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Julie Elisabeth Heggelund

Researcher - Department of Immunology

Email j.e.heggelund@medisin.uio.no

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Visiting address Sognsvannsveien 20 Rikshospitalet 0372 Oslo

Postal address Postboks 4950 Nydalen OUS HF Rikshospitalet 0424 Oslo

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Academic interests

I'm currently part of a multidisciplinary project on celiac disease at IMMI at Rikshospitalet. We aim to decipher the immunological mechanisms behind the development of the disease. My part of the project consists of studying the binding between gluten peptides from food and antibodies produced by the body, using methods such as X-ray crystallography, phage display and electron microscopy.

My postdoc project focused on membrane proteins involved in multiresistant tuberculosis. The project was a FRIPRO mobility project financed by the Research Council of Norway. I spent the first two years at the University of Leeds, UK, and the last year in the Økstad group at the Department of Pharmacy, including a collaboration with the Luecke group at NCMBM.

My PhD project focused on the X-ray crystallographic studies of the cholera toxin (from V. cholerae) and the heat-labile enterotoxin (from ETEC). In addition, I have investigated the binding of different ligands to the toxins using the methods SPR, ELISA, NMR and MST, including cell biology work. My main findings include five X-ray structures of the cholera toxin binding different blood-group oligosaccharides, complemented by SPR and STD-NMR data (Heggelund et al., PLOS Pathogens, 2016). The PhD project was supervised by Professor Ute Krengel. For more information, visit the Bacterial toxins webpage.

LinkedIn: no.linkedin.com/in/jeheggelund

Teaching

Lecturer in KJM1140 Autumn 2019 and Spring 2022 - Biochemistry 1 for chemists

Group teacher in the following subjects:

KJM1001 - Introduction to chemistry
KJM5310/9310 - Biomolecular structure and function
KJM4350 - Protein crystallography
MBV-KJM1030 - General chemistry and biological chemistry
KJM2200V - Biological chemistry for teachers
MBV3070 - Bioinformatics

Speaker at the following popular science events:

Unveiling of the Hassel exhibition, Department of Chemistry, 2019
Realistforeningens REALfrokost, 2016
The new Life Science building exhibition, 2014
Faglig pedagogisk dag, 2012/2013
Kjemi1-dagen, 2013/2014
Kjemi Grand Prix, 2012

Co-supervisor of students:

Helene, Master student, 60 stp, 2016
Tobias, KJM3020 - Undergraduate research, 20 stp, 2015
Victoria, KJM2020 - Undergraduate research, 20 stp, 2014
Daniel, Master student, 60 stp, 2015
Njáll, KJM2020, Undergraduate research, 20 stp, 2012
Aleksandra, ERASMUS project, 30 stp, 2012
Przemysław, ERASMUS project, 30 stp, 2011

Background

PhD in Structural biology, Department of Chemistry, UiO - 2015
- PhD thesis "Cholera toxin - carbohydrate interaction as the basis for cholera blood-group dependence" supervised by Prof. Ute Krengel
MSc in Molecular biosciences, IBV, UiO - 2011
- Master thesis "Human Endonuclease V - Cloning, expression, purification and biochemical characterization" supervised by Dr. Bjørn Dalhus, OUS.
BSc in Molecular biology and biological chemistry, IBV, UiO - 2009

