Lemke EA, Babu MM, Kriwacki RW, et al (2024) Intrinsic disorder: A term to define the specific physicochemical characteristic of protein conformational heterogeneity. Molecular Cell 84:1188–1190. https://doi.org/10.1016/j.molcel.2024.02.024

Krevert CS, Chavez D, Chatterjee S, et al (2023) Liquid–Liquid Phase Separation of the Intrinsically Disordered Domain of the Fused in Sarcoma Protein Results in Substantial Slowing of Hydration Dynamics. J Phys Chem Lett 14:11224–11234. https://doi.org/10.1021/acs.jpclett.3c02790

Bronkhorst AW, Lee CY, Möckel MM, et al (2023) An extended Tudor domain within Vreteno interconnects Gtsf1L and Ago3 for piRNA biogenesis in Bombyx mori. The EMBO Journal n/a:e114072. https://doi.org/10.15252/embj.2023114072

Rahmanto AS, Blum CJ, Scalera C, et al (2023) K6-linked ubiquitylation marks formaldehyde-induced RNA-protein crosslinks for resolution. Molecular Cell 0: https://doi.org/10.1016/j.molcel.2023.10.011

Fung HKH, Hayashi Y, Salo VT, et al (2023) Genetically encoded multimeric tags for subcellular protein localization in cryo-EM. Nat Methods 1–9. https://doi.org/10.1038/s41592-023-02053-0

Schlösser L, Sachse C, Low HH, Schneider D (2023) Conserved structures of ESCRT-III superfamily members across domains of life. Trends in Biochemical Sciences 48:993–1004. https://doi.org/10.1016/j.tibs.2023.08.009

Wierczeiko A, Pastore S, Mündnich S, et al (2023) NanopoReaTA: a user-friendly tool for nanopore-seq real-time transcriptional analysis. Bioinformatics 39:btad492. https://doi.org/10.1093/bioinformatics/btad492

Schumbera E, Mier P, Andrade-Navarro MA (2023) Phase separating Rho: a widespread regulatory function of disordered regions in proteins revealed in bacteria. Sig Transduct Target Ther 8:253. https://doi.org/10.1038/s41392-023-01505-5

Roth P, Meyer R, Harley I, et al (2023) Supramolecular assembly guided by photolytic redox cycling. Nat Synth. https://doi.org/10.1038/s44160-023-00343-1

Maltseva D, Chatterjee S, Yu C-C, et al (2023) Fibril formation and ordering of disordered FUS LC driven by hydrophobic interactions. Nat Chem 1–9. https://doi.org/10.1038/s41557-023-01221-1

Yu M, Heidari M, Mikhaleva S, et al (2023) Visualizing the disordered nuclear transport machinery in situ. Nature 617:162–169. https://doi.org/10.1038/s41586-023-05990-0

Agam G, Gebhardt C, Popara M, et al (2023) Reliability and accuracy of single-molecule FRET studies for characterization of structural dynamics and distances in proteins. Nat Methods 1–13. https://doi.org/10.1038/s41592-023-01807-0

Ebersberger S, Hipp C, Mulorz MM, et al (2023) FUBP1 is a general splicing factor facilitating 3′ splice site recognition and splicing of long introns. Molecular Cell 83:2653-2672.e15. https://doi.org/10.1016/j.molcel.2023.07.002

Scheidt T, Ruan H, Yu M, Lemke EA (2023) Stressing the role of a short linear motif in ataxin-2 condensation. Molecular Cell 83:1961–1963. https://doi.org/10.1016/j.molcel.2023.05.024

Wettermann S, Datta R, Virnau P (2023) Influence of ionic conditions on knotting in a coarse-grained model for DNA. Frontiers in Chemistry 10:. https://doi.org/10.3389/fchem.2022.1096014

Gruijs da Silva LA, Simonetti F, Hutten S, et al (2022) Disease-linked TDP-43 hyperphosphorylation suppresses TDP-43 condensation and aggregation. The EMBO Journal 41:e108443. https://doi.org/10.15252/embj.2021108443

Chakraborty S, Berac CM, Urschbach M, et al (2022) Predicting the Supramolecular Assembly of Amphiphilic Peptides from Comprehensive Coarse-Grained Simulations. ACS Appl Polym Mater 4:822–831. https://doi.org/10.1021/acsapm.1c01208

