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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. Bahena-Ceron, R., et al. (2024). RlmQ: a newly discovered rRNA modification enzyme bridging RNA modification and virulence traits in. doi: 10.1261/rna.079850.123
  2. 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
  3. 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
  4. 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
  5. Bielkova, Z., et al. (2024). Zero-field splitting in tetracoordinate Co(II) complexes containing heterocyclic aromatic ligands. J Mol Struc. doi: 10.1016/j.molstruc.2023.136667
  6. 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
  7. 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
  8. 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
  9. 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
  10. 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
  11. 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
  12. 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
  13. 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
  14. 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
  15. 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
  16. 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
  17. Durieux Trouilleton, Q., et al. (2024). Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers. doi: 10.1038/s41467-024-46601-4
  18. Dusková, M., et al. (2024). The shelf life of cooked sausages with reduced salt content. Acta Vet. BRNO. doi: 10.2754/avb202493010115
  19. 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
  20. 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
  21. 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
  22. 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
  23. 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
  24. 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
  25. 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
  26. 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
  27. Gutierrez-Galvez, 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
  28. 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
  29. Holler, C. V., et al. (2024). Allosteric changes in protein stability and dynamics as pathogenic mechanism for calmodulin variants not affecting Ca2+coordinating residues. Cell Calcium doi: 10.1016/j.ceca.2023.102831
  30. Honzejkova, K., et al. (2024). The cryo-EM structure of ASK1 reveals an asymmetric architecture allosterically modulated by TRX1. eLife. doi: 10.7554/eLife.95199
  31. Jalencas, X., et al. (2024). Design, quality and validation of the EU-OPENSCREEN fragment library poised to a high-throughput screening collection. RSC Med. Chem. doi: 10.1039/d3md00724c
  32. Janovsky, P., et al. (2024). para-Phenylenediamine Dimer as a Redox-Active Guest for Supramolecular Systems. Chem.-Eur. J. doi: 10.1002/chem.202400535
  33. Kejik, M., et al. (2024). Lewis Acidic Aluminosilicates: Synthesis, 27Al MQ/MAS NMR, and DFT-Calculated 27Al NMR Parameters. Inorg. Chem. doi: 10.1021/acs.inorgchem.3c04035
  34. Kotrbová, A. V., et al. (2024). Proteomic analysis of ascitic extracellular vesicles describes tumour microenvironment and predicts patient survival in ovarian cancer. J. Extracell. Vesicles. doi: 10.1002/jev2.12420
  35. Krischuns, T., et al. (2024). The host RNA polymerase II C-terminal domain is the anchor for replication of the influenza virus genome. Nat Commun doi: 10.1038/s41467-024-45205-2
