Nielsen, L.D., Foged, M.M., Albert, A., Bertelsen, A.B., Søltoft, C.L., Robinson, S.D., Petersen, S.V., Purcell, A.W., Olivera, B.M., Norton, R.S., Vasskog, T., Safavi-Hemami, H., Teilum, K. and Ellgaard, L. (2019) The three-dimensional structure of an H-superfamily conotoxin reveals a granulin fold arising from a common ICK cysteine framework. J. Biol. Chem., 294, 8745-8759. DOI:10.1074/jbc.RA119.007491

O’Brien, H., Kanemura, S., Okumura, M., Baskin, R.P., Bandyopadhyay, P.K., Ellgaard, L., Inaba, K. and Safavi-Hemami, H. (2018) Ero1-mediated Reoxidation of PDI accelerates the Folding of Cone Snail Toxins. Int. J. Mol. Sci., 19 (11), 3418; doi: 10.3390/ijms19113418.

Safavi-Hemami, H., Foged, M.M. and Ellgaard, L. (2018) Evolutionary Adaptations to Cysteine-rich Peptide Folding, pp. 99-128, in Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering, ed. M. Feige, Royal Society of Chemistry.

Ellgaard, L., Sevier, C.S. and Bulleid, N.J. (2018) How are Proteins Reduced in the Endoplasmic Reticulum? TiBS, 43, 32-43 (review).

Timms, R.T.*, Menzies, S.A.*, Tchasovnikarova, I.A.*, Christensen, L.C.*, Williamson, J.C., Antrobus, R., Dougan, G., Ellgaard, L. and Lehner, P.J. (2016) Genetic dissection of mammalian ERAD through comparative haploid and CRISPR forward genetic screens. Nat. Commun. 7, Article number: 11786, doi:10.1038/ncomms11786 (*equal contribution).

Safavi-Hemami, H., Li, Q., Jackson, R.L., Song, A.S., Boomsma, W., Bandyopadhyay, P.K., Gruber, C.W., Purcell, A.W., Yandell, M., Olivera, B.M. and Ellgaard, L. (2016) Rapid Expansion of the Protein Disulfide Isomerase Gene Family Facilitates the Folding of Venom Peptides. Proc. Natl. Acad. Sci. USA, 113, 3227-3232 (Faculty of 1000).

Ellgaard, L., McCaul, N., Chatsisvili, A. and Braakman, I. (2016) Co- and post-translational protein folding in the ER. Traffic, 17, 615-638 (invited review).

Boomsma, W.B., Nielsen, S.V., Lindorff-Larsen, K., Hartmann-Petersen, R. and Ellgaard, L. (2016) Bioinformatics analysis identifies several intrinsically disordered human E3 ubiquitin-protein ligases. PeerJ, 4:e1725; DOI 10.7717/peerj.1725.

Safavi-Hemami, H., Gajewiak, J., Karanth, S., Robinson, S.D., Ueberheide, B., Douglass, A.D., Schlegel, A., Imperial, J.S., Watkins, M., Bandyopadhyay, P.K., Yandell, M., Li, Q., Purcell, A.W., Norton, R.S., Ellgaard, L., Olivera, B.M. (2015) Specialized insulin is used for chemical warfare by fish-hunting cone snails. Proc. Natl. Acad. Sci. USA112, 1743-1748PNAS In This Issue highlight; F1000. (press: UCPH press releaseNational GeographicScienceDailyScienceNewScientistScienceNewsAustralian GeographicThe, Spiegel OnlineNeue Zürcher

Hagemann-Jensen, M., Uhlenbrock, F., Kehlet, S., Andresen, L., Gabel-Jensen, C., Ellgaard, L., Gammelgaard, B. and Skov, S. (2014) The Selenium Metabolite Methylselenol Regulates the Expression of Ligands that Trigger Immune Activation through the Lymphocyte Receptor NKG2D. J. Biol. Chem.289, 31576-31590.

Safavi-Hemami, H., Andersen, K.M. and Ellgaard, L. (2014) Giftsnegle som medicinskabe. Aktuel Naturvidenskab2, 12-16 (in Danish / cover).