Jin E, Fu S, Hanayama H, et al (2022) A Nanographene-Based Two-Dimensional Covalent Organic Framework as a Stable and Efficient Photocatalyst. Angewandte Chemie International Edition 61:e202114059. https://doi.org/10.1002/anie.202114059

Prawatborisut M, Oberländer J, Jiang S, et al (2022) Temperature-Responsive Nanoparticles Enable Specific Binding of Apolipoproteins from Human Plasma. Small 18:2103138. https://doi.org/10.1002/smll.202103138

Mosler T, Conte F, Longo GMC, et al (2021) R-loop proximity proteomics identifies a role of DDX41 in transcription-associated genomic instability. Nat Commun 12:7314. https://doi.org/10.1038/s41467-021-27530-y

Zegota MM, Müller MA, Lantzberg B, et al (2021) Dual Stimuli-Responsive Dynamic Covalent Peptide Tags: Toward Sequence-Controlled Release in Tumor-like Microenvironments. J Am Chem Soc 143:17047–17058. https://doi.org/10.1021/jacs.1c06559

Varga J, Kube M, Luck K, Schick S (2021) The BAF chromatin remodeling complexes: structure, function, and synthetic lethalities. Biochemical Society Transactions 49:1489–1503. https://doi.org/10.1042/BST20190960

Jin E, Yang Q, Ju C-W, et al (2021) A Highly Luminescent Nitrogen-Doped Nanographene as an Acid- and Metal-Sensitive Fluorophore for Optical Imaging. J Am Chem Soc 143:10403–10412. https://doi.org/10.1021/jacs.1c04880

Chen C, Singh MK, Wunderlich K, et al (2021) Polymer cyclization for the emergence of hierarchical nanostructures. Nat Commun 12:3959. https://doi.org/10.1038/s41467-021-24222-5

Dietz S, Almeida MV, Nischwitz E, et al (2021) The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1. Nat Commun 12:2668. https://doi.org/10.1038/s41467-021-22861-2

Dittrich F, Speck T, Virnau P (2021) Critical behavior in active lattice models of motility-induced phase separation. Eur Phys J E 44:53. https://doi.org/10.1140/epje/s10189-021-00058-1

Tubiana L, Kobayashi H, Potestio R, et al (2021) Comparing equilibration schemes of high-molecular-weight polymer melts with topological indicators. J Phys: Condens Matter 33:204003. https://doi.org/10.1088/1361-648X/abf20c

Worpenberg L, Paolantoni C, Longhi S, et al (2021) Ythdf is a N6-methyladenosine reader that modulates Fmr1 target mRNA selection and restricts axonal growth in Drosophila. The EMBO Journal 40:e104975. https://doi.org/10.15252/embj.2020104975

Weißbach S, Sys S, Hewel C, et al (2021) Reliability of genomic variants across different next-generation sequencing platforms and bioinformatic processing pipelines. BMC Genomics 22:62. https://doi.org/10.1186/s12864-020-07362-8

Datta R, Yelash L, Schmid F, et al (2021) Shear-Thinning in Oligomer Melts—Molecular Origins and Applications. Polymers 13:2806. https://doi.org/10.3390/polym13162806

Schüle M, Butto T, Dewi S, et al (2021) mTOR Driven Gene Transcription Is Required for Cholesterol Production in Neurons of the Developing Cerebral Cortex. International Journal of Molecular Sciences 22:6034. https://doi.org/10.3390/ijms22116034

Adamo G, Fierli D, Romancino DP, et al (2021) Nanoalgosomes: Introducing extracellular vesicles produced by microalgae. Journal of Extracellular Vesicles 10:e12081. https://doi.org/10.1002/jev2.12081

Schlisske S, Rosenauer C, Rödlmeier T, et al (2021) Ink Formulation for Printed Organic Electronics: Investigating Effects of Aggregation on Structure and Rheology of Functional Inks Based on Conjugated Polymers in Mixed Solvents. Advanced Materials Technologies 6:2000335. https://doi.org/10.1002/admt.202000335

