Umeå University's logo

umu.sePublications
Change search
Link to record
Permanent link

Direct link
Sauer-Eriksson, A. ElisabethORCID iD iconorcid.org/0000-0003-0124-0199
Alternative names
Publications (10 of 68) Show all publications
Tükenmez, H., Singh, P., Sarkar, S., Çakır, M., Oliveira, A. H., Lindgren, C., . . . Johansson, J. (2023). A highly substituted ring-fused 2-pyridone compound targeting PrfA and the efflux regulator BrtA in listeria monocytogenes [Letter to the editor]. mBio, 14(3), Article ID e0044923.
Open this publication in new window or tab >>A highly substituted ring-fused 2-pyridone compound targeting PrfA and the efflux regulator BrtA in listeria monocytogenes
Show others...
2023 (English)In: mBio, ISSN 2161-2129, E-ISSN 2150-7511, Vol. 14, no 3, article id e0044923Article in journal, Letter (Refereed) Published
Abstract [en]

Listeria monocytogenes is a facultative Gram-positive bacterium that causes listeriosis, a severe foodborne disease. We previously discovered that ring-fused 2-pyridone compounds can decrease virulence factor expression in Listeria by binding and inactivating the PrfA virulence activator. In this study, we tested PS900, a highly substituted 2-pyridone that was recently discovered to be bactericidal to other Gram-positive pathogenic bacteria, such as Staphylococcus aureus and Enterococcus faecalis. We show that PS900 can interact with PrfA and reduce the expression of virulence factors. Unlike previous ring-fused 2-pyridones shown to inactivate PrfA, PS900 had an additional antibacterial activity and was found to potentiate sensitivity toward cholic acid. Two PS900-tolerant mutants able to grow in the presence of PS900 carried mutations in the brtA gene, encoding the BrtA repressor. In wild-type (WT) bacteria, cholic acid binds and inactivates BrtA, thereby alleviating the expression of the multidrug transporter MdrT. Interestingly, we found that PS900 also binds to BrtA and that this interaction causes BrtA to dissociate from its binding site in front of the mdrT gene. In addition, we observed that PS900 potentiated the effect of different osmolytes. We suggest that the increased potency of cholic acid and osmolytes to kill bacteria in the presence of PS900 is due to the ability of the latter to inhibit general efflux, through a yet-unknown mechanism. Our data indicate that thiazolino 2-pyridones constitute an attractive scaffold when designing new types of antibacterial agents.

IMPORTANCE: Bacteria resistant to one or several antibiotics are a very large problem, threatening not only treatment of infections but also surgery and cancer treatments. Thus, new types of antibacterial drugs are desperately needed. In this work, we show that a new generation of substituted ring-fused 2-pyridones not only inhibit Listeria monocytogenes virulence gene expression, presumably by inactivating the PrfA virulence regulator, but also potentiate the bactericidal effects of cholic acid and different osmolytes. We identified a multidrug repressor as a second target of 2-pyridones. The repressor–2-pyridone interaction displaces the repressor from DNA, thus increasing the expression of a multidrug transporter. In addition, our data suggest that the new class of ring-fused 2-pyridones are efficient efflux inhibitors, possibly explaining why the simultaneous addition of 2-pyridones together with cholic acid or osmolytes is detrimental for the bacterium. This work proves conclusively that 2-pyridones constitute a promising scaffold to build on for future antibacterial drug design.

Place, publisher, year, edition, pages
American Society for Microbiology, 2023
Keywords
2-pyridones, BrtA, Listeria monocytogenes, PrfA, antibacterial, antibiotic
National Category
Biochemistry and Molecular Biology Microbiology in the medical area Organic Chemistry
Research subject
molecular cell biology
Identifiers
urn:nbn:se:umu:diva-214132 (URN)10.1128/mbio.00449-23 (DOI)000975886700001 ()37120759 (PubMedID)2-s2.0-85172894238 (Scopus ID)
Funder
Familjen Erling-Perssons StiftelseNIH (National Institutes of Health), RO1AI134847-01A1NIH (National Institutes of Health), 1IU19AI157797-01Olle Engkvists stiftelseVinnova, 2019-05491Swedish Research Council, 2020-02005Swedish Research Council, 2018-04589Swedish Research Council, 202105040J
Available from: 2023-09-05 Created: 2023-09-05 Last updated: 2023-10-13Bibliographically approved
Tischlik, S., Oelker, M., Rogne, P., Sauer-Eriksson, A. E., Drescher, M. & Wolf-Watz, M. (2023). Insights into Enzymatic Catalysis from Binding and Hydrolysis of Diadenosine Tetraphosphate by E. coli Adenylate Kinase. Biochemistry, 62(15), 2238-2243
Open this publication in new window or tab >>Insights into Enzymatic Catalysis from Binding and Hydrolysis of Diadenosine Tetraphosphate by E. coli Adenylate Kinase
Show others...
2023 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 62, no 15, p. 2238-2243Article in journal (Refereed) Published
Abstract [en]

