Reimer, L., Haikal, C.
, Gram, H., Theologidis, V., Kovacs, G., Ruesink, H., Baun, A., Nielsen, J., Otzen, D. E., Li, J.-Y.
& Jensen, P. H. (2022).
Low dose DMSO treatment induces oligomerization and accelerates aggregation of α-synuclein.
Scientific Reports,
12, Artikel 3737.
https://doi.org/10.1038/s41598-022-07706-2
Thiergart, T., Zgadzaj, R.
, Bozsóki, Z., Garrido-Oter, R.
, Radutoiu, S. & Schulze-Lefert, P. (2019).
Lotus japonicus Symbiosis Genes Impact Microbial Interactions between Symbionts and Multikingdom Commensal Communities.
mBio,
10(5), Artikel e01833-19.
https://doi.org/10.1128/mBio.01833-19
Yoon, H. J., Hossain, M. S., Held, M., Hou, H., Kehl, M., Tromas, A., Sato, S., Tabata, S.
, Andersen, S. U., Stougaard, J., Ross, L. & Szczyglowski, K. (2014).
Lotus japonicus SUNERGOS1 encodes a predicted subunit A of a DNA topoisomerase VI and is required for nodule differentiation and accommodation of rhizobial infection.
Plant Journal,
78(5), 811-821.
https://doi.org/10.1111/tpj.12520
Magne, K., George, J., Berbel Tornero, A., Broquet, B., Madueño, F.
, Andersen, S. U. & Ratet, P. (2018).
Lotus japonicus NOOT-BOP-COCH-LIKE1 is essential for nodule, nectary, leaf and flower development.
Plant Journal,
94(5), 880-894.
https://doi.org/10.1111/tpj.13905
Hashiguchi, M., Tanaka, H., Muguerza, M., Akashi, R.
, Sandal, N. N., Andersen, S. U. & Sato, S. (2018).
Lotus japonicus Genetic, Mutant, and Germplasm Resources.
Current protocols in plant biology,
3(2), e20070. Artikel e20070.
https://doi.org/10.1002/cppb.20070
Karlsson, P., Droce, A., Moser, J. M., Cuhlmann, S., Padilla, C. O., Heimann, P., Bartsch, J. W.
, Füchtbauer, A., Füchtbauer, E.-M. & Schmitt-John, T. (2013).
Loss of vps54 function leads to vesicle traffic impairment, protein mis-sorting and embryonic lethality.
International Journal of Molecular Sciences (Online),
14(6), 10908-10925.
https://doi.org/10.3390/ijms140610908,
https://doi.org/doi:10.3390/ijms140610908
Jensen, N., Daa Schrøder, H., Kildall Hejbøl, E.
, Füchtbauer, E.-M., de Oliveira, J. R. M.
& Pedersen, L. (2013).
Loss of function of Slc20a2 associated with familial idiopathic basal ganglia calcification in humans causes brain calcifications in mice.
Journal of Molecular Neuroscience,
51(3), 994-999.
https://doi.org/10.1007/s12031-013-0085-6
Thorsen, K., Dam, V. S., Kjaer-Sorensen, K., Pedersen, L. N., Skeberdis, V. A., Jurevičius, J., Treinys, R., Petersen, I. M. B. S., Nielsen, M. S.
, Oxvig, C., Morth, J. P., Matchkov, V. V., Aalkjær, C., Bundgaard, H.
& Jensen, H. K. (2017).
Loss-of-activity-mutation in the cardiac chloride-bicarbonate exchanger AE3 causes short QT syndrome.
Nature Communications,
8(1), Artikel 1696.
https://doi.org/10.1038/s41467-017-01630-0
Madsen, L. H., Fukai, E., Radutoiu, E. S., Yost, C. K.
, Sandal, N. N., Schauser, L. & Stougaard, J. (2005).
LORE1, an active low-copy-number TY3-gypsy retrotransposon family in the model legume Lotus japonicus.
Plant. J.,
44, 372-381.
Bertelsen, K., Vad, B., Nielsen, E. H. T., Hansen, S. K., Skrydstrup, T., Otzen, D., Vosegaard, T. & Nielsen, N. C. (2011).
Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: altered structural information in studies of antimicrobial peptides.
Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical,
115(8), 1767-1774.
https://doi.org/10.1021/jp110866g
Poulsen, N. A., Nielsen, E. E.
