Publications acknowledging Instruct-ERIC

2018

  1. Barbieri, L., et al. (2018). Intracellular metal binding and redox behavior of human DJ-1. Journal of Biological Inorganic Chemistry, 23(1), 61-69. doi:10.1007/s00775-017-1509-5
  2. Cerofolini, L., et al. (2018). Long-range paramagnetic NMR data can provide a closer look on metal coordination in metalloproteins. Journal of Biological Inorganic Chemistry, 23(1), 71-80. doi:10.1007/s00775-017-1511-y
  3. Ciofi-Baffoni, S., et al. (2018). Protein networks in the maturation of human iron-sulfur proteins. Metallomics, 10(1), 49-72. doi:10.1039/c7mt00269f
  4. Delaforge, E., et al. (2018). Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy. Journal of the American Chemical Society, 140(3), 1148-1158. doi:10.1021/jacs.7b12407
  5. Lee, S., et al. (2018). Structures of beta-klotho reveal a 'zip code'-like mechanism for endocrine FGF signalling. Nature, 553(7689), 501-+. doi:10.1038/nature25010
  6. Lin, Z. T., et al. (2018). Investigation of 20S-hydroxyvitamin D-3 analogs and their 1 alpha-OH derivatives as potent vitamin D receptor agonists with anti-inflammatory activities. Scientific Reports, 8, 11. doi:10.1038/s41598-018-19183-7
  7. Mazur, M., et al. (2018). Targeting Acidic Mammalian chitinase Is Effective in Animal Model of Asthma. Journal of Medicinal Chemistry, 61(3), 695-710. doi:10.1021/acs.jmedchem.7b01051
  8. Pflug, A., et al. (2018). Capped RNA primer binding to influenza polymerase and implications for the mechanism of cap-binding inhibitors. Nucleic Acids Research, 46(2), 956-971. doi:10.1093/nar/gkx1210
  9. Prezel, E., et al. (2018). Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles. Molecular Biology of the Cell, 29(2), 154-165. doi:10.1091/mbc.E17-06-0429
  10. Suarez, I., et al. (2018). Structural Insights in Multifunctional Papillomavirus Oncoproteins. Viruses-Basel, 10(1), 22. doi:10.3390/v10010037
  11. Adriaenssens, E. M., et al. (2017). Taxonomy of prokaryotic viruses: 2016 update from the ICTV bacterial and archaeal viruses subcommittee. Archives of Virology, 162(4), 1153-1157. doi:10.1007/s00705-016-3173-4
  12. Maione, V., et al. (2018). Investigating the role of the human CIA2A-CIAO1 complex in the maturation of aconitase. Biochimica et Biphysica Acta-General, 1862(9), 1980-1987. doi: 10.1016/j.bbagen.2018.05.019
  13. Stolt-Bergner, P., et al. (2018). Baculovirus-driven protein expression in insect cells: A benchmarking study. Journal of Structural Biology, 203(2), 71-80. doi:10.1016/j.jsb.2018.03.004
  14. Roca, C., et al. (2018). Deciphering the inhibition of the Neuronal Calcium sensor 1 and the Guanine exchange factor Ric8a with a small Phenothiazine molecule for the rational generation of therapeutic synapse function regulators. Journal of Medical Chemistry, 61(14), 5910-5921. doi:10.1021/acs.imedchem.8b00088
  15. Trundova, M., et al. (2018). Highly stable single-strand-specific 3'-nuclease/nucleotidase from Legionella pneumophila. International Journal of Biological Macromolecules, 114(1), 776-787. doi:10.1016/j.ijbiomac.2018.03.113
  16. Howard, E., et al. (2018). Structural basis of outstanding multivalent effects in Jack Bean- Mannosidase inhibition. Angewandte Chemie-International Edition, 57(27), 8002-8006. doi:10.1002/anie.201801202
  17. Afonine, P.V., et al. (2018) From deep TLS validation to ensembles of atomic models built from elemental motions. II. Analysis of TLS refinement results by explicit interpretation. Acta Crystallographica Section D-Structural, 74(7), 621-631. doi:10.1107/S2059798318005764
  18. Bedez, C., et al. (2018). Post-translational modifications in DNA topoisomerase 2 alpha highlight the role of a eukaryote-specific residue in the ATPase domain. Scientific Reports, 8(1), 9272. doi:10.1038/s41598-018-27606-8