Adenylate kinases play a crucial role in cellular energy homeostasis through the interconversion of ATP, AMP, and ADP in all living organisms. Here, we explore how adenylate kinase (AdK) from Escherichia coli interacts with diadenosine tetraphosphate (AP4A), a putative alarmone associated with transcriptional regulation, stress, and DNA damage response. From a combination of EPR and NMR spectroscopy together with X-ray crystallography, we found that AdK interacts with AP4A with two distinct modes that occur on disparate time scales. First, AdK dynamically interconverts between open and closed states with equal weights in the presence of AP4A. On a much slower time scale, AdK hydrolyses AP4A, and we suggest that the dynamically accessed substrate-bound open AdK conformation enables this hydrolytic activity. The partitioning of the enzyme into open and closed states is discussed in relation to a recently proposed linkage between active site dynamics and collective conformational dynamics.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2023
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-212552 (URN)10.1021/acs.biochem.3c00189 (DOI)001022362500001 ()37418448 (PubMedID)2-s2.0-85165636090 (Scopus ID)
Funder
EU, Horizon 2020, 772027─SPICE-ERC-2017-COGEU, European Research CouncilSwedish Research Council, 2019-03771Swedish Research Council, 2021-04513
Available from: 2023-08-08 Created: 2023-08-08 Last updated: 2023-08-08Bibliographically approved
Hainzl, T., Bonde, M., Almqvist, F., Johansson, J. & Sauer-Eriksson, A. E. (2023). Structural insights into CodY activation and DNA recognition [Letter to the editor]. Nucleic Acids Research, 51(14), 7631-7648
Open this publication in new window or tab >>Structural insights into CodY activation and DNA recognition
Show others...
2023 (English)In: Nucleic Acids Research, ISSN 0305-1048, E-ISSN 1362-4962, Vol. 51, no 14, p. 7631-7648Article in journal, Letter (Refereed) Published
Abstract [en]

Virulence factors enable pathogenic bacteria to infect host cells, establish infection, and contribute to disease progressions. In Gram-positive pathogens such as Staphylococcus aureus (Sa) and Enterococcus faecalis (Ef), the pleiotropic transcription factor CodY plays a key role in integrating metabolism and virulence factor expression. However, to date, the structural mechanisms of CodY activation and DNA recognition are not understood. Here, we report the crystal structures of CodY from Sa and Ef in their ligand-free form and their ligand-bound form complexed with DNA. Binding of the ligands - branched chain amino acids and GTP - induces conformational changes in the form of helical shifts that propagate to the homodimer interface and reorient the linker helices and DNA binding domains. DNA binding is mediated by a non-canonical recognition mechanism dictated by DNA shape readout. Furthermore, two CodY dimers bind to two overlapping binding sites in a highly cooperative manner facilitated by cross-dimer interactions and minor groove deformation. Our structural and biochemical data explain how CodY can bind a wide range of substrates, a hallmark of many pleiotropic transcription factors. These data contribute to a better understanding of the mechanisms underlying virulence activation in important human pathogens.

