Publications – Elisabeth Sauer-Eriksson

Zhang, J, Grundström, C, Brännström, K,  Iakovleva, I, Lindberg, M, Olofsson, A, Andersson PL & Sauer-Eriksson, A.E. Interspecies Variation between fish and human transthyretins in their binding of thyroid-disrupting chemicals. (2018) Environ. Sci. Technol. 52(20), 11865-11874.

Kulén, M, Lindgren, M, Hansen, S, Cairns, AG, Grundström, C, Begum, A, van der Lingen, I, Brännström, K, Hall, M, Sauer, UH, Johansson, J, Sauer-Eriksson, AE & Almqvist, F. Structure-Based Design of Inhibitors Targeting PrfA, the Master Virulence Regulator of Listeria monocytogenes. (2018) J Med Chem., 61(9):4165-4175.

Kovermann, M, Grundström, C, Sauer-Eriksson, A.E, Sauer, UH & Wolf-Watz, M. Structural basis for ligand binding to an enzyme by a conformational selection pathway. (2017) Proc Natl Acad Sci, 114(24):6298-6303.

Hall, M., Grundström, C., Begum, A., Lindberg, MJ., Sauer, US., Almqvist, F., Johansson, J. & Sauer-Eriksson, A.E. Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria. (2016) Proc Natl Acad Sci 113(51):14733-14738.

Zhang, J, Begum, A, Brännström, K, Grundström, C, Iakovleva, I, Olofsson, A, Sauer-Eriksson, A.E. & Andersson PL. A Structure-based Virtual Screening Protocol for in silico Identification of Potential Thyroid Disrupting Chemicals Targeting Transthyretin. (2016) Environ. Sci. Technol. 50(21), 11984-11993.

Iakovleva, I, Begum, A, Brännström, K, Wijsekera, A, Nilsson, L, Zhang, J, Andersson, PL, Sauer-Eriksson, A.E. & Olofsson A. Tetrabromobisphenol A Is an Efficient Stabilizer of the Transthyretin Tetramer. (2016) PloS One, 11(4):e0153529

Nilsson, L, Larsson, A, Begum, A, Iakovleva, I, Carlsson, M, Brännström, K, Sauer-Eriksson, A.E. & Olofsson A. Modifications of the 7-Hydroxyl Group of the Transthyretin Ligand Luteolin Provide Mechanistic Insights into Its Binding Properties and High Plasma Specificity. (2016) PloS One, 11(4):e0153112.

Good, J, Andersson, C., Wall, J., Hansen, S., Krishnan, S., Grundström, C., Niemiec, M., Vaitkevicius, K., Chorell, E., Sauer, U.H., Wittung-Stafshede, P., Sauer-Eriksson, E. A, Almqvist, F. & Johansson, J. Inactivating the Listeria monocytogenes virulence regulator PrfA with ring-fused 2-pyridones. (2016) Chemistry and Biology 23(3):404-14. (Cover page)

Edwin, A., Persson, C., Mayzel, M., Wai, S.N., Öhman, A., Karlsson, G.B. & Sauer-Eriksson, A.E. Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae. (2015) Protein Science 12:2076-80.

Hainzl T. & Sauer-Eriksson A.E. Signal-sequence induced conformational changes in the signal recognition particle (2015) Nature communications 6:7163.

Kovermann M, Ådén J, Grundström C, Sauer-Eriksson, A.E., Sauer UH & Wolf-Watz M. Structural basis for catalytically restrictive dynamics of a high-energy enzyme state. Nature communications (2015) 6:7644

Iakovleva I, Brännström K, Nilsson L, Gharibyan AL, Begum A, Anan I, Walfridsson M, Sauer-Eriksson A.E. & Olofsson A. Enthalpic Forces Correlate with the Selectivity of Transthyretin-Stabilizing Ligands in Human Plasma (2015) J Med Chem, 58(16), 6507-6515.

Iakovleva I, Begum A, Pokrzywa M, Walfridsson M, Sauer-Eriksson AE & Olofsson A. The flavonoid luteolin, but not luteolin-7-o-glucoside, prevents a transthyretin mediated toxic response. (2015) PLoS One 10(5):e0128222.

Benlloch, R., Shevela, D., Hainzl, T., Grundström, C., Shutova, T., Messinger, J., Samuelsson, G & Sauer-Eriksson, A.E. Crystal Structure and Functional Characterization of Photosystem II-Associated Carbonic Anhydrase CAH3 in Chlamydomonas reinhardtii..(2015) Plant Physiology, 167:3, 950-962.

Hogg, M., Osterman, P., Bylund, G.O., Ganai, R.A., Lundström, E.-B., Sauer-Eriksson, A.E. & Johansson, E. Structural basis for processive DNA synthesis by yeast DNA polymerase . (2014) Nature Structural and Molecular Biology, 21(1):49-55.

