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Publications

Below you will find the full list of peer-reviewed scientific publications that have acknowledged Instruct-ERIC funding and resources to carry out the research.

 

  Web of Science analysis of Instruct-ERIC publications

per UN Sustainable Development Goals

 

Simply select the dropdown and find all publications from that year.

 

2026

  1. Arshad, R., et al. (2026). Cryo-EM structure of photosystem II supercomplex from a green microalga with extreme phototolerance. Nat. Commun. doi: 10.1038/s41467-025-65861-2
  2. Atalah, J., et al. (2026). Structural and Biochemical Insights into the Broad-Spectrum TET enzyme from Methanocaldococcus jannaschii reveals the basis of substrate specificity in M42 aminopeptidases. J. Mol. Biol. doi: 10.1016/j.jmb.2025.169596
  3. Batchu, K., et al. (2026). Toward Nanodisc Tailoring for SANS Study of Membrane Proteins. Bioengineering-Basel doi: 10.3390/bioengineering13010087
  4. Bys, K., et al. (2026). Structural transformation and charge regulation of natural rubber-derived polymeric anticoagulants. Eur. Polym. J. doi: 10.1016/j.eurpolymj.2025.114440
  5. Cuccaro, R., et al. (2026). Human glutaredoxin 3: multiple domains for a unique function. J. Inorg. Biochem. doi: 10.1016/j.jinorgbio.2025.113103
  6. Elbadri, K., et al. (2026). Design and in vitro validation of Brome mosaic-virus-like particles for gene delivery and immunomodulation of melanoma. Mater. Today Bio doi: 10.1016/j.mtbio.2025.102693
  7. Finocchiaro, G., et al. (2026). Front-illuminated surface plasmon resonance biosensor for the study of light-responsive proteins and their interactions. Biosens. Bioelectron. doi: 10.1016/j.bios.2025.117998
  8. Flanders, P., et al. (2026). Structural and Dynamics Analyses of β-Lactam Inhibition of Streptococcus pneumoniae Penicillin-Binding Protein 1b (PBP1b) Guide Interrogation of Structure-Activity Relationships. ACS Chem. Biol. doi: 10.1021/acschembio.5c00788
  9. García-Fernández, D., et al. (2026). Covalent organic polymer-based biosensor for autism spectrum disorder biomarker detection. Microchim. Acta doi: 10.1007/s00604-025-07794-7
  10. Gerogianni, I., et al. (2026). Isolation and Biophysical Characterization of Lipoxygenase-1 from Soybean Seed, a Versatile Biocatalyst for Industrial Applications. Biomolecules doi: 10.3390/biom16010162
  11. Giordano, F., et al. (2026). Structure and function of persulfide dioxygenase from Pseudomonas aeruginosa: Implications on H2S homeostasis and interplay with nitric oxide. iScience. doi: 10.1016/j.isci.2025.114586
  12. Hongmanorom, P., et al. (2026). Metal oxide-promoted mesoporous silica as support for Ru-based CO2 methanation catalysts. Appl. Catal. B-Environ. Energy. doi: 10.1016/j.apcatb.2025.126142
  13. Ilca, S. L., et al. (2026). Capsid restructuring activates semi-conservative dsRNA transcription in cystovirus ɸ6. Mol. Cell. doi: 10.1016/j.molcel.2025.12.025
  14. Ji, J., et al. (2026). Myomerger-derived peptide enhances skeletal muscle tropism and reduces liver transduction of lipid nanoparticles for gene delivery. Mol. Ther. Nucl. Acids. doi: 10.1016/j.omtn.2025.102785
  15. Lai, F., et al. (2026). Postsynthetic Integration of Silver Atoms into Spin Crossover Hofmann-Type Clathrates. Inorg. Chem. doi: 10.1021/acs.inorgchem.5c04594
  16. Leonova, L., et al. (2026). Ethanol dehydration with aerosol-made mesoporous aluminosilicates featuring dispersed active sites. Catal. Today doi: 10.1016/j.cattod.2025.115494
