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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.

 

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

 

2024

  1. Abendstein, L., et al. (2024). DNA Nanostructure-Templated Antibody Complexes Provide Insights into the Geometric Requirements of Human Complement Cascade Activation. J. Am. Chem. Soc. doi: 10.1021/jacs.4c02772
  2. Adámková, K., et al. (2024). Substrate preference, RNA binding and active site versatility of Stenotrophomonas maltophilia nuclease SmNuc1, explained by a structural study. FEBS J. doi: 10.1111/febs.17265
  3. Afonine, P. V., et al. (2024). Accounting for nonuniformity of bulk‐solvent: A mosaic model. doi: 10.1002/pro.4909
  4. Akbari, S., et al. (2024). Novel bio-based branched unsaturated polyester resins for high-temperature applications. J. Polym. Environ. doi: 10.1007/s10924-023-03112-5
  5. Alberga, D., et al. (2024). DeLA-DrugSelf: Empowering multi-objective de novo design through SELFIES molecular representation. Comput. Biol. Med. doi: 10.1016/j.compbiomed.2024.108486
  6. Altincekic, N., et al. (2024). Targeting the Main Protease (Mpro, nsp5) by Growth of Fragment Scaffolds Exploiting Structure-Based Methodologies. ACS Chem. Biol. doi: 10.1021/acschembio.3c00720
  7. Anastasina, M., et al. (2024). The structure of immature tick-borne encephalitis virus supports the collapse model of flavivirus maturation. Sci. Adv. doi: 10.1126/sciadv.adl1888
  8. Arragain, B., et al. (2024). Structures of influenza A and B replication complexes give insight into avian to human host adaptation and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase. Nat. Commun. doi: 10.1038/s41467-024-51007-3
  9. Aubrun Fulbert, C., et al. (2024). Nanoscintillator Coating: A Key Parameter That Strongly Impacts Internalization, Biocompatibility, and Therapeutic Efficacy in Pancreatic Cancer Models. doi: 10.1002/smsc.202400041
  10. Avanzato, V., et al. (2024). A monoclonal antibody targeting the Nipah virus fusion glycoprotein apex imparts protection from disease. J. Virol. doi: 10.1128/jvi.00638-24
  11. Avanzato, V. A., et al. (2024). A monoclonal antibody targeting the Nipah virus fusion glycoprotein apex imparts protection from disease. J. Virol. doi: 10.1128/jvi.00638-24
  12. Avello, M. G., et al. (2024). Ni-NHC Nanoparticles in Micelles as an Effective and Reusable Catalyst for Hydrogenations and Reductive-Aminations in Water. ACS Sustain. Chem. Eng. doi: 10.1021/acssuschemeng.4c01636
  13. Bahena-Ceron, R., et al. (2024). RlmQ: a newly discovered rRNA modification enzyme bridging RNA modification and virulence traits in Staphylococcus aureus. RNA. doi: 10.1261/rna.079850.123
  14. Bahena-Ceron, R., et al. (2024). RlmQ: a newly discovered rRNA modification enzyme bridging RNA modification and virulence traits in. RNA. doi: 10.1261/rna.079850.123
  15. Bally, I., et al. (2024). Revisiting the interaction between complement lectin pathway protease MASP-2 and SARS-CoV-2 nucleoprotein. Front. Immunol. doi: 10.3389/fimmu.2024.1419165
  16. Baranova, I., et al. (2024). Hemoglobin-PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications. J. Phys. Chem. B. doi: 10.1021/acs.jpcb.4c03003
  17. Bargagna, B., et al. (2024). Defects in the Maturation of Mitochondrial Iron-Sulfur Proteins: Biophysical Investigation of the MMDS3 Causing Gly104Cys Variant of IBA57. Int. J. Mol. Sci. doi: 10.3390/ijms251910466
  18. Bárta, J., et al. (2024). Proteomic Profiles of Whole Seeds, Hulls, and Dehulled Seeds of Two Industrial Hemp (Cannabis sativa L.) Cultivars. Plants-Basel. doi: 10.3390/plants13010111
  19. Bartošík, V., et al. (2024). Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways. J. Biol. Chem. doi: 10.1016/j.jbc.2024.107551
  20. Batisse, C., et al. (2024). Integrase-LEDGF/p75 complex triggers the formation of biomolecular condensates that modulate HIV-1 integration efficiency in vitro. J. Biol. Chem. doi: 10.1016/j.jbc.2024.107374
  21. Bauda, E., et al. (2024). Ultrastructure of macromolecular assemblies contributing to bacterial spore resistance revealed by in situ cryo-electron tomography. Nat. Commun. doi: 10.1038/s41467-024-45770-6
  22. Baudoin, M., et al. (2024). To click or not to click for short pulse-labeling of the bacterial cell wall. RSC Adv. doi: 10.1039/d4ra04945d
  23. Bazayeva, M., et al. (2024). A database overview of metal‐coordination distances in metalloproteins. Acta Crystallogr D Struct Biol. doi: 10.1107/S2059798324003152
  24. Beernink, P., et al. (2024). Gonococcal Mimitope Vaccine Candidate Forms a Beta-Hairpin Turn and Binds Hydrophobically to a Therapeutic Monoclonal Antibody. JACS Au. doi: 10.1021/jacsau.4c00359
  25. Benallal, K., et al. (2024). Phlebotomine sand fly survey, blood meal source identification, and description of Sergentomyia imihra n. sp. in the central Sahara of Algeria. Parasites Vectors. doi: 10.1186/s13071-024-06542-9
  26. Benesova, I., et al. (2024). N-glycan profiling of tissue samples to aid breast cancer subtyping. Sci. Rep. doi: 10.1038/s41598-023-51021-3
  27. Bessonne, M., et al. (2024). Antiviral activity of intracellular nanobodies targeting the influenza virus RNA-polymerase core. PLoS Pathog. doi: 10.1371/journal.ppat.1011642
  28. Bielková, Z., et al. (2024). Zero-field splitting in tetracoordinate Co(II) complexes containing heterocyclic aromatic ligands. J. Mol. Struct. doi: 10.1016/j.molstruc.2023.136667
  29. Bigo-Simon, A., et al. (2024). 3D Cryo-Electron Microscopy Reveals the Structure of a 3-Fluorenylmethyloxycarbonyl Zipper Motif Ensuring the Self-Assembly of Tripeptide Nanofibers. ACS Nano. doi: 10.1021/acsnano.4c08043
  30. Boclinville, A., et al. (2024). Interaction studies between human papillomavirus virus-like particles and laminin 332 by affinity capillary electrophoresis assisted by bio-layer interferometry. Talanta. doi: 10.1016/j.talanta.2023.125602
  31. Borowska, A., et al. (2024). Structural basis of the obligatory exchange mode of human neutral amino acid transporter ASCT2. Nat. Commun. doi: 10.1038/s41467-024-50888-8