Edwin A., Grundström C., Wai, S.N., Öhman, A., Stier, G, & Sauer-Eriksson, A.E. Domain isolation, expression, purification and proteolytic activity of the metalloprotease PrtV from Vibrio cholerae (2014) Prot. Exp. Purif. 96:39-47.

Edwin A, Rompikuntal P, Björn E, Stier G, Wai SN & Sauer-Eriksson AE. Calcium binding by the PKD1 domain regulates interdomain flexibility in Vibrio cholerae metalloprotease PrtV. (2013) FEBS Open Bio. 3:263-70.

Paracuellos, P., Öhman, A., Sauer-Eriksson, A.E. & Uhlin, B.-E. Expression and purification of SfaXII, a protein involved in regulating adhesion and motility genes in extraintestinal pathogenic Escherichia coli (2012) Prot. Exp. Purif. 86(2):127-134

Eriksson, J., Grundström, C., Sauer-Eriksson, A.E., Sauer, U.H., Wolf-Watz, H. & Elofsson, M. Small molecule screening for inhibitors of the YopH phosphatase of Yersinia pseudotuberculosis. (2012) Adv. Exp. Med. Biol. 954:357-363

Hogg, M., Sauer-Eriksson, A.E. & Johansson, E. Promiscuous DNA synthesis by human DNA polymerase (2012) Nucleic Acids Research, 40(6):2611-22

Huang, S., Hainzl., T., Grundström, C., Forsman, C., Samuelsson, G. & Sauer-Eriksson, A.E. Structural studies of β-carbonic anhydrase from the green alga Coccomyxa: inhibitor complexes with anions and acetazolamide (2011) PLoS One, 6(12):e28458

Hainzl, T, Huang, S. Meriläinene, G., Brännström, K. & Sauer-Eriksson, A.E. Structural basis of signal-sequence recognition by the signal recognition particle. (2011) Nature Structural and Molecular Biology, 8(3):389-91.

Hultdin, U.W., Lindberg, S., Grundström, C., Huang, H., Uhlin, B.-E., & Sauer-Eriksson, A.E. Structure of FocB: a member of a family of transcription factors regulating fimbrial adhesin expression in uropathogenic E. coli (2010) FEBS J. 277: 3369-3381.

Hultdin, U.W., Lindberg, S., Grundström, C., Allgardsson, A., Huang, H., Stier, G., Öhman, A., Uhlin, B.-E., & Sauer-Eriksson, A.E. Purification, crystallization and preliminary data analysis of FocB: a transcription factor regulating fimbrial adhesin expression in uropatho-genic Escherichia coli. (2010) Acta Crystallogr Sect F 66, 337–341

Olofsson, A, Lindhagen-Persson, M, Vestling, M, Sauer-Eriksson, AE & Öhman, A. Quenched hydrogen deuterium exchange characterization of amyloid-b peptide aggregates formed in the presence of Cu2+ or Zn2+. (2009) FEBS J. 276(15):4051-60.

Lundberg, E., Olofsson, A., Westermark, GT & Sauer-Eriksson, A.E. Stability and fibril formation properties of human and fish transthyretin, and of the Escherichia coli transthyretin-related protein (2009) FEBS J. 276(7):1999-2011.

Olofsson A, Sauer-Eriksson AE, Ohman A. Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance. (2009) Anal Biochem. 385(2):374-6.

Morgado I, Melo EP, Lundberg E, Estrela NL, Sauer-Eriksson AE, Power DM. Hormone affinity and fibril formation of piscine transthyretin: the role of the N-terminal. (2008) Mol Cell Endocrinol. 295(1-2):48-58.

Olofsson A, Borowik T, Grobner G. & Sauer-Eriksson AE. Negatively Charged Phospholipid Membranes Induce Amyloid Formation of Medin via an alpha-Helical Intermediate. (2007) J Mol Biol. 374(1):186-94.

Hainzl T, Huang S. & Sauer-Eriksson AE. Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the freesignal-recognition particle. (2007) Proc Natl Acad Sci U S A. 104(38):14911-6.

Karlsson A. & Sauer-Eriksson AE. Heating of proteins as a means of improving crystallization: a successful case study on a highly amyloidogenic triple mutant of human transthyretin. (2007) Acta Crystallogr Sect F 63(Pt 8):695-700.

Olofsson, A., Lindhagen-Persson, M., Sauer-Eriksson, A.E. & Öhman, A. Amide solvent protection analysis demonstrate that Amyloid(beta)(1-40) and Amyloid(beta)(1-42) form different fibrillar structures under identical conditions (2007) Biochemical J 404(1):63-70.

