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Publikationer fra instituttet

Tidsskriftsforsider lavet af forskere fra MBG

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Pirhaghi, M., Najarzadeh, Z., Moosavi-Movahedi, F., Shafizadeh, M., Mamashli, F., Atarod, D., Ghasemi, A., Morshedi, D., Meratan, A. A., Otzen, D. E. & Saboury, A. A. (2023). The anti-platelet drug ticlopidine inhibits FapC fibrillation and biofilm production: Highlighting its antibiotic activity. B B A - Proteins and Proteomics, 1871(2), 140883. [140883]. https://doi.org/10.1016/j.bbapap.2022.140883

Li, Z., Anankanbil, S., Pedersen, J. N., Nadzieja, M. & Guo, Z. (2023). Nanocellulose fractionated from TEMPO-mediated oxidation of cellulose as an energy-free ingredient for stabilizing Pickering emulsion. Biochemical Engineering Journal, 191, [ 108795]. https://doi.org/10.1016/j.bej.2022.108795

Alijanvand, S. H., Ladefoged, L. K., Zubrienė, A., Sakalauskas, A., Christiansen, G., Dudutiene, V., Schiøtt, B., Matulis, D., Smirnovas, V. & Otzen, D. E. (2023). Inhibitory effects of fluorinated benzenesulfonamides on insulin fibrillation. International Journal of Biological Macromolecules, 227, 590-600. https://doi.org/10.1016/j.ijbiomac.2022.12.105

Mohammad-Beigi, H., Wijaya, W., Madsen, M., Hayashi, Y., Li, R., Maria Rovers, T. A., Jæger, T. C., Buell, A. K., Hougaard, A. B., Kirkensgaard, J. J. K., Westh, P., Ipsen, R. & Svensson, B. (2023). Association of caseins with β-lactoglobulin influenced by temperature and calcium ions: A multi-parameter analysis. Food Hydrocolloids, 137, [108373]. https://doi.org/10.1016/j.foodhyd.2022.108373

Li, Z., Anankanbil, S., Li, L., Lyu, J., Nadzieja, M. & Guo, Z. (2023). Alkylsuccinylated oxidized cellulose-based amphiphiles as a novel multi-purpose ingredient for stabilizing O/W emulsions. Food Hydrocolloids, 134, [108014]. https://doi.org/10.1016/j.foodhyd.2022.108014

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Josipovic, N., Ebbesen, K. K., Zirkel, A., Danieli-Mackay, A., Dieterich, C., Kurian, L., Hansen, T. B. & Papantonis, A. (2022). circRAB3IP modulates cell proliferation by reorganizing gene expression and mRNA processing in a paracrine manner. RNA (New York, N.Y.), 28(11), 1481-1495. https://doi.org/10.1261/rna.079195.122

Fukai, E., Yoshikawa, M., Shah, N., Sandal, N., Miyao, A., Ono, S., Hirakawa, H., Akyol, T. Y., Umehara, Y., Nonomura, K-I., Stougaard, J., Hirochika, H., Hayashi, M., Sato, S., Andersen, S. U. & Okazaki, K. (2022). Widespread and transgenerational retrotransposon activation in inter- and intra-species recombinant inbred populations of Lotus japonicus. The Plant Journal, 111(5), 1397-1410. https://doi.org/10.1111/tpj.15896

Neumann, C., Focht, D., Trampari, S., Lyons, J. A. & Nissen, P. (2022). Variations on a theme: Crystal forms of the amino-acid transporter MhsT. Acta Crystallographica Section F: Structural Biology Communications, 78(Part 8), 297-305. https://doi.org/10.1107/S2053230X22007154

Pothoulakis, G., Nguyen, M. T. A. & Andersen, E. S. (2022). Utilizing RNA origami scaffolds in Saccharomyces cerevisiae for dCas9-mediated transcriptional control. Nucleic Acids Research, 50(12), 7176-7187. https://doi.org/10.1093/nar/gkac470

Zev, S., Ringel, M., Driller, R., Loll, B., Brück, T. & Major, D. T. (2022). Understanding the competing pathways leading to hydropyrene and isoelisabethatriene. Beilstein Journal of Organic Chemistry, 18, 972-978. https://doi.org/10.3762/bjoc.18.97

