Schauser, L., Handberg, K.
, Sandal, N., Stiller, J., Thykjær, T., Pajuelo, E., Nielsen, A.
& Stougaard, J. (1998).
Symbiotic mutants deficient in nodule establishment identified after T-DNA transformation of Lotus japonicus.
Molecular Genetics and Genomics,
259(4), 414-23.
Cavassim, M. I. A., Moeskjær, S.
, Moslemi, C., Fields, B.
, Bachmann, A., Vilhjálmsson, B. J., Schierup, M. H., W Young, J. P.
& Andersen, S. U. (2020).
Symbiosis genes show a unique pattern of introgression and selection within a Rhizobium leguminosarum species complex.
Microbial Genomics,
6(4), Artikel 000351.
https://doi.org/10.1099/mgen.0.000351
Zuzic, L., Stange, A. D., Bavnhøj, L., Driller, J. H., Schiøtt, B. & Pedersen, B. P. (2023).
Sweet and sour transport: Simulation insights into H+/sugar symport in plants.
Biophysical Journal,
122(3S1), 197a.
https://doi.org/10.1016/j.bpj.2022.11.1201
Dasari, J. B., Soren, B. C., Ottaviani, A.
, Tesauro, C., Marino, S., Messina, B. & Fiorani, P. (2020).
Swapping of The N-Terminal Domain of Human Topoisomerase 1B with the Corresponding Plasmodium Falciparum Counterpart Strongly Impairs Enzyme Activity.
Reports of Biochemistry and Molecular Biology,
8(4), 366-375.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7275839/
Sun, M., Wang, M., Chen, M., Dagnæs-Hansen, F., Le, D. Q. S., Baatrup, A.
, Horsman, M. R., Kjems, J. & Bünger, C. (2014).
Sustained Drug Delivery Device for Treatment of Breast Cancer and Bone Metastases. #1167. Poster session præsenteret på Orthopedic Research Society annual meeting 2014, New Orleans, USA.
Cabré, E., Malmström, J.
, Sutherland, D., Perez-Gil, J.
& Otzen, D. (2009).
Surfactant protein SP-B strongly modifies surface collapse of phospholipid vesicles: Insights from a quartz crystal microbalance with dissipation.
Biophysical Journal,
97(3), 768-76.
https://doi.org/10.1016/j.bpj.2009.04.057
Andersen, M. Ø., Lichawska, A., Arpanaei, A., Jensen, S. M. R., Kaur, H., Oupicky, D.
, Besenbacher, F., Kingshott, P.
, Kjems, J. & Howard, K. A. (2010).
Surface functionalisation of PLGA nanoparticles for gene silencing.
Biomaterials,
31(21), 5671-5677.
https://doi.org/10.1016/j.biomaterials.2010.03.069
Xu, W., Wang, J.-G., Jacobsen, M. F., Mura, M., Yu, M., Kelly, R. E. A., Meng, Q.-Q., Lægsgaard, E., Stensgaard, I.
, Linderoth, T. R., Kjems, J., Kantorovich, L. N.
, Gothelf, K. V. & Besenbacher, F. (2010).
Supramolecular porous network formed by molecular recognition between chemically modified nucleobases guanine and cytosine.
Angewandte Chemie International Edition,
49(49), 9373-7.
https://doi.org/10.1002/anie.201003390
Buttenschøn, H. N., Foldager, L., Zacharov, T. F., Olsen, I. M. L., Deleuran, T., Nyegaard, M., Hansen, M. M., Kallunki, P., Christensen, K. V., Blackwood, D. H., Muir, W. J., Straarup, S. E.
, Als, T. D., Nordentoft, M.
, Børglum, A. & Mors, O. (2010).
Support for a bipolar affective disorder susceptibility locus on chromosome 12q24.3.
Psychiatric Genetics,
20(3), 93-101.
https://doi.org/10.1097/YPG.0b013e32833a2066
Matthiesen, C. L., Hu, L., Torslev, A. S., Poulsen, E. T.
, Larsen, U. G., Kjaer-Sorensen, K., Thomsen, J. S., Brüel, A., Enghild, J. J., Oxvig, C. & Petersen, S. V. (2021).
Superoxide dismutase 3 is expressed in bone tissue and required for normal bone homeostasis and mineralization.
Free Radical Biology and Medicine,
164, 399-409.
https://doi.org/10.1016/j.freeradbiomed.2021.01.027
Vanwetswinkel, S., Kriek, J.
, Andersen, G. R., Dijk, J. & Siegal, G. (2003).
1H, 15N and 13C resonance assignments of the highly conserved 19 dKa C-terminal domain from human elongation factor 1B gamma.
J. Biomol.,
26, 189-190.
Dai, N.
, Foldager, L., Gallego, J. A., Hack, L. M., Ji, Y., Lett, T. A. P., Liu, B., Loken, E. K., Mandelli, L., Mehta, D., Power, R. A., Sprooten, E., Stephens, S. H., Paska, A. V., Yan, J., Zai, C. C., Zai, G., Zhang-James, Y., O'Shea, A. & DeLisi, L. E. (2012).
Summaries from the XIX World Congress of Psychiatric Genetics, Washington, DC, September 10-14 2011.
American Journal of Medical Genetics. Part B: Neuropsychiatric Genetics,
159B(1), 128-129.
https://doi.org/10.1002/ajmg.b.32017
Estrela, N., Franquelim, H. G., Lopes, C., Tavares, E., Macedo, J. A., Christiansen, G.
, Otzen, D. E. & Melo, E. P. (2015).
Sucrose prevents protein fibrillation through compaction of the tertiary structure but hardly affects the secondary structure.
