Publications
Dynamic Single-Molecule
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Migrasome formation is initiated preferentially in tubular junctions by membrane tension
Zucker, B. et al.
2025
Biophysical Journal
https://doi.org/10.1016/j.bpj.2024.12.029
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Extracellular domain 2 of TSPAN4 governs its functions
Dharan, R. et al.
2024
Biophysical Reports
https://doi.org/10.1016/j.bpr.2024.100149
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Optical tweezers-controlled hotspot for sensitive and reproducible surface-enhanced Raman spectroscopy characterization of native protein structures
Dai, X. et al.
2021
Nature Communications
https://www.nature.com/articles/s41467-021-21543-3
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Identification and correction of miscalibration artifacts based on force noise for optical tweezers experiments
Freitag, M. et al.
2021
J. Chemical Physics
https://aip.scitation.org/doi/10.1063/5.0063690
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Experimental study of a nanoscale translocation ratchet
Molcrette, B. et al.
2022
PNAS
https://www.pnas.org/doi/pdf/10.1073/pnas.2202527119
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Supported Natural Membranes on Microspheres for Protein–Protein Interaction Studies
Cheppali, S. et al.
2022
ACS Appl. Mater. Interfaces
https://pubs.acs.org/doi/abs/10.1021/acsami.2c13095
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Tetraspanin 4 stabilizes membrane swellings and facilitates their maturation into migrasomes
Dharan, R. et al.
2023
Nature Communications
https://www.nature.com/articles/s41467-023-36596-9
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Membrane Tension Inhibits Lipid Mixing by Increasing the Hemifusion Stalk Energy
Shendrik, P. et al.
2023
ACS Nano
https://pubs.acs.org/doi/10.1021/acsnano.3c04293
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Efficient optical plasmonic tweezer-controlled single-molecule SERS characterization of pH-dependent amylin species in aqueous milieus
Fu, F. et al.
2023
Nature Communications
https://www.nature.com/articles/s41467-023-42812-3
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A circular zone of attachment to the extracellular matrix provides directionality to the motility of Toxoplasma gondii in 3D
Stadler, R. et al.
2022
eLife
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9839348/#article-1aff-info
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Single Cell Reactomics: Real‐Time Single‐Cell Activation Kinetics of Optically Trapped Macrophages
Vasse, G. F. et al.
2021
Small Methods
https://onlinelibrary.wiley.com/doi/full/10.1002/smtd.202000849
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3D nanofabricated soft microrobots with super-compliant picoforce springs as onboard sensors and actuators
Xu, H. et al.
2024
Nature Nanotechnology
https://www.nature.com/articles/s41565-023-01567-0
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Single cell force spectroscopy of erythrocytes at physiological and febrile temperatures reveals mechano-modulatory effects of atorvastatin
Sheikhhassani, V. et al.
2022
Soft matter
https://pubs.rsc.org/en/Content/ArticleLanding/2022/SM/D1SM01715B
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Single-cell analysis reveals chemokine-mediated differential regulation of monocyte mechanics
Evers, T. M. J. et al.
2022
iScience
https://www.sciencedirect.com/science/article/pii/S258900422101525X
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Single-Cell Mechanical Characterization of Human Macrophages
Evers, T. M. J. et al.
2022
Advanced Nanobiomed Research
https://onlinelibrary.wiley.com/doi/full/10.1002/anbr.202100133
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Weak catch bonds make strong networks
Mulla, Y. et al.
2022
Nature Materials
https://www.nature.com/articles/s41563-022-01288-0
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Microtubule Lattice Spacing Governs Cohesive Envelope Formation of Tau Family Proteins
Siahaan, V. et al.
2022
Nature Chemical Biology
https://www.nature.com/articles/s41589-022-01096-2
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Transmembrane proteins tetraspanin 4 and CD9 sense membrane curvature
Dharan, R. et al.
2022
PNAS
https://www.pnas.org/doi/abs/10.1073/pnas.2208993119
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Directed assembly of genetically engineered eukaryotic cells into living functional materials via ultrahigh-affinity protein interactions
Quikun, Y. et al.
2022
Science Advances
https://www.science.org/doi/10.1126/sciadv.ade0073
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Mechanics of serotonin-producing human entero-endocrine cells
Evers, T. M. J. et al.
