US 5795782A
· Church et al.
· 1998
[cited by applicant]
US 6015714A
· Baldarelli et al.
· 2000
[cited by applicant]
US 6267872B1
· Akeson et al.
· 2001
[cited by applicant]
US 6362001B1
· Cai et al.
· 2002
[cited by applicant]
US 6362002B1
· Denison et al.
· 2002
[cited by applicant]
US 6428959B1
· Deamer
· 2002
[cited by applicant]
US 6464842B1
· Golovchenko et al.
· 2002
[cited by applicant]
US 6465946B1
· Yoon et al.
· 2002
[cited by applicant]
US 6617113B2
· Deamer
· 2003
[cited by applicant]
US 6627067B1
· Branton et al.
· 2003
[cited by applicant]
US 6673615B2
· Denison et al.
· 2004
[cited by applicant]
US 6746594B2
· Akeson et al.
· 2004
[cited by applicant]
US 8673550B2
· Gundlach et al.
· 2014
[cited by applicant]
US 9766248B2
· Lindsay et al.
· 2017
[cited by applicant]
US 20030104428A1
· Branton et al.
· 2003
[cited by applicant]
US 20080287656A1
· Peters et al.
· 2008
[cited by applicant]
US 20110311965A1
· Maglia et al.
· 2011
[cited by applicant]
US 20200123594A1
· Rothberg et al.
· 2020
[cited by applicant]
US 20200348307A1
· Beierle et al.
· 2020
[cited by applicant]
US 20210340192A1
· Nivala
· 2021
[cited by applicant]
US 20220091093A1
· Wanunu et al.
· 2022
[cited by applicant]
US 20220242922A1
· Maglia et al.
· 2022
[cited by applicant]
US 20220277814A1
· Nivala
· 2022
[cited by applicant]
US 20220396758A1
· Nivala et al.
· 2022
[cited by applicant]
US 20220412948A1
· Maglia et al.
· 2022
[cited by applicant]
US 20230048421A1
· Zhang et al.
· 2023
[cited by applicant]
US 20230220002A1
· Long et al.
· 2023
[cited by applicant]
US 20240159768A1
· Lucas et al.
· 2024
[cited by applicant]
CN 104710519A
· 2015
[cited by applicant]
CN 112480204A
· 2021
[cited by applicant]
CN 112500459A
· 2021
[cited by applicant]
EP 2350122A1
· 2011
[cited by applicant]
EP 2978773A1
· 2016
[cited by applicant]
EP 2814939B1
· 2018
[cited by applicant]
EP 3485029A1
· 2019
[cited by applicant]
EP 3598133A1
· 2020
[cited by applicant]
EP 4070092B1
· 2023
[cited by applicant]
JP 2013540423A
· 2013
[cited by applicant]
WO WO0079257A1
· 2000
[cited by applicant]
WO WO2005124888A1
· 2005
[cited by applicant]
WO WO2006028508A2
· 2006
[cited by applicant]
WO WO2009020682A2
· 2009
[cited by applicant]
WO WO2010004265A1
· 2010
[cited by applicant]
WO WO2010034018A2
· 2010
[cited by applicant]
WO WO2010055307A1
· 2010
[cited by applicant]
WO WO2010082860A1
· 2010
[cited by applicant]
WO WO2013014451A1
· 2013
[cited by applicant]
WO WO2013123379
· 2013
[cited by examiner]
WO WO2013123379A2
· 2013
[cited by applicant]
WO WO2014153625A1
· 2014
[cited by applicant]
WO WO2014190299A2
· 2014
[cited by applicant]
WO WO2015040423A1
· 2015
[cited by applicant]
WO WO2016166232A1
· 2016
[cited by applicant]
WO WO2018012963A1
· 2018
[cited by applicant]
WO WO2020055246A1
· 2020
[cited by applicant]
WO WO2020160559A1
· 2020
[cited by applicant]
WO WO2021021592A1
· 2021
[cited by applicant]
WO WO2021101378A1
· 2021
[cited by applicant]
WO WO2021111125A1
· 2021
[cited by applicant]
WO WO2022020461A1
· 2022
[cited by applicant]
WO WO2023055246A1
· 2023
[cited by applicant]
Afshar Bakshloo, Mazdak, et al., Nanopore-Based Protein Identification. Journal of the American Chemical Society 144(6):2716-2725 (2022).
[cited by applicant]
Akeson, M, et al., Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid, and polyuridylic acid as homopolymers or as segments within single RNA molecules. Biophysical Journal 77(6):3227-3233…
[cited by applicant]
Akopian, Tatos, et al., Processive Degradation of Proteins and Other Catalytic Properties of the Proteasome From Thermoplasma Acidophilum. The Journal of biological chemistry 272(3):1791-1798 (1997).
[cited by applicant]
Aksoyoglu, Alphan, et al., Size-dependent forced PEG partitioning into channels: VDAC, OmpC, and α-hemolysin. Proc Natl Acad Sci U S A 113(32):9003-9008 (2016).
[cited by applicant]
Alfaro, Javier Antonio et al., The Emerging Landscape of Single-molecule Protein Sequencing Technologies. Nature Methods 18:604-617 (2021).
[cited by applicant]
An, Na, et al., Single-molecule investigation of G-quadruplex folds of the human telomere sequence in a protein nanocavity. Proceedings of the National Academy of Sciences of the United States of America 111(40):14325-1…
[cited by applicant]
Anderluh, Gregor et al.: Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria). Toxicon 40(2):111-124 (2002).
[cited by applicant]
André, Ingemar., et al., Prediction of the structure of symmetrical protein assemblies. Proc Natl Acad Sci U S A 104(45):17656-17661 (2007).
[cited by applicant]
Aqvist, et al., Dipoles localized at helix termini of proteins stabilize charges. Proc Natl Acad Sci U S A 88(5):2026-2030 (1991).
[cited by applicant]
Asandei, Alina, et al., Electroosmotic Trap Against the Electrophoretic Force Near a Protein Nanopore Reveals Peptide Dynamics During Capture and Translocation. ACS Applied Materials & Interfaces 8(20):13166-13179 (2016…
[cited by applicant]
Baaken, Gerhard, et al., High-resolution size-discrimination of single nonionic synthetic polymers with a highly charged biological nanopore. ACS Nano 9(6):6443-6449 (2015).
[cited by applicant]
Bacri, Laurent, et al., Discrimination of neutral oligosaccharides through a nanopore. Biochem Biophys Res Commun 412(4):561-564 (2011).