Meisl, G., Xu, C. K., Taylor, J. D., Michaels, T. C. T., Levin, A., Otzen, D., Klenerman, D., Matthews, S., Linse, S., Andreasen, M. & Knowles, T. P. J. (2022). Uncovering the universality of self-replication in protein aggregation and its link to disease. Science Advances, 8(32), [eabn6831]. https://doi.org/10.1126/sciadv.abn6831

Hangiu, O., Compte, M., Dinesen, A., Navarro, R., Tapia-Galisteo, A., Mandrup, O. A., Erce-Llamazares, A., Lázaro-Gorines, R., Nehme-Álvarez, D., Domínguez-Alonso, C., Harwood, S. L., Alfonso, C., Blanco, B., Rubio-Pérez, L., Jiménez-Reinoso, A., Díez-Alonso, L., Blanco, F. J., Sanz, L., Howard, K. A. & Álvarez-Vallina, L. (2022). Tumor targeted 4-1BB agonist antibody-albumin fusions with high affinity to FcRn induce anti-tumor immunity without toxicity. iScience, 25(9), [104958]. https://doi.org/10.1016/j.isci.2022.104958

Tapia-Galisteo, A., Sánchez Rodríguez, Í., Aguilar-Sopeña, O., Harwood, S. L., Narbona, J., Ferreras Gutierrez, M., Navarro, R., Martín-García, L., Corbacho, C., Compte, M., Lacadena, J., Blanco, F. J., Chames, P., Roda-Navarro, P., Álvarez-Vallina, L. & Sanz, L. (2022). Trispecific T-cell engagers for dual tumor-targeting of colorectal cancer. OncoImmunology, 11(1), [2034355]. https://doi.org/10.1080/2162402X.2022.2034355

Keller, J. G., Hymøller, K. M., Thorsager, M. E., Hansen, N. Y., Erlandsen, J. U., Tesauro, C., Simonsen, A. K. W., Andersen, A. B., Vandsø Petersen, K., Holm, L. L., Stougaard, M., Andresen, B. S., Kristensen, P., Frøhlich, R. & Knudsen, B. R. (2022). Topoisomerase 1 inhibits MYC promoter activity by inducing G-quadruplex formation. Nucleic Acids Research, 50(11), 6332-6342. https://doi.org/10.1093/nar/gkac482

Hansen, E. K. B., Fredsøe, J. H., Okholm, T. L. H., Ulhøi, B. P., Klingenberg, S., Jensen, J. B., Kjems, J., Bouchelouche, K., Borre, M., Damgaard, C. K., Pedersen, J. S., Kristensen, L. S. & Sørensen, K. D. (2022). The transcriptional landscape and biomarker potential of circular RNAs in prostate cancer. Genome Medicine, 14(1), [8]. https://doi.org/10.1186/s13073-021-01009-3

Møhlenberg, M., O’Brien, T. R. & Hartmann, R. (2022). The role of IFNL4 in liver inflammation and progression of fibrosis. Genes and Immunity, 23(3-4), 111-117. https://doi.org/10.1038/s41435-022-00173-9

Møhlenberg, M., Eriksen, P. L., Laursen, T. L., Nielsen, M. B., Hamilton-Dutoit, S. J., Grønbæk, H., Hartmann, R. & Thomsen, K. L. (2022). The presence of interferon affects the progression of non-alcoholic fatty liver disease. Genes and Immunity, 23(5), 157–165. https://doi.org/10.1038/s41435-022-00176-6

Dyla, M., González Foutel, N. S., Otzen, D. E. & Kjaergaard, M. (2022). The optimal docking strength for reversibly tethered kinases. Proceedings of the National Academy of Sciences of the United States of America, 119(25), [e2203098119]. https://doi.org/10.1073/pnas.2203098119

Salimi, M., Tabasi, F., Nazari, M., Ghazvineh, S. & Raoufy, M. R. (2022). The olfactory bulb coordinates the ventral hippocampus–medial prefrontal cortex circuit during spatial working memory performance. Journal of Physiological Sciences, 72(1), [9]. https://doi.org/10.1186/s12576-022-00833-5

Mogensen, E. H., Poulsen, E. T., Thøgersen, I. B., Yamamoto, K., Brüel, A. & Enghild, J. J. (2022). The low-density lipoprotein receptor-related protein 1 (LRP1) interactome in the human cornea. Experimental Eye Research, 219, [109081]. https://doi.org/10.1016/j.exer.2022.109081

Kristensen, L. S., Jakobsen, T., Hager, H. & Kjems, J. (2022). The emerging roles of circRNAs in cancer and oncology. Nature Reviews. Clinical Oncology, 19(3), 188-206. https://doi.org/10.1038/s41571-021-00585-y