  32. Bos, J., et al. (2024). Control of Bilayer Transport through a Photoswitchable Membrane-Stiffening Agent. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202420232
  33. Botova, M., et al. (2024). A specific phosphorylation-dependent conformational switch in SARS-CoV-2 nucleocapsid protein inhibits RNA binding. Sci. Adv. doi: 10.1126/sciadv.aax2323
  34. Bourgeais, M., et al. (2024). Chemo-enzymatic synthesis of tetrasaccharide linker peptides to study the divergent step in glycosaminoglycan biosynthesis. Glycobiology. doi: 10.1093/glycob/cwae016
  35. Bozděchová, L., et al. (2024). Optimizing ChIRP-MS for Comprehensive Profiling of RNA-Protein Interactions in Arabidopsis thaliana: A Telomerase RNA Case Study. Plants. doi: 10.3390/plants13060850
  36. Brezovská, B., et al. (2024). MoaB2, a newly identified transcription factor, binds to σA in Mycobacterium smegmatis. J. Bacteriol. doi: 10.1128/jb.00066-24
  37. Brillet, K., et al. (2024). Characterization of SLA RNA promoter from dengue virus and its interaction with the viral non-structural NS5 protein. Biochimie. doi: 10.1016/j.biochi.2024.02.005
  38. Brutscher, B. (2024). PRESERVE: adding variable flip-angle excitation to transverse relaxation-optimized NMR spectroscopy. Magn. Reson. doi: 10.5194/mr-5-131-2024
  39. Bugajova, M., et al. (2024). Glutamine and serum starvation alters the ATP production, oxidative stress, and abundance of mitochondrial RNAs in extracellular vesicles produced by cancer cells. Sci Rep. doi: 10.1038/s41598-024-73943-2
  40. Bulvas, O., et al. (2024). Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase. Nat. Commun. doi: 10.1038/s41467-024-50933-6
  41. Burmeister, W. P., et al. (2024). Structure and flexibility of the DNA polymerase holoenzyme of vaccinia virus. PLOS Path. doi: 10.1371/journal.ppat.1011652
  42. Busselez, J., et al. (2024). Remodelling of Rea1 linker domain drives the removal of assembly factors from pre-ribosomal particles. Nat. Commun. doi: 10.1038/s41467-024-54698-w
  43. Cai, Q., et al. (2024). LSD1 inhibition circumvents glucocorticoid-induced muscle wasting of male mice. Nat. Commun. doi: 10.1038/s41467-024-47846-9
  44. Cammarata, G., et al. (2024). The TOG5 domain of CKAP5 is required to interact with F-actin and promote microtubule advancement in neurons. Mol. Biol. Cell. doi: 10.1091/mbc.E24-05-0202
  45. Cassani, M., et al. (2024). YAP signaling regulates the cellular uptake and therapeutic effect of nanoparticles. Adv. Sci. doi: 10.1002/advs.202302965
  46. Catalano, F., et al. (2024). Conformational and dynamic properties of the KH1 domain of FMRP and its fragile X syndrome linked G266E variant. BBA-Proteins Proteomics. doi: 10.1016/j.bbapap.2024.141019
  47. Chakkarapani, L. D., et al. (2024). Selective and sensitive determination of phenolic compounds using carbon screen printing electrodes modified with reduced graphene oxide and silver nanoparticles. Appl. Mater. Today. doi: 10.1016/j.apmt.2024.102113
  48. Changela, H., et al. (2024). The evolution of organic material on Asteroid 162173 Ryugu and its delivery to Earth. Nat. Commun. doi: 10.1038/s41467-024-50004-w
  49. Chenavier, F., et al. (2024). Influenza a virus antiparallel helical nucleocapsid-like pseudo-atomic structure. Nucleic Acids Res. doi: 10.1093/nar/gkae1211
  50. Chikunova, A., et al. (2024). Conserved proline residues prevent dimerization and aggregation in the β‐lactamase BlaC. Protein Sci. doi: 10.1002/pro.4972
  51. Chvojka, M., et al. (2024). Synthesis of bambusurils with perfluoroalkylthiobenzyl groups as highly potent halide receptors. Org. Chem. Front. doi: 10.1039/d4qo01746c
  52. Clarke, J., et al. (2024). A broadly reactive ultralong bovine antibody that can determine the integrity of foot- and- mouth disease virus capsids. J. Gen. Virol. doi: 10.1099/jgv.0.002032
  53. Coelho, A., et al. (2024). Resonance assignments of cytochrome MtoD from the extracellular electron uptake pathway of sideroxydans lithotrophicus ES-1. Biomol. NMR Assign. doi: 10.1007/s12104-024-10180-8
  54. Cosottini, L., et al. (2024). Cage Architecture and Reactivity are Preserved in Cysteine-Mutated Ferritin. Eur. J. Inorg. Chem. doi: 10.1002/ejic.202400486
  55. Cosottini, L., et al. (2024). Unlocking the Power of Human Ferritin: Enhanced Drug Delivery of Aurothiomalate in A2780 Ovarian Cancer Cells. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202410791
  56. Costanzo, A., et al. (2024). Binding of steroid substrates reveals the key to the productive transition of the cytochrome P450 OleP. Structure. doi: 10.1016/j.str.2024.06.005
  57. Crha, R., et al. (2024). Hiding in plain sight: Complex interaction patterns between Tau and 14-3-3ζ protein variants. Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2024.130802
  58. Czubinski, J., et al. (2024). pH-Dependent oligomerisation of γ-conglutin: A key element to understand its molecular mechanism of action. Food Hydrocolloids. doi: 10.1016/j.foodhyd.2023.109386
  59. Dalwani, S., et al. (2024). Crystallographic fragment binding studies of the Mycobacterium tuberculosis trifunctional enzyme suggest binding pockets for the tails of the acyl-CoA substrates at its active sites and a potential substrate channeling path between them. Acta Crystallogr D Struct Biol. doi: 10.1107/S2059798324006557
  60. Daniel, E., et al. (2024). Managing macromolecular crystallographic data with a laboratory information management system. ACTA Crystallogr D Struct. Biol. doi: 10.1107/S2059798324005680
  61. De Caro, L., et al. (2024). Characterization of Surfactant Spheroidal Micelle Structure for Pharmaceutical Applications: A Novel Analytical Framework. Pharmaceutics doi: 10.3390/pharmaceutics16050604
  62. De Felice, S., et al. (2024). Crystal structure of human serum albumin in complex with megabody reveals unique human and murine cross-reactive binding site. Protein Sci. doi: 10.1002/pro.4887
  63. de Isidro-Gomez, F. P., et al. (2024). A deep learning approach to the automatic detection of alignment errors in cryo-electron tomographic reconstructions. J. Struct. Biol. doi: 10.1016/j.jsb.2023.108056
