§, # equal contribution; * corresponding author(s); bold: FMP members

Abed, H. B., J. Schoene, M. Christmann, M. Nazaré*, Organophosphorus-mediated N-N bond formation: facile access to 3-amino-2H-indazoles. Org Biomol Chem14, 8520-8528 (2016). https://doi.org/10.1039/c6ob01544a

Akbey*, U., H. Oschkinat*, Structural biology applications of solid state MAS DNP NMR. J Magn Reson269, 213-224 (2016). https://doi.org/10.1016/j.jmr.2016.04.003

Amelkina, O., L. Zschockelt, J. Painer, R. Serra, F. Villaespesa, E. Krause, K. Jewgenow, B. C. Braun, Progesterone, estrogen, and androgen receptors in the corpus luteum of the domestic cat, Iberian lynx (Lynx pardinus) and Eurasian lynx (Lynx lynx). Theriogenology86, 2107-2118 (2016). https://doi.org/10.1016/j.theriogenology.2016.06.026

Aretz, J., Y. Kondoh, K. Honda, U. R. Anumala, M. Nazaré, N. Watanabe, H. Osada, C. Rademacher*, Chemical fragment arrays for rapid druggability assessment. Chem Commun52, 9067-9070 (2016). https://doi.org/10.1039/c5cc10457b

Bandholtz, S., S. Erdmann, J. L. von Hacht, S. Exner, G. Krause, G. Kleinau, C. Grotzinger, Urolinin: The First Linear Peptidic Urotensin-II Receptor Agonist. J Med Chem59, 10100-10112 (2016). https://doi.org/10.1021/acs.jmedchem.6b00164

Baranovic, J., M. Chebli, H. Salazar, A. L. Carbone, K. Faelber, A. Y. Lau, O. Daumke, A. J. R. Plested, Dynamics of the Ligand Binding Domain Layer during AMPA Receptor Activation. Biophys J110, 896-911 (2016). https://doi.org/10.1016/j.bpj.2015.12.033

Baranovic, J., A. J. R. Plested, How to build the fastest receptor on earth. Biol Chem397, 195-205 (2016). Review, https://doi.org/10.1515/hsz-2015-0182

Bel Abed, H., J. Schoene, M. Christmann, M. Nazaré*, Organophosphorus-mediated N-N bond formation: facile access to 3-amino-2H-indazoles. Org Biomol Chem14, 8520-8528 (2016). https://doi.org/10.1039/c6ob01544a

Bertran-Vicente, J., M. Penkert, O. Nieto-Garcia, J. M. Jeckelmann, P. Schmieder, E. Krause, C. P. R. Hackenberger, Chemoselective synthesis and analysis of naturally occurring phosphorylated cysteine peptides. Nat Commun7, 12703 (2016). https://doi.org/10.1038/ncomms12703

Binolfi, A., A. Limatola, S. Verzini, J. Kosten, F. X. Theillet, H. M. Rose, B. Bekei, M. Stuiver, M. van Rossum, P. Selenko, Intracellular repair of oxidation-damaged alpha-synuclein fails to target C-terminal modification sites. Nat Commun7, 10251 (2016). https://doi.org/10.1038/ncomms10251

Bocsik, A., F. R. Walter, A. Gyebrovszki, L. Fulop, I. Blasig, S. Dabrowski, F. Otvos, A. Toth, G. Rakhely, S. Veszelka, M. Vastag, P. Szabo-Revesz, M. A. Deli, Reversible Opening of Intercellular Junctions of Intestinal Epithelial and Brain Endothelial Cells With Tight Junction Modulator Peptides. J Pharm Sci-Us105, 754-765 (2016). https://doi.org/10.1016/j.xphs.2015.11.018