  17. Ouzounthanasis, K., et al. (2026). Discovery of Fused Isoquinolinone/Triazole as a Scaffold for Tankyrase and PARP Inhibition. J. Med. Chem. doi: 10.1021/acs.jmedchem.5c02481
  18. Pierigé, M., et al. (2026). Exploring the flame retardant mechanism of α-amino acid-derived polyamidoamine-treated cotton: An EPR study. Colloid Surf. A-Physicochem. Eng. Asp. doi: 10.1016/j.colsurfa.2025.138787
  19. Rep, A., et al. (2026). Regulatory hotspot on the influenza A virus polymerase revealed through the structure of the NEP-polymerase complex. Sci. Adv. doi: 10.1126/sciadv.aeb4073
  20. Roux, M., et al. (2026). Synergistic Action of Crystallophore and Imaging-Crystallophore Enhances the Production and Imaging of Protein Crystals. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202525011
  21. Sadzak, A., et al. (2026). Oxidative degradation of polyunsaturated lipid membranes: Structural changes, mechanistic insights and flavonoid protection. J. Colloid Interface Sci. doi: 10.1016/j.jcis.2026.139894
  22. Serianni, V., et al. (2026). Molecular insight into 5′ RNA capping with NpnNs by bacterial RNA polymerase. Nat. Chem. Biol. doi: 10.1038/s41589-025-02134-5
  23. Siahaan, V., et al. (2026). Tau phosphorylation impedes functionality of protective tau envelopes. Nat. Chem. Biol. doi: 10.1038/s41589-025-02122-9
  24. Stojaspal, M., et al. (2026). Anemia-associated mutations disrupt the CDIN1-Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA-I) disease. FEBS J. doi: 10.1111/febs.70421
  25. Sudakov, A., et al. (2026). DNP-Enhanced Magic Angle Spinning Solid-State NMR Spectroscopy to Determine RNA–Ligand Interactions. J. Am. Chem. Soc. doi: 10.1021/jacs.5c17834
  26. Sudzinová, P., et al. (2026). Bacteria sense the antibiotic rifampicin through a widespread dual-promoter based alarm system. Nucleic Acids Res. doi: 10.1093/nar/gkaf1407

2025

  1. Abbas, M., et al. (2025). Lipopolysaccharide nanoparticles: A biomimetic platform to study bacterial surface. Biophys. J. doi: 10.1016/j.bpj.2025.06.036
  2. Abreu, C., et al. (2025). Insights into stability, dimerisation, and ligand binding properties of Siglec-7: Isotope labelling in HEK293 cells for protein characterisation by NMR spectroscopy. Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2025.142672
  3. Agarwal, M., et al. (2025). The Role of Light Irradiation and Dendrimer Generation in Directing Electrostatic Self-Assembly. Polymers doi: 10.3390/polym17020170
  4. Alaviuhkola, J., et al. (2025). Discovery of Inhibitors for Bacterial Arr Enzymes ADP-Ribosylating and Inactivating Rifamycin Antibiotics. ACS Chem. Biol. doi: 10.1021/acschembio.5c00164
  5. Alexandre, D., et al. (2025). Cellular modulation of a G-quadruplex structure found in the lung cancer-related microRNA-3196. Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2025.145263
  6. Alexandre, D., et al. (2025). miRNA-155-3p and miRNA-3196 as Potential Biomarkers in Liquid Biopsies of Non-Small Cell Lung Cancer Patients. Biomedicines doi: 10.3390/biomedicines13122946
  7. Alhalabi, A., et al. (2025). Designing atomically precise gold nanocluster architectures with DNA-guided self-assembly and biofunctionalization approaches. Nanoscale doi: 10.1039/d5nr00905g
  8. Alper, P., et al. (2025). RDMkit: A research data management toolkit for life sciences. Patterns doi: 10.1016/j.patter.2025.101345
  9. Alves, A., et al. (2025). I-motif formation in the promoter region of the B-MYB proto-oncogene. Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2025.139582
