Schartel L, Jann C, Wierczeiko A, et al (2024) Selective RNA pseudouridinylation in situ by circular gRNAs in designer organelles. Nat Commun 15:9177. https://doi.org/10.1038/s41467-024-53403-1

Junglas B, Kartte D, Kutzner M, et al (2024) Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies. Nat Struct Mol Biol 1–16. https://doi.org/10.1038/s41594-024-01399-z

Bhattacharjee R, Lemke EA (2024) Potential vs Challenges of Expanding the Protein Universe With Genetic Code Expansion in Eukaryotic Cells. Journal of Molecular Biology 168807. https://doi.org/10.1016/j.jmb.2024.168807

Changiarath A, Arya A, Xenidis VA, et al (2024) Sequence determinants of protein phase separation and recognition by protein phase-separated condensates through molecular dynamics and active learning. Faraday Discuss. https://doi.org/10.1039/d4fd00099d

Jann C, Giofré S, Bhattacharjee R, Lemke EA (2024) Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids. Chem Rev 124:10281–10362. https://doi.org/10.1021/acs.chemrev.3c00878

Geist JL, Lee CY, Strom JM, et al (2024) Generation of a high confidence set of domain-domain interface types to guide protein complex structure predictions by AlphaFold. Bioinformatics btae482. https://doi.org/10.1093/bioinformatics/btae482

Junglas B, Hudina E, Schönnenbeck P, et al (2024) Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies. Nat Struct Mol Biol 1–12. https://doi.org/10.1038/s41594-024-01359-7

Emmanouilidis L, Bartalucci E, Kan Y, et al (2024) A solid beta-sheet structure is formed at the surface of FUS droplets during aging. Nat Chem Biol 20:1044–1052. https://doi.org/10.1038/s41589-024-01573-w

Sushkin ME, Jung M, Lemke EA (2024) Tuning the Functionality of Designer Translating Organelles with Orthogonal tRNA Synthetase/tRNA Pairs. Journal of Molecular Biology 168728. https://doi.org/10.1016/j.jmb.2024.168728

Samanta A, Baranda Pellejero L, Masukawa M, Walther A (2024) DNA-empowered synthetic cells as minimalistic life forms. Nat Rev Chem 8:454–470. https://doi.org/10.1038/s41570-024-00606-1

Dormann D, Lemke EA (2024) Adding intrinsically disordered proteins to biological ageing clocks. Nat Cell Biol 26:851–858. https://doi.org/10.1038/s41556-024-01423-w

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

Quarta N, Bhandari TR, Girard M, et al (2024) Monomer unfolding of a bacterial ESCRT-III superfamily member is coupled to oligomer disassembly. Protein Science 33:e5187. https://doi.org/10.1002/pro.5187

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