  36. Kuiper, B. P., et al. (2024). Archaeal virus entry and egress. Microlife doi: 10.1093/femsml/uqad048
  37. Laulumaa, S., et al. (2024). Structure and interactions of the endogenous human Commander complex. Nat. Struct. Mol. Biol. doi: 10.1038/s41594-024-01246-1
  38. Liu, C., et al. (2024). Emerging variants develop total escape from potent monoclonal antibodies induced by BA.4/5 infection. Nat Commun. doi: 10.1038/s41467-024-47393-3
  39. Lopes-Nunes, J., et al. (2024). RNA-based liposomes for oral cancer: From biophysical characterization to biological evaluation. Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2023.129157
  40. Luchinat, E., et al. (2024). Ligand-Based Competition Binding by Real-Time 19F NMR in Human Cells. J Med Chem doi: 10.1021/acs.jmedchem.3c01600
  41. Magri, A., et al. (2024). Effect of active layer-by-layer edible coating on quality, biochemicals, and the antioxidant system in ready-to-eat 'Williams' pear fruit during cold storage. Postharvest Biol. Technol. doi: 10.1016/j.postharvbio.2024.112873
  42. Marrocco, F., et al. (2024). Nose-to-brain selective drug delivery to glioma via ferritin-based nanovectors reduces tumor growth and improves survival rate. Cell Death Dis. doi: 10.1038/s41419-024-06653-2
  43. Mierzwicka, J. M., et al. (2024). Engineering PD-1-targeted small protein variants for in vitro diagnostics and in vivo PET imaging. J. Transl. Med. doi: 10.1186/s12967-024-05210-x
  44. Montserrat-Gomez, M., et al. (2024). PDZome-wide and structural characterization of the PDZ-binding motif of VANGL2. Biochim Biophys Acta Proteins Proteom doi: 10.1016/j.bbapap.2023.140989
  45. Mottola, F., et al. (2024). Genotoxicity Assessment of Quinoin, a Ribosome Inactivating Protein from Quinoa Seeds, in the Teleost Danio rerio. Front. Biosci. doi: 10.31083/j.fbl2902051
  46. Mujawar, T., et al. (2024). A Platform for the Synthesis of Oxidation Products of Bilirubin. J. Am. Chem. Soc. doi: 10.1021/jacs.3c11778
  47. Mycroft-West, C. J., et al. (2024). Structural and mechanistic characterization of bifunctional heparan sulfate N-deacetylase-N-sulfotransferase 1. Nat. Commun. doi: 10.1038/s41467-024-45419-4
  48. Nieto-Fabregat, F., et al. (2024). Molecular recognition of Escherichia coli R1-type core lipooligosaccharide by DC-SIGN. iScience. doi: 10.1016/j.isci.2024.108792
  49. Nieto-Fabregat, F., et al. (2024). Atomic-Level Dissection of DC-SIGN Recognition of Bacteroides vulgatus LPS Epitopes. JACS Au. doi: 10.1021/jacsau.3c00748
  50. Paineau, E., et al. (2024). Nonclassical Growth Mechanism of Double-Walled Metal-Oxide Nanotubes Implying Transient Single-Walled Structures. Small. doi: 10.1002/smll.202308665
  51. Palma, E., et al. (2024). Targeting of G-quadruplex DNA with 99mTc(I)/Re(I) Tricarbonyl Complexes Carrying Pyridostatin Derivatives. Chem.-Eur. J. doi: 10.1002/chem.202400285
  52. Pattipeiluhu, R., et al. (2024). Liquid crystalline inverted lipid phases encapsulating siRNA enhance lipid nanoparticle mediated transfection. Nat. Commun. doi: 10.1038/s41467-024-45666-5
  53. Petit-Hartlein, I., et al. (2024). X-ray structure and enzymatic study of a bacterial NADPH oxidase highlight the activation mechanism of eukaryotic NOX. eLife. doi: 10.7554/eLife.93759
  54. Querci, L., et al. (2024). Paramagnetic Nuclear Magnetic Resonance: The Toolkit. Inorganics. doi: 10.3390/inorganics12010015
  55. Razew, A., et al. (2024). Monitoring Drug-Protein Interactions in the Bacterial Periplasm by Solution Nuclear Magnetic Resonance Spectroscopy. J. Am. Chem. Soc. doi: 10.1021/jacs.4c00604