Tags: Chemistry, Biological chemistry, Life Science, Antibiotic resistance

Heggelund, Julie Elisabeth; Ahmad, Ahmad Ali; Johannesen, Marie Kongshaug; Sekulic, Nikolina & Sollid, Ludvig Magne (2026). Cryo-EM structure of the complex between transglutaminase 2 and the 45 kDa domain of fibronectin. Journal of Biological Chemistry. ISSN 0021-9258. 302(9), p. 1–11. doi: 10.1016/j.jbc.2026.113326. Full text in Research Archive
Iversen, Rasmus; Heggelund, Julie Elisabeth; Das, Saykat; Høydahl, Lene Støkken & Sollid, Ludvig Magne (2025). Enzyme-activating B-cell receptors boost antigen presentation to pathogenic T cells in gluten-sensitive autoimmunity. Nature Communications. 16. doi: 10.1038/s41467-025-57564-5. Full text in Research Archive Show summary
Autoantibodies against the enzyme transglutaminase 3 (TG3) are characteristic to the gluten-sensitive skin disorder dermatitis herpetiformis (DH), which is an extraintestinal manifestation of celiac disease. We here demonstrate that TG3-specific B cells can activate gluten-specific CD4+ T cells through B-cell receptor (BCR)-mediated internalization of TG3-gluten enzyme-substrate complexes. Stereotypic anti-TG3 antibodies using IGHV2-5/IGKV4-1 gene segments enhance the catalytic activity of TG3, and this effect translates into increased gluten presentation to T cells when such antibodies are expressed as BCRs. The crystal structure of TG3 bound to an IGHV2-5/IGKV4-1 Fab shows that antibody binding to a β-sheet in the catalytic core domain causes the enzyme to adopt the active conformation. This mechanism explains the production of stereotypic anti-TG3 autoantibodies in DH and highlights a role for TG3-specific B cells as antigen-presenting cells for gluten-specific T cells. Similar boosting effects of autoreactive BCRs could be relevant for other autoimmune diseases, including rheumatoid arthritis.
Heggelund, Julie Elisabeth; Das, Saykat; Stamnæs, Jorunn; Iversen, Rasmus & Sollid, Ludvig Magne (2023). Autoantibody binding and unique enzyme-substrate intermediate conformation of human transglutaminase 3. Nature Communications. 14:6216 (1), p. 1–11. doi: 10.1038/s41467-023-42004-z. Full text in Research Archive Show summary
Abstract Transglutaminase 3 (TG3), the autoantigen of dermatitis herpetiformis (DH), is a calcium dependent enzyme that targets glutamine residues in polypeptides for either transamidation or deamidation modifications. To become catalytically active TG3 requires proteolytic cleavage between the core domain and two C-terminal β-barrels (C1C2). Here, we report four X-ray crystal structures representing inactive and active conformations of human TG3 in complex with a TG3-specific Fab fragment of a DH patient derived antibody. We demonstrate that cleaved TG3, upon binding of a substrate-mimicking inhibitor, undergoes a large conformational change as a β-sheet in the catalytic core domain moves and C1C2 detaches. The unique enzyme-substrate conformation of TG3 without C1C2 is recognized by DH autoantibodies. The findings support a model where B-cell receptors of TG3-specific B cells bind and internalize TG3-gluten enzyme-substrate complexes thereby facilitating gluten-antigen presentation, T-cell help and autoantibody production.
Heggelund, Julie Elisabeth; Heim, Joel Benjamin; Bajc, Gregor; Hodnik, Vesna; Anderluh, Gregor & Krengel, Ute (2019). Specificity of Escherichia coli heat-Labile enterotoxin investigated by single-site mutagenesis and crystallography. International Journal of Molecular Sciences. ISSN 1661-6596. 20(3). doi: 10.3390/ijms20030703. Full text in Research Archive Show summary
Diarrhea caused by enterotoxigenic Escherichia coli (ETEC) is one of the leading causes of mortality in children under five years of age and is a great burden on developing countries. The major virulence factor of the bacterium is the heat-labile enterotoxin (LT), a close homologue of the cholera toxin. The toxins bind to carbohydrate receptors in the gastrointestinal tract, leading to toxin uptake and, ultimately, to severe diarrhea. Previously, LT from human- and porcine-infecting ETEC (hLT and pLT, respectively) were shown to have different carbohydrate-binding specificities, in particular with respect to N-acetyllactosamine-terminating glycosphingolipids. Here, we probed 11 single-residue variants of the heat-labile enterotoxin with surface plasmon resonance spectroscopy and compared the data to the parent toxins. In addition we present a 1.45 Å crystal structure of pLTB in complex with branched lacto-N-neohexaose (Galβ4GlcNAcβ6[Galβ4GlcNAcβ3]Galβ4Glc). The largest difference in binding specificity is caused by mutation of residue 94, which links the primary and secondary binding sites of the toxins. Residue 95 (and to a smaller extent also residues 7 and 18) also contribute, whereas residue 4 shows no effect on monovalent binding of the ligand and may rather be important for multivalent binding and avidity.
Heim, Joel Benjamin; Hodnik, Vesna; Heggelund, Julie Elisabeth; Anderluh, Gregor & Krengel, Ute (2019). Crystal structures of cholera toxin in complex with fucosylated receptors point to importance of secondary binding site. Scientific Reports. 9 . doi: 10.1038/s41598-019-48579-2. Full text in Research Archive Show summary