Place, publisher, year, edition, pages
Oxford University Press, 2023
Keywords
CodY, virulence, protein-DNA complex structure
National Category
Biochemistry and Molecular Biology Bioinformatics and Systems Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:umu:diva-214131 (URN)10.1093/nar/gkad512 (DOI)001008706900001 ()2-s2.0-85168963845 (Scopus ID)
Projects
CodY
Funder
Swedish Research Council, ID 2019-03771Swedish Research Council, 2020-02005_3 toSwedish Research Council, 2018-04589Swedish Research Council, 2021-05040J
Available from: 2023-09-05 Created: 2023-09-05 Last updated: 2023-09-05Bibliographically approved
Tran, T. T., Mathmann, C. D., Gatica-Andrades, M., Rollo, R. F., Oelker, M., Ljungberg, J. K., . . . Blumenthal, A. (2022). Inhibition of the master regulator of Listeria monocytogenes virulence enables bacterial clearance from spacious replication vacuoles in infected macrophages. PLoS Pathogens, 18(1), Article ID e1010166.
Open this publication in new window or tab >>Inhibition of the master regulator of Listeria monocytogenes virulence enables bacterial clearance from spacious replication vacuoles in infected macrophages
Show others...
2022 (English)In: PLoS Pathogens, ISSN 1553-7366, E-ISSN 1553-7374, Vol. 18, no 1, article id e1010166Article in journal (Refereed) Published
Abstract [en]

A hallmark of Listeria (L.) monocytogenes pathogenesis is bacterial escape from maturing entry vacuoles, which is required for rapid bacterial replication in the host cell cytoplasm and cell-to-cell spread. The bacterial transcriptional activator PrfA controls expression of key virulence factors that enable exploitation of this intracellular niche. The transcriptional activity of PrfA within infected host cells is controlled by allosteric coactivation. Inhibitory occupation of the coactivator site has been shown to impair PrfA functions, but consequences of PrfA inhibition for L. monocytogenes infection and pathogenesis are unknown. Here we report the crystal structure of PrfA with a small molecule inhibitor occupying the coactivator site at 2.0 Å resolution. Using molecular imaging and infection studies in macrophages, we demonstrate that PrfA inhibition prevents the vacuolar escape of L. monocytogenes and enables extensive bacterial replication inside spacious vacuoles. In contrast to previously described spacious Listeria-containing vacuoles, which have been implicated in supporting chronic infection, PrfA inhibition facilitated progressive clearance of intracellular L. monocytogenes from spacious vacuoles through lysosomal degradation. Thus, inhibitory occupation of the PrfA coactivator site facilitates formation of a transient intravacuolar L. monocytogenes replication niche that licenses macrophages to effectively eliminate intracellular bacteria. Our findings encourage further exploration of PrfA as a potential target for antimicrobials and highlight that intra-vacuolar residence of L. monocytogenes in macrophages is not inevitably tied to bacterial persistence.

Place, publisher, year, edition, pages
Public Library Science, 2022
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-191906 (URN)10.1371/journal.ppat.1010166 (DOI)000741048100001 ()35007292 (PubMedID)2-s2.0-85123302993 (Scopus ID)
Funder
Australian Research Council, CE140100011Australian Research Council, 1160570Swedish Research Council, FL180100109
Note

Originally included in thesis in manuscript form. 

Available from: 2022-01-27 Created: 2022-01-27 Last updated: 2022-02-03Bibliographically approved
Verma, A., Åberg-Zingmark, E., Sparrman, T., Ul Mushtaq, A., Rogne, P., Grundström, C., . . . Wolf-Watz, M. (2022). Insights into the evolution of enzymatic specificity and catalysis: from Asgard archaea to human adenylate kinases [Letter to the editor]. Science Advances, 8(44), Article ID eabm4089.
Open this publication in new window or tab >>Insights into the evolution of enzymatic specificity and catalysis: from Asgard archaea to human adenylate kinases
Show others...
2022 (English)In: Science Advances, E-ISSN 2375-2548, Vol. 8, no 44, article id eabm4089Article in journal, Letter (Refereed) Published
Abstract [en]

Enzymatic catalysis is critically dependent on selectivity, active site architecture, and dynamics. To contribute insights into the interplay of these properties, we established an approach with NMR, crystallography, and MD simulations focused on the ubiquitous phosphotransferase adenylate kinase (AK) isolated from Odinarchaeota (OdinAK). Odinarchaeota belongs to the Asgard archaeal phylum that is believed to be the closest known ancestor to eukaryotes. We show that OdinAK is a hyperthermophilic trimer that, contrary to other AK family members, can use all NTPs for its phosphorylation reaction. Crystallographic structures of OdinAK-NTP complexes revealed a universal NTP-binding motif, while 19F NMR experiments uncovered a conserved and rate-limiting dynamic signature. As a consequence of trimerization, the active site of OdinAK was found to be lacking a critical catalytic residue and is therefore considered to be "atypical." On the basis of discovered relationships with human monomeric homologs, our findings are discussed in terms of evolution of enzymatic substrate specificity and cold adaptation.