2024
Mechanobiology in Medicine
https://www.sciencedirect.com/science/article/pii/S294990702400007X
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Probing Local Force Propagation in Tensed Fibrous Gels
Goren, S. et al.
2022
Small
https://onlinelibrary.wiley.com/doi/full/10.1002/smll.202202573
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Construction of multiphasic membraneless organelles towards spontaneous spatial segregation and directional flow of biochemical reactions
Zhorabek, F. et al.
2023
Chemical Science
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9890938/
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Advanced glycation end-products as mediators of the aberrant crosslinking of extracellular matrix in scarred liver tissue
Lyu, C. et al.
2023
Nature Biomedical Engineering
https://www.nature.com/articles/s41551-023-01019-z
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Cell protrusions and contractions generate long-range membrane tension propagation
De Belly, H. et al.
2023
Cell
https://doi.org/10.1016/j.cell.2023.05.014
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Dynamic encounters with red blood cells trigger splenic marginal zone B cell retention and function
Liu, D. et al.
2023
Nature Immunology
https://www.nature.com/articles/s41590-023-01690-z#citeas
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Determination of single-molecule loading rate during mechanotransduction in cell adhesion
Jo, M.H. et al.
2024
Science
https://www.science.org/doi/10.1126/science.adk6921
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Single-cell analysis of innate immune cell mechanics: an application to cancer immunology
Evers, T. M. J. et al.
2024
Material Advances
https://pubs.rsc.org/en/content/articlehtml/2024/ma/d3ma01107k
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Rethinking the relationships between gel like structure and sludge dewaterability based on a binary gel like structure model: Implications for the online sensing of dewaterability
Zhang, D. et al.
2024
Water Research
https://doi.org/10.1016/j.bpr.2024.100149
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Micro-tensile rheology of fibrous gels quantifies strain-dependent anisotropy
Goren, S. et al.
2024
Acta Biomaterialia
https://doi.org/10.1016/j.actbio.2024.03.028
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Ebola Virus Glycoprotein Strongly Binds to Membranes in the Absence of Receptor Engagement
Vaknin, A. et al.
2024
ACS Infect. Dis.
https://doi.org/10.1021/acsinfecdis.3c00622
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Mechano-inhibition of endocytosis sensitizes cancer cells to Fas-induced Apoptosis
Kural, M. H. et al.
2024
Cell Death & Disease
https://doi.org/10.1038/s41419-024-06822-3
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Plasma membrane abundance dictates phagocytic capacity and functional cross-talk in myeloid cells
Winer, B. Y. et al.
2024
Science Immunology
https://doi.org/10.1126/sciimmunol.adl2388
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Salt-Dependent Rheology and Surface Tension of Protein Condensates Using Optical Traps
Jawerth, L. et al.
2018
Physical Review Letters
https://journals.aps.org/prl/abstract/10.1103/PhysRevLett.121.258101
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Molecular Crowding Tunes Material States of Ribonucleoprotein Condensates
Kaur, T. et al.
2019
Biomolecules
https://www.mdpi.com/2218-273X/9/2/71
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Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
Gui, X., et al.
2019
Nature Communications
https://www.nature.com/articles/s41467-019-09902-7
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Protein condensates as aging Maxwell fluids
Jawerth, L. et al.
2020
Science
https://science.sciencemag.org/content/370/6522/1317
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Interplay between Short-Range Attraction and Long-Range Repulsion Controls Reentrant Liquid Condensation of Ribonucleoprotein–RNA Complexes
Alshareedah, I. et al.
2019
Journal of the American Chemical Society
https://pubs.acs.org/doi/full/10.1021/jacs.9b03689
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Phase transition of RNA−protein complexes into ordered hollow condensates
Alshareedah, I. et al.
2020
PNAS
https://www.pnas.org/content/early/2020/06/19/1922365117
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A Minimal Load-and-Lock Ru Luminescent DNA Probe
Newton, M. D. et al.
2021
Angew. Chem. Int. Ed.
https://onlinelibrary.wiley.com/doi/full/10.1002/anie.202108077
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Determinants for Fusion Speed of Biomolecular Droplets
Ghosh, A. et al.