Cholera is a life-threatening diarrhoeal disease caused by the human pathogen Vibrio cholerae. Infection occurs after ingestion of the bacteria, which colonize the human small intestine and secrete their major virulence factor – the cholera toxin (CT). The GM1 ganglioside is considered the primary receptor of the CT, but recent studies suggest that also fucosylated receptors such as histo-blood group antigens are important for cellular uptake and toxicity. Recently, a special focus has been on the histo-blood group antigen Lewisx (Lex), however, where and how the CT binds to Lex remains unclear. Here we report the high-resolution crystal structure (1.5 Å) of the receptor-binding B-subunits of the CT bound to the Lex trisaccharide, and complementary quantitative binding data for CT holotoxins. Lex, and also L-fucose alone, bind to the secondary binding site of the toxin, distinct from the GM1 binding site. In contrast, fucosyl-GM1 mainly binds to the primary binding site due to high-affinity interactions of its GM1 core. Lex is the first histo-blood group antigen of non-secretor phenotype structurally investigated in complex with CT. Together with the quantitative binding data, this allows unique insight into why individuals with non-secretor phenotype are more prone to severe cholera than so-called ‘secretors’.
Bjerregaard-Andersen, Kaare; Johannesen, Hedda; Abdel-Rahman, Noha Mansour Hassan; Heggelund, Julie Elisabeth; Hoås, Helene Mykland & Abraha, Fana [Show all 13 contributors for this article] (2018). Crystal structure of an L chain optimised 14F7 anti-ganglioside Fv suggests a unique tumour- specificity through an unusual H-chain CDR3 architecture. Scientific Reports. 8:10836, p. 1–11. doi: 10.1038/s41598-018-28918-5. Full text in Research Archive Show summary
Targeted cancer immunotherapy offers increased efficacy concomitantly with reduced side effects. One antibody with promising clinical potential is 14F7, which specifically recognises the NeuGc GM3 ganglioside. This antigen is found in the plasma membrane of a range of tumours, but is essentially absent from healthy human cells. 14F7 can discriminate NeuGc GM3 from the very similar NeuAc GM3, a common component of cell membranes. The molecular basis for this unique specificity is poorly understood. Here we designed and expressed 14F7-derived single-chain Fvs (scFvs), which retained the specificity of the parent antibody. Detailed expression and purification protocols are described as well as the synthesis of the NeuGc GM3 trisaccharide. The most successful scFv construct, which comprises an alternative variable light chain (VLA), allowed structure determination to 2.2 Å resolution. The structure gives insights into the conformation of the important CDR H3 loop and the suspected antigen binding site. Furthermore, the presence of VLA instead of the original VL elucidates how this subdomain indirectly stabilises the CDR H3 loop. The current work may serve as a guideline for the efficient production of scFvs for structure determination.
Hatlem, Daniel; Heggelund, Julie Elisabeth; Burschowsky, Daniel; Krengel, Ute & Kristiansen, Per Eugen (2017). 1H, 13C, 15N backbone assignment of the human heat-labile enterotoxin B-pentamer and chemical shift mapping of neolactotetraose binding. Biomolecular NMR Assignments. ISSN 1874-2718. 11(1), p. 99–104. doi: 10.1007/s12104-017-9728-9. Full text in Research Archive Show summary
The major virulence factor of enterotoxigenic Escherichia coli is the heat-labile enterotoxin (LT), an AB5 toxin closely related to the cholera toxin. LT consists of six subunits, the catalytically active A-subunit and five B-subunits arranged as a pentameric ring (LTB), which enable the toxin to bind to the epithelial cells in the intestinal lumen. LTB has two recognized binding sites; the primary binding site is responsible for anchoring the toxin to its main receptor, the GM1-ganglioside, while the secondary binding site recognizes blood group antigens. Herein, we report the 1H, 13C, 15N main chain assignment of LTB from human isolates (hLTB; 103 a.a. per subunit, with a total molecular mass of 58.5 kDa). The secondary structure was predicted based on 13C′, 13Cα, 13Cβ, 1HN and 15N chemical shifts and compared to a published crystal structure of LTB. Neolactotetraose (NEO) was titrated to hLTB and chemical shift perturbations were measured. The chemical shift perturbations were mapped onto the crystal structure, confirming that NEO binds to the primary binding site of hLTB and competes with GM1-binding. Our new data further lend support to the hypothesis that binding at the primary binding site is transmitted to the secondary binding site of the toxin, where it may influence the binding to blood group antigens. This research was first published in Biomolecular NMR Assignments. © Springer Verlag.
Heggelund, Julie Elisabeth; Varrot, Annabelle; Imberty, Anne & Krengel, Ute (2017). Histo-blood group antigens as mediators of infections. Current Opinion in Structural Biology. ISSN 0959-440X. 44, p. 190–200. doi: 10.1016/j.sbi.2017.04.001. Full text in Research Archive
