Publications acknowledging Instruct-ERIC


  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


  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. 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
  31. 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
  32. 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
  33. 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
  34. 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
  35. 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
  36. 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
  37. Natchiar, S. K., et al. (2017). Visualization of chemical modifications in the human 80S ribosome structure. Nature, 551(7681), 472-+. doi:10.1038/nature24482
  38. 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
  39. Nogueira, M. O., et al. (2017). Monitoring HPV-16 E7 phosphorylation events. Virology, 503, 70-75. doi:10.1016/j.virol.2016.12.030
  40. 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
  41. 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
  42. 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
  43. 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
  44. 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
  45. 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
  46. 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
  47. 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
  48. 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
  49. 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
  50. 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
  51. 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
  52. 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
  53. 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
  54. 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
  55. Schubert, A. F., et al. (2017). Structure of PINK1 in complex with its substrate ubiquitin. Nature, 552(7683), 51-+. doi:10.1038/nature24645
  56. 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
  57. 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
  58. 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
  59. 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
  60. 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
  61. 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
  62. 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
  63. 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


  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. 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
  7. 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
  8. 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
  9. 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
  10. 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
  11. 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
  12. 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
  13. 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
  14. 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
  15. 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
  16. 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
  17. 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
  18. de la Rosa-Trevin, J. M., et al. (2016). Scipion: A software framework toward integration, reproducibility and validation in 3D electron microscopy. Journal of Structural Biology, 195(1), 93-99. doi:10.1016/j.jsb.2016.04.010
  19. Feifel, S. C., et al. (2016). Insights into Interprotein Electron Transfer of Human Cytochrome c Variants Arranged in Multilayer Architectures by Means of an Artificial Silica Nanoparticle Matrix. ACS Omega, 1(6), 1058-1066. doi:10.1021/acsomega.6b00213
  20. Heinnburg, T., et al. (2016). Structure-Based Design and Synthesis of Novel Inhibitors Targeting HDAC8 from Schistosoma mansoni for the Treatment of Schistosomiasis. Journal of Medicinal Chemistry, 59(6), 2423-2435. doi:10.1021/acs.jmedchem.5b01478
  21. Henrich, E., et al. (2016). Lipid Requirements for the Enzymatic Activity of MraY Translocases and in Vitro Reconstitution of the Lipid II Synthesis Pathway. Journal of Biological Chemistry, 291(5), 2535-2546. doi:10.1074/jbc.M115.664292
  22. Howard, E. I., et al. (2016). High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution. Iucrj, 3, 115-126. doi:10.1107/s2052252515024161
  23. Kereiche, S., et al. (2016). The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease. Scientific Reports, 6. doi:10.1038/srep33631
  24. Khoshouei, M., et al. (2016). Volta phase plate cryo-EM of the small protein complex Prx3. Nature Communications, 7. doi:10.1038/ncomms10534