  64. De Keyser, P., et al. (2024). A nanobody-based microfluidic chip for fast and automated purification of protein complexes. Lab Chip. doi: 10.1039/d4lc00728j
  65. De Meutter, J., et al. (2024). Protein Microarrays for High Throughput Hydrogen/Deuterium Exchange Monitored by FTIR Imaging. Int. J. Mol. Sci. doi: 10.3390/ijms25189989
  66. De, S., et al. (2024). Bio‐Templated Silver Nanopatterns for Photothermal and Antifogging Coatings. Adv. Mater. Interfaces. doi: 10.1002/admi.202300828
  67. Deb, R., et al. (2024). Computational Design of Pore-Forming Peptides with Potent Antimicrobial and Anticancer Activities. J. Med. Chem. doi: 10.1021/acs.jmedchem.4c00912
  68. Degli Esposti, L., et al. (2024). Bioinspire d oriente d calcium phosphate nanocrystal arrays with bactericidal and osteogenic properties. Acta Biomater. doi: 10.1016/j.actbio.2024.08.001
  69. Delaunay, C., et al. (2024). Unprecedented selectivity for homologous lectin targets: differential targeting of the viral receptors L-SIGN and DC-SIGN. Chem. Sci. doi: 10.1039/d4sc02980a
  70. Dhakar, S. S., et al. (2024). High-throughput screening assay for PARP-HPF1 interaction inhibitors to affect DNA damage repair. Sci. Rep. doi: 10.1038/s41598-024-54123-8
  71. Dhillon, A., et al. (2024). Structural insights into the interaction between adenovirus C5 hexon and human lactoferrin. J. Virol. doi: 10.1128/jvi.01576-23
  72. Di Carluccio, C., et al. (2024). Molecular Insights into O-Linked Sialoglycans Recognition by the Siglec-Like SLBR-N (SLBR UB10712) of Streptococcus gordonii. ACS Central Sci. doi: 10.1021/acscentsci.3c01598
  73. Di Nisio, A., et al. (2024). Lipidomic Profile of Human Sperm Membrane Identifies a Clustering of Lipids Associated with Semen Quality and Function. Int. J. Mol. Sci. doi: 10.3390/ijms25010297
  74. Di Pietro, B., et al. (2024). Differential Anti-Inflammatory Effects of Electrostimulation in a Standardized Setting. Int J Mol Sci doi: 10.3390/ijms25189808
  75. Drápela, S., et al. (2024). Pre-existing cell subpopulations in primary prostate cancer tumors display surface fingerprints of docetaxel-resistant cells. Cell. Oncol. doi: 10.1007/s13402-024-00982-2
  76. Drys, M., et al. (2024). Structural Characterization of 6-Halo-6-Deoxycelluloses by Direct-Dissolution Solution-State NMR Spectroscopy. Macromol. Rapid Commun. doi: 10.1002/marc.202300698
  77. Dubiez, E., et al. (2024). Structural basis for competitive binding of productive and degradative co-transcriptional effectors to the nuclear cap-binding complex. Cell Rep. doi: 10.1016/j.celrep.2023.113639
  78. Dupé, S., et al. (2024). Quantum-confined bismuth iodide perovskite nanocrystals in mesoporous matrices. Nanoscale doi: 10.1039/d4nr00430b
  79. Durieux Trouilleton, Q., et al. (2024). Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers. Nat. Commun. doi: 10.1038/s41467-024-46601-4
  80. Dusková, M., et al. (2024). The microbial contaminants of plant-based meat analogues from the retail market. Int. J. Food Microbiol. doi: 10.1016/j.ijfoodmicro.2024.110869
  81. Dusková, M., et al. (2024). The shelf life of cooked sausages with reduced salt content. Acta Vet. BRNO. doi: 10.2754/avb202493010115
  82. Duyvesteyn, H., et al. (2024). Concerted deletions eliminate a neutralizingsupersite in SARS-CoV-2 BA.2.87.1 spike. Structure. doi: 10.1016/j.str.2024.07.020
  83. Dvorák, P., et al. (2024). Synthetically-primed adaptation of Pseudomonas putida to a non-native substrate D-xylose. Nat. Commun. doi: 10.1038/s41467-024-46812-9
  84. El Battioui, K., et al. (2024). In situ captured antibacterial action of membrane-incising peptide lamellae. Nat. Commun. . doi: 10.1038/s41467-024-47708-4
  85. Enebral-Romero, E., et al. (2024). Bismuthene- Tetrahedral DNA nanobioconjugate for virus detection. Biosens. Bioelectron. doi: 10.1016/j.bios.2024.116500
  86. Engilberge, S., et al. (2024). The TR-icOS setup at the ESRF: time-resolved microsecond UV–Vis absorption spectroscopy on protein crystals. Acta Crystallogr D. doi: 10.1107/S2059798323010483
  87. Eronen, V., et al. (2024). Structural insights into ternary immunocomplex formation and cross-reactivity: binding of an anti-immunocomplex FabB12 to Fab220-testosterone complex. FEBS J. doi: 10.1111/febs.17258
  88. Exertier, C., et al. (2024). Sorcin in Cancer Development and Chemotherapeutic Drug Resistance. Cancers. doi: 10.3390/cancers16162810
  89. Facen, E., et al. (2024). Novel, soluble 3-heteroaryl-substituted tanshinone mimics attenuate the inflammatory response in murine macrophages. Sci Rep. doi: 10.1038/s41598-024-73309-8
  90. Faltinek, L., et al. (2024). Bispecific Thio-Linked Disaccharides as Inhibitors of <i>Pseudomonas Aeruginosa</i> Lectins LecA (PA-IL) and LecB (PA-IIL): Dual-Targeting Strategy. Chem.-Eur. J. doi: 10.1002/chem.202403546
  91. Farci, D., et al. (2024). Structural characterization and functional insights into the type II secretion system of the poly-extremophile Deinococcus radiodurans. J. Biol. Chem. doi: 10.1016/j.jbc.2023.105537
  92. Ferrero, D. S., et al. (2024). Structure of the aminoterminal domain of the birnaviral multifunctional VP3 protein and its unexplored critical role. PNAS Nexus doi: 10.1093/pnasnexus/pgae521
  93. Fialova, T., et al. (2024). Light-triggered reactions in a new "light" of nanoparticles engineering. J. Photochem. Photobiol. A-Chem. doi: 10.1016/j.jphotochem.2024.115667
  94. Figueiredo, J., et al. (2024). G-quadruplex ligands in cancer therapy: Progress, challenges, and clinical perspectives. Life Sci. doi: 10.1016/j.lfs.2024.122481
  95. Fioretto, L., et al. (2024). The Janus effect of colloidal self-assembly on the biological response of amphiphilic drugs. Pharmacol. Res. doi: 10.1016/j.phrs.2024.107400
  96. Fiorucci, L., et al. (2024). Are Protein Conformational Ensembles in Agreement with Experimental Data? A Geometrical Interpretation of the Problem. J. Chem Inf. Model. doi: 10.1021/acs.jcim.4c00582
  97. Fischer, B., et al. (2024). Allosteric nanobodies to study the interactions between SOS1 and RAS. Nat. Commun. doi: 10.1038/s41467-024-50349-2