Hansen, HG, Søltoft, CL, Schmidt, JD, Birk, J., Appenzeller-Herzog, C. and Ellgaard, L. (2014) Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262. Biosci. Rep.34(2):art:e00103.doi:10.1042/

Ramming, T., Hansen, HG, Nagata, K., Ellgaard, L. and Appenzeller-Herzog, C. (2014). GPx8 peroxidase prevents leakage of H2O2 from the endoplasmic reticulum. Free radic. biol. med.70, 106–116.

Poulsen, E.G., Steinhauer, C., Lees, M., Lauridsen, A-M., Ellgaard, L. and Hartmann-Petersen, R. (2012) HUWE1 and TRIP12 collaborate in degradation of ubiquitin-fusion proteins and misframed ubiquitin. PLoS ONE7(11), e50548.

Hansen HG, Schmidt JD, Søltoft CL, Ramming T, Geertz-Hansen HM, Christensen B, Sørensen ES, Juncker AS, Appenzeller-Herzog C, and Ellgaard L. (2012) Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response. J. Biol. Chem.287, 39513-39523.

Christensen LC, Jensen NW, Vala A, Kamarauskaite J, Johansson L, Winther JR, Hofmann K, Teilum K, and Ellgaard L. (2012) The human selenoprotein VCP-interacting membrane protein (VIMP) is non-globular and harbors a reductase function in an intrinsically disordered region. J. Biol. Chem.287, 26388-26399.

Kriegenburg F, Ellgaard L, and Hartmann-Petersen R. (2012) Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation. FEBS J.279, 532-542.

Lynes, E.M., Bui, M., Yap, M.C., Benson, M.D., Schneider, B., Ellgaard, L., Berthiaume, L.G., and Simmen, T. (2012) Palmitoylated TMX and calnexin target to the mitochondria-associated membrane. EMBO J.31457-470.

Bulleid, N. J. and Ellgaard, L. (2011) Multiple ways to make disulfides. TiBS36, 485-492 (review / cover).

Riemer, J., Hansen, H. G., Appenzeller-Herzog, C., Johansson, L. and Ellgaard, L. (2011) Identification of the PDI-family member ERp90 as an interaction partner of ERFAD. PLoS ONE, 6(2), e17037.

Appenzeller-Herzog, C., Riemer, J., Zito, E., Chin, K-T., Ron D., Spiess, M. and Ellgaard, L. (2010) Disulfide production by Ero1α-PDI relay is rapid and effectively regulated. EMBO J., 29, 3318-3329.

Chao R., Nevin L., Agarwal P., Riemer J., Bai X., Delaney A., Akana M., Jimenezlopez N., Bardakjian T., Schneider A., Chassaing N., Schorderet D. F., Fitzpatrick D., Kwok P. Y., Ellgaard L., Gould D. B., Zhang Y., Malicki J., Baier H., Slavotinek A. (2010) A Male with Unilateral Microphthalmia Reveals a Role for TMX3 in Eye Development. PLoS One, 11;5:e10565.

Roth, D., Lynes, E., Riemer, J., Hansen, H. G., Althaus, N., Simmen, T., and Ellgaard, L. (2010) A di-arginine motif contributes to the ER-localization of the type I transmembrane ER oxidoreductase TMX4. Biochem. J.425, 195-295.

Riemer, J., Appenzeller-Herzog, C., Johansson, L.,  Bodenmiller, B., Hartmann-Petersen, R. and Ellgaard, L. (2009) A luminal flavoprotein in endoplasmic reticulum-associated degradation. Proc. Natl. Acad. Sci. USA106, 14831-14836.

Appenzeller-Herzog, C., Riemer, J., Christensen, B., Sørensen, E. S. and Ellgaard, L. (2008) A novel disulfide switch mechanism in Ero1α balances ER oxidation in human cells. EMBO J.27, 2977-87 ("Have you seen...?" commentary by Robert Freedman in EMBO J., 28, 169-170).

Appenzeller-Herzog, C. and Ellgaard, L. (2008) The human protein disulfide isomerase family: Versatility packed into a single fold. Biochim. Biophys. Acta1783, 535-548 (invited review).

Appenzeller-Herzog, C. and Ellgaard, L. (2008) In vivo reduction-oxidation state of protein disulfide isomerase: The two active sites independently occur in the reduced and oxidized forms. Antiox. Redox. Signal.10, 55-64.