  56. Ríhová, K., et al. (2024). Caspase-9 Is a Positive Regulator of Osteoblastic Cell Migration Identified by diaPASEF Proteomics. J. Proteome Res. doi: 10.1021/acs.jproteome.3c00641
  57. Sabo, J., et al. (2024). CKAP5 enables formation of persistent actin bundles templated by dynamically instable microtubules. Curr. Biol. doi: 10.1016/j.cub.2023.11.031
  58. Salo, A. M., et al. (2024). Collagen prolyl 4-hydroxylase isoenzymes I and II have sequence specificity towards different X-Pro-Gly triplets. Matrix Biol doi: 10.1016/j.matbio.2023.12.001
  59. Schiavina, M., et al. (2024). Intrinsically disordered proteins studied by NMR spectroscopy. J. Magn. Reson. Open. doi: 10.1016/j.jmro.2023.100143
  60. Shimshoni, E., et al. (2024). Integrated Metabolomics and Proteomics of Symptomatic and Early Presymptomatic States of Colitis. J. Proteome Res. doi: 10.1021/acs.jproteome.3c00860
  61. Smirnova, E., et al. (2024). Binding to nucleosome poises human SIRT6 for histone H3 deacetylation. eLife. doi: 10.7554/eLife.87989
  62. Soualmia, F., et al. (2024). Radical S-Adenosyl-L-Methionine Enzyme PylB: A C-Centered Radical to Convert L-Lysine into (3R)-3-Methyl-D-Ornithine. J. Am. Chem. Soc. doi: 10.1021/jacs.3c03747
  63. Sridhar, S., et al. (2024). Structural enzymology studies with the substrate 3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD. FEBS Open Bio. doi: 10.1002/2211-5463.13786
  64. Svestka, D., et al. (2024). Asymmetric Organocatalyzed Transfer Hydroxymethylation of Isoindolinones Using Formaldehyde Surrogates. Org. Lett. doi: 10.1021/acs.orglett.4c00818
  65. Ujfalusi-Pozsonyi, K., et al. (2024). ATP-dependent conformational dynamics in a photoactivated adenylate cyclase revealed by fluorescence spectroscopy and small-angle X-ray scattering. Commun. Biol. doi: 10.1038/s42003-024-05842-1
  66. Van der Verren, M., et al. (2024). Bifunctional Au-Sn-SiO2 catalysts promote the direct upgrading of glycerol to methyl lactate. Nanoscale. doi: 10.1039/d3nr06518a
  67. Vankova, P., et al. (2024). Insights into the pathogenesis of primary hyperoxaluria type I from the structural dynamics of alanine:glyoxylate aminotransferase variants. FEBS Lett. doi: 10.1002/1873-3468.14800
  68. Vela-Rodriguez, C., et al. (2024). Oligomerization mediated by the D2 domain of DTX3L is critical for DTX3L-PARP9 reading function of mono-ADP-ribosylated androgen receptor. Protein Sci doi: 10.1002/pro.4945
  69. Vernhes, E., et al. (2024). Antigen self-anchoring onto bacteriophage T5 capsid-like particles for vaccine design. npj Vaccines. doi: 10.1038/s41541-023-00798-5
  70. Visková, P., et al. (2024). In-cell NMR suggests that DNA i-motif levels are strongly depleted in living human cells. Nat. Commun. doi: 10.1038/s41467-024-46221-y
  71. Wazir, S., et al. (2024). Discovery of 2-Amide-3-methylester Thiophenes that Target SARS-CoV-2 Mac1 and Repress Coronavirus Replication, Validating Mac1 as an Antiviral Target. J Med Chem doi: 10.1021/acs.jmedchem.3c02451
  72. Zhou, D. M., et al. (2024). The SARS-CoV-2 neutralizing antibody response to SD1 and its evasion by BA.2.86. Nat. Commun. doi: 10.1038/s41467-024-46982-6

2023

  1. Abbas, M., et al. (2023). The unique 3D arrangement of macrophage galactose lectin enables Escherichia coli lipopolysaccharide recognition through two distinct interfaces. PNAS Nexus. doi: 10.1093/pnasnexus/pgad310
  2. Afonine, P. V., et al. (2023). Efficient structure-factor modeling for crystals with multiple components. Acta Crystallogr. Sect. A. doi: 10.1107/s205327332300356x