Proteins: Structure, Function, and Bioinformatics,
83(11), 2039-2051.
https://doi.org/10.1002/prot.24921
Laursen, L. S., Overgaard, M. T., Nielsen, C. G., Boldt, H. B., Hopman, K. H.
, Enghild, J. J., Conover, C. A., Sottrup-Jensen, L., Giudice, L. C.
& Oxvig, C. (2002).
Substrate specificity of the metalloproteinase PAPP-A assessed by mutagenesis and analysis of synthetic peptides. Substrate residues distant from the scissile bond are critical for proteolysis.
Biochem. J.,
367, 31-40.
Nagase, H., Ogata, Y., Suzuki, K.
, Enghild, J. J. & Salvesen, G. (1991).
Substrate specificities and activation mechanisms of matrix metalloproteinases.
Biochemical Society. Transactions,
19(3), 715-8.
Laursen, N. S.
, Andersen, K. R., Braren, I., Spilllner, E., Sottrup-Jensen, L.
& Andersen, G. R. (2011).
Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex.
E M B O Journal,
30(3), 606-616.
Ung, K. L., Schulz, L., Stokes, D. L., Hammes, U. Z.
& Pedersen, B. P. (2023).
Substrate recognition and transport mechanism of the PIN-FORMED auxin exporters.
Trends in Biochemical Sciences,
48(11), 937-948.
https://doi.org/10.1016/j.tibs.2023.07.006
Harwood, S. L., Nielsen, N. S., Pedersen, H.
, Kjøge, K., Nielsen, P. K.
, Andersen, G. R. & Enghild, J. J. (2020).
Substituting the Thiol Ester of Human A2M or C3 with a Disulfide Produces Native Proteins with Altered Proteolysis-Induced Conformational Changes.
Biochemistry,
59(51), 4799–4809.
https://doi.org/10.1021/acs.biochem.0c00803
Khalil, V., Faress, I., Mermet-Joret, N., Kerwin, P., Yonehara, K. & Nabavi, S. (2023).
Subcortico-amygdala pathway processes innate and learned threats.
eLife,
12, Artikel e85459.
https://doi.org/10.7554/eLife.85459
Lautrup, S., Caponio, D., Cheung, H. H., Piccoli, C.
, Stevnsner, T., Chan, W. Y. & Fang, E. F. (2019).
Studying Werner syndrome to elucidate mechanisms and therapeutics of human aging and age-related diseases.
Biogerontology,
20(3), 255-269.
https://doi.org/10.1007/s10522-019-09798-2
Andersen, A. H., Sørensen, B. S., Christiansen, K., Svejstrup, J. Q., Lund, K. & Westergaard, O. (1991).
Studies of the topoisomerase II-mediated cleavage and religation reactions by use of a suicidal double-stranded DNA substrate.
Journal of Biological Chemistry,
266(14), 9203-10.
Taylor, D. J., Nilsson, J., A. Rod, M.
, Andersen, G. R., Nissen, P. & Frank, J. (2007).
Structures of modified eEF2.80S ribosome complexes reveal the role of GTP hydrolysis in translocation.
E M B O Journal,
26(9), 2421-2431.
Muszyński, A., Heiss, C., Hjuler, C. T., Sullivan, J. T., Kelly, S. J.
, Stougaard, J., Azadi, P., Carlson, R. W. & Ronson, C. W. (2016).
Structures of exopolysaccharides involved in receptor-mediated perception of Mesorhizobium loti by Lotus japonicus.
Journal of Biological Chemistry,
291(40), 20946-20961.
https://doi.org/10.1074/jbc.M116.743856
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
Otzen, D. E., Itzhaki, L. S., Elmasry, N. F., Jackson, S. E. & Fersht, A. R. (1994).
Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.
Proceedings of the National Academy of Sciences,
91(22), 10422-10425.
https://doi.org/10.1073/pnas.91.22.10422
Daggett, V., Li, A., Itzhaki, L. S.
, Otzen, D. E. & Fersht, A. R. (1996).
Structure of the transition state for folding of a protein derived from experiment and simulation.
Journal of Molecular Biology,
257(2), 430-440.
https://doi.org/10.1006/jmbi.1996.0173
Nyborg, J.
, Nissen, P., Kjeldgaard, M.
, Thirup, S., Polekhina, G. & Clark, B. F. (1996).
Structure of the ternary complex of EF-Tu: macromolecular mimicry in translation.
Trends in Biochemical Sciences,
21(3), 81-2.
Falk, S., Finogenova, K., Sørensen, M. M., Benda, C.
, Lykke-Andersen, S., Jensen, T. H. & Conti, E. (2016).
Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors.
Nature Communications,
7, Artikel 13573.
https://doi.org/10.1038/ncomms13573
Kidmose, R. T., Vasiliev, N., Chetverin, A.
, Knudsen, C. R. & Andersen, G. R. (2010).
Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins.
Proceedings of the National Academy of Sciences,
107(24), 10884-10889.
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), Artikel 6084.
https://doi.org/10.1038/s41467-022-33698-8
Jensen, R. K., Plum, M., Tjerrild, L., Jakob, T.
, Spillner, E. & Andersen, G. R. (2015).
Structure of the omalizumab Fab.
Acta Crystallographica Section F: Structural Biology Communications,
71(Pt 4), 419-426.
https://doi.org/10.1107/S2053230X15004100
Midtgaard, S. F.
, Assenholt, J., Jonstrup, A. T.
, Van, L. B., Jensen, T. H. & Brodersen, D. E. (2006).
Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain.
Proceedings of the National Academy of Sciences,
103(32), 11898-11903.