  10. Angeles, D., et al. (2025). SpoIIIL is a forespore factor required for efficient cell-cell signalling during Bacillus subtilis sporulation. PLOS Gen. doi: 10.1371/journal.pgen.1011768
  11. Arnaud, C., et al. (2025). About proteins of a siphophage tail tip complex reverting to their pre-ejection fold after DNA ejection. Nat. Commun. doi: 10.1038/s41467-025-57874-8
  12. Arragain, B., et al. (2025). Structure of the tilapia lake virus nucleoprotein bound to RNA. Nucleic Acids Res. doi: 10.1093/nar/gkaf112
  13. Arranz, R., et al. (2025). Elucidating the structure and assembly mechanism of actinoporin pores in complex membrane environments. Sci. Adv. doi: 10.1126/sciadv.adv0683
  14. Ashraf, R., et al. (2025). RECQ4-MUS81 interaction contributes to telomere maintenance with implications to Rothmund-Thomson syndrome. Nat. Commun. doi: 10.1038/s41467-025-56518-1
  15. Atanasova, N. S., et al. (2025). Ice nucleation activity of two Antarctic sea ice bacteriophages PANV1 and OANV1 and the impact of freezing on their infectivity. Envir Adv doi: 10.1016/j.envadv.2025.100659
  16. Audibert, A., et al. (2025). Subunit-specific isotope labelling of heteromeric complexes using cell-free protein expression: application to the 760 kDa ClpXP molecular machine. RSC Chem. Biol. doi: 10.1039/d5cb00259a
  17. Baine, J. M., et al. (2025). alpha-Hydrazino Acids Inhibit Pyridoxal Phosphate-Dependent Decarboxylases via "Catalytically Correct" Ketoenamine Tautomers: A Special Motif for Chemical Biology and Drug Discovery? ACS Catal. doi: 10.1021/acscatal.5c00326
  18. Balarynová, J., et al. (2025). Translational and epitranscriptomic regulation of seed germination in Arabidopsis thaliana genotypes with contrasting dormancy phenotypes. Plant Mol.Biol. doi: 10.1007/s11103-025-01659-6
  19. Basoglu, A., et al. (2025). NMR-based-Metabolomics Evaluation in Dogs Infected with Canine Parvovirus: A New Approach for Biomarker/s. Vet. Ital. doi: 10.12834/VetIt.3578.29616.2
  20. Baudoin, M., et al. (2025). Cross-linking teichoic acids by click chemistry prevents bacterial cell growth. Chem. Commun. doi: 10.1039/d5cc02577j
  21. Beaumont, C., et al. (2025). hnRNP A1 induces aberrant CFTR exon 9 splicing via a newly discovered ESS element. Life Sci. Alliance doi: 10.26508/lsa.202402720
  22. Bernhard, H., et al. (2025). Structural basis of Spliced Leader RNA recognition by the Trypanosoma brucei cap-binding complex. Nat. Commun. doi: 10.1038/s41467-024-55373-w
  23. Bicer, D., et al. (2025). Structural basis of specific lysine transport by Pseudomonas aeruginosa permease LysP. Nat. Commun. doi: 10.1038/s41467-025-66618-7
  24. Biersteker, R., et al. (2025). Modulation of immunoglobulin G oligomerization by variable domain glycans: A mechanism to regulate complement activation. PNAS Nexus doi: 10.1093/pnasnexus/pgaf216
  25. Birgusova, E., et al. (2025). TP53 detection based on electrochemical genosensors with different types of gold nanoparticles. Microchem J. doi: 10.1016/j.microc.2025.112856
  26. Blazickova, J., et al. (2025). Overlapping and separable activities of BRA-2 and HIM-17 promote occurrence and regulation of pairing and synapsis during Caenorhabditis elegans meiosis. Nat. Commun. doi: 10.1038/s41467-025-57862-y
  27. Boclinville, A., et al. (2025). Isoelectric point determination by icIEF as quality control for structural and functional characterization of HPV16 virus-like particles. Anal. Chim. Acta. doi: 10.1016/j.aca.2025.344904