Lundberg, E., Bäckström, S., Sauer, U.H. & Sauer-Eriksson, A.E. The transthyretin-related protein: Structural investigation of a novel protein family. (2006) J Struct Biol., 155(3):445-57.

Gariani, T., Samuelsson, T. & Sauer-Eriksson, A.E. Conformational variability of the GTPase domain of the signal recognition particle receptor FtsY. (2006) J Struct Biol., 153(1):85-96.

Olofsson, A., Sauer-Eriksson, A.E. & Öhman, A. The solvent protection of alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy. (2006) J Biol Chem., 281(1):477-83.

Karlsson, A., Olofsson, A., Eneqvist T. & Sauer-Eriksson, A.E. Cys114-linked dimers of transthyretin are compatible with amyloid formation. (2005) Biochemistry, 44(39):13063-70.

Åberg, V., Norman, F. Chorell, E., Westermark, A, Olofsson, O., Sauer-Eriksson, A.E. & Almqvist, F. Microwave-assisted decarboxylation of bicyclic 2-pyridone scaffolds and identification of Abeta-peptide aggregation inhibitors. (2005) Org Biomol Chem., 3(15):2817-23.

Hörnberg, A., Hultdin, U., Olofsson, A. & Sauer-Eriksson, A.E.The effect of iodide and chloride on transthyretin structure and stability. (2005) Biochemistry, 44(26):9290-9.

Hainzl, T, Huang, S. & Sauer-Eriksson, A.E. Crystal structure of the S domain of SRP RNA: evidence for an induced fit mechanism (2005) RNA, 11(7):1043-50.

Hörnberg A, Olofsson A, Eneqvist T, Lundgren E, Sauer-Eriksson AE. The beta-strand D of transthyretin trapped in two discrete conformations. (2004) Biochim Biophys Acta. 1700(1):93-104.

Eneqvist T, Lundberg E, Karlsson A, Huang S, Santos CR, Power DM, Sauer-Eriksson AE. High resolution crystal structures of piscine transthyretin reveal different binding modes for triiodothyronine and thyroxine. (2004) J Biol Chem. 279(25):26411-6.

Sauer-Eriksson A.E. & Hainzl T. S-domain assembly of the signal recognition particle. (2003) Curr Opin Struct Biol. 13(1):64-70.

Eneqvist T, Lundberg E, Nilsson L, Abagyan R. & Sauer-Eriksson A.E. The transthyretin-related protein family. (2003) Eur J Biochem. 270(3):518-32.

Eneqvist T, Olofsson A, Ando Y, Miyakawa T, Katsuragi S, Jass J, Lundgren E. & Sauer-Eriksson A.E. Disulfide-bond formation in the transthyretin mutant Y114C prevents amyloid fibril formation in vivo and in vitro. (2002) Biochemistry, 41(44):13143-51.

Hainzl, T., Huang, S. & Sauer-Eriksson, A.E. Structure of the SRP19-RNA complex and implications for signal recognition particle assembly. (2002) Nature, 417, 767-771.

Huang, S., Sjöblom, B., Sauer-Eriksson, A.E. & Jonsson, B.-H. Organization of an efficient carbonic anhydrase: Implications for the mechanism based on structure-function studies of a T199P/C206S mutant. (2002) Biochemistry, 41(24), 7628-7635.

Eneqvist, T. & Sauer-Eriksson, A.E. Structural distribution of mutations associated with familial amyloidotic polyneuoropathy in human transthyretin. 2001, Amyloid, 149-168.

Eneqvist, T., Olofsson, A., Andersson, K, Lundgren, E. & Sauer-Eriksson, A.E. The slip: A novel concept in transthyretin amyloidosis. (2000) Mol. Cell, 6(5):1207-1218.

Hörnberg, A., Eneqvist, T., Olofsson, A., Lundgren, E. & Sauer-Eriksson, A.E. A comparative analysis of 23 structures of the amyloidogenic protein transthyretin (2000) J. Mol. Biol., 302(3),649-669.

Gariani, T. & Sauer-Eriksson, A.E. Crystallisation and preliminary X-ray diffraction studies of the signal recognition particle receptor FtsY from Mycoplasma mycoides. (2000) Acta Cryst D56,1030-1032.

Huang, S.-H., Xue, Y., Sauer-Eriksson, A.E., Chirica, L., Lindskog, S. & Jonsson, B.-H. (1998) Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetazolamide. J. Mol. Biol. 283, 301-310.

Sandholm-Kastrup, J., Sauer-Eriksson, A.E., Dalboge, H. & Flodgaard, H. (1997) X-ray Structure of the 154-Amino-Acid Form of Recombinant Human Basic Fibroblast Growth Factor. Comparison with the Truncated 146-Amino-Acid Form. Acta Cryst. D53, 160-168.