  19. Gogoi, P., et al. (2018). Aromatic-based design of highly active and noncalcemic vitamin D receptor agonists. Journal of Medicinal Chemistry, 61(11), 4928-4937. doi:10.1021/acs.jmedchem.8b00337
  20. Halby, L., et al. (2018). Hijacking DNA methyltransferase transition state analogues to produce chemical scaffolds for PRMT inhibitors. Philosophical Transactions of the Royal Society B-Biological Sciences, 373(1748), 20170072. doi:10.1098/rstb.2017.0072
  21. Luchinat, E., et al. (2018). In-cell NMR in human cells: direct protein expression allows structural studies of protein folding and maturation. Accounts of Chemical Research, 51(6), 1550-1557. doi:10.1021/acs.accounts.8b00147
  22. Afonine, P.K,. et al. (2018). Real-space refinement in PHENIX for cryo-EM and crystallography. Acta Crystallographica Section D-Structural, 74(SI-6), 531-544. doi:10.1101/249607
  23. Von Loeffelholz, O., et al. (2018). Volta phase plate data collection facilities image processing and cryo-EM structure determination. Journal of Structural Biology, 202(3), 191-199. doi:10.1016/j.jsb.2018.01.003
  24. Crespo, I., et al. (2018). Design, synthesis, structure-activity relationships and X-ray structural studies of novel 1-oxopyrimido[4,5-c]quinoline-2-acetic acid derivatives as selective and potent inhibitors of human aldose reductase. European Journal of Medicinal Chemistry, 152(1), 160-174. doi:10.1016/j.ejmech.2018.04.015
  25. Szekely, O., et al. (2018). High resolution 2D NMR of disordered proteins enhanced by hyperpolarized water. Analytical Chemistry, 90(10), 6169-6177. doi:10.1021/acs.analchem.8b00585
  26. Suarez, I.P., et al. (2018). Conformational sampling of the intrinsically disordered dsRBD-1 domain from Arabidopsis thaliana DCL1. Physical Chemistry Chemical Physics, 20(16), 11237-11246. doi:10.1039/C7CP07908G
  27. Schulze, W.M., et al. (2018). Structural analysis of human ARS2 as a platform for co-transcriptional RNA sorting. Nature Communications, 9(1), 1701. doi:10.1038/s41467-018-04142-7  
  28. Melcr, J., et al. (2018) Accurate binding of sodium and calcium to POPC bilayer by effective inclusion of electronic polarisation. Journal of Physical Chemistry, 122(16), 4546-4557. doi:0.1021/acs.jpcb.7b12510
  29. Tacnet-Delorme, P., et al. (2018). Proteinase 3 interferes with C1q-mediated clearance of apoptotic cells. Frontiers in Immunology, 9(1), 818. doi:10.3389/fimmu.2018.00818
  30. Bonnard, D., et al. (2018). Structure-function analyses unravel distinct effects of allosteric inhibitors of HIV-1 integrase on viral maturation and integration. Journal of biological Chemistry, 293(16), 6172-6186. doi:10.1074/jbc.M117.816793
  31. Kohler, M., et al. (2018). Binding specificites of nanobody center dot membrane protein complexes obtained from chemical cross-linking and high-mass MALDI mass spectrometry. Analytical Chemistry, 90(8), 5306-5313. doi:10.1021/acs.analchem.8b00236
  32. Timr, S,. et al. (2018). Calcium sensing by recoverin: effect of protein conformation on ion affinity. Journal of Physical Chemistry Letters, 9(7), 1613-1619. doi:10.1021/acs.jpclett.8b00495
  33. Mitri, E,. et al. (2018). N-15 isotopic labelling for in-cell protein studies by NMR spectroscopy and single-cell IR synchrotron radiation FTIR microscopy: a correlative study. Analyst, 143(5), 1171-1181. doi:10.1039/c7an01464c
  34. Jacquet, M., et al. (2018). C1q and Mannose-binding lectin interact with CR1 in the same region on CC P24-25 modules. Frontiers in Immunology, 9(1), 453. doi:10.3389/fimmu.2018.00453
  35. Simoben, C.V., et al. (2018). A novel class of schistosoma mansoni histone deacetylase 8 (HDAC8) inhibitors identified by structure-based virtual screening and in vitro testing. Molecules, 23(3), 566. doi:10.3390/molecules23030566.