Heggelund, Julie Elisabeth; Mackenzie, Alasdair; Martinsen, Tobias; Heim, Joël Benjamin; Cheshev, Pavel & Bernardi, Anna [Show all 7 contributors for this article] (2017). Towards new cholera prophylactics and treatment: Crystal structures of bacterial enterotoxins in complex with GM1 mimics. Scientific Reports. 7(2326). doi: 10.1038/s41598-017-02179-0. Full text in Research Archive Show summary
Cholera is a life-threatening disease in many countries, and new drugs are clearly needed. C-glycosidic antagonists may serve such a purpose. Here we report atomic-resolution crystal structures of three such compounds in complexes with the cholera toxin. The structures give unprecedented atomic details of the molecular interactions and show how the inhibitors efficiently block the GM1 binding site. These molecules are well suited for development into low-cost prophylactic drugs, due to their relatively easy synthesis and their resistance to glycolytic enzymes. One of the compounds links two toxin B-pentamers in the crystal structure, which may yield improved inhibition through the formation of toxin aggregates. These structures can spark the improved design of GM1 mimics, either alone or as multivalent inhibitors connecting multiple GM1-binding sites. Future developments may further include compounds that link the primary and secondary binding sites. Serving as decoys, receptor mimics may lessen symptoms while avoiding the use of antibiotics.
Heggelund, Julie Elisabeth; Burschowsky, Daniel; Bjørnestad, Victoria Ariel; Hodnik, Vesna; Anderluh, Gregor & Krengel, Ute (2016). High-Resolution Crystal Structures Elucidate the Molecular Basis of Cholera Blood Group Dependence. PLoS Pathogens. ISSN 1553-7366. 12(4), p. e1005567–e1005567. doi: 10.1371/journal.ppat.1005567. Full text in Research Archive Show summary
Cholera is the prime example of blood-group-dependent diseases, with individuals of blood group O experiencing the most severe symptoms. The cholera toxin is the main suspect to cause this relationship. We report the high-resolution crystal structures (1.1–1.6 Å) of the native cholera toxin B-pentamer for both classical and El Tor biotypes, in complexes with relevant blood group determinants and a fragment of its primary receptor, the GM1 ganglioside. The blood group A determinant binds in the opposite orientation compared to previously published structures of the cholera toxin, whereas the blood group H determinant, characteristic of blood group O, binds in both orientations. H-determinants bind with higher affinity than A-determinants, as shown by surface plasmon resonance. Together, these findings suggest why blood group O is a risk factor for severe cholera.
Heggelund, Julie Elisabeth; Bjørnestad, Victoria Ariel & Krengel, Ute (2015). Vibrio cholerae and Escherichia coli heat-labile enterotoxins and beyond. In Alouf, Joseph E; Ladant, Daniel & Popoff, Michel R (Ed.), The Comprehensive Sourcebook of Bacterial Protein Toxins, Fourth Edition. Elsevier. ISSN 9780128001882. p. 195–229. doi: 10.1016/B978-0-12-800188-2.00007-0. Full text in Research Archive Show summary
After a brief introduction highlighting the importance of the topic today, this chapter gives a historic review of cholera through the ages, including the discovery of the Vibrio cholerae bacterium and identification of its major virulence factor, the cholera toxin. It proceeds by describing homologous toxins of this growing family, such as the heat-labile enterotoxin from enterotoxigenic Escherichia coli strains (ETEC), which causes traveler’s diarrhea, followed by the description of the toxins’ three-dimensional (3D) structures and their interaction with intestinal receptors. The next section is devoted to the biological mechanisms by which cholera toxin and E. coli heat-labile enterotoxin mediate diarrhea. Finally, the text describes the toxins’ gene organization, regulation, and biogenesis, how toxins use environmental signals to optimize their biological effects, and how the cholera toxin and the toxin co-regulated pilus act together to cause disease. It then concludes by highlighting the recent advances and remaining mysteries, and by providing a link to toxin-based drug design.
Vasile, Francesca; Reina, José J.; Potenza, Donatella; Heggelund, Julie Elisabeth; Mackenzie, Alasdair & Krengel, Ute [Show all 7 contributors for this article] (2014). Comprehensive analysis of blood group antigen binding to classical and El Tor cholera toxin B-pentamers by NMR. Glycobiology. ISSN 0959-6658. 24(8), p. 766–778. doi: 10.1093/glycob/cwu040. Full text in Research Archive
Heggelund, Julie Elisabeth; Haugen, Espen; Lygren, Birgitte; Mackenzie, Alasdair; Roclöv, Åsa Holmner & Vasile, Francesca [Show all 9 contributors for this article] (2012). Both El Tor and classical cholera toxin bind blood group determinants. Biochemical and Biophysical Research Communications - BBRC. ISSN 0006-291X. 418(4), p. 731–735. doi: 10.1016/j.bbrc.2012.01.089. Full text in Research Archive
Fladeby, Cathrine; Vik, Erik Sebastian; Lærdahl, Jon Kristen; Neurauter, Christine Gran; Heggelund, Julie Elisabeth & Thorgaard, Eirik [Show all 10 contributors for this article] (2012). The Human Homolog of Escherichia coli Endonuclease V Is a Nucleolar Protein with Affinity for Branched DNA Structures. PLOS ONE. 7(11). doi: 10.1371/journal.pone.0047466. Full text in Research Archive