[cited by applicant]
Balijepalli, Arvind, et al., Theory of Polymer-nanopore Interactions Refined Using Molecular Dynamics Simulations. Journal of the American Chemical Society 135(18):7064-7072 (2013).
[cited by applicant]
Baniandres; Pablo Martin et al.: Enzyme-less Nanopore Detection of Post-translational Modifications Within Long Polypeptides. Nature Nanotechnology 18:1335-1340 (2023).
[cited by applicant]
Barkow, Sarah R, et al., Polypeptide translocation by the AAA+ ClpXP protease machine. Chemical Biology 16(6):605-612 (2009).
[cited by applicant]
Barlic, Ariana, et al., Lipid Phase Coexistence Favors Membrane Insertion of Equinatoxin-II, a Pore-forming Toxin from Actinia equina. Journal of Biological Chemistry 279(33):34209-34216 (2004).
[cited by applicant]
Bayat, Parisa et al., Comprehensive Structural Assignment of Glycosaminoglycan Oligo and Polysaccharides by Protein Nanopore. Nature Communications. vol. 13, No. 1 (2022): 12 pages.
[cited by applicant]
Baytshtok, Vladimir, et al., A Structurally Dynamic Region of the HsLU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure 24(10):1766-1777 (2016).
[cited by applicant]
Becker, Samuel H, et al., Bacterial Proteasomes: Mechanistic and Functional Insights. Microbiology and Molecular Biology Reviews :MMBR 81(1):1-20 (2016).
[cited by applicant]
Bell, Nicholas, Nanopores Formed by DNA Origami: A Review. FEBS letters 588(19):3564-3570 (2014).
[cited by applicant]
Bellomio, Augusto, et al., Purification, Cloning and Characterization of Fragaceatoxin C, A Novel Actinoporin From The Sea Anemone Actinia Fragacea. Toxicon 54(6):869-880 (2009).
[cited by applicant]
Benaroudj, Nadia, et al., ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. Molecular cell 1:69-78 (2003).
[cited by applicant]
Beta-channel forming cytolysin—Bacillus cytotoxicus | UniProtKB | UniProt. Accession No. A0A2S1A9G3_9BACI in UniProt 2002-2024.
[cited by applicant]
Bezrukov, S., et al., Dynamics and free energy of polymers partitioning into a nanoscale pore. Macromolecules 29, 8517-8522 (1996).
[cited by applicant]
Biesemans, Annemie., et al., A Protein Rotaxane Controls the Translocation of Proteins Across a ClyA Nanopore. Nano Lett 15(9):6076-6081 (2015).
[cited by applicant]
Boersma, Arnold J, et al., Continuous stochastic detection of amino acid enantiomers with a protein nanopore. Angewandte Chemie International Edition English 51(38):9606-9609 (2012).
[cited by applicant]
Booner, Oscar, et al., Osmotic and Activity Coefficients of Sodium and Potassium Glutamate at 298.15 K. Journal of Chemical & Engineering Data 26:147-148 (1981).
[cited by applicant]
Bouchnak, Imen, et al., Structure, function, and substrates of Clp AAA+ protease systems in cyanobacteria, plastids, and apicoplasts: A comparative analysis. Journal of Biological Chemistry 296:1-16 (2021).
[cited by applicant]
Brauning, Bastian, et al., Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. Nature communications 9:1-14 (2018).
[cited by applicant]
Brinkerhoff, Henry, et al., Multiple Rereads of Single Proteins at Single-amino Acid Resolution Using Nanopores. Science 374(6574):1509-1513 (2021).
[cited by applicant]
Buchberger, Alexander, et al., Roles of Cdc48 in Regulated Protein Degradation in Yeast. Sub-cellular Biochemistry 66:195-222 (2013).
[cited by applicant]
Burns, Jonathan, et al., Lipid-bilayer-spanning DNA nanopores with a bifunctional porphyrin anchor. Angewandte Chemie 52(46):12069-12072 (2013).
[cited by applicant]
Butler, Tom Z, et al., Single-molecule DNA Detection With an Engineered MspA Protein Nanopore. Proceedings of the National Academy of Sciences of the United States of America 105(52):20647-20652 (2008).
[cited by applicant]
Cao, Chan, et al., Discrimination of oligonucleotides of different lengths with a wild-type aerolysin nanopore. Nature Nanotechnology 11(8):713-718 (2016).
[cited by applicant]
Cao; Chan et al.: Single-molecule sensing of peptides and nucleic acids by engineered aerolysin nanopores. Nature Communications 10: 4918 (2019).
[cited by applicant]
Castanzo, Dominic, et al., The AAA+ ATPase Msp1 is a Processive Protein Translocase with Robust Unfoldase Activity. Proceedings of the National Academy of Sciences of the United States of America 117(26):14970-14977 (20…
[cited by applicant]
Chen, Baoyu, et al., Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Structure 18(11):1420-1430 (2010).
[cited by applicant]
Chinappi, Mauro, et al., Analytical Model for Particle Capture in Nanopores Elucidates Competition Among Electrophoresis, Electroosmosis, and Dielectrophoresis. ACS Nano 14(11):15816-15828 (2020).
[cited by applicant]
Chinappi, Mauro et al.: Protein sequencing via nanopore based devices: a nanofluidics perspective. Journal of Physics: Condensed Matter, Institute of Physics Publishing, Bristol, GB 30(20):204002 (2018), XP020327001. DO…
[cited by applicant]
Clarke et al., Continuous base identification for single-molecule nanopore DNA sequencing. Nat Nanotechnol. 4(4):265-270 (2009).
[cited by applicant]
Cressiot, Benjamin, et al., Dynamics and Energy Contributions for Transport of Unfolded Pertactin Through a Protein Nanopore. ACS Nano 9(9):9050-61 (2015).
[cited by applicant]
Cressiot, Benjamin, et al., Protein Transport Through a Narrow Solid-state Nanopore at High Voltage: Experiments and Theory. American Chemical Society nano 6(7):6236-6243 (2012).
[cited by applicant]
Cressiot, Benjamin, et al., Thermostable Virus Portal Proteins as Reprogrammable Adapters for Solid-state Nanopore Sensors. Nature Communications 9(4652):1-7 (2018).
[cited by applicant]
Crnković, Ana, et al., Biological Nanopores: Engineering on Demand. Life (Basel) 11(1):27 (2021).