  98. Flood, R. J., et al. (2024). Multivalent Calixarene Complexation of a Designed Pentameric Lectin. Biomacromolecules doi: 10.1021/acs.biomac.3c01280
  99. Fojtík, L., et al. (2024). Structural Characterization of Monoclonal Antibodies and Epitope Mapping by FFAP Footprinting. Anal. Chem. doi: 10.1021/acs.analchem.3c04161
  100. Franek, M., et al. (2024). Histone Chaperone Deficiency in Arabidopsis Plants Triggers Adaptive Epigenetic Changes in Histone Variants and Modifications. Mol. Cell. Proteomics. doi: 10.1016/j.mcpro.2024.100795
  101. Frohlich, J., et al. (2024). Epigenetic and transcriptional control of adipocyte function by centenarian-associated SIRT6 N308K/A313S mutant. Clin Epigenetics doi: 10.1186/s13148-024-01710-1
  102. Fulbert, C. A., et al. (2024). Nanoscintillator Coating: A Key Parameter That Strongly Impacts Internalization, Biocompatibility, and Therapeutic Efficacy in Pancreatic Cancer Models. Small Sci. doi: 10.1002/smsc.202400041
  103. Gáborová, M., et al. (2024). Diterpenes Isolated from Three Different Plectranthus Sensu Lato Species and Their Antiproliferative Activities against Gynecological and Glioblastoma Cancer Cells. ACS Omega. doi: 10.1021/acsomega.4c00800
  104. Gabriel, F., et al. (2024). Structural basis of thiamine transport and drug recognition by SLC19A3. Nat. Commun. doi: 10.1038/s41467-024-52872-8
  105. Gamboa, J., et al. (2024). Aptamers for the Delivery of Plant-Based Compounds: A Review. Pharmaceutics doi: 10.3390/pharmaceutics16040541
  106. Gao, Y., et al. (2024). Cryo-EM structure of cytochrome bo3 quinol oxidase assembled in peptidiscs reveals an “open” conformation for potential ubiquinone-8 release. Biochim Biophys Acta Bioenerg doi: 10.1016/j.bbabio.2024.149045
  107. Garcia-Fernandez, D., et al. (2024). A "signal off-on" fluorescence bioassay based on 2D-MoS2-tetrahedral DNA bioconjugate for rapid virus detection. Talanta doi: 10.1016/j.talanta.2023.125497
  108. Garcia-Vello, P., et al. (2024). The lipooligosaccharide of the gut symbiont Akkermansia muciniphila exhibits a remarkable structure and TLR signaling capacity. Nat. Commun. doi: 10.1038/s41467-024-52683-x
  109. Garehbaghi, S., et al. (2024). An enzyme cascade biosensor based on multiwalled carbon nanotube-RuO2 nanocomposite for selective amperometric determination of lactose in milk samples. Microchem J. doi: 10.1016/j.microc.2024.111138
  110. Gedeon, A., et al. (2024). Molecular mechanism of a triazole-containing inhibitor of Mycobacterium tuberculosis DNA gyrase. iScience. doi: 10.1016/j.isci.2024.110967
  111. Gemander, N., et al. (2024). Hybrid Immunity Overcomes Defective Immune Response to COVID-19 Vaccination in Kidney Transplant Recipients. Kidney Int. Rep. doi: 10.1016/j.ekir.2023.12.008
  112. Ghini, V. (2024). Cell Metabolomics to Guide the Design of Metal-Based Compounds. Inorganics. doi: 10.3390/inorganics12060168
  113. Ghini, V., et al. (2024). NMR Metabolomics of Primary Ovarian Cancer Cells in Comparison to Established Cisplatin-Resistant and -Sensitive Cell Lines. Cells. doi: 10.3390/cells13080661
  114. Gigli, L., et al. (2024). Machine Learning-Enhanced Quantum Chemistry-Assisted Refinement of the Active Site Structure of Metalloproteins. Inorg. Chem. doi: 10.1021/acs.inorgchem.4c01274
  115. Giraud, A., et al. (2024). Enabling site-specific NMR investigations of therapeutic Fab using a cell-free based isotopic labeling approach: application to anti-LAMP1 Fab. J. Biomol. NMR. doi: 10.1007/s10858-023-00433-4
  116. Gómez-Bouzó, U., et al. (2024). Design, Synthesis, and Biological Evaluation of New Type of Gemini Analogues with a Cyclopropane Moiety in Their Side Chain. J. Med. Chem. doi: 10.1021/acs.jmedchem.4c00854
  117. Graziani, C., et al. (2024). The Z isomer of pyridoxilidenerhodanine 5′-phosphate is an efficient inhibitor of human pyridoxine 5′-phosphate oxidase, a crucial enzyme in vitamin B6 salvage pathway and a potential chemotherapeutic target. FEBS J. doi: 10.1111/febs.17274
  118. Grifagni, D., et al. (2024). Biochemical and cellular characterization of the CISD3 protein: Molecular bases of cluster release and destabilizing effects of nitric oxide. J. Biol. Chem. doi: 10.1016/j.jbc.2024.105745
  119. Griffith-Jones, S., et al. (2024). Structural basis for RAD18 regulation by MAGEA4 and its implications for RING ubiquitin ligase binding by MAGE family proteins. EMBO J. doi: 10.1038/s44318-024-00058-9
  120. Guérin, M., et al. (2024). Production, purification, and quality assessment of borrelial proteins CspZ from Borrelia burgdorferi and FhbA from Borrelia hermsii. Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-024-13195-2
  121. Gutiérrez-Gálvez, L., et al. (2024). Free PCR virus detection via few-layer bismuthene and tetrahedral DNA nanostructured assemblies. Talanta. doi: 10.1016/j.talanta.2023.125405
  122. Hausnerová, V. V., et al. (2024). RIP-seq reveals RNAs that interact with RNA polymerase and primary sigma factors in bacteria. Nucleic Acids Res. doi: 10.1093/nar/gkae081
  123. Havlickova, P., et al. (2024). Practical courses on advanced methods in macromolecular crystallization: 20 years of history and future perspectives. J. Appl. Crystallogr. doi: 10.1107/S1600576724007106
  124. Helabad, M., et al. (2024). Integrative determination of atomic structure of mutant huntingtin exon 1 fibrils implicated in Huntington disease. Nat. Commun. doi: 10.1038/s41467-024-55062-8
  125. Henderikx, R. J., et al. (2024). VitroJet: new features and case studies. Acta Crystallogr D Struct Biol. . doi: 10.1107/S2059798324001852
  126. Herrera‐González, I., et al. (2024). High‐Mannose Oligosaccharide Hemimimetics that Recapitulate the Conformation and Binding Mode to Concanavalin A, DC‐SIGN and Langerin. Chemistry. doi: 10.1002/chem.202303041
  127. Hillier, J., et al. (2024). Structural insights into Frizzled3 through nanobody modulators. Nat. Commun. doi: 10.1038/s41467-024-51451-1
  128. Hoffmann, G., et al. (2024). Targeting a microbiota Wolbachian aminoacyl-tRNA synthetase to block its pathogenic host. Sci Adv doi: 10.1126/sciadv.ado1453
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2013