Harwood, S. L., Diep, K., Nielsen, N. S., Jensen, K. T. & Enghild, J. J. (2022). The conformational change of the protease inhibitor α₂-macroglobulin is triggered by the retraction of the cleaved bait region from a central channel. Journal of Biological Chemistry, 298(8), [102230]. https://doi.org/10.1016/j.jbc.2022.102230

Rasmussen, H. Ø., Wollenberg, D. T. W., Wang, H., Andersen, K. K., Oliveira, C. L. P., Jørgensen, C. I., Jørgensen, T. J. D., Otzen, D. E. & Pedersen, J. S. (2022). The changing face of SDS denaturation: Complexes of Thermomyces lanuginosus lipase with SDS at pH 4.0, 6.0 and 8.0. Journal of Colloid and Interface Science, 614, 214-232. https://doi.org/10.1016/j.jcis.2021.12.188

Gu, T., Just, J., Stenz, K. T., Yan, Y., Sieljacks, P., Wang, J., Groennebaek, T. S., Jakobsgaard, J. E., Rindom, E., Herskind, J., Gravholt, A., Lassen, T. R., Jørgensen, M., Bæk, R., Gutiérrez-Jiménez, E., Iversen, N. K., Rasmussen, P. M., Nyengaard, J. R., Jørgensen, M. M. ... Drasbek, K. R. (2022). The Role of Plasma Extracellular Vesicles in Remote Ischemic Conditioning and Exercise-Induced Ischemic Tolerance. International Journal of Molecular Sciences , 23(6), [3334]. https://doi.org/10.3390/ijms23063334

Khateb, H., Sørensen, R. S., Cramer, K., Eklund, A. S., Kjems, J., Meyer, R. L., Jungmann, R. & Sutherland, D. S. (2022). The Role of Nanoscale Distribution of Fibronectin in the Adhesion of Staphylococcus aureus Studied by Protein Patterning and DNA-PAINT. ACS Nano, 16(7), 10392-10403. https://doi.org/10.1021/acsnano.2c00630

Frank, M., Cortleven, A., Pěnčík, A., Novak, O. & Schmülling, T. (2022). The Photoperiod Stress Response in Arabidopsis thaliana Depends on Auxin Acting as an Antagonist to the Protectant Cytokinin. International Journal of Molecular Sciences , 23(6). https://doi.org/10.3390/ijms23062936

Fruergaard, M. U., Dach, I., Andersen, J. L., Ozol, M., Shasavar, A., Quistgaard, E. M. H., Poulsen, H., Fedosova, N. & Nissen, P. (2022). The Na,K-ATPase in complex with beryllium fluoride mimics an ATPase phosphorylated state. Journal of Biological Chemistry, 298(9), [102317]. https://doi.org/10.1016/j.jbc.2022.102317

Farzadfard, A., Pedersen, J. N., Meisl, G., Somavarapu, A. K., Alam, P., Goksøyr, L., Nielsen, M. A., Sander, A. F., Knowles, T. P. J., Pedersen, J. S. & Otzen, D. E. (2022). The C-terminal tail of α-synuclein protects against aggregate replication but is critical for oligomerization. Communications Biology, 5(1), [123]. https://doi.org/10.1038/s42003-022-03059-8

Jakobsen, A. K., Yuusufi, S., Madsen, L. B., Meldgaard, P., Knudsen, B. R. & Stougaard, M. (2022). TDP1 and TOP1 as targets in anticancer treatment of NSCLC: Activity and protein level in normal and tumor tissue from 150 NSCLC patients correlated to clinical data. Lung Cancer, 164, 23-32. https://doi.org/10.1016/j.lungcan.2021.12.010

Nguyen, M. T. A., Pothoulakis, G. & Andersen, E. S. (2022). Synthetic Translational Regulation by Protein-Binding RNA Origami Scaffolds. A C S Synthetic Biology, 11(5). https://doi.org/10.1021/acssynbio.1c00608

Fuertes, M., Selas, A., Trejo, A., Knudsen, B. R., Palacios, F. & Alonso, C. (2022). Synthesis of hybrid phosphorated indenoquinolines and biological evaluation as topoisomerase I inhibitors and antiproliferative agents. Bioorganic and Medicinal Chemistry Letters, 57, [128517]. https://doi.org/10.1016/j.bmcl.2021.128517