View all works in NVA

Heggelund, Julie Elisabeth (2026). Activating antibodies in Dermatitis Herpetiformis: X-ray crystal structures. Full text in Research Archive
Heggelund, Julie Elisabeth (2025). Interpreting crystal structures as a non-crystallographer. Full text in Research Archive
Heggelund, Julie Elisabeth & Iversen, Rasmus (2025). Article prize presentation: Enzyme-activating B-cell receptors boost antigen presentation to pathogenic T cells in gluten-sensitive autoimmunity. Full text in Research Archive
Heggelund, Julie Elisabeth (2025). Transglutaminase 3 – structure explains function. Full text in Research Archive
Heggelund, Julie Elisabeth (2025). Hvordan binder antistoffer hos DH-pasienter transglutaminase 3? Full text in Research Archive
Heggelund, Julie Elisabeth (2025). 3D structures of Transglutaminase 3 explains the effect of autoantibodies. Full text in Research Archive
Heggelund, Julie Elisabeth (2025). Modulating the activity of Transglutaminase 3. Full text in Research Archive
Heggelund, Julie Elisabeth (2023). Structural studies of transglutaminase 3. Full text in Research Archive
Heggelund, Julie Elisabeth (2023). Poster: Autoantibody binding and unique enzyme-substrate intermediate conformation of human transglutaminase 3. Full text in Research Archive
Heggelund, Julie Elisabeth (2023). Four crystal structures give insights into the enzymatic mechanism of transglutaminase 3. ESRF Highlight, Spotlight on Science. Full text in Research Archive
Heggelund, Julie Elisabeth (2022). Structural studies of Transglutaminase 3. Full text in Research Archive
Heggelund, Julie Elisabeth (2022). Phage display to improve the lives of celiac disease patients. Full text in Research Archive
Heggelund, Julie Elisabeth (2022). Poster: Phage display to improve the lives of celiac disease patients. Full text in Research Archive
Heggelund, Julie Elisabeth (2020). Development of inhibitors of drug-efflux transporters to fight antibiotic resistance. Full text in Research Archive
Heggelund, Julie Elisabeth (2020). Development of inhibitors of drug-efflux transporters to fight antibiotic resistance. Full text in Research Archive
Heggelund, Julie Elisabeth (2020). Legemidler mot sykdommer i sentralnervesystemet kan hjelpe mot antibiotikaresistens. Full text in Research Archive
Heggelund, Julie Elisabeth (2020). Tuberkulose-vaksine i kampen mot SARS-CoV-2. Full text in Research Archive
Heggelund, Julie Elisabeth (2019). Development of inhibitors of drug-efflux transporters to fight antibiotic resistance (IBA). Full text in Research Archive
Heggelund, Julie Elisabeth (2019). Medisinsk forskning må bli mer fantasifull og åpen hvis vi skal lykkes i å lage nye, gode legemidler for framtiden. Full text in Research Archive
Heggelund, Julie Elisabeth (2019). Development of inhibitors of drug-efflux transporters to fight antibiotic resistance. Full text in Research Archive
Heggelund, Julie Elisabeth (2019). High-resolution crystal structures elucidate the molecular basis of cholera blood group dependence. Full text in Research Archive
Heggelund, Julie Elisabeth; Heim, Joel Benjamin & Krengel, Ute (2019). Cholera blood group association elucidated with synchrotron radiation. Full text in Research Archive
Johannesen, Hedda; Bjerregaard-Andersen, Kaare; Heggelund, Julie Elisabeth; Løset, Geir Åge & Krengel, Ute (2019). 14F7 - A tumour specific antibody. Full text in Research Archive
