D. J., Assadipapari, M., Sanderson, G., Zheng, Z., Xu, L., Zargarbashi, S., Hickman, G. J., Cousins, R. B., et al. (2023) · Nano Letters · doi:10.1021/acs.nanolett.3c00042 · Cited by 37