Ruffini N, Klingenberg S, Schweiger S, Gerber S (2020) Common Factors in Neurodegeneration: A Meta-Study Revealing Shared Patterns on a Multi-Omics Scale. Cells 9:2642. https://doi.org/10.3390/cells9122642

Pieszka M, Han S, Volkmann C, et al (2020) Controlled Supramolecular Assembly Inside Living Cells by Sequential Multistaged Chemical Reactions. J Am Chem Soc 142:15780–15789. https://doi.org/10.1021/jacs.0c05261

Singh MK, Hu M, Cang Y, et al (2020) Glass Transition of Disentangled and Entangled Polymer Melts: Single-Chain-Nanoparticles Approach. Macromolecules 53:7312–7321. https://doi.org/10.1021/acs.macromol.0c00550

Prozeller D, Rosenauer C, Morsbach S, Landfester K (2020) Immunoglobulins on the surface of differently charged polymer nanoparticles. Biointerphases 15:031009. https://doi.org/10.1116/6.0000139

Koch AHR, Morsbach S, Bereau T, et al (2020) Probing Nanoparticle/Membrane Interactions by Combining Amphiphilic Diblock Copolymer Assembly and Plasmonics. J Phys Chem B 124:742–750. https://doi.org/10.1021/acs.jpcb.9b10469

Dold A, Han H, Liu N, et al (2020) Makorin 1 controls embryonic patterning by alleviating Bruno1-mediated repression of oskar translation. PLOS Genetics 16:e1008581. https://doi.org/10.1371/journal.pgen.1008581

Chen C, Wunderlich K, Mukherji D, et al (2020) Precision Anisotropic Brush Polymers by Sequence Controlled Chemistry. J Am Chem Soc 142:1332–1340. https://doi.org/10.1021/jacs.9b10491

Fischer A, Schmid F, Speck T (2020) Quorum-sensing active particles with discontinuous motility. Phys Rev E 101:012601. https://doi.org/10.1103/PhysRevE.101.012601

Jiang S, Prozeller D, Pereira J, et al (2020) Controlling protein interactions in blood for effective liver immunosuppressive therapy by silica nanocapsules. Nanoscale 12:2626–2637. https://doi.org/10.1039/C9NR09879H

Jangizehi A, Schmid F, Besenius P, et al (2020) Defects and defect engineering in Soft Matter. Soft Matter 16:10809–10859. https://doi.org/10.1039/D0SM01371D

Liu X, Chen S-Y, Chen Q, et al (2020) Nanographenes: Ultrastable, Switchable, and Bright Probes for Super-Resolution Microscopy. Angewandte Chemie International Edition 59:496–502. https://doi.org/10.1002/anie.201909220

Lückerath T, Koynov K, Loescher S, et al (2020) DNA–Polymer Nanostructures by RAFT Polymerization and Polymerization-Induced Self-Assembly. Angewandte Chemie International Edition 59:15474–15479. https://doi.org/10.1002/anie.201916177

Alberg I, Kramer S, Schinnerer M, et al (2020) Polymeric Nanoparticles with Neglectable Protein Corona. Small 16:1907574. https://doi.org/10.1002/smll.201907574

Gai M, Simon J, Lieberwirth I, et al (2020) A bio-orthogonal functionalization strategy for site-specific coupling of antibodies on vesicle surfaces after self-assembly. Polymer Chemistry 11:527–540. https://doi.org/10.1039/C9PY01136F

Frey M-L, Simon J, Brückner M, et al (2020) Bio-orthogonal triazolinedione (TAD) crosslinked protein nanocapsules affect protein adsorption and cell interaction. Polymer Chemistry 11:3821–3830. https://doi.org/10.1039/D0PY00087F

Wagner J, Dillenburger M, Simon J, et al (2020) Amphiphilic dendrimers control protein binding and corona formation on liposome nanocarriers. Chemical Communications 56:8663–8666. https://doi.org/10.1039/D0CC02486D

Wagner J, Li L, Simon J, et al (2020) Amphiphilic Polyphenylene Dendron Conjugates for Surface Remodeling of Adenovirus 5. Angewandte Chemie 132:5761–5769. https://doi.org/10.1002/ange.201913708