Böhme, M. A., C. Beis, S. Reddy-Alla, E. Reynolds, M. M. Mampell, A. T. Grasskamp, J. Lutzkendorf, D. D. Bergeron, J. H. Driller, H. Babikir, F. Gottfert, I. M. Robinson, C. J. O'Kane, S. W. Hell, M. C. Wahl, U. Stelzl, B. Loll, A. M. Walter*, S. J. Sigrist*, Active zone scaffolds differentially accumulate Unc13 isoforms to tune Ca2+ channel-vesicle coupling. Nat Neurosci19, 1311-1320 (2016). https://doi.org/10.1038/nn.4364

Boschert, V., C. Frisch, J. W. Back, K. van Pee, S. E. Weidauer, E. M. Muth, P. Schmieder, M. Beerbaum, A. Knappik, P. Timmerman, T. D. Mueller, The sclerostin-neutralizing antibody AbD09097 recognizes an epitope adjacent to sclerostin's binding site for the Wnt co-receptor LRP6. Open Biol6, 160120 (2016). https://doi.org/10.1098/rsob.160120

Bretschneider, C. O., U. Akbey, F. Aussenac, G. L. Olsen, A. Feintuch, H. Oschkinat, L. Frydman, On The Potential of Dynamic Nuclear Polarization Enhanced Diamonds in Solid-State and Dissolution (CNMR)-C-13 Spectroscopy. Chemphyschem17, 2691-2701 (2016). https://doi.org/10.1002/cphc.201600301

Brown, N. W., A. M. Marmelstein, D. Fiedler, Chemical tools for interrogating inositol pyrophosphate structure and function. Chem Soc Rev45, 6311-6326 (2016). Review, doi.org/10.1039/c6cs00193a

Buttgereit, J., J. Shanks, D. Li, G. Hao, A. Athwal, T. H. Langenickel, H. Wright, A. C. D. Goncalves, J. Monti, R. Plehm, E. Popova, F. Qadri, I. Lapidus, B. Ryan, C. Ozcelik, D. J. Paterson, M. Bader*, N. Herring, C-type natriuretic peptide and natriuretic peptide receptor B signalling inhibits cardiac sympathetic neurotransmission and autonomic function. Cardiovasc Res112, 637-644 (2016). https://doi.org/10.1093/cvr/cvw184

Carbone, A. L., A. J. R. Plested, Superactivation of AMPA receptors by auxiliary proteins. Nat Commun7, 10178 (2016). https://doi.org/10.1038/ncomms10178

Castejon, D., P. Fricke, M. I. Cambero, A. Herrera, Automatic H-1-NMR Screening of Fatty Acid Composition in Edible Oils. Nutrients8, 93 (2016). https://doi.org/10.3390/nu8020093

Castro*, V., L. Bertrand, M. Luethen, S. Dabrowski, J. Lombardi, L. Morgan, N. Sharova, M. Stevenson, I. E. Blasig*, M. Toborek*, Occludin controls HIV transcription in brain pericytes via regulation of SIRT-1 activation. FASEB J30, 1234-1246 (2016). https://doi.org/10.1096/fj.15-277673

Chanduri, M., A. Rai, A. B. Malla, M. X. Wu, D. Fiedler, R. Mallik, R. Bhandari, Inositol hexakisphosphate kinase 1 (IP6K1) activity is required for cytoplasmic dynein-driven transport. Biochem J473, 3031-3047 (2016). https://doi.org/10.1042/Bcj20160610

D'Andrea, E. D., A. Diehl, P. Schmieder, H. Oschkinat, J. R. Pires, Chemical shift assignments and secondary structure prediction for Q4DY78, a conserved kinetoplastid-specific protein from Trypanosoma cruzi. Biomol NMR Assign10, 325-328 (2016). https://doi.org/10.1007/s12104-016-9693-8

de Oliveira, G. A. P., M. D. Marques, C. Cruzeiro-Silva, Y. Cordeiro, C. Schuabb, A. H. Moraes, R. Winter, H. Oschkinat, D. Foguel, M. S. Freitas, J. L. Silva, Structural basis for the dissociation of alpha-synuclein fibrils triggered by pressure perturbation of the hydrophobic core. Sci Rep6, 37990 (2016). https://doi.org/10.1038/srep37990