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  9. Bertini, I., et al. (2013). Formation Kinetics and Structural Features of Beta-Amyloid Aggregates by Sedimented Solute NMR. Chembiochem, 14(14), 1891-1897. doi:10.1002/cbic.201300141
  10. Bertini, I., et al. (2013). SedNMR: On the Edge between Solution and Solid-State NMR. Accounts of Chemical Research, 46(9), 2059-2069. doi:10.1021/ar300342f
  11. Bhaumik, A., et al. (2013). NMR crystallography on paramagnetic systems: solved and open issues. Crystengcomm, 15(43), 8639-8656. doi:10.1039/c3ce41485j
  12. Bieniossek, C., et al. (2013). The architecture of human general transcription factor TFIID core complex. Nature, 493(7434), 699-702. doi:10.1038/nature11791
  13. Breyton, C., et al. (2013). Assessing the Conformational Changes of pb5, the Receptor-binding Protein of Phage T5, upon Binding to Its Escherichia coli Receptor FhuA. Journal of Biological Chemistry, 288(42), 30763-30772. doi:10.1074/jbc.M113.501536
  14. Cerofolini, L., et al. (2013). Examination of Matrix Metalloproteinase-1 in Solution A PREFERENCE FOR THE PRE-COLLAGENOLYSIS STATE. Journal of Biological Chemistry, 288(42), 30659-30671. doi:10.1074/jbc.M113.477240
  15. de la Rosa-Trevin, J. M., et al. (2013). Xmipp 3.0: An improved software suite for image processing in electron microscopy. Journal of Structural Biology, 184(2), 321-328. doi:10.1016/j.jsb.2013.09.015
  16. Delvecchio, M., et al. (2013). Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation. Nature Structural & Molecular Biology, 20(9), 1040-+. doi:10.1038/nsmb.2642
  17. Dian, C., et al. (2013). Structure of a Truncation Mutant of the Nuclear Export Factor CRM1 Provides Insights into the Auto-Inhibitory Role of Its C Terminal Helix. Structure, 21(8), 1338-1349. doi:10.1016/j.str.2013.06.003
  18. Duan, C. X., et al. (2013). Structural Evidence for a Two-Regime Photobleaching Mechanism in a Reversibly Switchable Fluorescent Protein. Journal of the American Chemical Society, 135(42), 15841-15850. doi:10.1021/ja406860e
  19. Durand, A., et al. (2013). Structure, assembly and dynamics of macromolecular complexes by single particle cryo-electron microscopy. Journal of Nanobiotechnology, 11. doi:10.1186/1477-3155-11-s1-s4
  20. Duval, M., et al. (2013). Escherichia coli Ribosomal Protein S1 Unfolds Structured mRNAs Onto the Ribosome for Active Translation Initiation. Plos Biology, 11(12). doi:10.1371/journal.pbio.1001731
  21. Fallecker, C., et al. (2013). Structural and functional characterization of the single-chain Fv fragment from a unique HCV E1E2-specific monoclonal antibody. Febs Letters, 587(20), 3335-3340. doi:10.1016/j.febslet.2013.07.057
  22. Favini-Stabile, S., et al. (2013). MreB and MurG as scaffolds for the cytoplasmic steps of peptidoglycan biosynthesis. Environmental Microbiology, 15(12), 3218-3228. doi:10.1111/1462-2920.12171
  23. Ferella, L., et al. (2013). SedNMR: a web tool for optimizing sedimentation of macromolecular solutes for SSNMR. Journal of Biomolecular Nmr, 57(4), 319-326. doi:10.1007/s10858-013-9795-x
  24. Fragai, M., et al. (2013). Practical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins. Journal of Biomolecular Nmr, 57(2), 155-166. doi:10.1007/s10858-013-9776-0
  25. Hanhijarvi, K. J., et al. (2013). DNA Ejection from an Archaeal Virus-A Single-Molecule Approach. Biophysical Journal, 104(10), 2264-2272. doi:10.1016/j.bpj.2013.03.061
  26. Le Rouzic, E., et al. (2013). Dual inhibition of HIV-1 replication by integrase-LEDGF allosteric inhibitors is predominant at the post-integration stage. Retrovirology, 10. doi:10.1186/1742-4690-10-144
  27. Le Roy, A., et al. (2013). Sedimentation velocity analytical ultracentrifugation in hydrogenated and deuterated solvents for the characterization of membrane proteins. Methods Mol Biol, 1033, 219-251. doi:10.1007/978-1-62703-487-6_15
  28. Luchinat, C., et al. (2013). Water and Protein Dynamics in Sedimented Systems: A Relaxometric Investigation. Chemphyschem, 14(13), 3156-3161. doi:10.1002/cphc.201300167
  29. Maillot, B., et al. (2013). Structural and Functional Role of INI1 and LEDGF in the HIV-1 Preintegration Complex. Plos One, 8(4). doi:10.1371/journal.pone.0060734
  30. Marabini, R., et al. (2013). On the development of three new tools for organizing and sharing information in three-dimensional electron microscopy. Acta Crystallographica Section D-Biological Crystallography, 69, 695-700. doi:10.1107/s0907444913007038
  31. Mas, G., et al. (2013). Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins. Journal of Biomolecular Nmr, 57(3), 251-262. doi:10.1007/s10858-013-9785-z
  32. Meyer, S., et al. (2013). Multi-Host Expression System for Recombinant Production of Challenging Proteins. Plos One, 8(7). doi:10.1371/journal.pone.0068674
  33. Mori, M., et al. (2013). Discovery of a New Class of Potent MMP Inhibitors by Structure-Based Optimization of the Arylsulfonamide Scaffold. Acs Medicinal Chemistry Letters, 4(6), 565-569. doi:10.1021/ml300446a
  34. Neves, D., et al. (2013). Structure of Internalin InIK from the Human Pathogen Listeria monocytogenes. Journal of Molecular Biology, 425(22), 4520-4529. doi:10.1016/j.jmb.2013.08.010