Place, publisher, year, edition, pages
American Association for the Advancement of Science (AAAS), 2022
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:umu:diva-201106 (URN)10.1126/sciadv.abm4089 (DOI)000918406800003 ()36332013 (PubMedID)2-s2.0-85141889911 (Scopus ID)
Funder
Swedish Research Council, 2017-04203Swedish Research Council, 2019-03771Swedish Research Council, 2016-03599Knut and Alice Wallenberg Foundation, 2016-03599The Kempe Foundations, SMK-1869Carl Tryggers foundation , 17.504NIH (National Institutes of Health), (R01GM132481
Note

The Protein Expertise Platform (PEP) at the Umeå University is acknowledged for providing reagents for protein production, and M. Lindberg at PEP is appreciated for preparation of plasmids. We acknowledge MAX IV Laboratory (Lund, Sweden) for time on BioMAX and DESY (Hamburg, Germany) for time on PETRA-3. All NMR experiments were performed at the Swedish NMR Center at Umeå University. We also acknowledge the Swedish National Infrastructure for Computing (SNIC) at the High Performance Computing Center North (HPC2N) and the National Energy Research Scientific Computing Center (NERSC) for computational resources.

Available from: 2022-11-19 Created: 2022-11-19 Last updated: 2023-09-05Bibliographically approved
Iakovleva, I., Hall, M., Oelker, M., Sandblad, L., Anan, I. & Sauer-Eriksson, A. E. (2021). Structural basis for transthyretin amyloid formation in vitreous body of the eye. Nature Communications, 12(1), Article ID 7141.
Open this publication in new window or tab >>Structural basis for transthyretin amyloid formation in vitreous body of the eye
Show others...
2021 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 12, no 1, article id 7141Article in journal (Refereed) Published
Abstract [en]

Amyloid transthyretin (ATTR) amyloidosis is characterized by the abnormal accumulation of ATTR fibrils in multiple organs. However, the structure of ATTR fibrils from the eye is poorly understood. Here, we used cryo-EM to structurally characterize vitreous body ATTR fibrils. These structures were distinct from previously characterized heart fibrils, even though both have the same mutation and type A pathology. Differences were observed at several structural levels: in both the number and arrangement of protofilaments, and the conformation of the protein fibril in each layer of protofilaments. Thus, our results show that ATTR protein structure and its assembly into protofilaments in the type A fibrils can vary between patients carrying the same mutation. By analyzing and matching the interfaces between the amino acids in the ATTR fibril with those in the natively folded TTR, we are able to propose a mechanism for the structural conversion of TTR into a fibrillar form.

Place, publisher, year, edition, pages
Nature Publishing Group, 2021
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-190576 (URN)10.1038/s41467-021-27481-4 (DOI)000728313100019 ()34880242 (PubMedID)2-s2.0-85120856247 (Scopus ID)
Funder
Swedish Research Council, 2015-03607
Available from: 2021-12-20 Created: 2021-12-20 Last updated: 2023-03-28Bibliographically approved
Hansen, S., Hall, M., Grundström, C., Brännström, K., Sauer-Eriksson, A. E. & Johansson, J. (2020). A Novel Growth-Based Selection Strategy Identifies New Constitutively Active Variants of the Major Virulence Regulator PrfA in Listeria monocytogenes. Journal of Bacteriology, 202(11), Article ID e00115-20.
Open this publication in new window or tab >>A Novel Growth-Based Selection Strategy Identifies New Constitutively Active Variants of the Major Virulence Regulator PrfA in Listeria monocytogenes
Show others...
2020 (English)In: Journal of Bacteriology, ISSN 0021-9193, E-ISSN 1098-5530, Vol. 202, no 11, article id e00115-20Article in journal (Refereed) Published
Abstract [en]