, Schierup, M. H., Loeschcke, V. & Grønkjær, P. (2006).
Long-term stability and effective population size in North Sea and Baltic Sea cod (Gadus morhua). Molecular Ecology,
15, 321-331.
Tschernoster, N., Erger, F., Kohl, S., Reusch, B., Wenzel, A., Walsh, S., Thiele, H., Becker, C., Franitza, M., Bartram, M. P., Kömhoff, M., Schumacher, L., Kukat, C., Borodina, T., Quedenau, C., Nürnberg, P.
, Rinschen, M. M., Driller, J. H., Pedersen, B. P. ... Altmüller, J. (2023).
Long-read sequencing identifies a common transposition haplotype predisposing for CLCNKB deletions.
Genome Medicine,
15(1), Artikel 62.
https://doi.org/10.1186/s13073-023-01215-1
Salentijn, E. M. J.
, Sandal, N. N., Klein-Lankhorst, R., Lange, W., De Bock, T. S. M.
, Marcker, K. A. & Stiekema, W. J. (1994).
Long-range organization of a satellite DNA family flanking the beet cyst nematode resistance locus (Hs1) on chromosome-1 of B. patellaris and B. procumbens.
Theoretical and Applied Genetics,
89(4), 459-466.
https://doi.org/10.1007/BF00225381
Ntini, E., Louloupi, A., Liz, J., Muino, J. M., Marsico, A.
& Ørom, U. A. V. (2018).
Long ncRNA A-ROD activates its target gene DKK1 at its release from chromatin.
Nature Communications,
9, Artikel 1636.
https://doi.org/10.1038/s41467-018-04100-3
Mortensen, L. M., Lundbye-Christensen, S., Schmidt, E. B., Calder, P. C.
, Schierup, M. H., Tjønneland, A.
, Parner, E. T. & Overvad, K. (2017).
Long-chain n-3 and n-6 polyunsaturated fatty acids and risk of atrial fibrillation: Results from a Danish cohort study.
P L o S One,
12(12), e0190262. Artikel e0190262.
https://doi.org/10.1371/journal.pone.0190262
Lin, M. F., Kheradpour, P., Washietl, S., Parker, B. J.
, Pedersen, J. S. & Kellis, M. (2011).
Locating protein-coding sequences under selection for additional, overlapping functions in 29 mammalian genomes.
Genome Research,
21(11), 1916-28.
https://doi.org/10.1101/gr.108753.110
Sorensen, E. S., Rasmussen, L. K., Moller, L., Jensen, P. H., Hojrup, P.
& Petersen, T. E. (1994).
Localization of transglutaminase-reactive glutamine residues in bovine osteopontin.
Biochemical Journal,
304(1), 13-16.
https://doi.org/10.1042/bj3040013
Bonno, M.
, Oxvig, C., Kephart, G. M., Wagner, J. M.
, Kristensen, T., Sottrup-Jensen, L. & Gleich, G. J. (1994).
Localization of pregnancy-associated plasma protein-A and colocalization of pregnancy-associated plasma protein-A messenger ribonucleic acid and eosinophil granule major basic protein messenger ribonucleic acid in placenta.
Laboratory Investigation,
71(4), 560-566.
http://www.ncbi.nlm.nih.gov/pubmed/7526035
Christensen, B. M., Sørensen, E. S., Højrup, P.
, Petersen, T. E. & Rasmussen, L. K. (1996).
Localization of potential transglutaminase cross-linking sites in bovine caseins.
Journal of Agricultural and Food Chemistry,
44(7), 1943-1947.
https://doi.org/10.1021/jf9602131
Thomsen, R., Libri, D., Boulay, J., Rosbash, M.
& Jensen, T. H. (2003).
Localization of nuclear retained mRNAs in Saccharomyces cerevisiae.
RNA,
9, 1049-1057.
https://doi.org/10.1261/rna.5170303
Husted, L. B.
, Sørensen, E. S., Armstrong, P. B., Quigley, J. P.
, Kristensen, L. & Sottrup-Jensen, L. (2002).
Localization of carbohydrate attachment sites and disulfide bridges in limulus alpha 2-macroglobulin. Evidence for two forms differing primarily in their bait region sequences.