  35. Noirclerc-Savoye, M., et al. (2013). Reconstitution of Membrane Protein Complexes Involved in Pneumococcal Septal Cell Wall Assembly. Plos One, 8(9). doi:10.1371/journal.pone.0075522
  36. Nozach, H., et al. (2013). High throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E. coli. Microbial Cell Factories, 12. doi:10.1186/1475-2859-12-37
  37. Papillon, J., et al. (2013). Structural insight into negative DNA supercoiling by DNA gyrase, a bacterial type 2A DNA topoisomerase. Nucleic Acids Research, 41(16), 7815-7827. doi:10.1093/nar/gkt560
  38. Pastor-Flores, D., et al. (2013). PIF-Pocket as a Target for C. albicans Pkh Selective Inhibitors. Acs Chemical Biology, 8(10), 2283-2292. doi:10.1021/cb400452z
  39. Peralta, B., et al. (2013). Mechanism of Membranous Tunnelling Nanotube Formation in Viral Genome Delivery. Plos Biology, 11(9). doi:10.1371/journal.pbio.1001667
  40. Petoukhov, M. V., et al. (2013). Reconstruction of Quaternary Structure from X-ray Scattering by Equilibrium Mixtures of Biological Macromolecules. Biochemistry, 52(39), 6844-6855. doi:10.1021/bi400731u
  41. Pietila, M. K., et al. (2013). Modified coat protein forms the flexible spindle-shaped virion of haloarchaeal virus His1. Environmental Microbiology, 15(6), 1674-1686. doi:10.1111/1462-2920.12030
  42. Pietila, M. K., et al. (2013). Insights into Head-Tailed Viruses Infecting Extremely Halophilic Archaea. Journal of Virology, 87(6), 3248-3260. doi:10.1128/jvi.03397-12
  43. Pietila, M. K., et al. (2013). Structure of the archaeal head-tailed virus HSTV-1 completes the HK97 fold story. Proceedings of the National Academy of Sciences of the United States of America, 110(26), 10604-10609. doi:10.1073/pnas.1303047110
  44. Ravantti, J., et al. (2013). Automatic comparison and classification of protein structures. Journal of Structural Biology, 183(1), 47-56. doi:10.1016/j.jsb.2013.05.007
  45. Ravera, E., et al. (2013). Dynamic Nuclear Polarization of Sedimented Solutes. Journal of the American Chemical Society, 135(5), 1641-1644. doi:10.1021/ja312553b
  46. Ravera, E., et al. (2013). Experimental Determination of Microsecond Reorientation Correlation Times in Protein Solutions. Journal of Physical Chemistry B, 117(13), 3548-3553. doi:10.1021/jp312561f
  47. Rennella, E., et al. (2013). Oligomeric States along the Folding Pathways of beta 2-Microglobulin: Kinetics, Thermodynamics, and Structure. Journal of Molecular Biology, 425(15), 2722-2736. doi:10.1016/j.jmb.2013.04.028
  48. Rissanen, I., et al. (2013). Bacteriophage P23-77 Capsid Protein Structures Reveal the Archetype of an Ancient Branch from a Major Virus Lineage. Structure, 21(5), 718-726. doi:10.1016/j.str.2013.02.026
  49. Rousseau, A., et al. (2013). TRAF4 Is a Novel Phosphoinositide-Binding Protein Modulating Tight Junctions and Favoring Cell Migration. Plos Biology, 11(12). doi:10.1371/journal.pbio.1001726
  50. Sencilo, A., et al. (2013). Snapshot of haloarchaeal tailed virus genomes. Rna Biology, 10(5), 803-816. doi:10.4161/rna.24045
  51. Signor, L., et al. (2013). Matrix-assisted Laser Desorption/Ionization Time of Flight (MALDI-TOF) Mass Spectrometric Analysis of Intact Proteins Larger than 100 kDa. Jove-Journal of Visualized Experiments(79). doi:10.3791/50635
  52. Simonetti, A., et al. (2013). Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor. Proceedings of the National Academy of Sciences of the United States of America, 110(39), 15656-15661. doi:10.1073/pnas.1309578110
  53. Simonetti, A., et al. (2013). Structure of the protein core of translation initiation factor 2 in apo, GTP-bound and GDP-bound forms. Acta Crystallographica Section D-Biological Crystallography, 69, 925-933. doi:10.1107/s0907444913006422
  54. Sun, X. Y., et al. (2013). Rescue of Maturation Off-Pathway Products in the Assembly of Pseudomonas Phage phi 6. Journal of Virology, 87(24), 13279-13286. doi:10.1128/jvi.02285-13
  55. Takacs, M., et al. (2013). The Asymmetric Binding of PGC-1 alpha to the ERR alpha and ERR gamma Nuclear Receptor Homodimers Involves a Similar Recognition Mechanism. Plos One, 8(7). doi:10.1371/journal.pone.0067810
  56. Urzhumtsev, A., et al. (2013). TLS from fundamentals to practice. Crystallography Reviews, 19(4), 230-270. doi:10.1080/0889311x.2013.835806
  57. Urzhumtseva, L., et al. (2013). On effective and optical resolutions of diffraction data sets. Acta Crystallographica Section D-Biological Crystallography, 69, 1921-1934. doi:10.1107/s0907444913016673
  58. Vitale, R., et al. (2013). Lipid fingerprints of intact viruses by MALDI-TOF/mass spectrometry. Biochimica Et Biophysica Acta-Molecular and Cell Biology of Lipids, 1831(4), 872-879. doi:10.1016/j.bbalip.2013.01.011
  59. Zanier, K., et al. (2013). Structural basis for hijacking of cellular LxxLL motifs by papillomavirus E6 oncoproteins. Science, 339(6120), 694-698. doi:10.1126/science.1229934
  60. Zapun, A., et al. (2013). In vitro Reconstitution of Peptidoglycan Assembly from the Gram-Positive Pathogen Streptococcus pneumoniae. Acs Chemical Biology, 8(12), 2688-2696. doi:10.1021/cb400575t