Larsen, K. E. (Producent). (2022). Sus scrofa domesticus mesenecephalic astrocyte-derived neurotrophic factor (MANF) gene, promoter region and partial cds. GenBank Access No. OK337617. Datasæt

Larsen, K. E. (Producent). (2022). Sus scrofa domesticus cerebral dopamine neurotrophic factor (CDNF) mRNA, complete cds. GenBank Access No. OK268246. Datasæt

Tesch-Römer, C., Wahl, H-W., Rattan, S. & Ayalon, L. (2022). Successful Ageing: Ambition and Ambivalence. Oxford University Press. https://doi.org/10.1093/med/9780192897534.001.0001

Ung, K. L., Winkler, M., Schulz, L., Kolb, M., Janacek, D. P., Dedic, E., Stokes, D. L., Hammes, U. Z. & Pedersen, B. P. (2022). Structures and mechanism of the plant PIN-FORMED auxin transporter. Nature, 609(7927), 605-610. https://doi.org/10.1038/s41586-022-04883-y

Pedersen, H., Jensen, R. K., Hansen, A. G., Petersen, S. V., Thiel, S., Laursen, N. S. & Andersen, G. R. (2022). Structure-Guided Engineering of a Complement Component C3-Binding Nanobody Improves Specificity and Adds Cofactor Activity. Frontiers in Immunology, 13, [872536]. https://doi.org/10.3389/fimmu.2022.872536

Kobberø, S. D., Gajhede, M., Mirza, O. A., Kløverpris, S., Kjær, T. R., Mikkelsen, J. H., Boesen, T. & Oxvig, C. (2022). Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism. Nature Communications, 13(1), [6084]. https://doi.org/10.1038/s41467-022-33698-8

Langousis, G., Cavadini, S., Boegholm, N., Lorentzen, E., Kempf, G. & Matthias, P. (2022). Structure of the ciliogenesis-associated CPLANE complex. Science Advances, 8(15), [eabn0832]. https://doi.org/10.1126/sciadv.abn0832

Lorentzen, J., Pedersen, D. V., Gadeberg, T. A. F. & Andersen, G. R. (2022). Structure determination of an unstable macromolecular complex enabled by nanobody-peptide bridging. Protein Science, 31(10), [e4432]. https://doi.org/10.1002/pro.4432

Gerlach, P., Garland, W., Lingaraju, M., Salerno-Kochan, A., Bonneau, F., Basquin, J., Jensen, T. H. & Conti, E. (2022). Structure and regulation of the nuclear exosome targeting complex guides RNA substrates to the exosome. Molecular Cell, 82(13), 2505-2518.e7. https://doi.org/10.1016/j.molcel.2022.04.011

Braunger, K., Ahn, J., Jore, M. M., Johnson, S., Tang, T. T. L., Pedersen, D. V., Andersen, G. R. & Lea, S. M. (2022). Structure and function of a family of tick-derived complement inhibitors targeting properdin. Nature Communications, 13, [317]. https://doi.org/10.1038/s41467-021-27920-2

Hartmann, S., Ling, M., Dreyer, L. S. A., Zipori, A., Finster, K., Grawe, S., Jensen, L. Z., Borck, S., Reicher, N., Niedermeier, D., Jones, N. C., Hoffmann, S. V., Wex, H., Rudich, Y., Boesen, T. & Santl-Temkiv, T. (2022). Structure and Protein-Protein Interactions of Ice Nucleation Proteins Drive Their Activity. Frontiers in Microbiology, 13, [872306]. https://doi.org/10.3389/fmicb.2022.872306

Bisiak, F., Chrenková, A., Zhang, S. D., Pedersen, J. N., Otzen, D. E., Zhang, Y. E. & Brodersen, D. E. (2022). Structural variations between small alarmone hydrolase dimers support different modes of regulation of the stringent response. Journal of Biological Chemistry, 298(7), [102142]. https://doi.org/10.1016/j.jbc.2022.102142

Nielsen, J., Brandt, J., Boesen, T., Hummelshøj, T., Slaaby, R., Schluckebier, G. & Nissen, P. (2022). Structural investigations of full-length insulin receptor dynamics and signalling. Journal of Molecular Biology, 434(5), [167458]. https://doi.org/10.1016/j.jmb.2022.167458

Jensen, R. K., Pedersen, H., Lorentzen, J., Laursen, N. S., Vorup-Jensen, T. & Andersen, G. R. (2022). Structural insights into the function-modulating effects of nanobody binding to the integrin receptor α_Mβ₂. Journal of Biological Chemistry, 298(8), [102168]. https://doi.org/10.1016/j.jbc.2022.102168