2020
J. Phys. Chem. B
https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.202006711
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Quantifying Viscosity and Surface Tension of Multi-Component Protein-Nucleic Acid Condensates
Alshareedah, I. et al.
2021
Biophysical Journal
https://www.cell.com/biophysj/pdf/S0006-3495(21)00035-7.pdf#%20
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Sequence-encoded and Composition-dependent Protein-RNA Interactions Control Multiphasic Condensate Morphologies
Kaur, T. et al.
2021
Nature Communications
https://www.nature.com/articles/s41467-021-21089-4
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Single-molecule and ensemble methods to probe RNP nucleation and condensate properties
Rhine, K. et al.
2021
Methods
https://www.sciencedirect.com/science/article/pii/S1046202321000499
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Direct visualization of the effect of DNA structure and ionic conditions on HU–DNA interactions
Lin, S. N. et al.
2021
Scientific Reports
https://www.nature.com/articles/s41598-021-97763-w#citeas
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F/YGG-motif is an intrinsically disordered nucleic-acid binding motif
Van Lindt, J. et al.
2022
RNA biology
https://www.tandfonline.com/doi/full/10.1080/15476286.2022.2066336
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Shear relaxation governs fusion dynamics of biomolecular condensates
Ghosh, A. et al.
2021
Nature Communications
https://www.nature.com/articles/s41467-021-26274-z
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Programmable viscoelasticity in protein-RNA condensates with disordered sticker-spacer polypeptides
Alshareedah, I. et al.
2021
Nature Communications
https://www.nature.com/articles/s41467-021-26733-7
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Controlling synthetic membraneless organelles by a red-light-dependent singlet oxygen-generating protein
Li, M. et al,
2022
Nature Communications
https://www.nature.com/articles/s41467-022-30933-0
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Macromolecular Regulation of the Material Properties of Biomolecular Condensates
Kota, D. et al.
2022
J. Phys. Chem. Lett.
https://pubs.acs.org/doi/abs/10.1021/acs.jpclett.2c00824
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Bloom syndrome helicase compresses single-stranded DNA into phase-separated condensates
Wang, T. et al.
2022
Angew. Chem. Int. Ed.
https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.202209463
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Extreme dynamics in a biomolecular condensate
Galvanetto, N. et al.
2023
Nature Communications
https://doi.org/10.1038/s41586-023-06329-5
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Targeted perturbation of signaling-driven condensates
Gui, T. et al.
2023
Molecular Cell
https://doi.org/10.1016/j.molcel.2023.10.023
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Adenosine Triphosphate Mediates Phase Separation of Disordered Basic Proteins by Bridging Intermolecular Interaction Networks
Kota, D. et al.
2024
JACS
https://pubs.acs.org/doi/full/10.1021/jacs.3c09134
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RNAs undergo phase transitions with lower critical solution temperatures
Wadsworth, G. M. et al.,
2023
Nature Chemistry
https://www.nature.com/articles/s41557-023-01353-4
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Phase-separated ParB enforces diverse DNA compaction modes and stabilizes the parS-centered partition complex
Zhao, Y. et al.
2024
Nucleic Acids Research
https://doi.org/10.1093/nar/gkae533
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Determinants of viscoelasticity and flow activation energy in biomolecular condensates
Alshareedah, I. et al.
2024
Science Advances
https://www.science.org/doi/full/10.1126/sciadv.adi6539
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Sequence-specific interactions determine viscoelasticity and ageing dynamics of protein condensates
Alshareedah, I. et al.
2024
Nature Physics
https://doi.org/10.1038/s41567-024-02558-1
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Viscoelastic properties of vimentin originate from nonequilibrium conformational changes
Block, J. et al.
2018
Science Advances
http://advances.sciencemag.org/content/4/6/eaat1161
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Nonlinear Loading-Rate-Dependent Force Response of Individual Vimentin Intermediate Filaments to Applied Strain
Block, J. et al.
2017
Physical Review Letters
https://journals.aps.org/prl/abstract/10.1103/PhysRevLett.118.048101
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Vimentin Intermediate Filaments Undergo Irreversible Conformational Changes during Cyclic Loading
Forsting, J. et al.
2019
Nano Letters
https://pubs.acs.org/doi/full/10.1021/acs.nanolett.9b02972
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Lateral Subunit Coupling Determines Intermediate Filament Mechanics
Lorenz, C. et al.