2012

  1. Aalto, A. P., et al. (2012). Snapshot of virus evolution in hypersaline environments from the characterization of a membrane-containing Salisaeta icosahedral phage 1. Proceedings of the National Academy of Sciences of the United States of America, 109(18), 7079-7084. doi:10.1073/pnas.1120174109
  2. Bertini, I., et al. (2012). On the use of ultracentrifugal devices for sedimented solute NMR. Journal of Biomolecular Nmr, 54(2), 123-127. doi:10.1007/s10858-012-9657-y
  3. Bieniossek, C., et al. (2012). MultiBac: expanding the research toolbox for multiprotein complexes. Trends in Biochemical Sciences, 37(2), 49-57. doi:10.1016/j.tibs.2011.10.005
  4. Burkhardt, J., et al. (2012). Unusual N-terminal alpha alpha beta alpha beta beta alpha Fold of PilQ from Thermus thermophilus Mediates Ring Formation and Is Essential for Piliation. Journal of Biological Chemistry, 287(11), 8484-8494. doi:10.1074/jbc.M111.334912
  5. Busschots, K., et al. (2012). Substrate-Selective Inhibition of Protein Kinase PDK1 by Small Compounds that Bind to the PIF-Pocket Allosteric Docking Site. Chemistry & Biology, 19(9), 1152-1163. doi:10.1016/j.chembiol.2012.07.017
  6. Jaakkola, S. T., et al. (2012). Closely Related Archaeal Haloarcula hispanica Icosahedral Viruses HHIV-2 and SH1 Have Nonhomologous Genes Encoding Host Recognition Functions. Journal of Virology, 86(9), 4734-4742. doi:10.1128/jvi.06666-11
  7. Kandiba, L., et al. (2012). Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid. Molecular Microbiology, 84(3), 578-593. doi:10.1111/j.1365-2958.2012.08045.x
  8. Kliefoth, M., et al. (2012). Genetic analysis of MA4079, an aldehyde dehydrogenase homolog, in Methanosarcina acetivorans. Archives of Microbiology, 194(2), 75-85. doi:10.1007/s00203-011-0727-4
  9. Oksanen, H. M., et al. (2012). Monolithic ion exchange chromatographic methods for virus purification. Virology, 434(2), 271-277. doi:10.1016/j.virol.2012.09.019
  10. Perez, A. B., et al. (2012). Extraction of Glomalin and Associated Compounds with Two Chemical Solutions in Cultivated Tepetates of Mexico. Communications in Soil Science and Plant Analysis, 43(1-2), 28-35. doi:10.1080/00103624.2012.631403
  11. Ruskamo, S., et al. (2012). The C-terminal rod 2 fragment of filamin A forms a compact structure that can be extended. Biochemical Journal, 446, 261-269. doi:10.1042/bj20120361
  12. Senčilo, A., et al. (2012). Related haloarchaeal pleomorphic viruses contain different genome types. Nucleic Acids Research, 40(12), 5523-5534. doi:10.1093/nar/gks215
  13. Sun, X. Y., et al. (2012). Probing, by Self-Assembly, the Number of Potential Binding Sites for Minor Protein Subunits in the Procapsid of Double-Stranded RNA Bacteriophage phi 6. Journal of Virology, 86(22), 12208-12216. doi:10.1128/jvi.01505-12
  14. Thielmann, Y., et al. (2012). The ESFRI Instruct Core Centre Frankfurt: automated high-throughput crystallization suited for membrane proteins and more. J Struct Funct Genomics, 13(2), 63-69. doi:10.1007/s10969-011-9118-y
  15. Trowitzsch, S., et al. (2012). MultiBac complexomics. Expert Review of Proteomics, 9(4), 363-373. doi:10.1586/epr.12.32 