Listeria monocytogenes is a Gram-positive pathogen able to cause severe human infections. Its major virulence regulator is the transcriptional activator PrfA, a member of the Crp/Fnr family of transcriptional regulators. To establish a successful L. monocytogenes infection, the PrfA protein needs to be in an active conformation, either by binding the cognate inducer glutathione (GSH) or by possessing amino acid substitutions rendering the protein constitutively active (PrfA*). By a yet unknown mechanism, phosphotransferase system (PTS) sugars repress the activity of PrfA. We therefore took a transposon-based approach to identify the mechanism by which PTS sugars repress PrfA activity. For this, we screened a transposon mutant bank to identify clones able to grow in the presence of glucose-6-phosphate as the sole carbon source. Surprisingly, most of the isolated transposon mutants also carried amino acid substitutions in PrfA. In transposon-free strains, the PrfA amino acid substitution mutants displayed growth, virulence factor expression, infectivity, and DNA binding, agreeing with previously identified PrIA* mutants. Hence, the initial growth phenotype observed in the isolated clone was due to the amino acid substitution in PrfA and unrelated to the loci inactivated by the transposon mutant. Finally, we provide structural evidence for the existence of an intermediately activated PrfA state, which gives new insights into PrfA protein activation. IMPORTANCE The Gram-positive bacterium Listeria monocytogenes is a human pathogen affecting mainly the elderly, immunocompromised people, and pregnant women. It can lead to meningoencephalitis, septicemia, and abortion. The major virulence regulator in L. monocytogenes is the PrfA protein, a transcriptional activator. Using a growth-based selection strategy, we identified mutations in the PrfA protein leading to constitutively active virulence factor expression. We provide structural evidence for the existence of an intermediately activated PrfA state, which gives new insights into PrfA protein activation.

Place, publisher, year, edition, pages
American Society for Microbiology, 2020
Keywords
Listeria monocytogenes, PrfA, PrfA*, crystal structure, LLO, ActA
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-171908 (URN)10.1128/JB.00115-20 (DOI)000532732400005 ()32179627 (PubMedID)2-s2.0-85084695335 (Scopus ID)
Available from: 2020-06-17 Created: 2020-06-17 Last updated: 2023-03-23Bibliographically approved
Rogne, P., Sauer-Eriksson, E., Sauer, U. H., Hedberg, C. & Wolf-Watz, M. (2020). Principles of ATP and GTP Selectivity in NMP Kinases. Paper presented at 64th Annual Meeting of the Biophysical-Society, FEB 15-19, 2020, San Diego, CA. Biophysical Journal, 118(3), 193A-193A
Open this publication in new window or tab >>Principles of ATP and GTP Selectivity in NMP Kinases
Show others...
2020 (English)In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 118, no 3, p. 193A-193AArticle in journal, Meeting abstract (Other academic) Published
Place, publisher, year, edition, pages
Cell Press, 2020
National Category
Biophysics
Identifiers
urn:nbn:se:umu:diva-169050 (URN)10.1016/j.bpj.2019.11.1168 (DOI)000513023201213 ()
Conference
64th Annual Meeting of the Biophysical-Society, FEB 15-19, 2020, San Diego, CA
Note

Supplement: 1

Meeting Abstract: 939-Pos

Available from: 2020-03-19 Created: 2020-03-19 Last updated: 2020-03-19Bibliographically approved
Rogne, P., Dulko-Smith, B., Goodman, J., Rosselin, M., Grundström, C., Hedberg, C., . . . Wolf-Watz, M. (2020). Structural Basis for GTP versus ATP Selectivity in the NMP Kinase AK3. Biochemistry, 59(38), 3570-3581
Open this publication in new window or tab >>Structural Basis for GTP versus ATP Selectivity in the NMP Kinase AK3
Show others...
2020 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 59, no 38, p. 3570-3581Article in journal (Refereed) Published
Abstract [en]