  36. Murrali, M.G., et al. (2018). C-13 APSY-NMR for sequential assignment of intrinsically disordered proteins. Journal of Biomolecular NMR, 70(3), 167-175. doi:10.1007/s10858-018-0167-4
  37. Luchinat, E., et al. (2018). Identification of a novel nucleophosmin-interaction motif in the tumor suppressor p14arf. Febs Journal, 285(5), 832-847. doi:10.1111/febs.14373
  38. Cattiaux, L., et al. (2018). New branched amino acids for high affinity dedrimeric DC-SIGN ligands. Bioorganic and Medicinal Chemistry, 26(5), 1006-1015. doi:10.1016/j.humimm.2010.01.021
  39. Osmani, N., et al. (2018). An Arf6-and caveolae-dependant pathway links hemidesmosome remodeling and mechanoresponse. Molecular Biology of the Cell, 29(4), 435-451. doi:10.1091/mbc.E17-06-0356
  40. Koning, R. I., et al. (2018). Advances in cryo-electron tomography for biology and medicine. Annals of Atonomy-Anatomischer Anzeiger, 217(1), 82-96. doi:10.1016/j.aanat.2018.02.004

2017

  1. Albanese, P., et al. (2017). Pea PSII-LHCII supercomplexes form pairs by making connections across the stromal gap. Scientific Reports, 7. doi:10.1038/s41598-017-10700-8
  2. Anderson, L., et al. (2017). Histone deacetylase inhibition modulates histone acetylation at gene promoter regions and affects genome-wide gene transcription in Schistosoma mansoni. Plos Neglected Tropical Diseases, 11(4). doi:10.1371/journal.pntd.0005539
  3. Atherton, J., et al. (2017). The divergent mitotic kinesin MKLP2 exhibits atypical structure and mechanochemistry. Elife, 6. doi:10.7554/eLife.27793
  4. Bednar, J., et al. (2017). Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1. Molecular Cell, 66(3), 384-+. doi:10.1016/j.molcel.2017.04.012
  5. Belorusova, A. Y., et al. (2017). Structure-activity relationship study of vitamin D analogs with oxolane group in their side chain. European Journal of Medicinal Chemistry, 134, 86-96. doi:10.1016/j.ejmech.2017.03.081
  6. Belorusova, A. Y., et al. (2017). Structural analysis and biological activities of BXL0124, a gemini analog of vitamin D. Journal of Steroid Biochemistry and Molecular Biology, 173, 69-74. doi:10.1016/j.jsbmb.2016.09.015
  7. Benleulmi, M. S., et al. (2017). Modulation of the functional association between the HIV-1 intasome and the nucleosome by histone amino-terminal tails. Retrovirology, 14. doi:10.1186/s12977-017-0378-x
  8. Bertarello, A., et al. (2017). Paramagnetic Properties of a Crystalline Iron-Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy. Inorganic Chemistry, 56(11), 6624-6629. doi:10.1021/acs.inorgchem.7b00674
  9. Brancaccio, D., et al. (2017). 4Fe-4S Cluster Assembly in Mitochondria and Its Impairment by Copper. Journal of the American Chemical Society, 139(2), 719-730. doi:10.1021/jacs.6b09567
  10. Bruno, S., et al. (2017). Magnesium and calcium ions differentially affect human serine racemase activity and modulate its quaternary equilibrium toward a tetrameric form. Biochimica Et Biophysica Acta-Proteins and Proteomics, 1865(4), 381-387. doi:10.1016/j.bbapap.2017.01.001
  11. Calderone, V., et al. (2017). Solving the crystal structure of human calcium-free S100Z: the siege and conquer of one of the last S100 family strongholds. Journal of Biological Inorganic Chemistry, 22(4), 519-526. doi:10.1007/s00775-017-1437-4
  12. Cao, S. Y., et al. (2017). Structural Insight into Ubiquitin-Like Protein Recognition and Oligomeric States of JAMM/MPNI+ Proteases. Structure, 25(6), 823-+. doi:10.1016/j.str.2017.04.002