Wilmanns, M., Lappalainen, P., Kelly, M., Sauer-Eriksson, A.E. & Saraste, M. (1995) Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with and engineered dinuclear copper center. Proc. Natl. Acad. Sci. USA, 92, 11955-11959.

Sauer-Eriksson, A.E., Kleywegt, G.J., Uhlen, M. & Jones, T.A. (1995) Crystal structure of the C2 fragment of Streptococcal protein G in complex with the Fc domain of human IgG. Structure, 2, 265-278.

Eriksson, A.E., Cousens, L.S. & Matthews, B.W. (1993) Refinement of the structure of human basic fibroblast growth factor at 1.6 Å resolution and analysis of presumed heparin binding sites by selenate substitution. Protein Science, 2, 1274-1284.

Eriksson , A.E. & Liljas, A. (1993) Refined structure of bovine carbonic anhydrase III at 2.0 Å resolution. Proteins: Struct.Funct. Genet., 16, 29-42.

Eriksson, A.E., Baase, W.A. & Matthews, B.W. (1993) Similar hydrophobic replacements of Leu 99 and Phe 153 within the core of T4 lysozyme have different structural and thermodynamic consequences. J. Mol. Biol., 229, 747-769.

Eriksson, A.E., Baase, W.A., Zhang, X-J., Heinz, D.W., Blaber, M., Baldwin, E.P. and Matthews, B.W. (1992) The response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science, 255, 178-183.

Eriksson, A.E., Baase, W.A., Wozniak, J.A. & Matthews, B.W. (1992) A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene. Nature, 355, 371-373.

Eriksson, A.E., Cousens, L.S., Weaver, L.H. & Matthews, B.W. (1991) Three dimensional structure of human basic fibroblast growth factor. Proc. Natl. Acad. Sci. USA, 88, 3441-3445.

Eriksson, A.E., Kylsten, P.M., Jones, T.A. & Liljas, A. (1988) Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: A penta-coordinated binding of the SCN- ion to the zinc at high pH. Proteins: Struct. Funct. Genet. 4, 283-293.

Eriksson, A.E., Jones, T.A. & Liljas, A. (1988) Refined structure of human carbonic anhydrase II at 2.0 Å resolution. Proteins: Struct. Funct. Genet. 4, 274-282.

Eriksson, A.E. & Liljas, A. (1986) Crystallization of and preliminary X-ray data for bovine carbonic anhydrase III. J. Biol. Chem. 261, 16247-16248.

Invited Reviews

Eriksson, A.E., Jones, T.A. & Liljas, A. (1986) Crystallographic studies on human carbonic anhydrase II. In “Zinc Enzymes” (Gray, H. and Bertini, I., eds.),Birkhauser, Boston/Basel/Stuttgart, pp. 317-328.

Eriksson, A.E. & Liljas, A. (1991) X-ray crystallographic studies of carbonic anhydrase isozymes I, II, and III. In: “The Carbonic Anhydrases” (Dodgson, S.J., Tashian, R.E., Gros, G. and Carter, N.D., eds.) Plenum Publishing Corporation, pp. 33-48.

Lindahl, M., Vidgren, J., Eriksson, A.E., Habash, J., Harrop, S., Helliwell, J., Liljas,A., Lindeskog, M. & Walker, N. (1991) In: “Carbonic Anhydrase: From biochemistry and genetics to physiology and clinical medicine” (Botrè, F., Gros, G. and Storey, B.T., eds.) VCH, Weinheim/New York/Basel/Cambridge, pp. 111-118.

Baase, W.A., Eriksson, A.E., Zhang, X.-J., Heinz, D.W., Sauer, U., Blaber, M., Baldwin, E.P., Wozniak, J.A. and Matthews, B.W. Dissection of protein structure and folding by directed mutagenesis. (1992) Faraday Discuss., 93, 173-181.

Sauer-Eriksson, AE, Linusson, A & Lundberg, E. Transthyretin-related and transthyretin-like proteins. In “Recent Advances in Transthyretin Evolution, Structure and Biological Functions”, Richardson, S.J., Cody, V. (Eds.), 2009, ISBN 978-3-642-00645-6, Springer, Chapter 7, pp. 109-122.

Sauer-Eriksson, AE, Huang, S., & Hainzl, T. “Assembly and function of the signal recognition particle from archaea”. In Erice, International school of crystallography 2010: Structure and function from macromolecular crystallography: organization in space and time”, Meeting report in NATO Science for Peace and Security Series, Springer, Eds; Corrondo, M.A. and Spadon, P., p 125-135.

Sauer-Eriksson, AE, Liljas, A., & Käck, H. Popular science in honor of the international year of crystallography. An article called “Tillåter smart design” about the concept of drug design. In “Kemivärlden Biotech med kemisk tidskrift”, Volume 7-8, August, 2014, page 20-21