Haugstetter, J., Maurer, M. A., Blicher, T., Pagac, M., Wider, G. and Ellgaard, L. (2007) Structure-function analysis of the ER oxidoreductase TMX3: inter-domain stabilization of the N-terminal redox-active domain. J. Biol. Chem.280, 33859-33867.

Schelhaas, M., Pelkmans, L., Malmström, J., Haugstetter, J., Ellgaard, L., Grünewald, K., and Helenius, A. (2007) Simian Virus 40 Depends on ER Protein Folding and Quality Control Factors for Entry into Host Cells. Cell131, 516-529 (Faculty of 1000News and Views).

Kulp, M. S., Frickel, E-M., Ellgaard, L. and Weissman, J. S. (2006) Domain architecture of protein disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation. J. Biol. Chem.281, 876-884 (Paper of the Week).

Haugstetter, J., Blicher, T. and Ellgaard, L. (2005) Identification and characterization of a novel thioredoxin-like transmembrane protein of the endoplasmic reticulum. J. Biol. Chem.280, 8371-8380.

Ellgaard, L. and Ruddock, L.W. (2005) The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep.6, 28-32 (review).

Ellgaard, L. (2004) Catalysis of disulphide bond formation in the endoplasmic reticulum. Biochem. Soc. Trans., 32, 663-667 (review).

Frickel, E-M., Frei, P., Bouvier, M., Stafford, W. F., Helenius, A., Glockshuber, R. and Ellgaard, L. (2004) ERp57 is a multifunctional thiol-disulfide oxidoreductase. J. Biol. Chem., 279, 18277-18287.

Kapoor, M.*, Ellgaard, L.*, Pai, J. G., Schirra, C., Gemma, E., Oscarson, S., Helenius, A. and Surolia, A. (2004) Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: Pivotal roles of Tyrosine-109 and Aspartate-135 in carbohydrate recognition. Biochemistry43, 97-106 (*equal contribution).

Ellgaard, L. and Frickel, E-M. (2003) Calnexin, calreticulin and ERp57: teammates in glycoprotein folding. Cell Biochem. Biophys.39, 223-248 (review).

Ellgaard, L. and Helenius, A. (2003) Quality control in the endoplasmic reticulum. Nature Rev. Mol. Cell Biol.4, 181-191 (review / cover).
Kapoor, M., Srinivas, H., Kandiah, E., Gemma, E., Ellgaard, L., Oscarson, S., Helenius, A. and Surolia, A. (2003) Interactions of substrate with calreticulin, an endoplasmic reticulum chaperone. J. Biol. Chem., 278, 6194-6200.

Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. and Wüthrich, K. (2002) NMR structures of 36- and 73-residue fragments of the calreticulin P-domain. J. Mol. Biol.322, 773-784.

Frickel, E-M., Riek, R., Jelesarov, I., Helenius, A., Wüthrich, K. and Ellgaard, L. (2002) TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc. Natl. Acad. Sci. USA99, 1954-1959 (Faculty of 1000).

Ellgaard, L. and Helenius, A. (2001) ER quality control: towards an understanding at the molecular level. Curr. Opin. Cell Biol.13, 431-437 (review).

Ellgaard, L., Riek, R., Herrmann, T., Braun, D., Güntert, P., Helenius, A. and Wüthrich, K. (2001) NMR structure of the calreticulin P-domain. Proc. Natl. Acad. Sci. USA98, 3133-3138.

Ellgaard, L., Riek, R., Braun, D., Herrmann, T., Helenius, A. and Wüthrich, K. (2001) Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment. FEBS Lett.488, 69-73.

Ellgaard, L., Molinari M. and Helenius, A. (1999) Setting the standards: Quality control in the secretory pathway. Science286, 1882-1888 (review / cover).

Rettenberger, P. M, Oka, K., Ellgaard, L., Petersen, H. H., Christensen, A., Monard, D., Etzerodt, M., Chan, L. and Andreasen, P. A. (1999) Differential ligand binding properties of naturally ocurring variants of the human very low density lipoprotein receptor. Absence of the third complement-type repeat encoded by exon 4 is associated with reduced binding of Mr 40,000 receptor-associated-protein. J. Biol. Chem.274, 8973-8980.