  13. Cerofolini, L., et al. (2017). Synthesis and binding monitoring of a new nanomolar PAMAM-based matrix metalloproteinases inhibitor (MMPIs). Bioorganic & Medicinal Chemistry, 25(2), 523-527. doi:10.1016/j.bmc.2016.11.028
  14. Cerofolini, L., et al. (2017). High-Resolution Solid-State NMR Characterization of Ligand Binding to a Protein Immobilized in a Silica Matrix. Journal of Physical Chemistry B, 121(34), 8094-8101. doi:10.1021/acs.jpcb.7b05679
  15. Cerutti, N., et al. (2017). Antigp41 membrane proximal external region antibodies and the art of using the membrane for neutralization. Current Opinion in Hiv and Aids, 12(3), 250-256. doi:10.1097/coh.0000000000000364
  16. Chebaro, Y., et al. (2017). Allosteric Regulation in the Ligand Binding Domain of Retinoic Acid Receptor gamma. Plos One, 12(1). doi:10.1371/journal.pone.0171043
  17. Chen, G. F., et al. (2017). Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state. Nature Communications, 8. doi:10.1038/s41467-017-02056-4
  18. Collins, P. J., et al. (2017). Epithelial chemokine CXCL14 synergizes with CXCL12 via allosteric modulation of CXCR4. Faseb Journal, 31(7), 3084-3097. doi:10.1096/fj.201700013R
  19. Cuenca-Alba, J., et al. (2017). ScipionCloud: An integrative and interactive gateway for large scale cryo electron microscopy image processing on commercial and academic clouds. Journal of Structural Biology, 200(1), 20-27. doi:10.1016/j.jsb.2017.06.004
  20. Cura, V., et al. (2017). Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors. Febs Journal, 284(1), 77-96. doi:10.1111/febs.13953
  21. Engilberge, S., et al. (2017). Crystallophore: a versatile lanthanide complex for protein crystallography combining nucleating effects, phasing properties, and luminescence. Chemical Science, 8(9), 5909-5917. doi:10.1039/c7sc00758b
  22. Fraga, H., et al. (2017). Solid-State NMR H-N-(C)-H and H-N-C-C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins. Chemphyschem, 18(19), 2697-2703. doi:10.1002/cphc.201700572
  23. Franco-Echevarria, E., et al. (2017). The crystal structure of mammalian inositol 1,3,4,5,6-pentakisphosphate 2-kinase reveals a new zinc-binding site and key features for protein function. Journal of Biological Chemistry, 292(25), 10534-10548. doi:10.1074/jbc.M117.780395
  24. Franco-Echevarria, E., et al. (2017). Crystallization and Preliminary X-Ray Diffraction Analysis of a Mammal Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase. Protein Journal, 36(4), 240-248. doi:10.1007/s10930-017-9717-y
  25. Giuntini, S., et al. (2017). Characterization of the Conjugation Pattern in Large Polysaccharide-Protein Conjugates by NMR Spectroscopy. Angewandte Chemie-International Edition, 56(47), 14997-15001. doi:10.1002/anie.201709274
  26. Giuntini, S., et al. (2017). Atomic structural details of a protein grafted onto gold nanoparticles. Scientific Reports, 7. doi:10.1038/s41598-017-18109-z
  27. Haselbach, D., et al. (2017). Long-range allosteric regulation of the human 26S proteasome by 20S proteasome-targeting cancer drugs. Nature Communications, 8. doi:10.1038/ncomms15578
  28. Hoang, T. V., et al. (2017). Automatic segmentation of high pressure frozen and freeze-substituted mouse retina nuclei from FIB-SEM tomograms. Journal of Structural Biology, 197(2), 123-134. doi:10.1016/j.jsb.2016.10.005
  29. Kalouskova, B., et al. (2017). Recombinant expression of natural killer cell activating immunocomplex NKp80:AICL and its structural characterisation. Febs Journal, 284, 192-192.