Heggelund, Julie Elisabeth; Hausvik, Emil; Carvalho, Luiz; Økstad, Ole Andreas Løchen; Martinez, Aurora & Goldman, Adrian (2018). Targeting MFS transporters to switch off antibiotic resistance in tuberculosis. Full text in Research Archive
Heggelund, Julie Elisabeth (2018). The constant threat from infectious disease: From cholera to antibiotic resistance. Full text in Research Archive
Heggelund, Julie Elisabeth (2018). LCP-krystallisering på synkrotronen. www.mn.uio.no/farmasi. Full text in Research Archive
Heggelund, Julie Elisabeth (2018). Combatting antibiotic resistance: Targeting MFS transporters from Mycobacterium tuberculosis. Full text in Research Archive
Johannesen, Hedda; hoås, Helene Mykland; Heggelund, Julie Elisabeth; Bjerregaard-Andersen, Kaare; Løset, Geir Åge & Krengel, Ute (2018). 14F7, An anti-ganglioside scFv for cancer therapies. Full text in Research Archive
Johannesen, Hedda; Mykland, Helene Hoås; Heggelund, Julie Elisabeth; Bjerregaard-Andersen, Kaare; Løset, Geir Åge & Krengel, Ute (2018). An anti-ganglioside scFv for cancer therapies. Full text in Research Archive
Johannesen, Hedda; Hoås, Helene Mykland; Heggelund, Julie Elisabeth; Bjerregaard-Andersen, Kaare; Løset, Geir Åge & Krengel, Ute (2018). 14F7, an antibody that recognises a tumour-specific ganglioside with high specificity. Full text in Research Archive
Johannesen, Hedda; Bjerregaard-Andersen, Kaare; Heggelund, Julie Elisabeth; Løset, Geir Åge & Krengel, Ute (2018). NeuGc GM3 - a cancer-specific ganglioside that is recognised by the antibody 14F7. Full text in Research Archive
Heggelund, Julie Elisabeth (2017). Crystal structures of bacterial enterotoxins in complex with GM1 inhibitors: towards new cholera prophylactics and treatment. Full text in Research Archive
Heggelund, Julie Elisabeth (2017). Bakterier sender antibiotika ut av cellene før de rekker å virke. www.mn.uio.no/farmasi. Full text in Research Archive
Heggelund, Julie Elisabeth (2017). Selvlysende tuberkuloseproteiner. www.mn.uio.no/farmasi. Full text in Research Archive
Heim, Joël Benjamin; Heggelund, Julie Elisabeth & Krengel, Ute (2016). Cholera blood-group dependence and role of secretor status. Full text in Research Archive
Heim, Joël Benjamin; Heggelund, Julie Elisabeth & Krengel, Ute (2016). Cholera blood-group dependence and role of secretor status. Full text in Research Archive
Heggelund, Julie Elisabeth (2016). High-Resolution Crystal Structures Elucidate the Molecular Basis of Cholera Blood Group Dependence. Full text in Research Archive
Heggelund, Julie Elisabeth & Manna, Dipankar (2016). Proteiner fra sopp kan drepe kreftceller. Titan.uio.no. Full text in Research Archive
Heggelund, Julie Elisabeth (2016). REALfrokost: Kolera rammer mennesker med blodtype 0 hardest. Full text in Research Archive
Heggelund, Julie Elisabeth (2016). Kolera rammer mennesker med blodtype 0 hardest. Forskning.no. ISSN 1891-635X. Full text in Research Archive
Heggelund, Julie Elisabeth (2016). Derfor rammes de med blodtype 0 hardest av kolera. Titan.uio.no. Full text in Research Archive
Heggelund, Julie Elisabeth (2016). Siste nytt fra proteinkrystallografiens høyborg. NBS-nytt. ISSN 0801-3535. 1, p. 36–37. Full text in Research Archive
Heim, Joël Benjamin; Heggelund, Julie Elisabeth & Krengel, Ute (2016). How does blood group secretor status protect from cholera intoxication? – Structure and interaction analysis of carbohydrate binding. Full text in Research Archive
Heggelund, Julie Elisabeth (2015). Blood group oligosaccharide binding to cholera toxin revealed by X-ray crystallography. Full text in Research Archive