ATP and GTP are exceptionally important molecules in biology with multiple, and often discrete, functions. Therefore, enzymes that bind to either of them must develop robust mechanisms to selectively utilize one or the other. Here, this specific problem is addressed by molecular studies of the human NMP kinase AK3, which uses GTP to phosphorylate AMP. AK3 plays an important role in the citric acid cycle, where it is responsible for GTP/GDP recycling. By combining a structural biology approach with functional experiments, we present a comprehensive structural and mechanistic understanding of the enzyme. We discovered that AK3 functions by recruitment of GTP to the active site, while ATP is rejected and nonproductively bound to the AMP binding site. Consequently, ATP acts as an inhibitor with respect to GTP and AMP. The overall features with specific recognition of the correct substrate and nonproductive binding by the incorrect substrate bear a strong similarity to previous findings for the ATP specific NMP kinase adenylate kinase. Taken together, we are now able to provide the fundamental principles for GTP and ATP selectivity in the large NMP kinase family. As a side-result originating from nonlinearity of chemical shifts in GTP and ATP titrations, we find that protein surfaces offer a general and weak binding affinity for both GTP and ATP. These nonspecific interactions likely act to lower the available intracellular GTP and ATP concentrations and may have driven evolution of the Michaelis constants of NMP kinases accordingly.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2020
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-176305 (URN)10.1021/acs.biochem.0c00549 (DOI)000576743500007 ()32822537 (PubMedID)2-s2.0-85091890831 (Scopus ID)
Available from: 2020-11-04 Created: 2020-11-04 Last updated: 2023-03-23Bibliographically approved
Krypotou, E., Scortti, M., Grundström, C., Oelker, M., Luisi, B. F., Sauer-Eriksson, A. E. & Vazquez-Boland, J. (2019). Control of Bacterial Virulence through the Peptide Signature of the Habitat. Cell Reports, 26(7), 1815-1827
Open this publication in new window or tab >>Control of Bacterial Virulence through the Peptide Signature of the Habitat
Show others...
2019 (English)In: Cell Reports, E-ISSN 2211-1247, Vol. 26, no 7, p. 1815-1827Article in journal (Refereed) Published
Abstract [en]

To optimize fitness, pathogens selectively activate their virulence program upon host entry. Here, we report that the facultative intracellular bacterium Listeria monocytogenes exploits exogenous oligopeptides, a ubiquitous organic N source, to sense the environment and control the activity of its virulence transcriptional activator, PrfA. Using a genetic screen in adsorbent- treated ( PrfA-inducing) medium, we found that PrfA is functionally regulated by the balance between activating and inhibitory nutritional peptides scavenged via the Opp transport system. Activating peptides provide essential cysteine precursor for the PrfA-inducing cofactor glutathione ( GSH). Non-cysteine-containing peptides cause promiscuous PrfA inhibition. Biophysical and co-crystallization studies reveal that peptides inhibit PrfA through steric blockade of the GSH binding site, a regulation mechanism directly linking bacterial virulence and metabolism. L. monocytogenes mutant analysis in macrophages and our functional data support a model in which changes in the balance of antagonistic Oppimported oligopeptides promote PrfA induction intra-cellularly and PrfA repression outside the host.

Place, publisher, year, edition, pages
Elsevier, 2019
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-156873 (URN)10.1016/j.celrep.2019.01.073 (DOI)000458403600013 ()30759392 (PubMedID)2-s2.0-85060870276 (Scopus ID)
Available from: 2019-03-11 Created: 2019-03-11 Last updated: 2024-01-17Bibliographically approved
Projects
Structural and functional studies on the signal recognition particle [2008-04303_VR]; Umeå UniversityExploring mechanisms for amyloid formation and for bacteria-host cell interactions. [2009-03708_VR]; Umeå UniversityRNA and RNP structures: elucidating the molecular function of ribonucleoprotein assemblies in protein targeting and viral infections [2011-06009_VR]; Umeå UniversityStrukturella studier på amyloida proteiner samt på proeiner involverade i bakterie-värdcell interaktioner [2012-02664_VR]; Umeå UniversityRNA and RNP structures: elucidating the molecular function of ribonucleoprotein assemblies in protein targeting and viral infections [2014-04493_VR]; Umeå UniversityStructure-Function Studies of Amyloid Proteins and Virulence-Associated Proteins [2015-03607_VR]; Umeå UniversityDevelopment of Drugs to Block Bacterial Virulence Factors [2019-03771_VR]; Umeå University
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0003-0124-0199

Search in DiVA

Show all publications