  28. Bolognesi, T., et al. (2025). Exploring the Role of Structural and Dynamic Complexity in SARS-CoV-2 Nucleocapsid Protein-Heparin Interactions by NMR. J. Mol. Biol. doi: 10.1016/j.jmb.2025.169437
  29. Bolognesi, T., et al. (2025). NMR insights on multidomain proteins: the case of the SARS-CoV-2 nucleoprotein. Prog. Nucl. Magn. Reson. Spectrosc. doi: 10.1016/j.pnmrs.2025.101577
  30. Bosak, J., et al. (2025). Proteome Analysis of Seven Treponema pallidum subsp. pallidum Strains Grown In Vitr o. J. Proteome Res. doi: 10.1021/acs.jproteome.5c00624
  31. Bosetti, C., et al. (2025). Re-evaluation of PTEN as an ADP-ribosylated tankyrase binding partner. FEBS J. doi: 10.1111/febs.70035
  32. Bouchama, F., et al. (2025). Rabies Virus Phosphoprotein Exhibits Thermoresponsive Phase Separation with a Lower Critical Solution Temperature. J. Mol. Biol. doi: 10.1016/j.jmb.2024.168889
  33. Bracaglia, L., et al. (2025). Decoding Order and Disorder in Proteins by NMR Spectroscopy. J. Am. Chem. Soc. doi: 10.1021/jacs.4c14959
  34. Brandis, D., et al. (2025). The Internal Structural Dynamics of Elastin-Like Polypeptide Assemblies by 13C-Direct Detected NMR Spectroscopy. Anal. Chem. doi: 10.1021/acs.analchem.4c05163
  35. Brimson, J. M. (2025). Sigma-1 Receptors & Disease (S1RaD) 2025. Geriatric Pharma doi: 10.1080/2994399X.2024.2454759
  36. Broc, M., et al. (2025). A scaffold for quinone channeling between membrane and soluble bacterial oxidoreductases. Nat. Struct. Mol. Biol. doi: 10.1038/s41594-025-01607-4
  37. Brola, T., et al. (2025). Cryo-EM structure of N-glycosylated Pomacea canaliculata hemocyanin provides insights into its role in the immune response of gastropods. FEBS J. doi: 10.1111/febs.70378
  38. Brungs, C., et al. (2025). MSnLib: efficient generation of open multi-stage fragmentation mass spectral libraries. Nat. Methods doi: 10.1038/s41592-025-02813-0
  39. Bruno, F., et al. (2025). pyIHM: Indirect Hard Modeling, in Python. Anal. Chem. doi: 10.1021/acs.analchem.4c06484
  40. Bukhdruker, S., et al. (2025). Proteorhodopsin insights into the molecular mechanism of vectorial proton transport. Sci. Adv. doi: 10.1126/sciadv.adu5303
  41. Bulvas, O., et al. (2025). Conformational landscape of the mycobacterial inosine 5′-monophosphate dehydrogenase octamerization interface. J. Struct. Biol. doi: 10.1016/j.jsb.2025.108198
  42. Buoli Comani, V., et al. (2025). Hemoglobin Receptor Redundancy in Staphylococcus Aureus: Molecular Flexibility as a Determinant of Divergent Hemophore Activity. J Struct Biol X doi: 10.1016/j.yjsbx.2025.100138
  43. Burbidge, O., et al. (2025). Nanobodies restore stability to cancer-associated mutants of tumor suppressor protein p16INK4a. Structure doi: 10.1016/j.str.2025.07.017
  44. Burkhart, I., et al. (2025). The Zuo1 C-terminal domain stabilizes DNA guanosine quadruplex (G4) structures located on Chromosome IX in Saccharomyces cerevisiae. Nucleic Acids Res. doi: 10.1093/nar/gkaf1055
  45. Campbell, J., et al. (2025). Mechanistic insights into TTLL11 polyglutamylase-mediated primary tubulin chain elongation. Sci. Adv. doi: 10.1126/sciadv.adw1561
  46. Cancade-Veyre, L., et al. (2025). Brucella NyxA and NyxB dimerization enhances effector function during infection. FEBS Lett. doi: 10.1002/1873-3468.70069
  47. Caramello, N., et al. (2025). The in crystallo optical spectroscopy toolbox. J. Appl. Crystallogr. doi: 10.1107/S1600576725003541