[cited by applicant]
Dal-Peraro, Matteo, et al., Pore-forming toxins: ancient, but never really out of fashion. Nature reviews. Microbiology 14(2):77-92 (2016).
[cited by applicant]
Database UniProt B9W5G6 XP002796191.
[cited by applicant]
Delta-Actitoxin-Aeq1b-like [Orbicella faveolata]. BioProject PRJNA381078, XP-020600665.1. (2017) https://www.ncbi.nlm.nih.gov/protein/1176123762?sat=4&satkey=191642050.
[cited by applicant]
Derrington, Ian M, et al., Nanopore DNA sequencing with MspA. Proceedings of the National Academy of Sciences of the United States of America 107(37):16060-16065 (2010).
[cited by applicant]
Derrington, Ian M. et al.: Subangstrom single-molecule measurements of motor proteins using a nanopore. Nature Biotechnology Sep. 28, 2015.
[cited by applicant]
Dong, Changjiang et al.: The structure of Wza, the translocon for group 1 capsular polysaccharides in
[cited by applicant]
Dong, Changjiang, et al., Wza the Translocon for
[cited by applicant]
Dougana, David, et al., AAA+ proteins and substrate recognition, it all depends on their partner in crime. FEBS Letters 529:6-10 (2002).
[cited by applicant]
Effantin, Gregory, et al., Binding of the ClpA Unfoldase Opens the Axial Gate of ClpP Peptidase. The Journal of Biological Chemistry 285(19):14834-14840 (2010).
[cited by applicant]
EP17734851.3 European Examination Report dated Feb. 12, 2020.
[cited by applicant]
EP20206642.9 Extended European Search Report dated May 3, 2021.
[cited by applicant]
Erlandson, Karl, et al., A Role for the Two-helix Finger of the Seca ATpase in Protein Translocation. Nature. vol. 455, 7215:984-987 (2008).
[cited by applicant]
European Patent Application No. EP22204590 European Extended Search Report dated Aug. 14, 2023.
[cited by applicant]
Faller, Michael, et al., The structure of a mycobacterial outer-membrane channel. Science 303(5661):1189-1192 (2004).
[cited by applicant]
Flynn, Julia, et al., Overlapping Recognition Determinants Within the ssrA Degradation Tag Allow Modulation of Proteolysis. Proceedings of the National Academy of Sciences of the United States of America 98(19):10584-10…
[cited by applicant]
Forouzan, Dara, et al., The Archaeal Proteasome is Regulated by a Network of AAA ATPases. The Journal of Biological Chemistry 287(46):39254-62 (2012).
[cited by applicant]
Forster, Andreas et al.: The 1.9 Å structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions. Molecular Cell 18:589-599 (2005). DOI 10.1016/j.molcel.2005.04.016.
[cited by applicant]
Franceschini, Lorenzo, et al., A nanopore machine promotes the vectorial transport of DNA across membranes. Nature Communications 4(2415): 8 Pages (2013).
[cited by applicant]
Frees, Dorte, et al., Clp ATPases Are Required for Stress Tolerance, Intracellular Replication and Biofilm Formation in
[cited by applicant]
Furini, Simone, et al., Model-based Prediction of the Alpha-hemolysin Structure in the Hexameric State. Biophysical journal 95 (5): 2265-2274 (2008).
[cited by applicant]
García-Ortega, Lucia, et al., The Behavior of Sea Anemone Actinoporins at the Water-membrane Interface. Biochimica Et Biophysica Acta 1808 (9):2275-2288 (2011).
[cited by applicant]
Gerega, Alexandra, et al., VAT, the Thermoplasma Homolog of Mammalian p97/VCP, is an N Domain-regulated Protein Unfoldase. The Journal of Biological Chemistry 280(52):42856-42862 (2020).
[cited by applicant]
Gimenez-Andres, Manuel, et al., The Many Faces of Amphipathic Helices. Biomolecules 8(45):1-14 (2018).
[cited by applicant]
Glynn, Steven E, et al., Dynamic and Static Components Power Unfolding in Topologically Closed Rings of a AAA+ Proteolytic Machine. Nature Structural & Molecular Biology 19(6):616-622 (2012).
[cited by applicant]
Gonzalez-Perez, Alfredo, et al., Biomimetic Triblock Copolymer Membrane Arrays: A Stable Template for Functional Membrane Proteins. Langmuir 25(18):10447-10450 (2009).
[cited by applicant]
Gouaux, J.E, et al., Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore. Proceedings of the National Academy of Sciences of the United States of America…
[cited by applicant]
Gu, Li-qun, et al., Electroosmotic Enhancement of the Binding of a Neutral Molecule to a Transmembrane Pore. Proceedings of the National Academy of Sciences of the United States of America 100(26):15498-503 (2003).
[cited by applicant]
Gu, Li-qun, et al., Interaction of the Noncovalent Molecular Adapter, Beta-cyclodextrin, With the Staphylococcal Alpha-hemolysin Pore. Biophysical journal 79(4):1967-75 (2000).
[cited by applicant]
Gu, Li-qun, et al., Stochastic Sensing of Organic Analytes by a Pore-forming Protein Containing a Molecular Adapter. Nature 398:686-690(1999).
[cited by applicant]
Guimaraes, Carla P, et al., Site-specific C-terminal and internal loop labeling of proteins using sortase-mediated reactions. Nature Protocols 8(9):1787-1799 (2013).
[cited by applicant]
Hammerstein, Anne, et al., Subunit Dimers of Alpha-hemolysin Expand the Engineering Toolbox for Protein Nanopores. The Journal of Biological Chemistry 286(16):14324-34 (2011).
[cited by applicant]
Hardy, Simon.P, et al., CytK Toxin of Bacillus Cereus Forms Pores in Planar Lipid Bilayers and is Cytotoxic to Intestinal Epithelia. FEMS Microbiology Letters 197:47-51 (2001).
[cited by applicant]
Henning-Knechtel; Anja et al.: DNA-assisted oligomerization of pore-forming toxin monomers into precisely-controlled protein channels. Nucleic Acids Research 45(21):12057-12068 (2017).
[cited by applicant]
Heron, Andrew, et al., Simultaneous Measurement of Ionic Current and Fluorescence from Single Protein Pores. Journal of the American Chemical Society 131(5):1652-1653 (2009).
[cited by applicant]
Hille, Bertil, Ion Channels of Excitable Membranes, Third edition. Sinauer Associates Inc 37 Pages (2001).