  30. Koning, R.I. et al (2017). Advances in cryo-electron tomography for biology and medicine. Annals of Anatomy-Anatomischer Anzeiger, 217: 82-96. doi:10.1016/j.aanat.2018.02.004
  31. Li, Y. E., et al. (2017). Identification of high-confidence RNA regulatory elements by combinatorial classification of RNA-protein binding sites. Genome Biology, 18. doi:10.1186/s13059-017-1298-8
  32. Lin, Z. T., et al. (2017). 1 alpha,20S-Dihydroxyvitamin D-3 Interacts with Vitamin D Receptor: Crystal Structure and Route of Chemical Synthesis. Scientific Reports, 7. doi:10.1038/s41598-017-10917-7
  33. Liu, G. Q., et al. (2017). One-thousand-fold enhancement of high field liquid nuclear magnetic resonance signals at room temperature. Nature Chemistry, 9(7), 676-680. doi:10.1038/nchem.2723
  34. Luchinat, E., et al. (2017). A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants. Scientific Reports, 7. doi:10.1038/s41598-017-17815-y
  35. Mansilla, A., et al. (2017). Interference of the complex between NCS-1 and Ric8a with phenothiazines regulates synaptic function and is an approach for fragile X syndrome. Proceedings of the National Academy of Sciences of the United States of America, 114(6), E999-E1008. doi:10.1073/pnas.1611089114
  36. Martinez-Zapien, D., et al. (2017). The crystal structure of the 5 ' functional domain of the transcription riboregulator 7SK. Nucleic Acids Research, 45(6), 3568-3579. doi:10.1093/nar/gkw1351
  37. Nasta, V., et al. (2017). Structural insights into the molecular function of human 2Fe-2S BOLA1-GRX5 and 2Fe-2S BOLA3-GRX5 complexes. Biochimica Et Biophysica Acta-General Subjects, 1861(8), 2119-2131. doi:10.1016/j.bbagen.2017.05.005
  38. Natchiar, S. K., et al. (2017). Visualization of chemical modifications in the human 80S ribosome structure. Nature, 551(7681), 472-+. doi:10.1038/nature24482
  39. Nikolaev, M., et al. (2017). Integral Membrane Proteins Can Be Crystallized Directly from Nanodiscs. Crystal Growth & Design, 17(3), 945-948. doi:10.1021/acs.cgd.6b01631
  40. Nogueira, M. O., et al. (2017). Monitoring HPV-16 E7 phosphorylation events. Virology, 503, 70-75. doi:10.1016/j.virol.2016.12.030
  41. Noguera, M. E., et al. (2017). Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants. Scientific Reports, 7. doi:10.1038/srep42343
  42. Orlov, I., et al. (2017). The integrative role of cryo electron microscopy in molecular and cellular structural biology. Biology of the Cell, 109(2), 81-93. doi:10.1111/boc.201600042
  43. Osman, R., et al. (2017). Calreticulin Release at an Early Stage of Death Modulates the Clearance by Macrophages of Apoptotic Cells. Frontiers in Immunology, 8. doi:10.3389/fimmu.2017.01034
  44. Peng, G. Y., et al. (2017). Insight into the remarkable affinity and selectivity of the aminobenzosuberone scaffold for the M1 aminopeptidases family based on structure analysis. Proteins-Structure Function and Bioinformatics, 85(8), 1413-1421. doi:10.1002/prot.25301
  45. Perez, C., et al. (2017). Structural basis of inhibition of lipid-linked oligosaccharide flippase PglK by a conformational nanobody. Scientific Reports, 7. doi:10.1038/srep46641
  46. Pietila, M. K., et al. (2017). Polyprotein Processing as a Determinant for In Vitro Activity of Semliki Forest Virus Replicase. Viruses-Basel, 9(10). doi:10.3390/v9100292
  47. Portaliou, A. G., et al. (2017). Hierarchical protein targeting and secretion is controlled by an affinity switch in the type III secretion system of enteropathogenic Escherichia coli. Embo Journal, 36(23), 3517-3531. doi:10.15252/embj.201797515
  48. Pozzi, C., et al. (2017). Chemistry at the protein-mineral interface in L-ferritin assists the assembly of a functional (mu(3)-oxo)Tris (mu(2)-peroxo) triiron(III) cluster. Proceedings of the National Academy of Sciences of the United States of America, 114(10), 2580-2585. doi:10.1073/pnas.1614302114
  49. Radu, L., et al. (2017). The intricate network between the p34 and p44 subunits is central to the activity of the transcription/DNA repair factor TFIIH. Nucleic Acids Research, 45(18), 10872-10883. doi:10.1093/nar/gkx743