Journal of Biological Chemistry,
277(46), 43698-43706.
Chen, B. K., Leiferman, K. M., Pittelkow, M. R., Overgaard, M. T.
, Oxvig, C. & Conover, C. A. (2003).
Localization and regulation of pregnancy-associated plasma protein a expressionin healing human skin.
Journal of Clinical Endocrinology and Metabolism,
88, 4465-4471.
Albertsen, M., Teperek, M.
, Elholm, G., Füchtbauer, E.-M. & Lykke-Hartmann, K. (2010).
Localization and Differential Expression of the Krüppel-Associated Box Zinc Finger Proteins 1 and 54 in Early Mouse Development.
D N A and Cell Biology,
29(10), 589-601.
https://doi.org/10.1089/dna.2010.1040
Rojek, A., Füchtbauer, E.-M., Füchtbauer, A., Jelen, S., Malmendal, A., Fenton, R. A. & Nielsen, S. (2013).
Liver-specific Aquaporin 11 knockout mice show rapid vacuolization of the rough endoplasmic reticulum in periportal hepatocytes after feeding amino acids.
American Journal of Physiology: Gastrointestinal and Liver Physiology,
304(5), G501-G515.
https://doi.org/10.1152/ajpgi.00208.2012
Frislev, H. K. S., Jessen, C. M., Oliveira, C. L. P., Pedersen, J. S. & Otzen, D. E. (2016).
Liprotides made of α-lactalbumin and cis fatty acids form core-shell and multi-layer structures with a common membrane-targeting mechanism.
B B A - Proteins and Proteomics,
1864(7), 847-859.
https://doi.org/10.1016/j.bbapap.2016.04.003
Maolanon, N. N.
, Blaise, M., Sørensen, K. K., Thygesen, M. B., Cló, E., Sullivan, J. T., Ronson, C. W.
, Stougaard, J., Blixt, K. O. & Jensen, K. J. (2014).
Lipochitin Oligosaccharides Immobilized through Oximes in Glycan Microarrays Bind LysM Proteins.
ChemBioChem,
15(3), 425-434.
https://doi.org/10.1002/cbic.201300520
Andersen, C., Grønnemose, A. L., Pedersen, J. N., Nowak, J. S., Christiansen, G., Nielsen, J., Mulder, F. A. A., Otzen, D. E. & Jørgensen, T. J. D. (2021).
Lipid Peroxidation Products HNE and ONE Promote and Stabilize Alpha-Synuclein Oligomers by Chemical Modifications.
Biochemistry,
60(47), 3644-3658.
https://doi.org/10.1021/acs.biochem.1c00478
Jørgensen, P., Milkovic, L., Zarkovic, N., Waeg, G.
& Rattan, S. I. S. (2014).
Lipid peroxidation-derived 4-hydroxynonenal-modified proteins accumulate in human facial skin fibroblasts during ageing in vitro.
Biogerontology,
15(1), 105-110.
https://doi.org/10.1007/s10522-013-9482-z
Sprenger, R. R., Ostenfeld, M. S., Bjørnshave, A.
, Rasmussen, J. T. & Ejsing, C. S. (2024).
Lipidomic Characterization of Whey Concentrates Rich in Milk Fat Globule Membranes and Extracellular Vesicles.
Biomolecules,
14(1), Artikel 55.
https://doi.org/10.3390/biom14010055
Song, P., Yang, C., Thomsen, J. S., Dagnaes-Hansen, F., Jakobsen, M., Bruel, A., Deleuran, B. & Kjems, J. (2019).
Lipidoid-siRNA Nanoparticle-Mediated IL-1 beta Gene Silencing for Systemic Arthritis Therapy in a Mouse Model.
Molecular Therapy,
27(8), 1424-1435.
https://doi.org/10.1016/j.ymthe.2019.05.002
Subrizi, A., Yang, C., Ilmarinen, T., Skottman, H., Urtti, A.
& Kjems, J. (2018).
Lipidoid-siRNA formulations promote gene silencing in differentiated and nondividing ARPE-19, primary porcine and human embryonic stem cell-derived retinal pigment epithelial cells. Abstract fra Annual Meeting of the Association-for-Research-in-Vision-and-Ophthalmology (ARVO), Honolulu.
https://iovs.arvojournals.org/article.aspx?articleid=2693003&resultClick=1