Heggelund, Julie Elisabeth (2015). Blood group oligosaccharide binding to cholera toxin revealed by X-ray crystallography. Full text in Research Archive
Heggelund, Julie Elisabeth (2015). High-resolution X-ray structures reveal the cholera toxin binding to blood group oligosaccharides. Full text in Research Archive
Heggelund, Julie Elisabeth (2015). Cholera blood-group dependence and protection by human milk elucidated by SPR and X-ray crystallography. Full text in Research Archive
Heggelund, Julie Elisabeth (2014). Cholera’s blood-group dependence elucidated by X-ray crystallography and ELISA. Full text in Research Archive
Hatlem, Daniel; Heggelund, Julie Elisabeth; Burschowsky, Daniel; Kristiansen, Per Eugen & Krengel, Ute (2014). Characterization of Lipopolysaccharide Binding to the E.coli Heat-labile Enterotoxin. Full text in Research Archive
Heggelund, Julie Elisabeth; Prydz, Kristian & Krengel, Ute (2014). Cholera blood-group dependence investigated by X-ray crystallography, CaCo-2 cells and ELISA. Full text in Research Archive
Heggelund, Julie Elisabeth (2014). Cholera blood-group dependence elucidated by X-ray crystallography, ELISA and SPR. Full text in Research Archive
Heggelund, Julie Elisabeth (2014). Mine drømmer om det nye livsvitenskapsbygget. Full text in Research Archive
Hatlem, Daniel; Heggelund, Julie Elisabeth; Burschowsky, Daniel; Kristiansen, Per Eugen & Krengel, Ute (2013). Characterization of Lipopolysaccharide binding to E.coli Heat-labile Enterotoxin. Full text in Research Archive
Heggelund, Julie Elisabeth & Krengel, Ute (2013). Kolera og blodgrupper. Full text in Research Archive
Heggelund, Julie Elisabeth (2013). Kolera på atomnivå 2. Full text in Research Archive
Heggelund, Julie Elisabeth (2013). Cholera toxin - and binding to blood group glycans. Full text in Research Archive
Heggelund, Julie Elisabeth; Prydz, Kristian & Krengel, Ute (2013). Cholera toxin's blood-group dependence investigated with CaCo-2 cells and ELISA. Full text in Research Archive
Heggelund, Julie Elisabeth & Krengel, Ute (2013). Exploring Cholera Toxin and Heat-Labile Enterotoxin Binding Specificity using SPR and Protein NMR. Full text in Research Archive
Krengel, Ute; Heggelund, Julie Elisabeth & Jemterud, Torkild (2012). Interview om Nobel pris i Kjemi 2012. [Radio]. NRK (podcast Ekko viten). Full text in Research Archive
Heggelund, Julie Elisabeth & Krengel, Ute (2012). Kjemi Grand Prix - Molecular basis of cholera blood group dependence. Full text in Research Archive
Heggelund, Julie Elisabeth & Krengel, Ute (2012). From heat-labile enterotoxin to cholera toxin - residue by residue. Full text in Research Archive
Heggelund, Julie Elisabeth (2012). Kolera - Røntgenstråler og blodtyper. Full text in Research Archive
Heggelund, Julie Elisabeth (2012). Kolera på atomnivå. Full text in Research Archive
Heggelund, Julie Elisabeth & Krengel, Ute (2012). Molecular basis of cholera blood group dependence. Full text in Research Archive
Heggelund, Julie Elisabeth (2012). Molecular basis of cholera blood group dependence. Full text in Research Archive
Vogt, Yngve; Krengel, Ute & Heggelund, Julie Elisabeth (2012). Røntgenkjemiker løser koleragåte. [Journal]. Apollon. Full text in Research Archive
Heggelund, Julie Elisabeth (2011). Human Endonuclease V has specific affinity for branched DNA. Full text in Research Archive
Heggelund, Julie Elisabeth; Krengel, Ute & Prydz, Kristian (2015). Cholera toxin – carbohydrate interaction as the basis for cholera blood-group dependence. Akademika publishing. Full text in Research Archive