  50. Ravera, E., et al. (2017). Perspectives on paramagnetic NMR from a life sciences infrastructure. Journal of Magnetic Resonance, 282, 154-169. doi:10.1016/j.jmr.2017.07.013
  51. Ruiz, F. X., et al. (2017). Structural basis for the inhibition of AKR1B10 by the C3 brominated TTNPB derivative UVI2008. Chemico-Biological Interactions, 276, 174-181. doi:10.1016/j.cbi.2017.01.026
  52. Sanchez-Garcia, R., et al. (2017). 3DCONS-DB: A Database of Position-Specific Scoring Matrices in Protein Structures. Molecules, 22(12). doi:10.3390/molecules22122230
  53. Santos-Perez, I., et al. (2017). Membrane-assisted viral DNA ejection. Biochimica Et Biophysica Acta-General Subjects, 1861(3), 664-672. doi:10.1016/j.bbagen.2016.12.013
  54. Sayers, Z., et al. (2017). G Protein Signaling in Plants: Characterization of Alpha and Gamma Subunits. Biophysical Journal, 112(3), 189A-190A. doi:10.1016/j.bpj.2016.11.1052
  55. Schenck, S., et al. (2017). Generation and Characterization of Anti-VGLUT Nanobodies Acting as Inhibitors of Transport. Biochemistry, 56(30), 3962-3971. doi:10.1021/acs.biochem.7b00436
  56. Schubert, A. F., et al. (2017). Structure of PINK1 in complex with its substrate ubiquitin. Nature, 552(7683), 51-+. doi:10.1038/nature24645
  57. Sharov, G., et al. (2017). Structure of the transcription activator target Tra1 within the chromatin modifying complex SAGA. Nature Communications, 8. doi:10.1038/s41467-017-01564-7
  58. Sorzano, C. O. S., et al. (2017). A Survey of the Use of Iterative Reconstruction Algorithms in Electron Microscopy. Biomed Research International. doi:10.1155/2017/6482567
  59. Stranava, M., et al. (2017). Coordination and redox state-dependent structural changes of the heme-based oxygen sensor AfGcHK associated with intraprotein signal transduction. Journal of Biological Chemistry, 292(51), 20921-20935. doi:10.1074/jbc.M117.817023
  60. Sun, Z. Y., et al. (2017). Double-stranded RNA virus outer shell assembly by bona fide domain-swapping. Nature Communications, 8. doi:10.1038/ncomms14814
  61. Takis, P. G., et al. (2017). Gelified Biofluids for High-Resolution Magic Angle Spinning H-1 NMR Analysis: The Case of Urine. Analytical Chemistry, 89(2), 1054-1058. doi:10.1021/acs.analchem.6b04318
  62. van Haren, M. J., et al. (2017). Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1. Proceedings of the National Academy of Sciences of the United States of America, 114(14), 3625-3630. doi:10.1073/pnas.1618401114
  63. Waberer, L., et al. (2017). The synaptic vesicle protein SV31 assembles into a dimer and transports Zn2+. Journal of Neurochemistry, 140(2), 280-293. doi:10.1111/jnc.13886
  64. Wutz, D., et al. (2017). Photochromic histone deacetylase inhibitors based on dithienylethenes and fulgimides. Organic & Biomolecular Chemistry, 15(22), 4882-4896. doi:10.1039/c7ob00976c

2016

  1. Andralojc, W., et al. (2016). Inter-helical conformational preferences of HIV-1 TAR-RNA from maximum occurrence analysis of NMR data and molecular dynamics simulations. Physical Chemistry Chemical Physics, 18(8), 5743-5752. doi:10.1039/c5cp03993b
  2. Andronov, L., et al. (2016). SharpViSu: integrated analysis and segmentation of super-resolution microscopy data. Bioinformatics, 32(14), 2239-2241. doi:10.1093/bioinformatics/btw123
  3. Andronov, L., et al. (2016). ClusterViSu, a method for clustering of protein complexes by Voronoi tessellation in super-resolution microscopy. Scientific Reports, 6. doi:10.1038/srep24084
  4. Asencio-Hernandez, J., et al. (2016). NMR WaterLOGSY Reveals Weak Binding of Bisphenol A with Amyloid Fibers of a Conserved 11 Residue Peptide from Androgen Receptor. Plos One, 11(9). doi:10.1371/journal.pone.0161948
  5. Baldoneschi, V., et al. (2016). Active-Site Targeting Paramagnetic Probe for Matrix Metalloproteinases. Chempluschem, 81(12), 1333-1338. doi:10.1002/cplu.201600375
  6. Barbieri, L. et al (2016). Characterization of proteins by in-cell NMR spectroscopy in cultured mammalian cells. Nature Protocols, 11: 1101-1111. doi:10.1038/nprot2016061.