[cited by applicant]
Ho, Ching-Wen., et al., Engineering a nanopore with co-chaperonin function. Sci Adv 1(11):1-9 (2015).
[cited by applicant]
Horton, Robert, et al. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77(1):61-68 (1989).
[cited by applicant]
Huang, Gang, et al., Detection of Single Amino Acid Differences in Haemoglobin From Blood Samples Using a Nanopore. ChemRxiv: 24 Pages (2021).
[cited by applicant]
Huang, Gang, et al., Electro-Osmotic Capture and Ionic Discrimination of Peptide and Protein Biomarkers With Frac Nanopores. Nature Communications 8(935): 11 Pages (2017).
[cited by applicant]
Huang, Gang, et al., Electro-Osmotic Vortices Promote the Capture of Folded Proteins by PlyAB Nanopores. Nano Letters 20(5):3819-3827 (2020).
[cited by applicant]
Huang, Gang et al., FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution. Nature Communications 10:1-10 (2019).
[cited by applicant]
Huang, Gang, et al., PlyAB Nanopores Detect Single Amino Acid Differences in Folded Haemoglobin From Blood. Angewandte Chemie International Edition 61(34): 8 Pages (2022).
[cited by applicant]
Huang, Kevin: Engineering biological nanopores for proteomics study. University of Groningen (2019). DOI: 10.33612/diss.102598418.
[cited by applicant]
Huang, Rui, et al., Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study. Proceedings of the National Academy of Sciences of the United States of America 1-10 (2016).
[cited by applicant]
Huang, Shuo, et al., High-Throughput Optical Sensing of Nucleic Acids in a Nanopore Array. Nature Nanotechnology 10:986-991 (2015).
[cited by applicant]
Huber, Eva, et al., A Unified Mechanism for Proteolysis and Autocatalytic Activation in the 20s Proteasome. Nature communications 7:1-10 (2016).
[cited by applicant]
Huber, Eva, et al., The mammalian proteasome activator PA28 forms an asymmetric α4β3 complex. Structure 25(10):1473-1480 (2017).
[cited by applicant]
Humbard, Matthew A, et al., Ubiquitin-like Small Archaeal Modifier Proteins (SAMPs) in Haloferax Volcanii. Nature 463:54-60 (2010).
[cited by applicant]
Ivanov, Aleksandar P, et al., DNA tunneling detector embedded in a nanopore. Nano Letters 11(1):279-285 (2011).
[cited by applicant]
Jiang, Jiansen, et al., Atomic structure of anthrax protective antigen pore elucidates toxin translocation. Nature 521(7553):545-549 (2015).
[cited by applicant]
Kasianowicz, J J, et al., Characterization of individual polynucleotide molecules using a membrane channel. Proceedings of the National Academy of Sciences of the United States of America 93(24):13770-13773 (1996).
[cited by applicant]
Kavalchuk, Mikhail, et al., Structural Basis of Prokaryotic Ubiquitin-like Protein Engagement and Translocation by the Mycobacterial Mpa-proteasome Complex. Nature Communications 13(1):276 (2022).
[cited by applicant]
Kennedy, Eamonn., et al., Reading the primary structure of a protein with 0.07 nm3 resolution using a subnanometre-diameter pore. Nat Nanotechnol 11(11):968-976 (2016).
[cited by applicant]
Kim, Yong-In, et al., Dynamics of Substrate Denaturation and Translocation by the Clpxp Degradation Machine. Molecular cell 5(4):639-648 (2000).
[cited by applicant]
Kisselev, Alexei, et al., Why Does Threonine, and Not Serine, Function as the Active Site Nucleophile in Proteasomes?. The Journal of Biological Chemistry 275(20):14831-14837 (2000).
[cited by applicant]
Kowalczyk, Stefan W, et al., Detection of Local Protein Structures Along DNA Using Solid-state Nanopores. Nano Letters 10(1):324-328 (2010).
[cited by applicant]
Krasilnikov, Oleg V, et al., Single Polymer Molecules in a Protein Nanopore in the Limit of a Strong Polymer-Pore Attraction. Physical Review Letters 97(1): 4 Pages (2006).
[cited by applicant]
Kravats, Andrea, et al., Unfolding and translocation pathway of substrate protein controlled by structure in repetitive allosteric cycles of the ClpY ATPase. Proceedings of the National Academy of Sciences of the United…
[cited by applicant]
Krishnan R, Smrithi, et al., Autonomously Assembled Synthetic Transmembrane Peptide Pore. Journal of the American Chemical Society 141(7):2949-2959 (2019).
[cited by applicant]
Krishnan Smrithi et al., Designed Alpha-helical Barrels for Charge-selective Peptide Translocation. Chemical Science 12(2):639-649 (2021).
[cited by applicant]
Kristan, Katarina Crnigoj, et al., Molecular Mechanism of Pore Formation by Actinoporins. Toxicon 54(8):1125-34 (2009).
[cited by applicant]
Kuehn et al., Proteasome activator PA28 and its interaction with 20 S proteasomes. Archives of biochemistry and biophysics 329(1):87-96 (1996).
[cited by applicant]
Lamichhane, Usha, et al., Peptide translocation through the mesoscopic channel: binding kinetics at the single molecule level. Eur Biophys J 42(5):363-369 (2013).
[cited by applicant]
Langklotz, Sina, et al., Structure and Function of the Bacterial AAA Protease FtsH. Biochim Biophys Acta 1823(1):40-48 (2012).
[cited by applicant]
Li, Bisheng, et al., Black Phosphorus, a Rising Star 2D Nanomaterial in the Post-Graphene Era: Synthesis, Properties, Modifications, and Photocatalysis Applications. Small 15:1-30 (2019).
[cited by applicant]
Li, et al., Detection of Peptides with Different Charges and Lengths by Using the Aerolysin Nanopore.4, 1-5 (2018).
[cited by applicant]
Li, Jianfeng, et al., A comparative study of point-to-point algorithms for matching spectra. Chemometrics and Intelligent Laboratory Systems 82(1-2): 50-58 (2006).
[cited by applicant]
Liu, Huanting, et al., An Efficient One-step Site-directed Deletion, Insertion, Single and Multiple-site Plasmid Mutagenesis Protocol. BMC biotechnology 8:91 (2008).
