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Nuc-MS makes use of top–down mass spectrometry in ‘native’ mode to quantitatively interrogate histone proteoforms and their post-translational modifications in a single experiment.
Paired-Tag offers a multiomics assay for joint profiling of histone modifications and gene expression in single nuclei, and is applied to mouse frontal cortex and hippocampus for measuring cell-type-resolved chromatin state and transcriptome.
Total Variational Inference is a framework for end-to-end analysis of paired transcriptome and protein measurements such as CITE-seq data in single cells.
Reconstruction of light-field microscopy data with a deep-learning network achieves high reconstruction speed and reduces artifacts, as illustrated for moving C. elegans and beating zebrafish hearts.
The software M establishes a reference-based multi-particle refinement framework for cryo-EM data. Combined with CTF correction and map denoising, M enables residue-level structure determination inside cells.
Application of a single layer of graphene to untreated wet mammalian cells enables mass spectrometry imaging of cellular membranes of live cells in solution at subcellular resolution.
CryoDRGN is an unsupervised machine learning algorithm that reconstructs continuous distributions of three-dimensional density maps from heterogeneous single-particle cryo-EM data.
This study explores the performance of deep-learning models for super-resolution imaging and introduces models that utilize frequency content information in the Fourier domain to improve SIM reconstruction under low-SNR conditions.
This work presents a sequencing strategy based on unique molecular identifiers that improves long-read consensus sequence accuracy of targeted amplicons as well as shotgun whole-genome fragments.
The iterative Build and Retrieve (BaR) methodology facilitates the solving of cryo-EM structures of multiple membrane (and soluble) proteins simultaneously, including small and low-abundance membrane proteins.
Megabodies, built by grafting nanobodies onto larger protein scaffolds, help alleviate problems of particle size and preferential orientation at the water–air interfaces during cryo-EM based structure determination experiments and are shown to be generalizable to soluble and membrane-bound proteins.
Cell surface thermal proteome profiling allows characterization of ligand-induced changes in protein abundances and thermal stabilities at the plasma membrane.