Rasmussen, L. K., Ellgaard, L., Jensen, P. H. and Sørensen, E. S. (1999) Localization of a single transglutaminase-reactive glutamine in the third domain of RAP, the α2macroglobulin receptor-associated protein. J. Prot. Chem.18, 69-73.

Tauris, J., Ellgaard, L., Jacobsen, C., Nielsen, M. S., Madsen, P., Thøgersen, H. C., Gliemann, J., Petersen, C. M. and Moestrup, S. K. (1998) The carboxy-terminal domain of the receptor-associated protein binds to the Vps10p domain of sortilin. FEBS Lett.429, 27-30.


Nielsen, P. R., Ellgaard, L., Etzerodt, M., Thøgersen, H. C. and Poulsen, F. M. (1997) The solution structure of the N-terminal domain of α2macroglobulin receptor associated protein. Proc. Natl. Acad. Sci. USA94, 7521-7525.

Ellgaard, L., Holtet, T. L., Nielsen, P. R., Etzerodt, M. and Thøgersen, H. C. (1997) Dissection of the domain architecture of the α2macroglobulin receptor associated protein. Eur. J. Biochem.244, 544-551.

Petersen, C. M., Ellgaard, L., Nykjær, A., Vilhardt, F., Vorum, H., Thøgersen, H. C., Nielsen, M. S., Jacobsen, C., Moestrup, S. K. and Gliemann, J. (1996) The receptor-associated protein (RAP) binds calmodulin and is phosphorylated by calmodulin-dependent kinase II. EMBO J., 15, 4165-4173.

Ellgaard, L., Holtet, T. L., Moestrup, S. K., Etzerodt, M. and Thøgersen, H. C. (1995) Nested sets of protein fragments and their use in epitope mapping: characterization of the epitope for the S4D5 monoclonal antibody binding to receptor associated protein. J. Immunol. Methods, 180, 53-61.

Heegaard, C. W., Simonsen, A. C. W., Oka, K., Kjøller, L., Christensen, A., Madsen, B., Ellgaard, L., Chan, L. and Andreasen, P. A. (1995) Very low density lipoprotein receptor binds and mediates endocytosis of urokinase-type plasminogen activator/type-1 plasminogen activator inhibitor complex. J. Biol. Chem., 270, 20855-20861.

Kjøller, L., Simonsen, A. C. W., Ellgaard, L. and Andreasen, P. A. (1995) Differential regulation of urokinase-type-1 inhibitor complex endocytosis by phorbol esters in different cell lines is associated with differential regulation of α2macroglobulin receptor and urokinase receptor expression. Mol. Cell. Endocrinol.109, 209-217.

Simonsen, A. C. W., Heegaard, C. W., Rasmussen, L. K., Ellgaard, L., Kjøller, L., Christensen, A., Etzerodt, M. and Andreasen, P. A. (1994) Very low density lipoprotein receptor from mammary gland and mammary epithelial cell lines binds and mediates endocytosis of Mr 40,000 receptor associated protein. FEBS Lett., 354, 279-283.

Book chapters
Ellgaard, L. and Helenius, A. (2003) A chaperone system for glycoprotein folding: The calnexin/calreticulin cycle. In Calreticulin, second edition, Eds. Eggleton, P. and Michalak, M., Landes Bioscience,19-29.

Ellgaard, L. and Helenius, A. (2000) Folding of influenza hemagglutinin in the living cell. In "Mechanisms of Protein Folding: Frontiers in Molecular Biology" (second edition), Ed. Pain, R., Oxford University Press, 352-363.

Ellgaard, L., Stage, P., Etzerodt, M. and Thøgersen, H. C. The role of α2macroglobulin receptor associated protein as a chaperone for multifunctional receptors (1998). In "Lipid and Protein Traffic - Pathways and Molecular Mechanisms". Ed. Op den Kamp, J.A.F., NATO ASI Series, subseries H, Springer Verlag, 106, 95-104.

European commission/Success stories: Sea snail poison promises new medicines (

European commission/Result in Brief: Specialized insulin in the venom of cone snails: a new drug for diabetes? (

Meeting reports
Benham AM (2009) Protein folding and disulfide bond formation in the eukaryotic cell: meeting report based on the presentations at the European Network Meeting on Protein Folding and Disulfide Bond Formation 2009 (Elsinore, Denmark). FEBS J.276, 6905-11.