  7. Baser, B., et al. (2016). A method for specifically targeting two independent genomic integration sites for co-expression of genes in CHO cells. Methods, 95, 3-12. doi:10.1016/j.ymeth.2015.11.022
  8. Bernacchioni, C., et al. (2016). Ferroxidase Activity in Eukaryotic Ferritin is Controlled by Accessory-Iron-Binding Sites in the Catalytic Cavity. Chemistry-a European Journal, 22(45), 16213-16219. doi:10.1002/chem.201602842
  9. Bleckmann, M., et al. (2016). Fast Plasmid Based Protein Expression Analysis in Insect Cells Using an Automated SplitGFP Screen. Biotechnology and Bioengineering, 113(9), 1975-1983. doi:10.1002/bit.25956
  10. Botte, M., et al. (2016). A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion. Scientific Reports, 6. doi:10.1038/srep38399
  11. Bourbigot, S., et al. (2016). Solution structure of the 5 '-terminal hairpin of the 7SK small nuclear RNA. Rna, 22(12), 1844-1858. doi:10.1261/rna.056523.116
  12. Brandt, K., et al. (2016). Stoichiometry and deletion analyses of subunits in the heterotrimeric F-ATP synthase c ring from the acetogenic bacterium Acetobacterium woodii. Febs Journal, 283(3), 510-520. doi:10.1111/febs.13606
  13. Carlon, A., et al. (2016). How to tackle protein structural data from solution and solid state: An integrated approach. Progress in Nuclear Magnetic Resonance Spectroscopy, 92-93, 54-70. doi:10.1016/j.pnmrs.2016.01.001
  14. Carlon, A., et al. (2016). Improved Accuracy from Joint X-ray and NMR Refinement of a Protein-RNA Complex Structure. Journal of the American Chemical Society, 138(5), 1601-1610. doi:10.1021/jacs.5b11598
  15. Cerofolini, L., et al. (2016). Bilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Structure and Proteolytic Activity. Scientific Reports, 6. doi:10.1038/srep29511
  16. Chang, V. T., et al. (2016). Initiation of T cell signaling by CD45 segregation at 'close contacts'. Nature Immunology, 17(5), 574-+. doi:10.1038/ni.3392
  17. Claes, K., et al. (2016). Modular Integrated Secretory System Engineering in Pichia pastoris To Enhance G-Protein Coupled Receptor Expression. Acs Synthetic Biology, 5(10), 1070-1075. doi:10.1021/acssynbio.6b00032
  18. Cousido-Siah, A., et al. (2016). IDD388 Polyhalogenated Derivatives as Probes for an Improved Structure-Based Selectivity of AKR1B10 Inhibitors. Acs Chemical Biology, 11(10), 2693-2705. doi:10.1021/acschembio.6b00382
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2015

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2014

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2013

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2012

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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). C-13 Direct-Detection Biomolecular NMR Spectroscopy in Living Cells. Angewandte Chemie-International Edition, 50(10), 2339-2341. doi:10.1002/anie.201006636
  3. 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
  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. 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
  10. 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
  11. 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
  12. 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
  13. 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. Bermel, W., et al. (2010). Exclusively Heteronuclear NMR Experiments to Obtain Structural and Dynamic Information on Proteins. Chemphyschem, 11(3), 689-695. doi:10.1002/cphc.200900772
  2. Borsi, V., et al. (2010). Entropic Contribution to the Linking Coefficient in Fragment Based Drug Design: A Case Study. Journal of Medicinal Chemistry, 53(10), 4285-4289. doi:10.1021/jm901723z
  3. Marcia, M., et al. (2010). Characterizing a monotopic membrane enzyme. Biochemical, enzymatic and crystallization studies on Aquifex aeolicus sulfide:quinone oxidoreductase. Biochimica Et Biophysica Acta-Biomembranes, 1798(11), 2114-2123. doi:10.1016/j.bbamem.2010.07.033
  4. Pogoryelov, D., et al. (2010). Microscopic rotary mechanism of ion translocation in the F-0 complex of ATP synthases. Nature Chemical Biology, 6(12), 891-899. doi:10.1038/nchembio.457
  5. Trowitzsch, S., et al. (2010). New baculovirus expression tools for recombinant protein complex production. Journal of Structural Biology, 172(1), 45-54. doi:10.1016/j.jsb.2010.02.010

2009

  1. Bieniossek, C., et al. (2009). Automated unrestricted multigene recombineering for multiprotein complex production. Nature Methods, 6(6), 447-U468. doi:10.1038/nmeth.1326
  2. 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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