Draffehn, S., J. Eichhorst, B. Wiesner, M. U. Kumke, Insight into the Modification of Polymeric Micellar and Liposomal Nanocarriers by Fluorescein-Labeled Lipids and Uptake-Mediating Lipopeptides. Langmuir32, 6928-6939 (2016). https://doi.org/10.1021/acs.langmuir.6b01487

Eccles, R. L., M. T. Czajkowski, C. Barth, P. M. Müller, E. McShane, S. Grunwald, P. Beaudette, N. Mecklenburg, R. Volkmer, K. Zühlke, G. Dittmar, M. Selbach, A. Hammes, O. Daumke, E. Klussmann, S. Urbe, O. Rocks, Bimodal antagonism of PKA signalling by ARHGAP36. Nat Commun7, 12963 (2016). https://doi.org/10.1038/ncomms12963

Fang, L., Q. H. Zhu, M. Neuenschwander, E. Specker, A. Wulf-Goldenberg, W. I. Weis, J. P. von Kries, W. Birchmeier, A Small-Molecule Antagonist of the beta-Catenin/TCF4 Interaction Blocks the Self-Renewal of Cancer Stem Cells and Suppresses Tumorigenesis. Cancer Res76, 891-901 (2016). https://doi.org/10.1158/0008-5472.Can-15-1519

Feleciano, D. R., K. Arnsburg, J. Kirstein, Interplay between redox and protein homeostasis. Worm5, e1170273 (2016). Review, https://doi.org/10.1080/21624054.2016.1170273

Feleciano, D. R., J. Kirstein, Collapse of redox homeostasis during aging and stress. Mol Cell Oncol3, e10911060 (2016). Review, https://doi.org/10.1080/23723556.2015.1091060

Fricke, P., D. Mance, V. Chevelkov, K. Giller, S. Becker, M. Baldus, A. Lange, High resolution observed in 800 MHz DNP spectra of extremely rigid type III secretion needles. J Biomol NMR65, 121-126 (2016). https://doi.org/10.1007/s10858-016-0044-y

Fritsch, J., R. Fickers, J. Klawitter, V. Sarchen, P. Zingler, D. Adam, O. Janssen, E. Krause, S. Schütze, TNF induced cleavage of HSP90 by cathepsin D potentiates apoptotic cell death. Oncotarget7, 75774-75789 (2016). https://doi.org/10.18632/oncotarget.12411

Gabriel, C. H., F. Gross, M. Karl, H. Stephanowitz, A. F. Hennig, M. Weber, S. Gryzik, I. Bachmann, K. Hecklau, J. Wienands, J. Schuchhardt, H. Herzel, A. Radbruch, E. Krause, R. Baumgrass, Identification of Novel Nuclear Factor of Activated T Cell (NFAT)-associated Proteins in T Cells. J Biol Chem291, 24172-24187 (2016). https://doi.org/10.1074/jbc.M116.739326

Geiger, Y., H. E. Gottlieb, U. Akbey, H. Oschkinat, G. Goobes, Studying the Conformation of a Silaffin-Derived Pentalysine Peptide Embedded in Bioinspired Silica using Solution and Dynamic Nuclear Polarization Magic-Angle Spinning NMR. J Am Chem Soc138, 5561-5567 (2016). https://doi.org/10.1021/jacs.5b07809

Geiger^§, M. A., M. Orwick-Rydmark^§, K. Marker, W. T. Franks, D. Akhmetzyanov, D. Stöppler, M. Zinke, E. Specker, M. Nazaré, A. Diehl, B. J. van Rossum, F. Aussenac, T. Prisner, U. Akbey, H. Oschkinat*, Temperature dependence of cross-effect dynamic nuclear polarization in rotating solids: advantages of elevated temperatures. Phys Chem Chem Phys18, 30696-30704 (2016). https://doi.org/10.1039/c6cp06154k

Gödde, K., O. Gschwend, D. Puchkov, C. K. Pfeffer, A. Carleton*, T. J. Jentsch*, Disruption of Kcc2-dependent inhibition of olfactory bulb output neurons suggests its importance in odour discrimination. Nat Commun7, 12043 (2016). https://doi.org/10.1038/ncomms12043