  48. Carazo, J. (2025). On interrogating electron microscopy images to discover proteins in the cell. IUCrJ doi: 10.1107/S2052252525001861
  49. Carré, L., et al. (2025). Determination of in cellulo proteome molecular dynamics in different halophilic Archaea. J. R. Soc. Interface doi: 10.1098/rsif.2024.0630
  50. Cassani, M., et al. (2025). Regulation of cell–nanoparticle interactions through mechanobiology. Nano Lett. doi: 10.1021/acs.nanolett.4c04290
  51. Castel, J., et al. (2025). Mechanism of Inhibition of the MeTC7 Ligand That Covalently Binds to VDR To Reduce PD-L1 Expression. J. Med. Chem. doi: 10.1021/acs.jmedchem.5c02589
  52. Cavazzoli, G., et al. (2025). Increasing the Chemical Space of L-SIGN Specific Glycomimetics. J. Med. Chem. doi: 10.1021/acs.jmedchem.5c01448
  53. Cempírek, J., et al. (2025). Ertlite, NaAl3Al6(Si4B2O18)(BO3)3(OH)3O, a new mineral species of the tourmaline supergroup. Am. Miner. doi: 10.2138/am-2025-9816
  54. Chagny, E., et al. (2025). Wide Diversity and Complex Evolution of M42 Aminopeptidases With Contrasted Functional Properties in Archaea. Mol. Biol. Evol. doi: 10.1093/molbev/msaf233
  55. Chattopadhyay, S., et al. (2025). Flexibility-Aided Orientational Self-Sorting and Transformations of Bioactive Homochiral Cuboctahedron Pd12L16. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202513902
  56. Chaudhari, A., et al. (2025). Light-dependent flavin redox and adduct states control the conformation and DNA-binding activity of the transcription factor EL222. Nucleic Acids Res. doi: 10.1093/nar/gkaf215
  57. Chen, B., et al. (2025). Coming Clean and Avoiding Bubble Trouble-Using Detergents Wisely in the Purification of Membrane Proteins for Cryo-EM Studies. Biomolecules doi: 10.3390/biom15091315
  58. Chen, Z., et al. (2025). Structural mimicry of UM171 and neomorphic cancer mutants co-opts E3 ligase KBTBD4 for HDAC1/2 recruitment. Nat. Commun. doi: 10.1038/s41467-025-58350-z
  59. Chochola, V., et al. (2025). TYRAY-Functionalized Alginate Bioinks for 3D Bioprinting Support Stem Cell Culture and Endothelial Network Formation. ACS Biomater. Sci. Eng. doi: 10.1021/acsbiomaterials.5c01132
  60. Chvojka, M., et al. (2025). Substituent effects of fluorinated bambusurils on their anion transport. Org. Biomol. Chem. doi: 10.1039/d5ob00400d
  61. Ciaffaglione, V., et al. (2025). SUMO-2 activity is inhibited by non-covalent interactions with the A(3 peptide: an exploration of potential pathogenic mechanisms in Alzheimer's disease. Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2025.146632
  62. Ciofalo, C., et al. (2025). Benchmarking Zinc-Binding Site Predictors: A Comparative Analysis of Structure-Based Approaches. J. Chem Inf. Model. doi: 10.1021/acs.jcim.5c00549
  63. Colautti, J., et al. (2025). Cryo-EM structure of a type VI secretion system-delivered membrane-depolarizing toxin involved in bacterial antagonism. Cell Reports doi: 10.1016/j.celrep.2025.116263
  64. Collin-Faure, V., et al. (2025). A comparison of the effects of polystyrene and polycaprolactone nanoplastics on macrophages. Environ. Sci.-Nano doi: 10.1039/d5en00074b
  65. Coquille, S., et al. (2025). Allostery and Evolution: A Molecular Journey Through the Structural and Dynamical Landscape of an Enzyme Super Family. Mol. Biol. Evol. doi: 10.1093/molbev/msae265
  66. Costantino, A., et al. (2025). Intracellular Binding of Novel Fluorinated Compounds to Carbonic Anhydrase Isoforms Explored by In-Cell 19F NMR. J. Med. Chem. doi: 10.1021/acs.jmedchem.5c02227