Sahin, C., Østerlund, E. C., Österlund, N., Costeira-Paulo, J., Pedersen, J. N., Christiansen, G., Nielsen, J., Grønnemose, A. L., Amstrup, S. K., Tiwari, M. K., Rao, R. S. P., Bjerrum, M. J., Ilag, L. L., Davies, M. J., Marklund, E. G., Pedersen, J. S., Landreh, M., Møller, I. M., Jørgensen, T. J. D. & Otzen, D. E. (2022). Structural Basis for Dityrosine-Mediated Inhibition of α-Synuclein Fibrillization. Journal of the American Chemical Society, 144(27), 11949-11954. https://doi.org/10.1021/jacs.2c03607

Winkler, M. B. L., Nel, L., Frain, K. M., Dedic, E., Olesen, E. & Pedersen, B. P. (2022). Sterol uptake by the NPC system in eukaryotes: a Saccharomyces cerevisiae perspective. FEBS Letters, 596(2), 160-179. https://doi.org/10.1002/1873-3468.14253

Matzke, M., Toft, S., Bechsgaard, J., Pold Vilstrup, A., Uhl, G., Künzel, S., Tuni, C. & Bilde, T. (2022). Sperm competition intensity affects sperm precedence patterns in a polyandrous gift-giving spider. Molecular Ecology, 31(8), 2435-2452. https://doi.org/10.1111/mec.16405

Toth, A. E., Helms, H. C., Harazin, A., Johnsen, K. B., Goldeman, C., Burkhart, A., Thomsen, M. S., Kempen, P. J., Klepe, A., Lipka, D. V., Møller, P. L., Andresen, T. L., Nyegaard, M., Moos, T., Brodin, B. & Nielsen, M. S. (2022). Sortilin regulates blood-brain barrier integrity. The FEBS Journal, 289(4), 1062-1079. https://doi.org/10.1111/febs.16225

Keller, J. G., Mizielinski, K., Petersen, K. V., Stougaard, M., Knudsen, B. R. & Tesauro, C. (2022). Simple and Fast Rolling Circle Amplification-Based Detection of Topoisomerase 1 Activity in Crude Biological Samples. Journal of visualized experiments : JoVE, (190). https://doi.org/10.3791/64484

Keller-Socin, J. G., Petersen, K. V., Knudsen, B. R. & Tesauro, C. (2022). Simple and Fast DNA-Based Tool to Investigate Topoisomerase 1 Activity, a Biomarker for Drug Susceptibility in Colorectal Cancer. I Simple and Fast DNA-Based Tool to Investigate Topoisomerase 1 Activity, a Biomarker for Drug Susceptibility in Colorectal Cancer InTechOpen. https://doi.org/doi.org/10.5772/intechopen.105758

Murphy, K. M., Poretsky, E., Liu, H., Micic, N., Nyhuis, A., Bohlmann, J., Schmelz, E. A., Zerbe, P., Huffaker, A. & Bjarnholt, N. (2022). Shielding the oil reserves: The scutellum as a source of chemical defenses. Plant Physiology, 188(4), 1944-1949. https://doi.org/10.1093/plphys/kiac038

Petersen, K. V., Tesauro, C., Hede, M. S., Pages, C., Marcussen, L. B., Keller, J. G., Bugge, M., Holm, K., Bjergbæk, L., Stougaard, M., Wejse, C. & Knudsen, B. R. (2022). Rolling Circle Enhanced Detection of Specific Restriction Endonuclease Activities in Crude Cell Extracts. Sensors, 22(20), [7763]. https://doi.org/10.3390/s22207763

Harwood, S. L., Andersen, G. R. & Enghild, J. J. (2022). Recent cryogenic electron microscopy structures of human A2M may not be representative of the native protein. Proceedings of the National Academy of Sciences of the United States of America, 119(37), [e2210218119]. https://doi.org/10.1073/pnas.2210218119

Gockert, M., Schmid, M., Jakobsen, L., Jens, M., Andersen, J. S. & Jensen, T. H. (2022). Rapid factor depletion highlights intricacies of nucleoplasmic RNA degradation. Nucleic Acids Research, 50(3), 1583-1600. https://doi.org/10.1093/nar/gkac001

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Revideret 13.01.2023

Lisbeth Heilesen