04.29 Reversible strain-promoted DNA polymerization, 10.1126/sciadv.ado8020
04.15 Transient DNA binding to gapped DNA substrates links DNA sequence to the single-molecule kinetics of protein-DNA interactions, https://doi.org/10.1101/2022.02.27.482175
04.01 Single-molecule imaging and molecular dynamics simulations reveal early activation of the MET receptor in cells, https://doi.org/10.1038/s41467-024-53772-7
03.18 Target DNA-dependent activation mechanism of the prokaryotic immune system SPARTA, https://doi.org/10.1093/nar/gkad1248
03.05
Computational design of serine hydrolases, https://doi.org/10.1126/science.adu2454
Engineering modular and tunable single-molecule sensors by decoupling sensing from signal output, https://doi.org/10.1038/s41565-024-01804-0
Label-free detection and profiling of individual solution-phase molecules, https://doi.org/10.1038/s41586-024-07370-8
02.12
Massively parallel measurement of protein–protein interactions by sequencing using MP3-seq, https://doi.org/10.1038/s41589-024-01718-x
De novo designed proteins neutralize lethal snake venom toxins, https://doi.org/10.1038/s41586-024-08393-x
Single-Molecule Investigation of the Protein–Aptamer Interactions and Sensing Application Inside the Single Glass Nanopore, https://doi.org/10.1021/acs.analchem.2c02660
01.15 Supervised multi-frame dual-channel denoising enables long-term single-molecule FRET under extremely low photon budget, https://doi.org/10.1038/s41467-024-54652-w
01.06 Tracking transcription–translation coupling in real time, https://doi.org/10.1038/s41586-024-08308-w
2024
12.18 Transcriptome-scale super-resolved imaging in tissues by RNA seqFISH, https://doi.org/10.1038/s41586-019-1049-y
12.10 Spatially resolved, highly multiplexed RNA profiling in single cells, https://doi.org/10.1126/science.aaa6090
12.04 Single-molecule spectroscopy of protein conformational dynamics in live eukaryotic cells, https://doi.org/10.1038/nmeth.3475
11.27 Single-molecule fluorescence multiplexing by muti-parameter spectroscopic detection of nanostructured FRET labels, https://doi.org/10.1038/s41565-024-01672-8
11.20 ABEL-FRET: tether-free single-molecule FRET with hydrodynamic profiling, https://doi.org/10.1038/s41592-021-01173-9
11.13 Spatially resolved, highly multiplexed RNA profiling in single cells, https://doi.org/10.1126/science.aaa6090
11.06 Quantifying T cell receptor mechanics at membrane junctions using DNA origami tension sensors, https://doi.org/10.1038/s41565-024-01723-0
10.30 RNA-guided RNA silencing by an Asgard archaeal Argonaute, https://doi.org/10.1038/s41467-024-49452-1
10.23 Mechanical force regulates ligand binding and function of PD-1, https://doi.org/10.1038/s41467-024-52565-2
10.16 Multi-pass, single-molecule nanopore reading of long protein strands. https://doi.org/10.1038/s41586-024-07935-7
10.02 A single-vesicle content mixing assay for SNARE-mediated membrane fusion. https://doi.org/10.1038/ncomms1054
09.25 Quantitative analysis of RNA-protein interactions on a massively parallel array reveals biophysical and evolutionary landscapes. https://doi.org/10.1038/nbt.2880
09.13 Exploring molecular biology in sequence space: The road to next-generation single-molecule biophysics, https://doi.org/10.1016/j.molcel.2022.04.024
09.04 A single-vesicle content mixing assay for SNARE-mediated membrane fusion, https://doi.org/10.1038/ncomms1054
08.28 Distance Dependence of Single-Fluorophore Quenching by Gold Nanoparticles Studied on DNA Origami, https://doi.org/10.1021/nn2050483
08.21 TCR–peptide–MHC interactions in situ show accelerated kinetics and increased affinity. https://doi.org/10.1038/nature08746
08.14 Predicting the sequence specificities of DNA- and RNA-binding proteins by deep learning. https://doi.org/10.1038/nbt.3300
08.07 Single-molecule FRET imaging of GPCR dimers in living cells. https://doi.org/10.1038/s41592-021-01081-y
07.31 DropBlot: single-cell western blotting of chemically fixed cancer cells, https://doi.org/10.1038/s41467-024-50046-0
07.17 Torsional Stiffness of Extended and Plectonemic DNA, https://doi.org/10.1103/PhysRevLett.127.028101
07.10 Biological Nanopore Approach for Single-Molecule Protein Sequencing, https://doi.org/10.1002/ange.202013462
07.03 Single-Molecule Peptide Identification Using Fluorescence Blinking Fingerprints, https://doi.org/10.1021/jacs.2c12561
06.26 A DNA origami-based device for investigating DNA bending proteins by transmission electron microscopy, https://doi.org/10.1039/D2NR05366G
06.19 A Systems Approach to Measuring the Binding Energy Landscapes of Transcription Factors, https://doi.org/10.1126/science.1131007
06.12 Affinity microfluidics enables high-throughput protein degradation analysis in cell-free extracts, https://doi.org/10.1038/s42003-022-04103-3
04.17 Mapping Single-Molecule Protein Complexes in 3D with DNA Nanoswitch Calipers, https://pubs.acs.org/doi/10.1021/jacs.3c10262
04.11 Supported Bilayer Electrophoresis under Controlled Buffer Conditions, https://doi.org/10.1021/ac1028819
04.03 An electroactive microwell array device to realize simultaneous trapping of single cancer cells and clusters, https://doi.org/10.1039/D2LC00171C
03.28 An electroactive microwell array device to realize simultaneous trapping of single cancer cells and clusters, https://doi.org/10.1039/D2LC00171C
03.20 ProtSeq: Toward high-throughput, single-molecule protein sequencing via amino acid conversion into DNA barcodes, https://doi.org/10.1016/j.isci.2021.103586
03.13 Protein Separation by Electrophoretic–Electroosmotic Focusing on Supported Lipid Bilayers, https://pubs.acs.org/doi/10.1021/ac201768k
03.06 Enzyme-less nanopore detection of post-translational modifications within long polypeptides, https://doi.org/10.1038/s41565-023-01462-8
02.27 Single molecule electrometry, https://doi.org/10.1038/nnano.2017.26
02.22 Real-time dynamic single-molecule protein sequencing on an integrated semiconductor device, https://doi.org/10.1126/science.abo7651
02.07 Single molecule digital sizing:, https://doi.org/10.1101/2023.07.12.548675
01.24 Multi-pass, single-molecule nanopore reading of long protein strands with single-amino acid sensitivity:, https://doi.org/10.1101/2023.10.19.563182
01.03 Real-Time Structural Biology of DNA and DNA-Protein Complexes on an Optical Microscope, https://doi.org/10.1101/2023.11.21.567962
2023
12.27 Single Protein molecules separation, tracking and counting in ultra-thin silicon channels, https://doi.org/10.1101/2023.11.09.566381
12.20 Optical imaging of single-protein size, charge, mobility, and binding, https://doi.org/10.1038/s41467-020-18547-w