  25. Kobbi, L., et al. (2016). An evolutionary conserved Hexim1 peptide binds to the Cdk9 catalytic site to inhibit P-TEFb. Proceedings of the National Academy of Sciences of the United States of America, 113(45), 12721-12726. doi:10.1073/pnas.1612331113
  26. Koning, R. I., et al. (2016). Asymmetric cryo-EM reconstruction of phage MS2 reveals genome structure in situ. Nature Communications, 7. doi:10.1038/ncomms12524
  27. Latrick, C. M., et al. (2016). Molecular basis and specificity of H2A.Z-H2B recognition and deposition by the histone chaperone YL1. Nature Structural & Molecular Biology, 23(4), 309-316. doi:10.1038/nsmb.3189
  28. Lepage, M. L., et al. (2016). Iminosugar-Cyclopeptoid Conjugates Raise Multivalent Effect in Glycosidase Inhibition at Unprecedented High Levels. Chemistry-a European Journal, 22(15), 5151-5155. doi:10.1002/chem.201600338
  29. Levy, N., et al. (2016). Production of unstable proteins through the formation of stable core complexes. Nature Communications, 7. doi:10.1038/ncomms10932
  30. Luchinat, E., et al. (2016). Sequential protein expression and selective labeling for in-cell NMR in human cells. Biochimica Et Biophysica Acta-General Subjects, 1860(3), 527-533. doi:10.1016/j.bbagen.2015.12.023
  31. Marabini, R., et al. (2016). The Electron Microscopy eXchange (EMX) initiative. Journal of Structural Biology, 194(2), 156-163. doi:10.1016/j.jsb.2016.02.008
  32. Martelli, T., et al. (2016). Atomic-Level Quality Assessment of Enzymes Encapsulated in Bioinspired Silica. Chemistry-a European Journal, 22(1), 425-432. doi:10.1002/chem.201503613
  33. Martin, F., et al. (2016). Ribosomal 18S rRNA base pairs with mRNA during eukaryotic translation initiation. Nature Communications, 7. doi:10.1038/ncomms12622
  34. Martinez-Lumbreras, S., et al. (2016). Gbp2 interacts with THO/TREX through a novel type of RRM domain. Nucleic Acids Research, 44(1), 437-448. doi:10.1093/nar/gkv1303
  35. Martinez-Zapien, D., et al. (2016). Structure of the E6/E6AP/p53 complex required for HPV-mediated degradation of p53. Nature, 529(7587), 541-+. doi:10.1038/nature16481
  36. Meyer, S., et al. (2016). Backbone H-1, N-15, C-13 NMR assignment of the 518-627 fragment of the androgen receptor encompassing N-terminal and DNA binding domains. Biomolecular Nmr Assignments, 10(1), 175-178. doi:10.1007/s12104-015-9661-8
  37. Myasnikov, A. G., et al. (2016). Structure-function insights reveal the human ribosome as a cancer target for antibiotics. Nature Communications, 7. doi:10.1038/ncomms12856
  38. Nguyen-Huynh, N. T., et al. (2016). Monitoring of the retinoic acid receptor-retinoid X receptor dimerization upon DNA binding by native mass spectrometry. Biophysical Chemistry, 210, 2-8. doi:10.1016/j.bpc.2015.10.006
  39. Otero, R., et al. (2016). Carborane-based design of a potent vitamin D receptor agonist. Chemical Science, 7(2), 1033-1037. doi:10.1039/c5sc03084f
  40. Pasi, M., et al. (2016). DNA minicircles clarify the specific role of DNA structure on retroviral integration. Nucleic Acids Research, 44(16), 7830-7847. doi:10.1093/nar/gkw651
  41. Pietila, M. K., et al. (2016). Pleolipoviridae, a newly proposed family comprising archaeal pleomorphic viruses with single-stranded or double-stranded DNA genomes. Archives of Virology, 161(1), 249-256. doi:10.1007/s00705-015-2613-x
  42. Pilsl, M., et al. (2016). Structure of the initiation-competent RNA polymerase I and its implication for transcription. Nature Communications, 7. doi:10.1038/ncomms12126
  43. Podobnik, M., et al. (2016). Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly. Nature Communications, 7. doi:10.1038/ncomms11598
  44. Rammohan, N., et al. (2016). Nanodiamond-Gadolinium(III) Aggregates for Tracking Cancer Growth In Vivo at High Field. Nano Letters, 16(12), 7551-7564. doi:10.1021/acs.nanolett.6b03378
  45. Ravera, E., et al. (2016). Solid-State NMR of PEGylated Proteins. Angewandte Chemie-International Edition, 55(7), 2446-2449. doi:10.1002/anie.201510148
  46. Ravera, E., et al. (2016). Basic facts and perspectives of Overhauser DNP NMR. Journal of Magnetic Resonance, 264, 78-87. doi:10.1016/j.jmr.2015.12.013
  47. Ravera, E., et al. (2016). Biosilica and bioinspired silica studied by solid-state NMR. Coordination Chemistry Reviews, 327, 110-122. doi:10.1016/j.ccr.2016.06.003
  48. Ravera, E., et al. (2016). A critical assessment of methods to recover information from averaged data. Physical Chemistry Chemical Physics, 18(8), 5686-5701. doi:10.1039/c5cp04077a
  49. Renner, M., et al. (2016). Nucleocapsid assembly in pneumoviruses is regulated by conformational switching of the N protein. Elife, 5, e12627. doi:10.7554/eLife.12627
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