  3. Akbari, S., et al. (2023). Novel Bio-based Branched Unsaturated Polyester Resins for High-Temperature Applications. J. Polym. Environ. doi: 10.1007/s10924-023-03112-5
  4. Albani, S., et al. (2023). Determination and Kinetic Characterization of a New Potential Inhibitor for AmsI Protein Tyrosine Phosphatase from the Apple Pathogen Erwinia amylovora. Molecules. doi: 10.3390/molecules28237774
  5. Alexander, L. T., et al. (2023). Protein target highlights in CASP15: Analysis of models by structure providers. Proteins. doi: 10.1002/prot.26545
  6. Alvarez, H. A., et al. (2023). Lipid exchange in crystal-confined fatty acid binding proteins: X-ray evidence and molecular dynamics explanation. Proteins. doi: 10.1002/prot.26546
  7. Amstrup, S. K., et al. (2023). Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase. Nat. Commun. doi: 10.1038/s41467-023-36604-y
  8. Arias-Alpizar, G., et al. (2023). Phase-Separated Liposomes Hijack Endogenous Lipoprotein Transport and Metabolism Pathways to Target Subsets of Endothelial Cells In Vivo. Adv. Healthc. Mater. doi: 10.1002/adhm.202202709
  9. Arragain, B., et al. (2023). Structural and functional analysis of the minimal orthomyxovirus-like polymerase of Tilapia Lake Virus from the highly diverged Amnoonviridae family. Nat. Commun. doi: 10.1038/s41467-023-44044-x
  10. Azad, K., et al. (2023). Structural basis of CHMP2A-CHMP3 ESCRT-III polymer assembly and membrane cleavage. Nat. Struct. Mol. Biol. doi: 10.1038/s41594-022-00867-8
  11. Baishya, K., et al. (2023). Bio-AFM exploits enhanced response of human gingival fibroblasts on TiO2 nanotubular substrates with thin TiO2 coatings. Appl. Surf. Sci. Adv. doi: 10.1016/j.apsadv.2023.100459
  12. Banneville, A. S. (2023). Structural and functional characterization of DdrC, a novel DNA damage-induced nucleoid associated protein involved in DNA compaction (vol 50, pg 7680, 2022). Nucleic Acids Res. doi: 10.1093/nar/gkad041
  13. Barchet, C., et al. (2023). Focused classifications and refinements in high-resolution single particle cryo-EM analysis. J. Struct. Biol. doi: 10.1016/j.jsb.2023.108015
  14. Bargagna, B., et al. (2023). Understanding the Molecular Basis of the Multiple Mitochondrial Dysfunctions Syndrome 2: The Disease-Causing His96Arg Mutation of BOLA3. Int. J. Mol. Sci. doi: 10.3390/ijms241411734
  15. Bargagna, B., et al. (2023). Unraveling the mechanism of 4Fe-4S cluster assembly on the N-terminal cluster binding site of NUBP1. Protein Sci. doi: 10.1002/pro.4625
  16. Bayfield, O. W., et al. (2023). Structural atlas of a human gut crassvirus. Nature. doi: 10.1038/s41586-023-06019-2
  17. Becker, L. M., et al. (2023). The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy of Aromatic Residues. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202219314
  18. Beinsteiner, B., et al. (2023). Structural insights into the HNF4 biology. Front. Endocrinol. doi: 10.3389/fendo.2023.1197063
  19. Bellomo, G., et al. (2023). Cerebrospinal fluid lipoproteins inhibit alpha-synuclein aggregation by interacting with oligomeric species in seed amplification assays. Mol. Neurodegener. doi: 10.1186/s13024-023-00613-8
  20. Bertrand, Q., et al. (2023). Biochemical, structural and dynamical characterizations of the lactate dehydrogenase from Selenomonas ruminantium provide information about an intermediate evolutionary step prior to complete allosteric regulation acquisition in the super family of lactate and malate dehydrogenases. J. Struct. Biol. doi: 10.1016/j.jsb.2023.108039