2019
Physical Review Letters
https://journals.aps.org/prl/abstract/10.1103/PhysRevLett.123.188102
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Vimentin Intermediate Filaments Stabilize Dynamic Microtubules by Direct
Schaedel, L. et al.
2021
Interactions Nature Communications
https://www.nature.com/articles/s41467-021-23523-z
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Pathogenic Mutations in the Kinesin-3 Motor KIF1A Diminish Force Generation and Movement Through Allosteric Mechanisms
Budaitis, B. G. et al.
2021
Journal of Cell Biology
https://rupress.org/jcb/article/220/4/e202004227/211720/Pathogenic-mutations-in-the-kinesin-3-motor-KIF1A
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The post-PAM interaction of RNA-guided spCas9 with DNA dictates its target binding and dissociation
Zhang, Q. et al.
2019
Science Advances
https://advances.sciencemag.org/content/5/11/eaaw9807
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A conserved ATP- and Scc2/4-dependent activity for cohesin in tethering DNA molecules
Gutierrez-Escribano, P. et al.
2019
Science Advances
https://advances.sciencemag.org/content/5/11/eaay6804
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Synaptotagmin-1 and Doc2b Exhibit Distinct Membrane-Remodeling Mechanisms
Sorkin, R. et al.
2020
Biophysical Journal
https://www.sciencedirect.com/science/article/abs/pii/S0006349519344066
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Tuning intermediate filament mechanics by indirect and direct charge variations
Schepers, A. V. et al.
2020
Nanoscale
https://pubs.rsc.org/en/content/articlelanding/2020/NR/D0NR02778B#!divAbstract
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Molecular mechanism for direct actin force-sensing by α-catenin
Mei, L. et al.
2020
eLife
https://elifesciences.org/articles/62514
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Post-Translational Modifications Soften Vimentin Intermediate Filaments
Kraxner, J. et al.
2020
Nanoscale
https://pubs.rsc.org/-/content/articlelanding/2021/nr/d0nr07322a#!divAbstract
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A Highly Conserved 310-Helix Within the Kinesin Motor Domain is Critical for Kinesin Function and Human Health
Lam, A. J. et al.
2021
Science Advances
https://advances.sciencemag.org/content/7/18/eabf1002
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The short isoform of the host antiviral protein ZAP acts as an inhibitor of SARS-CoV-2 programmed ribosomal frameshifting
Zimmer, M. et al.
2021
Nature Communications
https://www.nature.com/articles/s41467-021-27431-0
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Anillin propels myosin-independent constriction of actin rings
Kučera, O. et al.
2021
Nature Communications
https://www.nature.com/articles/s41467-021-24474-1
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Multiscale mechanics and temporal evolution of vimentin intermediate filament networks
Schepers, A. V. et al.
2021
PNAS
https://www.pnas.org/content/118/27/e2102026118
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Structural mechanism of outer kinetochore Dam1-Ndc80 complex assembly on microtubules
Muir, K. W. et al.
2023
Science
https://doi.org/10.1126/science.adj8736
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Kinesin-1-transported liposomes prefer to go straight in 3D microtubule intersections by a mechanism shared by other molecular motors
Bensel, B. M. et al.
2024
PNAS
https://doi.org/10.1073/pnas.2407330121
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Kinesin-14 HSET and KlpA are non-processive microtubule motors with load-dependent power strokes
Liu, X. et al.
2024
Nature Communications
https://doi.org/10.1038/s41467-024-50990-x
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Processive extrusion of polypeptide loops by a Hsp100 disaggregase
Avellaneda, M. et al.
2020
Nature Communications
https://www.nature.com/articles/s41586-020-1964-y
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Simultaneous sensing and imaging of individual biomolecular complexes enabled by modular DNA–protein coupling
Avellaneda, M. et al.
2020
Communications Chemistry
https://www.nature.com/articles/s42004-020-0267-4
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Facile tethering of stable and unstable proteins for optical tweezers experiments
Maciuba, K. et al.
2021
Biophysical Journal
https://www.cell.com/biophysj/pdf/S0006-3495(21)00393-3.pdf
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The ribosome modulates folding inside the ribosomal exit tunnel
Wruck, F. et al.