Götz, F., Y. Roske, M. S. Schulz, K. Autenrieth, D. Bertinetti, K. Faelber, K. Zühlke, A. Kreuchwig, E. J. Kennedy, G. Krause, O. Daumke, F. W. Herberg, U. Heinemann, E. Klussmann, AKAP18:PKA-RII alpha structure reveals crucial anchor points for recognition of regulatory subunits of PKA. Biochem J473, 1881-1894 (2016). https://doi.org/10.1042/Bcj20160242

Grauel^§, M. K., M. Maglione^§, S. Reddy-Alla^§, C. G. Willmes, M. M. Brockmann, T. Trimbuch, T. Rosenmund, M. Pangalos, G. Vardar, A. Stumpf, A. M. Walter, B. R. Rost, B. J. Eickholt, V. Haucke, D. Schmitz, S. J. Sigrist, C. Rosenmund, RIM-binding protein 2 regulates release probability by fine-tuning calcium channel localization at murine hippocampal synapses. Proc Natl Acad Sci USA113, 11615-11620 (2016). https://doi.org/10.1073/pnas.1605256113

Gupta, R., M. M. Lu, G. J. Hou, M. A. Caporini, M. Rosay, W. Maas, J. Struppe, C. Suiter, J. Ahn, I. J. L. Byeon, W. T. Franks, M. Orwick-Rydmark, A. Bertarello, H. Oschkinat, A. Lesage, G. Pintacuda, A. M. Gronenborn, T. Polenova, Dynamic Nuclear Polarization Enhanced MAS NMR Spectroscopy for Structural Analysis of HIV-1 Protein Assemblies. J Phys Chem B120, 329-339 (2016). https://doi.org/10.1021/acs.jpcb.5b12134

Hager, A., M. X. Wu, H. C. Wang, N. W. Brown, S. B. Shears, N. Veiga*, D. Fiedler*, Cellular Cations Control Conformational Switching of Inositol Pyrophosphate Analogues. Chem Eur J22, 12406-12414 (2016). https://doi.org/10.1002/chem.201601754

Hanske, J., S. Aleksic, M. Ballaschk, M. Jurk, E. Shanina, M. Beerbaum, P. Schmieder, B. G. Keller, C. Rademacher, Intradomain Allosteric Network Modulates Calcium Affinity of the C-Type Lectin Receptor Langerin. J Am Chem Soc138, 12176-12186 (2016). https://doi.org/10.1021/jacs.6b05458

Hartl, D., G. Nebrich, O. Klein, H. Stephanowitz, E. Krause, M. Rohe, SORLA regulates calpain-dependent degradation of synapsin. Alzheimers Dement12, 952-963 (2016). https://doi.org/10.1016/j.jalz.2016.02.008

Hauser, A., R. Bohlmann, Preparation of Aldehydes by Oxidation of Benzylic Amines with Selectfluor (F-TEDA-BF4). Synlett27, 1870-1872 (2016). https://doi.org/10.1055/s-0035-1561642

Herrera, C. G., M. C. Carus-Cadavieco, S. Jego, A. Ponomarenko, T. Korotkova, A. Adamantidis, Hypothalamic feedforward inhibition of thalamocortical network controls arousal and consciousness. Nat Neurosci19, 290-298 (2016). https://doi.org/10.1038/nn.4209

Hoffmann, E., K. Streichert, N. Nischan, C. Seitz, T. Brunner, S. Schwagerus, C. P. R. Hackenberger*, M. Rubini*, Stabilization of bacterially expressed erythropoietin by single site-specific introduction of short branched PEG chains at naturally occurring glycosylation sites. Mol Biosyst12, 1750-1755 (2016). https://doi.org/10.1039/c5mb00857c