[cited by applicant]
Liu, Wenxing et. al., Probing Protein Nanopores With Poly Ethylene Glycols. Proteomics. vol. 22, No. 5-6 (2022): 16 pages.
[cited by applicant]
Liu, Xi, et al., High Expression of Nfat2 Contributes to Carboplatin Resistance in Lung Cancer. Experimental and Molecular Pathology 110:104290 (2019).
[cited by applicant]
Lowe, Jan, et al., Crystal structure of the 20S Proteasome From the archaeon T. acidophilum at 3.4 A resolution. Science 268(5210):533-539 (1995).
[cited by applicant]
Lucas, Florian Leonardus Rudolfus, et al., Protein identification by nanopore peptide profiling. Nature Communications 12(5795): 9 Pages (2021).
[cited by applicant]
Lucas, Florian Leonardus Rudolfus, et al., The Manipulation of the Internal Hydrophobicity of FraC Nanopores Augments Peptide Capture and Recognition. ACS Nano 15(6):9600-9613 (2021).
[cited by applicant]
Ma, Wenzhe, et al., Specificity of Trypsin and Chymotrypsin: Loop-motion-controlled Dynamic Correlation as a Determinant. Biophysical journal 89 (2):1183-1193 (2005).
[cited by applicant]
Macrander, Jason, et al., Evolution of the Cytolytic Pore-Forming Proteins (Actinoporins) in Sea Anemones. Toxins 8(12):1-16 (2016).
[cited by applicant]
Maglia, Giovanni, et al., Analysis of Single Nucleic Acid Molecules With Protein Nanopores. Methods in Enzymology 475:591-623 (2010).
[cited by applicant]
Maglia, Giovanni, et al., Enhanced translocation of single DNA molecules through alpha-hemolysin nanopores by manipulation of internal charge. Proceedings of the National Academy of Sciences of the United States of Amer…
[cited by applicant]
Maillard, Rodrigo A, et al., ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates. Cell 145(3):459-469 (2011).
[cited by applicant]
Manning, Gerald S, The Persistence Length of DNA is Reached From the Persistence Length of Its Null Isomer Through an Internal Electrostatic Stretching Force. Biophysical Journal 91(10):3607-3616 (2006).
[cited by applicant]
Manrao, Elizabeth A, et al., Nucleotide discrimination with DNA immobilized in the MspA nanopore. PLOS One 6(10): 7 Pages (2011).
[cited by applicant]
Manrao, Elizabeth, et al., Reading DNA at Single-nucleotide Resolution With a Mutant MspA Nanopore and phi29 DNA Polymerase. Nature Biotechnology 30(4):349-353 (2012).
[cited by applicant]
Martin, Andreas, et al., Pore Loops of the AAA+ ClpX Machine Grip Substrates to Drive Translocation and Unfolding. Nature Structural & Molecular Biology 15(11):1147-1151 (2008).
[cited by applicant]
Martin, Andreas, et al., Rebuilt AAA + Motors Reveal Operating Principles for ATP-Fuelled Machines. Nature 437:1115-1120 (2005).
[cited by applicant]
Mathe, Jerome, et al., Nanopore unzipping of individual DNA hairpin molecules. Biophysical Journal 87(5):3205-3212 (2004).
[cited by applicant]
Mechaly, Ariel E, et al., Structural Insights Into the Oligomerization and Architecture of Eukaryotic Membrane Pore-forming Toxins. Structure 19 (2):181-91 (2011).
[cited by applicant]
Mechaly; Ariel E. et al.: Structural Insights into the Oligomerization and Architecture of Eukaryotic Membrane Pore-Forming Toxins. Structure 19:181-191 (2011).
[cited by applicant]
Merstorf, Celine, et al., Wild Type, Mutant Protein Unfolding and Phase Transition Detected by Single-nanopore Recording. ACS Chemical Biology 7(4):652-658 (2012).
[cited by applicant]
Mesa-Galloso, Haydee et al.: Disrupting a key hydrophobic pair in the oligomerization interface of the actinoporins impairs their pore-forming activity. Protein Science 26:550-565 (2017). https://onlinelibrary.wiley.com…
[cited by applicant]
Miethke, Marcus, et al., Involvement of Bacillus Subtilis ClpE in CtsR Degradation and Protein Quality Control. Journal of Bacteriology 188(13):4610-4619 (2006).
[cited by applicant]
Miles, George, et al., Assembly of the Bi-component Leukocidin Pore Examined by Truncation Mutagenesis. The Journal of Biological Chemistry 281(4):2205-14 (2006).
[cited by applicant]
Miles, George, et al., The Staphylococcal Leukocidin Bicomponent Toxin Forms Large Ionic Channels. Biochemistry 40(29):8514-8522 (2001).
[cited by applicant]
Mishra, Ribhav, et al., Proteasome-mediated Proteostasis: Novel Medicinal and Pharmacological Strategies for Diseases. Medicinal Research Reviews 38(6):1916-1973 (2018).
[cited by applicant]
Mitchell, Jonathan, et al., Sequence-Dependent Persistence Lengths of DNA. Journal of Chemical Theory and Computation 13(4):1539-1555 (2017).
[cited by applicant]
Mohammad, Mohammad, et al., Controlling a single protein in a nanopore through electrostatic traps. 130(12):4081-4088 (2008).
[cited by applicant]
Morante, Koldo, et al., A Pore-Forming Toxin Requires a Specific Residue for Its Activity in Membranes with Particular Physicochemical Properties. Journal of Biological Chemistry 290(17):10850-10861 (2015).
[cited by applicant]
Morante, Koldo et al.: Functional characterization of Val60, a key residue involved in the membrane-oligomerization of fragaceatoxin C, an actinoporin from Actinia fragacea. FEBS Letters 589(15):1840-1846 (2015). https:…
[cited by applicant]
Motone; Keisuke et al.: Herding cats: Label-based approaches in protein translocation through nanopore sensors for single-molecule protein sequence analysis. Science 24:103032 (2021).
[cited by applicant]
Motone, Keisuke et. al., Multi-pass, Single-molecule Nanopore Reading of Long Protein Strands With Single-amino Acid Sensitivity. bioRxiv : The Preprint Server for Biology (2023): 47 pages.
[cited by applicant]
Motone; Keisuke et al.: Not if but when nanopore protein sequencing meets single-cell proteomics. Nature Methods 20:336-338 (2023).
[cited by applicant]
Movileanu, Liviu, et al., Interactions of peptides with a protein pore. Biophysical Journal 89(2):1030-1045 (2005).