  21. Besson, S., et al. (2023). Stimulation of the immune system by a tumor antigen-bearing adenovirus-inspired VLP allows control of melanoma growth. Mol.Ther.-Methods Clin. Dev. doi: 10.1016/j.omtm.2022.12.003
  22. Bissardon, C., et al. (2023). Intracellular Fate of Sub-Toxic Concentration of Functionalized Selenium Nanoparticles in Aggressive Prostate Cancer Cells. Nanomaterials. doi: 10.3390/nano13232999
  23. Blahut, J., et al. (2023). Optimal control derived sensitivity-enhanced CA-CO mixing sequences for MAS solid-state NMR - Applications in sequential protein backbone assignments. J. Magn. Reson. Open. doi: 10.1016/j.jmro.2023.100122
  24. Boehringer, N., et al. (2023). Genome- and metabolome-guided discovery of marine BamA inhibitors revealed a dedicated darobactin halogenase. Cell Chem. Biol. doi: 10.1016/j.chembiol.2023.06.011
  25. Bonhomme, S., et al. (2023). Architecture of a PKS-NRPS hybrid megaenzyme involved in the biosynthesis of the genotoxin colibactin. Structure. doi: 10.1016/j.str.2023.03.012
  26. Bonnard, D., et al. (2023). Biological and Structural Analyses of New Potent Allosteric Inhibitors of HIV-1 Integrase. Antimicrob. Agents Chemother. doi: 10.1128/aac.00462-23
  27. Brandmeier, J. C., et al. (2023). Digital and Analog Detection of SARS-CoV-2 Nucleocapsid Protein via an Upconversion-Linked Immunosorbent Assay. Anal. Chem. doi: 10.1021/acs.analchem.2c05670
  28. Breine, A., et al. (2023). Bypassing the Need for Cell Permeabilization: Nanobody CDR3 Peptide Improves Binding on Living Bacteria. Bioconjugate Chem. doi: 10.1021/acs.bioconjchem.3c00116
  29. Brunetti, A., et al. (2023). Graphene-Oxide Mediated Chemodivergent Ring-Opening of Cyclobutanols. Chin. J. Chem. doi: 10.1002/cjoc.202200757
  30. Bruno, F., et al. (2023). Sensitivity considerations on denoising series of spectra by singular value decomposition. Magn. Reson. Chem. doi: 10.1002/mrc.5338
  31. Bruno, F., et al. (2023). Spin Label Study of the Orientational Preferences of Lysozyme in a Bioinspired Silica Composite. J. Compos. Sci. doi: 10.3390/jcs7050188
  32. Buchtelova, M., et al. (2023). Insight into peculiar adhesion of cells to plasma-chemically prepared multifunctional "amino-glue" surfaces. Plasma Process Polym. doi: 10.1002/ppap.202200157
  33. Bustad, H. J., et al. (2023). One ring closer to a closure: the crystal structure of the ES3 hydroxymethylbilane synthase intermediate. FEBS J. doi: 10.1111/febs.16982
  34. Calatrava, A., et al. (2023). A survey of the European Open Science Cloud services for expanding the capacity and capabilities of multidisciplinary scientific applications. Comput. Sci. Rev. doi: 10.1016/j.cosrev.2023.100571
  35. Camacho-Zarco, A. R., et al. (2023). Multivalent Dynamic Colocalization of Avian Influenza Polymerase and Nucleoprotein by Intrinsically Disordered ANP32A Reveals the Molecular Basis of Human Adaptation. J. Am. Chem. Soc. doi: 10.1021/jacs.3c06965
  36. Camponeschi, F., et al. (2023). Metal trafficking in the cell: Combining atomic resolution with cellular dimension. FEBS Lett. doi: 10.1002/1873-3468.14524
  37. Carniato, F., et al. (2023). Novel Nanogels Loaded with Mn(II) Chelates as Effective and Biologically Stable MRI Probes. Small. doi: 10.1002/smll.202302868
  38. Cassani, M., et al. (2023). YAP Signaling Regulates the Cellular Uptake and Therapeutic Effect of Nanoparticles. Adv. Sci. doi: 10.1002/advs.202302965
  39. Cavini, I. A., et al. (2023). X-ray structure of the metastable SEPT14-SEPT7 coiled coil reveals a hendecad region crucial for heterodimerization. Acta Crystallogr. D Struct. Biol. doi: 10.1107/s2059798323006514