Hu, H., S. A. Haas, J. Chelly, H. Van Esch, M. Raynaud, A. P. M. de Brouwer, S. Weinert, G. Froyen, S. G. M. Frints, F. Laumonnier, T. Zemojtel, M. I. Love, H. Richard, A. K. Emde, M. Bienek, C. Jensen, M. Hambrock, U. Fischer, C. Langnick, M. Feldkamp, W. Wissink-Lindhout, N. Lebrun, L. Castelnau, J. Rucci, R. Montjean, O. Dorseuil, P. Billuart, T. Stuhlmann, M. Shaw, M. A. Corbett, A. Gardner, S. Willis-Owen, C. Tan, K. L. Friend, S. Belet, K. E. P. van Roozendaal, M. Jimenez-Pocquet, M. P. Moizard, N. Ronce, R. Sun, S. O'Keeffe, R. Chenna, A. Van Bommel, J. Göke, A. Hackett, M. Field, L. Christie, J. Boyle, E. Haan, J. Nelson, G. Turner, G. Baynam, G. Gillessen-Kaesbach, U. Müller, D. Steinberger, B. Budny, M. Badura-Stronka, A. Latos-Bielenska, L. B. Ousager, P. Wieacker, G. R. Criado, M. L. Bondeson, G. Anneren, A. Dufke, M. Cohen, L. Van Maldergem, C. Vincent-Delorme, B. Echenne, B. Simon-Bouy, T. Kleefstra, M. Willemsen, J. P. Fryns, K. Devriendt, R. Ullmann, M. Vingron, K. Wrogemann, T. F. Wienker, A. Tzschach, H. van Bokhoven, J. Gecz, T. J. Jentsch, W. Chen, H. H. Ropers, V. M. Kalscheuer, X-exome sequencing of 405 unresolved families identifies seven novel intellectual disability genes. Mol Psychiatr21, 133-148 (2016). https://doi.org/10.1038/mp.2014.193

Jagtap, A. P., M. A. Geiger, D. Stöppler, M. Orwick-Rydmark, H. Oschkinat*, S. T. Sigurdsson*, bcTol: a highly water-soluble biradical for efficient dynamic nuclear polarization of biomolecules. Chem Commun52, 7020-7023 (2016). https://doi.org/10.1039/c6cc01813k

Jayapaul*, J., S. Arns, M. Bunker, M. Weiler, S. Rutherford, P. Comba, F. Kiessling*, In vivo evaluation of riboflavin receptor targeted fluorescent USPIO in mice with prostate cancer xenografts. Nano Res9, 1319-1333 (2016). https://doi.org/10.1007/s12274-016-1028-7

Jentsch, T. J., VRACs and other ion channels and transporters in the regulation of cell volume and beyond. Nat Rev Mol Cell Bio17, 293-307 (2016). Review, https://doi.org/10.1038/nrm.2016.29

Jentsch*, T. J., D. Lutter, R. Planells-Cases, F. Ullrich, F. K. Voss, VRAC: molecular identification as LRRC8 heteromers with differential functions. Pflug Arch Eur J Phy468, 385-393 (2016). Review, https://doi.org/10.1007/s00424-015-1766-5

Johannes, J., D. Braun, A. Kinne, D. Rathmann, J. Köhrle, U. Schweizer, Few Amino Acid Exchanges Expand the Substrate Spectrum of Monocarboxylate Transporter 10. Mol Endocrinol30, 796-808 (2016). https://doi.org/10.1210/me.2016-1037

Ketel, K., M. Krauss, A. S. Nicot, D. Puchkov, M. Wieffer, R. Müller, D. Subramanian, C. Schultz, J. Laporte, V. Haucke, A phosphoinositide conversion mechanism for exit from endosomes. Nature529, 408-412 (2016). https://doi.org/10.1038/nature16516

Khatri, Y., M. Ringle, M. Lisurek, J. P. von Kries, J. Zapp, R. Bernhardt, Substrate Hunting for the Myxobacterial CYP260A1 Revealed New 1-alpha Hydroxylated Products from C-19 Steroids. ChemBioChem17, 90-101 (2016). https://doi.org/10.1002/cbic.201500420