[cited by applicant]
Movileanu, Liviu, et al., Interrogating single proteins through nanopores: challenges and opportunities. Trends in Biotechnology 27(6):333-341 (2009).
[cited by applicant]
Muccio, Giovanni Di, et al., Geometrically Induced Selectivity and Unidirectional Electroosmosis in Uncharged Nanopores. ACS Nano 16(6):8716-8728 (2022).
[cited by applicant]
Mullner, Daniel, et al., fastcluster: Fast Hierarchical, Agglomerative Clustering Routines for R and Python. Journal of Statistical Software 53(9): 1-18 (2013).
[cited by applicant]
Niitsu: AI et al.: Membrane-spanning α-helical barrels as tractable protein-design targets. Phil. Trans. R. Soc. B 372:20160213 (2016).
[cited by applicant]
Nivala, Jeff, et al., Discrimination Among Protein Variants Using an Unfoldase-coupled Nanopore. ACS Nano 8(12):12365-12375 (2014).
[cited by applicant]
Nivala, Jeff, et al., Unfoldase-mediated Protein Translocation Through an α-hemolysin Nanopore. Nature Biotechnology 31(3):247-250 (2013).
[cited by applicant]
Noakes, Matthew, et al., Increasing the Accuracy of Nanopore DNA Sequencing Using a Time-varying Cross Membrane Voltage. Nature Biotechnology 37(6):651-656 (2019).
[cited by applicant]
Nouwen, Nico, et al., Charged Amino Acids in a Preprotein Inhibit SecA-dependent Protein Translocation. Journal of Molecular Biology 386(4):1000-1010 (2009).
[cited by applicant]
Nuijens, Timo, et al., Engineering a Diverse Ligase Toolbox for Peptide Segment Condensation. Advanced Synthesis and catalysis 358: 9 Pages (2016).
[cited by applicant]
Olivare, Adrian, et al., Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines. Nature reviews. Microbiology, vol. 14(1):33-44(2016).
[cited by applicant]
Ortega, Joaquin, et al., Visualization of Substrate Binding and Translocation by the Atp-dependent Protease, ClpXp, Molecular cell 6(6):1515-1521 (2000).
[cited by applicant]
Oukhaled, Abdel., et al., Transport of long neutral polymers in the semidilute regime through a protein nanopore. Phys Rev Lett 108(8):1-4 (2012).
[cited by applicant]
Oukhaled, G, et al., Unfolding of Proteins and Long Transient Conformations Detected by Single Nanopore Recording. Physical review letters 98(15):158101 (2007).
[cited by applicant]
Pastoriza-Gallego, Manuela, et al., Evidence of Unfolded Protein Translocation through a Protein Nanopore. ACS Nano 8(11):11350-11360 (2014).
[cited by applicant]
Pavlenok, Mikhail, et al., Control of Subunit Stoichiometry in Single-chain MspA Nanopores. Biophysical Journal 121(5):742-754 (2022).
[cited by applicant]
PCT/NL2017/050331 International Search Report and Written Opinion dated Sep. 5, 2017.
[cited by applicant]
PCT/NL2019/050588 International Search Report dated Dec. 17, 2019.
[cited by applicant]
PCT/NL2020/050726 International Search Report and Written Opinion dated Feb. 19. 2021.
[cited by applicant]
PCT/NL2022/050266 International Search Report dated Nov. 28, 2022.
[cited by applicant]
PCT/NL2023/050568 International Search Report dated Jan. 24, 2024.
[cited by applicant]
Piguet, Fabien, et al., Identification of single amino acid differences in uniformly charged homopolymeric peptides with aerolysin nanopore. Nature Communications 9(966): 13 Pages (2018).
[cited by applicant]
Piguet, Fabien, et al., Identification of single amino acid differences in uniformly charged homopolymeric peptides with aerolysin nanopore. Nature communications 9(966):1-13 (2018).
[cited by applicant]
Purnell, Robert F, et al., Discrimination of single base substitutions in a DNA strand immobilized in a biological nanopore. ACS Nano 3(9):2533-2538 (2009).
[cited by applicant]
Qiao Dan et al., Synthetic Macrocycle Nanopore for Potassium-Selective Transmembrane Transport. Journal of the American Chemical Society 143(39):15975-15983 (2021).
[cited by applicant]
Rincon-Restrepo, Marcela., et al., Controlled translocation of individual DNA molecules through protein nanopores with engineered molecular brakes. 11(2):746-750 (2011).
[cited by applicant]
Ripstein, Zev, et al., Structure of a AAA+ unfoldase in the process of unfolding substrate. eLife 6:e25754 (2017).
[cited by applicant]
Robertson, Joseph W F, et al., Nanopore Sensing: a Physical-chemical Approach. Biochimica Et Biophysica Acta. Biomembranes 1863 (9):1-15 (2021).
[cited by applicant]
Robertson, Joseph W F, et al., Single-molecule mass spectrometry in solution using a solitary nanopore. Proceedings of the National Academy of Sciences of the United States of America 104(20):8207-8211 (2007).
[cited by applicant]
Robertson; Joseph W.F.: Nanopore sensing: A physical-chemical approach. Biochimica et Biophysica Acta (BBA)—Biomembranes 1863(9):183644 (2021).
[cited by applicant]
Rodriguez-Vazquez, Nuria, et al., Membrane-targeted Self-assembling Cyclic Peptide Nanotubes. Current Topics in Medicinal Chemistry 14(23):2647-61 (2014).
[cited by applicant]
Rojko, Nejc et al.: Pore Formation by Actinoporins, Cytolysins From Sea Anemones. Biochimica et Biophysica Acta 1858(3):446-456 (2016).
[cited by applicant]
Ros, U, et al., Differences in Activity of Actinoporins are Related with the Hydrophobicity of Their N-Terminus. Biochimie 116:70-78 (2015).
[cited by applicant]
Ros, Uris, et al., Differences in Activity of Actinoporins are Related With the Hydrophobicity of Their N-Terminus. Biochimie 116:70-78 (2015).
[cited by applicant]
Rosen, Christian B, et al., Single-molecule Site-specific Detection of Protein Phosphorylation With a Nanopore. Nature Biotechnology 32(2):179-181 (2014).
[cited by applicant]
Rosen, Christian B, et al., Targeting the N Terminus for Site-selective Protein Modification. Nature Chemical Biology 13(7):697-705 (2017).