2021
Communications Biology
https://www.nature.com/articles/s42003-021-02055-8
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Optical Tweezers to Study RNA-Protein Interactions in Translation Regulatio
Pekarek, L. et al.
2022
JoVE
https://www.jove.com/t/62589/optical-tweezers-to-study-rna-protein-interactions-translation
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Minimalist design of polymer-oligopeptide hybrid as intrinsically disordered protein-mimicking scaffold for artificial membraneless organelle
Liu, J. et al.
2022
ACS Cent. Sci.
https://pubs.acs.org/doi/10.1021/acscentsci.1c01021
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Protein chain collapse modulation and folding stimulation by GroEL-ES
Naqvi, M. et al.
2022
Science Advances
https://www.science.org/doi/10.1126/sciadv.abl6293
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POTATO: An automated pipeline for batch analysis of optical tweezers data
Buck, S. et al.
2022
Biophysical Journal
https://www.sciencedirect.com/science/article/abs/pii/S0006349522005409
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Single-molecule experiments reveal the elbow as an essential folding guide in SMC coiled-coil arms
Freitag, M. et al.
2022
Biophysical Journal
https://www.cell.com/biophysj/pdf/S0006-3495(22)00855-4.pdf
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The activated ClpP peptidase forcefully grips a protein substrate
Walker, S. D. et al.
2022
Biophysical Journal
https://www.sciencedirect.com/science/article/pii/S000634952200724X
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Single-molecule force spectroscopy of toehold-mediated strand displacement
Walbrun, A. et al.
2024
Nature Communications
https://doi.org/10.1038/s41467-024-51813-9
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Cis-mediated interactions of the SARS-CoV-2 frameshift RNA alter its conformations and affect function
Pekarek, L. et al.
2022
NAR
https://academic.oup.com/nar/advance-article/doi/10.1093/nar/gkac1184/6946986
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Mechanistic Insights into the Folding Mechanism of Region V in Ice-Binding Protein Secreted by Marinomonas primoryensi Revealed by Single-Molecule Force Spectroscopy
Wang, H. et al.
2023
Langmuir
https://pubs.acs.org/doi/10.1021/acs.langmuir.3c02257
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A molecular optomechanics approach reveals functional relevance of force transduction across talin and desmoplakin
Sadhanasatish, T. et al.
2023
Science Advances
https://doi.org/10.1126/sciadv.adg3347
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Cytosolic Interactome Protects Against Protein Unfolding in a Single Molecule Experiment
Scalvini, B. et al.
2023
Advanced Biology
https://doi.org/10.1002/adbi.202300105
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Free-energy measuring nanopore device
Gavrilov, M. et al.
2023
Physical Review E
https://journals.aps.org/pre/accepted/3d07cY91P671618ac29421d365d9135ae5e1b5457
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Aha1 regulates Hsp90’s conformation and function in a stoichiometry-dependent way
Mondol, T. et al.
2023
Biophysical Journal
https://doi.org/10.1016/j.bpj.2023.07.020
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Membrane-induced 2D phase separation of the focal adhesion protein talin
Litschel, T. et al.
2024
Nature Communications
https://doi.org/10.1038/s41467-024-49222-z
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Probing the stability and interdomain interactions in the ABC transporter OpuA using single-molecule optical tweezers
Van Der Sleen, L. et al.
2024
Cell Reports
https://doi.org/10.1016/j.celrep.2024.114110
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Stick-slip unfolding favors self-association of expanded HTT mRNA
O’Brien, B. M. et al.
2024
Nature Communications
https://doi.org/10.1038/s41467-024-52764-x
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Human RPA activates BLM’s bidirectional DNA unwinding from a nick
Qin, Z. et al.
2020
eLife
https://elifesciences.org/articles/54098
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DNA stretching induces Cas9 off-target activity
Newton, M. D. et al.
2019
Nature Structural & Molecular Biology
https://www.nature.com/articles/s41594-019-0188-z
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Reversible histone glycation is associated with disease-related changes in chromatin architecture
Zheng, Q. et al.
2019
Nature Communications
https://www.nature.com/articles/s41467-019-09192-z
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Sites of high local frustration in DNA origami
Kosinski, R. et al.
2019
Nature Communications
https://www.nature.com/articles/s41467-019-09002-6
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