Kono, M., D. Heincke, L. Wilcke, T. W. Y. Wong, C. Bruns, S. Herrmann, T. Spielmann, T. W. Gilberger, Pellicle formation in the malaria parasite. J Cell Sci129, 673-680 (2016). https://doi.org/10.1242/jcs.181230

Korchak, S., W. Kilian, L. Schröder, L. Mitschang, Design and comparison of exchange spectroscopy approaches to cryptophane-xenon host-guest kinetics. J Magn Reson265, 139-145 (2016). https://doi.org/10.1016/j.jmr.2016.02.005

Korotkova, T., A. Ponomarenko, in In Vivo Neuropharmacology and Neurophysiology, A. Philippu, Ed. (Springer Nature, New York, 2016), pp. 67-88. Book Chapter

Kozian*, D. H., E. von Haeften, S. Joho, W. Czechtizky, U. R. Anumala, P. Roux, A. Dudda, A. Evers, M. Nazaré*, Modulation of Hexadecyl-LPA-Mediated Activation of Mast Cells and Microglia by a Chemical Probe for LPA5. ChemBioChem17, 861-865 (2016). https://doi.org/10.1002/cbic.201500559

Krauss*, M., V. Haucke*, Directing lipid transport at membrane contact sites. Nat Cell Biol18, 461-463 (2016). Editorial, https://doi.org/DOI 10.1038/ncb3345

Kuijpers, M., V. Haucke, Autophagosome Formation by Endophilin Keeps Synapses in Shape. Neuron92, 675-677 (2016). Editorial, https://doi.org/10.1016/j.neuron.2016.11.016

Kuropka, B., B. Schraven, S. Kliche, E. Krause, C. Freund, Tyrosine-phosphorylation of the scaffold protein ADAP and its role in T cell signaling. Expert Rev Proteomic13, 545-554 (2016). Review, https://doi.org/10.1080/14789450.2016.1187565

Lange, S., W. T. Franks, N. Rajagopalan, K. Döring, M. A. Geiger, A. Linden, B. J. van Rossum, G. Kramer, B. Bukau, H. Oschkinat, Structural analysis of a signal peptide inside the ribosome tunnel by DNP MAS NMR. Sci Adv2, e1600379 (2016). https://doi.org/10.1126/sciadv.1600379

Lehmann, M., G. Lichtner, H. Klenz, J. Schmoranzer, Novel organic dyes for multicolor localization-based super-resolution microscopy. J Biophotonics9, 161-170 (2016). https://doi.org/10.1002/jbio.201500119

Liao, Z. B., Z. G. Yang, A. Piontek, M. Eichner, G. Krause, L. X. Li, J. Piontek, J. J. Zhang, Specific Binding of a Mutated Fragment of Clostridium Perfringens Enterotoxin to Endothelial Claudin-5 and Its Modulation of Cerebral Vascular Permeability. Neuroscience327, 53-63 (2016). https://doi.org/10.1016/j.neuroscience.2016.04.013

Liokatis*, S., R. Klingberg, S. Tan, D. Schwarzer, Differentially Isotope-Labeled Nucleosomes To Study Asymmetric Histone Modification Crosstalk by Time-Resolved NMR Spectroscopy. Angew Chem Int Ed55, 8262-8265 (2016). https://doi.org/10.1002/anie.201601938

Liu^§, L. Y., H. Sun^§, C. Griesinger, J. K. Liu, The Use of a Combination of RDC and Chiroptical Spectroscopy for Determination of the Absolute Configuration of Fusariumin A from the Fungus Fusarium sp. Nat Product Bioprosp6, 41-48 (2016). https://doi.org/10.1007/s13659-015-0084-0

Loof, D., M. Hiller, H. Oschkinat, K. Koschek, Quantitative and Qualitative Analysis of Surface Modified Cellulose Utilizing TGA-MS. Materials9, 415 (2016). https://doi.org/10.3390/ma9060415