[cited by applicant]
Sauciuc Adina et al., An Engineered Electroosmotic Flow Transports Unravelled Proteins Across Nanopores. bioRxiv (2023).
[cited by applicant]
Sauciuc, Adina et. al., Translocation of Linearized Full-length Proteins Through an Engineered Nanopore Under Opposing Electrophoretic Force. Nature Biotechnology (2023): 63 pages.
[cited by applicant]
Sauer, Rolf, et al., Preoperative Versus Postoperative Chemoradiotherapy for Rectal Cancer. The New England Journal of Medicine. 351(17):1731-1740 (2004).
[cited by applicant]
Schmidt, Bernhard, Hydrophilic Polymers. Polymers (Basel) 11(4): 693 (2019).
[cited by applicant]
Schon, Peter, et al., Equinatoxin II Permeabilizing Activity Depends on the Presence of Sphingomyelin and Lipid Phase Coexistence. Biophysical Journal 95(2):691-698 (2008).
[cited by applicant]
Scott, Alistair, et al., Constructing Ion Channels From Water-soluble A-helical Barrels. Nature chemistry 13(7):643-650 (2021).
[cited by applicant]
Seemüller, Erika, et al., Proteasome From Thermoplasma Acidophilum: A Threonine Protease. Science 268(5210):579-82 (1995).
[cited by applicant]
Serek-Heuberger, Justyna, et al., Two Unique Membrane-bound Aaa Proteins From Sulfolobus Solfataricus. Biochemical Society Transactions 37(1):118-122 (2009).
[cited by applicant]
Shimizu, Keisuke, et al., De Novo Design of a Nanopore for Single-molecule Detection That Incorporates a β-hairpin Peptide. Nature Nanotechnology 17(1):67-75 (2022).
[cited by applicant]
Singh, Satyendra, et al., Functional Domains of the ClpA and ClpX Molecular Chaperones Identified by Limited Proteolysis and Deletion Analysis. The Journal of Biological Chemistry 276(31):29420-29429 (2001).
[cited by applicant]
Soskine, Misha, et al., Single-molecule Analyte Recognition With Clya Nanopores Equipped With Internal Protein Adaptors. Journal of the American Chemical Society 137(17):5793-5797 (2015).
[cited by applicant]
Soskine, Misha, et al., Tuning the size and properties of ClyA nanopores assisted by directed evolution. Journal of the American Chemical Society 135(36):13456-13463 (2013).
[cited by applicant]
Spaan, András, et al., Leukocidins: staphylococcal bi-component pore-forming toxins find their receptors. Nature reviews. Microbiology 15(7):435-447 (2019).
[cited by applicant]
Spruijt, Evan, et al., DNA scaffolds support stable and uniform peptide nanopores. Nature Nanotechnology 13:739-745 (2018).
[cited by applicant]
Stadtmueller, Beth M. et al.: Proteasome Activators. Molecular Cell 41:8-19 (2011).
[cited by applicant]
Stefureac, Radu, et al., Nanopore Analysis of a Small 86-residue Protein. Small 4(1):59-63 (2008).
[cited by applicant]
Stefureac, Radu, et al., Transport of Alpha-helical Peptides Through Alpha-hemolysin and Aerolysin Pores. Biochemistry 45(30):9172-9 (2006).
[cited by applicant]
Stoddart, David., et al., DNA stretching and optimization of nucleobase recognition in enzymatic nanopore sequencing Nanotechnology 26(8):10-16 (2015).
[cited by applicant]
Stoddart, David, et al., Functional Truncated Membrane Pores. Proceedings of the National Academy of Sciences of the United States of America 111(7):2425-2430 (2014).
[cited by applicant]
Stoddart, David, et al., Multiple base-recognition sites in a biological nanopore: two heads are better than one. Angewandte Chemie International Edition English 49(3):556-559 (2010).
[cited by applicant]
Stoddart, David, et al., Nucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore. Nano Letters 10(9):3633-3637 (2010).
[cited by applicant]
Stoddart, David, et al., Single-nucleotide discrimination in immobilized DNA oligonucleotides with a biological nanopore. Proceedings of the National Academy of Sciences of the United States of America 106(19):7702-7707…
[cited by applicant]
Stranges, Benjamin, et al., Design and Characterization of a Nanopore-coupled Polymerase for Single-molecule Dna Sequencing by Synthesis on an Electrode Array. Proceedings of the National Academy of Sciences of the Unit…
[cited by applicant]
Stryer: Biochemistry 4th Ed. WH Freeman, New York. p. 18-23 (1995).
[cited by applicant]
Sugiyama, Masaaki, et al., Spatial Arrangement and Functional Role of a Subunits of Proteasome Activator Pa28 in Hetero-oligomeric Form. Biochemical and biophysical research communications 432:141-145 (2013).
[cited by applicant]
Talaga, David S, et al., Single-molecule Protein Unfolding in Solid State Nanopores. Journal of the American Chemical Society 131(26):9287-9297 (2009).
[cited by applicant]
Tanaka, Koji, et al., Bidirectional Transformation of a Metamorphic Protein between the Water-Soluble and Transmembrane Native States. Biochemistry 54(46):6863-6866 (2015).
[cited by applicant]
Tanaka, Koji et al.: Structural Basis for Self-assembly of a Cytolytic Pore Lined by Protein and Lipid. Nature Communications 6: 6337 (2015).
[cited by applicant]
Thapa, Parashar, et al., Native chemical ligation: a boon to peptide chemistry. Molecules 19(9): 14461-83 (2014).
[cited by applicant]
Too, Priscilla Hiu-mei, et al., Slippery Substrates Impair Function of a Bacterial Protease ATPase by Unbalancing Translocation Versus Exit. The Journal of Biological Chemistry 288(19):13243-57 (2013).
[cited by applicant]
Toplak, Ana, et al., Peptiligase an Enzyme for efficient Chemoenzymatic peptide Synthesis and Cyclization in Water. Advanced Synthesis and catalysis 358:2140-2147 (2016).
[cited by applicant]
Tsutsui, Makusu, et al., Sparse Multi-nanopore Osmotic Power Generators. Cell Press Physical Science 3:1-12 (2022).
[cited by applicant]
UniProt XP 002796191, Review, 2009.
[cited by applicant]
U.S. Appl. No. 16/317,119 Office Action dated Apr. 28, 2021.