  67. Coufal, R., et al. (2025). Fluorescent Nanoporous Materials from Polypropylene-Based Covalent Adaptable Networks. ACS Omega doi: 10.1021/acsomega.4c10168
  68. Coulon, R., et al. (2025). Transforming solid-state nuclear magnetic resonance towards a chemistry-ready technique. Solid State Nucl. Magn. Reson. doi: 10.1016/j.ssnmr.2025.102048
  69. Creanza, T., et al. (2025). Transformer Decoder Learns from a Pretrained Protein Language Model to Generate Ligands with High Affinity. J. Chem Inf. Model. doi: 10.1021/acs.jcim.4c02019
  70. Curro, F., et al. (2025). Fast and Straightforward Lipid Quantification in Pharmaceutical Compositions Using NMR. ACS Omega doi: 10.1021/acsomega.5c09329
  71. d'Acapito, A., et al. (2025). Comparative anatomy of siphophage tails before and after interaction with their receptor. Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2025.103045
  72. D'Ercole, C., et al. (2025). Early stress detection in forest trees using a nanobody-functionalized electrochemical biosensor for ascorbate peroxidase. Plant Stress doi: 10.1016/j.stress.2025.100844
  73. da Silva, J., et al. (2025). The structure of His15 acetamide-modified hen egg-white lysozyme: a nice surprise from an old friend. Acta Crystallogr. F. doi: 10.1107/S2053230X2500010X
  74. Dal Maso, T., et al. (2025). Developing nanobodies as allosteric molecular chaperones of glucocerebrosidase function. Nat. Commun. doi: 10.1038/s41467-025-60134-4
  75. Das, G., et al. (2025). Targeting prostate cancer by new bispecific monocyte engager directed to prostate-specific membrane antigen. PLoS One doi: 10.1371/journal.pone.0307353
  76. De Caro, L., et al. (2025). Characterization of VitE-TPGS Micelles Linked to Poorly Soluble Pharmaceutical Compounds Exploiting Pair Distribution Function's Moments. Pharmaceutics doi: 10.3390/pharmaceutics17040431
  77. de Isidro-Gómez, F., et al. (2025). Automatic detection of alignment errors in cryo-electron tomography. J. Struct. Biol. doi: 10.1016/j.jsb.2024.108153
  78. De Keyser, P., et al. (2025). A biosensor-based phage display selection method for automated, high-throughput Nanobody discovery. Biosens. Bioelectron. doi: 10.1016/j.bios.2024.116951
  79. De Summa, S., et al. (2025). Baseline metabolic signatures predict clinical outcomes in immunotherapy-treated melanoma patients: a pilot study. Front. Immunol. doi: 10.3389/fimmu.2025.1536710
  80. De'Ath, C., et al. (2025). Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography. J. Appl. Crystallogr. doi: 10.1107/S1600576724011191
  81. Delalande, F., et al. (2025). Holdup Multiplex Assay for High-Throughput Measurement of Protein-Ligand Affinity Constants Using a Mass Spectrometry Readout. J. Am. Chem. Soc. doi: 10.1021/jacs.4c11102
  82. Dépéry, L., et al. (2025). Anti-SARS-CoV-2 serology based on ancestral RBD antigens does not correlate with the presence of neutralizing antibodies against Omicron variants. Microbiol. Spectr. doi: 10.1128/spectrum.01568-24
  83. Di Carluccio, C., et al. (2025). Fusobacterium nucleatum Lipopolysaccharides O-Antigen Defines a Novel Siglec-7 Binding Epitope. JACS Au doi: 10.1021/jacsau.5c00810
  84. Di Carluccio, C., et al. (2025). Insights into Siglec-7 Binding to Gangliosides: NMR Protein Assignment and the Impact of Ligand Flexibility. Adv. Sci. doi: 10.1002/advs.202415782
  85. Diana, R., et al. (2025). B3GALT6 mutations lead to compromised connective tissue biomechanics in Ehlers-Danlos syndrome. JCI Insight doi: 10.1172/jci.insight.179474