Lopes da Silva, M., M. N. O'Connor, J. Kriston-Vizi, I. J. White, R. Al-Shawi, J. P. Simons, J. Mössinger, V. Haucke, D. F. Cutler*, Type II PI4-kinases control Weibel-Palade body biogenesis and von Willebrand factor structure in human endothelial cells. J Cell Sci129, 2096-2105 (2016). https://doi.org/10.1242/jcs.187864

Marat, A. L., V. Haucke, Phosphatidylinositol 3-phosphates-at the interface between cell signalling and membrane traffic. EMBO J35, 561-579 (2016). Review, https://doi.org/10.15252/embj.201593564

Markó, L., E. Vigolo, C. Hinze, J. K. Park, G. Roel, A. Balogh, M. Choi, A. Wübken, J. Cording, I. E. Blasig, F. C. Luft, C. Scheidereit, K. M. Schmidt-Ott, R. Schmidt-Ullrich, D. N. Müller, Tubular Epithelial NF-kappa B Activity Regulates Ischemic AKI. J Am Soc Nephrol27, 2658-2669 (2016). https://doi.org/10.1681/Asn.2015070748

Muenzner^§, M., N. Tappenbeck^§, F. Gembardt, R. Rülke, J. Furkert, M. F. Melzig, W. E. Siems, G. A. Brockmann, T. Walther, Green tea reduces body fat via upregulation of neprilysin. Int J Obesity40, 1850-1855 (2016). https://doi.org/10.1038/ijo.2016.172

Müntener, T., D. Haussinger*, P. Selenko, F. X. Theillet*, In-Cell Protein Structures from 2D NMR Experiments. J Phys Chem Lett7, 2821-2825 (2016). https://doi.org/10.1021/acs.jpclett.6b01074

Mylona, A., F. X. Theillet, C. Foster, T. M. Cheng, F. Miralles, P. A. Bates, P. Selenko, R. Treisman, Opposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation. Science354, 233-237 (2016). https://doi.org/10.1126/science.aad1872

Nagaraj, M., T. W. Franks, S. Saeidpour, T. Schubeis, H. Oschkinat, C. Ritter, B. J. van Rossum, Surface Binding of TOTAPOL Assists Structural Investigations of Amyloid Fibrils by Dynamic Nuclear Polarization NMR Spectroscopy. ChemBioChem17, 1308-1311 (2016). https://doi.org/10.1002/cbic.201600185

Nieto-Garcia, O., P. R. Wratil, L. D. Nguyen, V. Böhrsch, S. Hinderlich, W. Reutter, C. P. R. Hackenberger, Inhibition of the key enzyme of sialic acid biosynthesis by C6-Se modified N-acetylmannosamine analogs. Chem Sci7, 3928-3933 (2016). https://doi.org/10.1039/c5sc04082e

Nischan, N., M. A. Kasper, T. Mathew, C. P. R. Hackenberger, Bis(arylmethyl)-substituted unsymmetrical phosphites for the synthesis of lipidated peptides via Staudinger-phosphite reactions. Org Biomol Chem14, 7500-7508 (2016). https://doi.org/10.1039/c6ob00843g

Pfeiffer, A., H. Stephanowitz, E. Krause, C. Volkwein, C. Hirsch, E. Jarosch, T. Sommer, A Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins. J Biol Chem291, 12195-12207 (2016). https://doi.org/10.1074/jbc.M115.703256

Plested, A. J., Single-Channel Recording of Ligand-Gated Ion Channels. Cold Spring Harb Protoc2016, pdb.top087239 (2016). https://doi.org/10.1101/pdb.top087239

Plested, A. J., J. Baranovic, Single-Channel Recording of Glycine Receptors in Human Embryonic Kidney (HEK) Cells. Cold Spring Harb Protoc2016, pdb.prot091652 (2016). https://doi.org/10.1101/pdb.prot091652

Plested, A. J. R., Structural mechanisms of activation and desensitization in neurotransmitter-gated ion channels. Nature Structural and Molecular Biology23, 494-502 (2016). Review, https://doi.org/10.1038/nsmb.3214

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