[cited by applicant]
Van Der Verren, Sander E, et al., A Dual-constriction Biological Nanopore Resolves Homonucleotide Sequences With High Fidelity. Nature biotechnology 38:1415-1420 (2020).
[cited by applicant]
Versloot, Roderick Corstiaan Abraham, et al., β-Barrel Nanopores with an Acidic-Aromatic Sensing Region Identify Proteinogenic Peptides at Low pH. ACS Nano 16(5):7258-7268 (2022).
[cited by applicant]
Vorobieva, Anastassia A, De Novo Design of Transmembrane β Barrels. Science 371(6531):1-25 (2021).
[cited by applicant]
Wallace et al.: Identification of epigenetic DNA modifications with a protein nanopore. Chemical Communications 46:8195-8197 (2010).
[cited by applicant]
Wang, Jimin, et al., The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis. Cell 91(4):447-456 (1997).
[cited by applicant]
Wanunu, Meni, et al., DNA translocation governed by interactions with solid-state nanopores. Biophys J 95(10):4716-4725 (2008).
[cited by applicant]
Wanunu, Meni., et al., Electrostatic focusing of unlabelled DNA into nanoscale pores using a salt gradient. Nat Nanotechnol 5(2):160-165 (2010).
[cited by applicant]
Watanabe, Hirokazu, et al., Analysis of Pore Formation and Protein Translocation Using Large Biological Nanopores. Analytical Chemistry 89(21):11269-11277 (2017).
[cited by applicant]
Wei, Bryan, et al., Complex Shapes Self-assembled From Single-stranded DNA tiles. Nature 485(7400):623-626 (2012).
[cited by applicant]
Wendell, David, et al., Translocation of double-stranded DNA through membrane-adapted phi29 motor protein nanopores. Nature Nanotechnology 4(11):765-72 (2009).
[cited by applicant]
Wilson, Jason S. et al.: Identification and structural analysis of the tripartite α-pore forming toxin of Aeromonas hydrophila. Nature Communications 10:2900 (2019).
[cited by applicant]
Wloka, Carsten, et al., Alpha-Helical Fragaceatoxin C Nanopore Engineered for Double-Stranded and Single-Stranded Nucleic Acid Analysis. Angewandte Chemie 55(40):12494-12498 (2016).
[cited by applicant]
Wong, C T A, et al., Polymer Capture by Electro-osmotic Flow of Oppositely Charged Nanopores. The Journal of chemical physics 126(16):164903 (2007).
[cited by applicant]
Xue, Liang, et al., Solid-state Nanopore Sensors. Nature Reviews Materials 21 Pages (2020).
[cited by applicant]
Ye, Cheng, et al., Pandemic-scale Phylogenetics. bioRxiv : the preprint server for biology 1-16 (2021).
[cited by applicant]
Ying, Yi-Lun, et al., Handling a Protein With a Nanopore Machine. Nature Chemistry 13:1160-1162 (2021).
[cited by applicant]
Yu, Luning et al.: Unidirectional Single-File Transport of Full-Length Proteins Through a Nanopore. Nature Biotechnology 41:1130-1139 (2023).
[cited by applicant]
Yusupov, Marat, et al., Crystal Structure of the Ribosome at 5.5 a Resolution. Science 292(5518):883-896 (2001).
[cited by applicant]
Zhang, Shengli, et al., Bottom-up Fabrication of a Proteasome-nanopore That Unravels and Processes Single Proteins. Nature Chemistry 13(12):1192-1199 (2021).
[cited by applicant]
Zhao, Qitao, et al., Study of Peptide Transport Through Engineered Protein Channels. The Journal of Physical Chemistry B 133 (11):3572-3578 (2009).
[cited by applicant]
Zhao, Yanan, et al., Single Molecule Spectroscopy of Amino Acids and Peptides by Recognition Tunneling. Nature Nanotechnology 9(6):466-473 (2014).
[cited by applicant]
Zhao, Yingqi, et al., Label-Free Optical Analysis of Biomolecules in Solid-State Nanopores: Toward Single-Molecule Protein Sequencing. ACS Photonics 9:730-742 (2022).
[cited by applicant]
Ziemski, Michal, et al., Cdc48-Like Protein of Actinobacteria (Cpa) is a Novel Proteasome Interactor in Mycobacteria and Related Organisms. Elife 29(7):e34055 (2018).
[cited by applicant]
Balakrishna, B.H. et al.: Binding of a pleurotolysin ortholog from Pleurotus eryngii to sphingomyelin and cholesterol-rich membrane domains. Journal of Lipid Research (2013).
[cited by applicant]
Cajado-Carvalho, Daniela et al.: Insights into the Hypertensive Effects of Tityus serrulatus Scorpion Venom: Purification of an Angiotensin-Converting Enzyme-Like Peptidase. Toxins 8(12)348:1-16 (2016. https://doi.org/1…
[cited by applicant]
Weber, DK: Characterization of the Lipid-Binding Site of Equinatoxin II by NMR and Molecular Dynamics Simulation. Biophysical Journal 108(8):1987-1996 2015.
[cited by applicant]
Bakrac, Biserka, et al., Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin. Journal of Biological Chemistry 283(27):18665-18677 (2008).
[cited by applicant]
Chavis, Amy E, et al., Single Molecule Nanopore Spectrometry for Peptide Detection. ACS Sensors 2(9):1319-1328 (2017).
[cited by applicant]
Klavius, G. M. et al, Low temperature incommensurately modulated and noncollinear spin structure in FeCr2S4. Journal of Physics: Condensed Matter 22(5):1-21 (2010).
[cited by applicant]
Laszlo, Andrew H, et al., Decoding long nanopore sequencing reads of natural DNA. Nature Biotechnology 32(8):829-833 (2014).
[cited by applicant]
Lee, Irene et al., Functional Mechanics of the ATP-dependent Lon Protease-Lessons From Endogenous Protein and Synthetic Peptide Substrates. Biochimica Et Biophysica Acta 1784(5):727-35 (2008).
[cited by applicant]
Li, Shuang et al. Detection of peptides with different charge and length by aerolysin nanopore. ChemElectroChem 6(1):126-129 (2018).
[cited by applicant]
Lide, David R, et al., CRC Handbook of Chemistry and Physics, 84th edition. Journal of the American Chemical Society 126(5):1585-1588 (2003).
[cited by applicant]
PCT/NL2023/050570 International Search Report and Written Opinion dated Apr. 5, 2024.
[cited by applicant]