  86. Diaz-Martin, S., et al. (2025). Structural and functional characterization of TgGSK3, a druggable kinase in Toxoplasma gondii. Nat. Commun. doi: 10.1038/s41467-025-64701-7
  87. Dragone, M., et al. (2025). β-Cyclodextrin Inclusion Complexes with Model Pentapeptides: Role of the Tyrosine Position within the Peptide Chain. ChemistryOpen doi: 10.1002/open.202500223
  88. Dubiez, E., et al. (2025). Structural basis for the synergistic assembly of the snRNA export complex. Nat. Struct. Mol. Biol. doi: 10.1038/s41594-025-01595-5
  89. Duong, M., et al. (2025). A FRET-Based High-Throughput Screening Assay for the Discovery of Mycobacterium tuberculosis DNA ADP-Ribosylglycohydrolase DarG Inhibitors. ACS Infect. Dis. doi: 10.1021/acsinfecdis.5c00695
  90. Duplissy, J., et al. (2025). A Field Pilot Study of the Aero Quattro Air Purifier Operated Directly on the Air Ventilation of A Navigating Cruise Ship: Effect on New Particle Formation and Effectiveness Against the Airborne Phi6 Model Virus. Aerosol Air Qual. Res doi: 10.1007/s44408-025-00079-x
  91. Dušková, M., et al. (2025). Occurrence, growth, and virulence genes of Bacillus cereus in ready-to-cook plant-based meat analogues. Acta Vet. BRNO doi: 10.2754/avb202594040317
  92. Dutta, P., et al. (2025). Structural basis for human chondroitin sulfate chain polymerization. Nat. Commun. doi: 10.1038/s41467-025-66787-5
  93. Dutta, P., et al. (2025). Mapping and quantification of potato virus A RNA genomes within viral particles and polysomes in infected plant cells. J. Virol. Methods. doi: 10.1016/j.jviromet.2024.115066
  94. Dvorak, J., et al. (2025). Proof-of-concept MALDI-TOF-MS assay for the detection of Toxin B enzymatic activity in Clostridioides difficile infection. Microbiol. Spectr. doi: 10.1128/spectrum.02453-24
  95. El-Dahshan, O., et al. (2025). Hydrothermal microwave synthesis of water soluble NIR-II emitting Ag2S quantum dots. Nanoscale doi: 10.1039/d5nr00052a
  96. Elliott, I., et al. (2025). Structure-guided disulfide engineering restricts antibody conformation to elicit TNFR agonism. Nat. Commun. doi: 10.1038/s41467-025-58773-8
  97. Exertier, C., et al. (2025). Specialty grand challenges in theoretical modeling, structure prediction and design. Frontiers Media SA doi: 10.3389/fchbi.2025.1635423
  98. Exertier, C., et al. (2025). Gaseous ligand binding to Porphyromonas gingivalis HmuY hemophore-like protein in complex with heme. J. Inorg. Biochem. doi: 10.1016/j.jinorgbio.2025.112879
  99. Fakhouri, H., et al. (2025). Analytical ultracentrifugation as a tool for exploring COSAN assemblies. Europ Biophys J doi: 10.1007/s00249-025-01746-y
  100. Fearon, D., et al. (2025). Accelerating Drug Discovery With High-Throughput Crystallographic Fragment Screening and Structural Enablement. Appl. Res. doi: 10.1002/appl.202400192
  101. Figueiredo, J., et al. (2025). Synthesis of 1,10-Phenanthroline-2,9-bistriazoles: Evaluation as G-Quadruplex Binders and Anti-Tumor Activity. ChemMedChem doi: 10.1002/cmdc.202400591
  102. Fioretto, L., et al. (2025). Small molecules as ligands in the tuning of immune regulatory receptors. Front. Immunol. doi: 10.3389/fimmu.2025.1648691
  103. Fiorucci, L., et al. (2025). Extracting Trends From NMR Data With TrAGICo: A Python Toolbox. Magn. Reson. Chem. doi: 10.1002/mrc.5537
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2024

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