  40. Cawez, F., et al. (2023). Development of Nanobodies as Theranostic Agents against CMY-2-Like Class C beta-Lactamases. Antimicrob. Agents Chemother. doi: 10.1128/aac.01499-22
  41. Cerofolini, L., et al. (2023). Solid-state NMR - a complementary technique for protein framework characterization. doi: 10.1039/d2cc05725e
  42. Cerofolini, L., et al. (2023). Integration of NMR Spectroscopy in an Analytical Workflow to Evaluate the Effects of Oxidative Stress on Abituzumab: Beyond the Fingerprint of mAbs. Anal. Chem. doi: 10.1021/acs.analchem.3c00317
  43. Cerofolini, L., et al. (2023). Combining Solid-State NMR with Structural and Biophysical Techniques to Design Challenging Protein-Drug Conjugates. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202303202
  44. Chaudhari, A. S., et al. (2023). Genetically encoded non-canonical amino acids reveal asynchronous dark reversion of chromophore, backbone, and side-chains in EL222. Protein Sci. doi: 10.1002/pro.4590
  45. Chenavier, F., et al. (2023). Cryo-EM structure of influenza helical nucleocapsid reveals NP-NP and NP-RNA interactions as a model for the genome encapsidation. Sci. Adv. doi: 10.1126/sciadv.adj9974
  46. Chenthamarakshan, V., et al. (2023). Accelerating drug target inhibitor discovery with a deep generative foundation model. Sci. Adv. doi: 10.1126/sciadv.adg7865
  47. Chmelova, K., et al. (2023). Multimeric structure of a subfamily III haloalkane dehalogenase-like enzyme solved by combination of cryo-EM and x-ray crystallography. Protein Sci. doi: 10.1002/pro.4751
  48. Chocholova, E., et al. (2023). Extraction Protocol for Parallel Analysis of Proteins and DNA from Ancient Teeth and Dental Calculus. J. Proteome Res. doi: 10.1021/acs.jproteome.3c00370
  49. Chvojka, M., et al. (2023). Tuning CH Hydrogen Bond-Based Receptors toward Picomolar Anion Affinity via the Inductive Effect of Distant Substituents. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202318261
  50. Chyba, J., et al. (2023). Nature of NMR Shifts in Paramagnetic Octahedral Ru(III) Complexes with Axial Pyridine-Based Ligands. Inorg. Chem. doi: 10.1021/acs.inorgchem.2c03282
  51. Cisse, A., et al. (2023). Targeting structural flexibility in low density lipoprotein by integrating cryo-electron microscopy and high-speed atomic force microscopy. Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2023.126345
  52. Combes, A., et al. (2023). Mixing versus Polymer Chemistry in the Synthesis of Loaded Polymer Nanoparticles through Nanoprecipitation. Langmuir. doi: 10.1021/acs.langmuir.3c02468
  53. Combes, A., et al. (2023). Mixing versus Polymer Chemistry in the Synthesis of Loaded Polymer Nanoparticles through Nanoprecipitation. Langmuir. doi: 10.1021/acs.langmuir.3c02468
  54. Conesa, P., et al. (2023). Scipion3: A workflow engine for cryo-electron microscopy image processing and structural biology. Biol. Imaging. doi: 10.1017/S2633903X23000132
  55. Correa, Y., et al. (2023). High-Density Lipoprotein function is modulated by the SARS-CoV-2 spike protein in a lipid-type dependent manner. J. Colloid Interface Sci. doi: 10.1016/j.jcis.2023.04.137
  56. Cosottini, L., et al. (2023). Bioconjugation of the gold drug auranofin to human ferritin yields a potent cytotoxin. J. Drug Deliv. Sci. Technol. doi: 10.1016/j.jddst.2023.104822
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  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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