2011

  1. Banci, L., et al. (2011). NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Diemutase. Journal of the American Chemical Society, 133(2), 345-349. doi:10.1021/ja1069689
  2. Bertini, I., et al. (2011). High-Resolution Characterization of Intrinsic Disorder in Proteins: Expanding the Suite of C-13-Detected NMR Spectroscopy Experiments to Determine Key Observables. Chembiochem, 12(15), 2347-2352. doi:10.1002/cbic.201100406
  3. Bertini, I., et al. (2011). C-13 Direct-Detection Biomolecular NMR Spectroscopy in Living Cells. Angewandte Chemie-International Edition, 50(10), 2339-2341. doi:10.1002/anie.201006636
  4. Bertini, I., et al. (2011). A New Structural Model of A beta(40) Fibrils. Journal of the American Chemical Society, 133(40), 16013-16022. doi:10.1021/ja2035859
  5. Daniel, E., et al. (2011). xtalPiMS: A PiMS-based web application for the management and monitoring of crystallization trials. Journal of Structural Biology, 175(2), 230-235. doi:10.1016/j.jsb.2011.05.008
  6. Hedderich, T., et al. (2011). PICKScreens, A New Database for the Comparison of Crystallization Screens for Biological Macromolecules. Crystal Growth & Design, 11(2), 488-491. doi:10.1021/cg101267n
  7. Imasaki, T., et al. (2011). Architecture of the Mediator head module. Nature, 475(7355), 240-U245. doi:10.1038/nature10162
  8. Morris, C., et al. (2011). The Protein Information Management System (PiMS): a generic tool for any structural biology research laboratory. Acta Crystallographica Section D-Biological Crystallography, 67, 249-260. doi:10.1107/s0907444911007943
  9. Perrakis, A., et al. (2011). From SPINE to SPINE-2 complexes and beyond. J Struct Biol, 175(2), 105. doi:10.1016/j.jsb.2011.05.013
  10. Popoff, V., et al. (2011). Several ADP-ribosylation Factor (Arf) Isoforms Support COPI Vesicle Formation. Journal of Biological Chemistry, 286(41), 35634-35642. doi:10.1074/jbc.M111.261800
  11. Praper, T., et al. (2011). Perforin activity at membranes leads to invaginations and vesicle formation. Proceedings of the National Academy of Sciences of the United States of America, 108(52), 21016-21021. doi:10.1073/pnas.1107473108
  12. Trowitzsch, S., et al. (2011). Light it up: Highly efficient multigene delivery in mammalian cells. Bioessays, 33(12), 946-955. doi:10.1002/bies.201100109
  13. Vijayachandran, L. S., et al. (2011). Robots, pipelines, polyproteins: Enabling multiprotein expression in prokaryotic and eukaryotic cells. Journal of Structural Biology, 175(2), 198-208. doi:10.1016/j.jsb.2011.03.007
  14. Yumerefendi, H., et al. (2011). Library-based methods for identification of soluble expression constructs. Methods, 55(1), 38-43. doi:10.1016/j.ymeth.2011.06.007
  15. Zhao, Y. G., et al. (2011). Automation of large scale transient protein expression in mammalian cells. Journal of Structural Biology, 175(2), 209-215. doi:10.1016/j.jsb.2011.04.017

2010

  1. Banci, L., et al. (2011). NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Diemutase. Journal of the American Chemical Society, 133(2), 345-349. doi:10.1021/ja1069689
  2. Bertini, I., et al. (2011). High-Resolution Characterization of Intrinsic Disorder in Proteins: Expanding the Suite of C-13-Detected NMR Spectroscopy Experiments to Determine Key Observables. Chembiochem, 12(15), 2347-2352. doi:10.1002/cbic.201100406
  3. Bertini, I., et al. (2011). C-13 Direct-Detection Biomolecular NMR Spectroscopy in Living Cells. Angewandte Chemie-International Edition, 50(10), 2339-2341. doi:10.1002/anie.201006636
  4. Bertini, I., et al. (2011). A New Structural Model of A beta(40) Fibrils. Journal of the American Chemical Society, 133(40), 16013-16022. doi:10.1021/ja2035859
  5. Daniel, E., et al. (2011). xtalPiMS: A PiMS-based web application for the management and monitoring of crystallization trials. Journal of Structural Biology, 175(2), 230-235. doi:10.1016/j.jsb.2011.05.008
  6. Hedderich, T., et al. (2011). PICKScreens, A New Database for the Comparison of Crystallization Screens for Biological Macromolecules. Crystal Growth & Design, 11(2), 488-491. doi:10.1021/cg101267n
  7. Imasaki, T., et al. (2011). Architecture of the Mediator head module. Nature, 475(7355), 240-U245. doi:10.1038/nature10162
  8. Morris, C., et al. (2011). The Protein Information Management System (PiMS): a generic tool for any structural biology research laboratory. Acta Crystallographica Section D-Biological Crystallography, 67, 249-260. doi:10.1107/s0907444911007943
  9. Perrakis, A., et al. (2011). From SPINE to SPINE-2 complexes and beyond. J Struct Biol, 175(2), 105. doi:10.1016/j.jsb.2011.05.013
  10. Popoff, V., et al. (2011). Several ADP-ribosylation Factor (Arf) Isoforms Support COPI Vesicle Formation. Journal of Biological Chemistry, 286(41), 35634-35642. doi:10.1074/jbc.M111.261800
  11. Praper, T., et al. (2011). Perforin activity at membranes leads to invaginations and vesicle formation. Proceedings of the National Academy of Sciences of the United States of America, 108(52), 21016-21021. doi:10.1073/pnas.1107473108
  12. Trowitzsch, S., et al. (2011). Light it up: Highly efficient multigene delivery in mammalian cells. Bioessays, 33(12), 946-955. doi:10.1002/bies.201100109
  13. Vijayachandran, L. S., et al. (2011). Robots, pipelines, polyproteins: Enabling multiprotein expression in prokaryotic and eukaryotic cells. Journal of Structural Biology, 175(2), 198-208. doi:10.1016/j.jsb.2011.03.007
  14. Yumerefendi, H., et al. (2011). Library-based methods for identification of soluble expression constructs. Methods, 55(1), 38-43. doi:10.1016/j.ymeth.2011.06.007
  15. Zhao, Y. G., et al. (2011). Automation of large scale transient protein expression in mammalian cells. Journal of Structural Biology, 175(2), 209-215. doi:10.1016/j.jsb.2011.04.017

2009

  1. Bieniossek, C., et al. (2009). Towards eukaryotic structural complexomics. J Struct Funct Genomics, 10(1), 37-46. doi:10.1007/s10969-008-9047-6
  2. Bieniossek, C., et al. (2009). Automated unrestricted multigene recombineering for multiprotein complex production. Nature Methods, 6(6), 447-U468. doi:10.1038/nmeth.1326
  3. Spadiut, O., et al. (2009). Improving thermostability and catalytic activity of pyranose 2-oxidase     from Trametes multicolor by rational and semi-rational design. Febs Journal, 276(3), 776-792. Doi:10.1111/j.1742-4658.2008.06823.x
 
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