{"id":9,"date":"2020-10-01T12:38:55","date_gmt":"2020-10-01T12:38:55","guid":{"rendered":"https:\/\/site.uit.no\/norstruct\/?page_id=9"},"modified":"2026-07-02T11:56:53","modified_gmt":"2026-07-02T11:56:53","slug":"publications","status":"publish","type":"page","link":"https:\/\/site.uit.no\/norstruct\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"<h2><strong>2026<\/strong><\/h2>\n<div class=\"citation-text\">Skogvold ACA, Leiros I, Engh RA, Erlandsen H. Biochemical characterization and mutational analysis of the tetrameric DABA transaminase EctB from the Arctic bacterium Marinobacter sp. CK1. FEBS J. 2026 Jun;293(12):3545-3564. doi: 10.1111\/febs.70441. Epub 2026 Feb 6. PMID: 41652856.<\/div>\n<div>\n<h2><strong>2025<\/strong><\/h2>\n<p>Skogvold ACA, Brakestad HT, Erlandsen H, Leiros I. Crystal structure and biochemical analysis of the dimeric transaminase DoeD provides insights into ectoine degradation. FEBS J. 2025 Jun;292(11):2918-2934. doi: 10.1111\/febs.70043. Epub 2025 Feb 27. PMID: 40014458.<\/p>\n<p>Rothweiler U, Leiros HKS, Williamson A. Crystal structure of ATP-dependent DNA ligase from Rhizobium phage vB_RleM_P10VF. Acta Crystallogr F Struct Biol Commun. 2025 Jun 1;81(Pt 6):249-254. doi: 10.1107\/S2053230X2500411X. Epub 2025 May 14. PMID: 40365832; PMCID: PMC12121391.<\/p>\n<p>Singh M, Boomgaren M, Bakht P, Ihle P, Leiros HS, Bayer A, Pathania R. Design and SAR Analysis of Phenylboronic Acid-Based Inhibitors for Sensitizing KPC-2-Producing <i>Klebsiella pneumoniae<\/i> to \u03b2-Lactam Antibiotics. J Med Chem. 2025 Jul 10;68(13):13421-13435. doi: 10.1021\/acs.jmedchem.5c00058. Epub 2025 Jun 27. Erratum in: J Med Chem. 2025 Sep 25;68(18):19791. doi: 10.1021\/acs.jmedchem.5c02500. PMID: 40579355.<\/p>\n<\/div>\n<div class=\"citation-text\">Flygel TT, Bargheet A, Abotsi RE, Claassen-Weitz S, Simms V, Hjerde E, Mwaikono KS, Mchugh G, Hameiri-Bowen D, Pettersen VK, Ferrand RA, Nicol M, Cavanagh JP, Flaegstad T, Sovershaeva E. Effect of long-term azithromycin treatment on gut microbial diversity in children and adolescents with HIV-associated chronic lung disease. EBioMedicine. 2025 Aug;118:105832. doi: 10.1016\/j.ebiom.2025.105832. Epub 2025 Jul 5. PMID: 40616901; PMCID: PMC12272486.<\/div>\n<h2><strong>2024<\/strong><\/h2>\n<div class=\"citation-text\">Kumar N, Taneja A, Ghosh M, Rothweiler U, Sundaresan NR, Singh M. Harmonin homology domain-mediated interaction of RTEL1 helicase with RPA and DNA provides insights into its recruitment to DNA repair sites. Nucleic Acids Res. 2024 Feb 9;52(3):1450-1470. doi: 10.1093\/nar\/gkad1208. PMID: 38153196; PMCID: PMC10853778.<\/div>\n<div><\/div>\n<div>Stelzer R, Rzoska-Smith E, Gundes\u00f8 S, Rothweiler U, Williamson A. Using Modified Synthetic Oligonucleotides to Assay Nucleic Acid-Metabolizing Enzymes. J Vis Exp. 2024 Jul 5;(209). doi: 10.3791\/66930. PMID: 39037258.<\/div>\n<div><\/div>\n<div>\n<div class=\"citation-text\">Kondratieva A, Palica K, Fr\u00f8hlich C, Hovd RR, Leiros HS, Erdelyi M, Bayer A. Fluorinated captopril analogues inhibit metallo-\u03b2-lactamases and facilitate structure determination of NDM-1 binding pose. Eur J Med Chem. 2024 Feb 15;266:116140. doi: 10.1016\/j.ejmech.2024.116140. Epub 2024 Jan 10. PMID: 38242072.<\/div>\n<\/div>\n<h2><strong>2023<\/strong><\/h2>\n<div class=\"citation-text\">\n<div class=\"citation-text\">Junghare M, Manavalan T, Fredriksen L, Leiros I, Altermark B, Eijsink VGH, Vaaje-Kolstad G. Biochemical and structural characterisation of a family GH5 cellulase from endosymbiont of shipworm P. megotara. Biotechnol Biofuels Bioprod. 2023 Apr 4;16(1):61. doi: 10.1186\/s13068-023-02307-1. PMID: 37016457; PMCID: PMC10071621.<\/div>\n<p>Rainsford P, Rylandsholm FG, Jakubec M, Silk M, Juskewitz E, Ericson JU, Svendsen JS, Engh RA, Isaksson J. Label-free measurement of antimicrobial peptide interactions with lipid vesicles and nanodiscs using microscale thermophoresis. Sci Rep. 2023 Aug 3;13(1):12619. doi: 10.1038\/s41598-023-39785-0. PMID: 37537266; PMCID: PMC10400562.<\/p>\n<\/div>\n<div>\n<div class=\"citation-text\">Kondratieva A, Palica K, Fr\u00f8hlich C, Hovd RR, Leiros HS, Erdelyi M, Bayer A. Fluorinated captopril analogues inhibit metallo-\u03b2-lactamases and facilitate structure determination of NDM-1 binding pose. Eur J Med Chem. 2024 Feb 15;266:116140. doi: 10.1016\/j.ejmech.2024.116140. Epub 2024 Jan 10. PMID: 38242072.<\/div>\n<div><\/div>\n<\/div>\n<div>\n<div class=\"citation-text\">Hamre AG, Al-Sadawi R, Johannesen KM, Bisarro B, Kjendseth \u00c5R, Leiros HS, S\u00f8rlie M. Initial characterization of an iron superoxide dismutase from Thermobifida fusca. J Biol Inorg Chem. 2023 Oct;28(7):689-698. doi: 10.1007\/s00775-023-02019-9. Epub 2023 Sep 19. PMID: 37725277; PMCID: PMC10520107.<\/div>\n<div><\/div>\n<div>Palica K, Deufel F, Skagseth S, Di Santo Metzler GP, Thoma J, Andersson Rasmussen A, Valkonen A, Sunnerhagen P, Leiros HS, Andersson H, Erdelyi M. \u03b1-Aminophosphonate inhibitors of metallo-\u03b2-lactamases NDM-1 and VIM-2. RSC Med Chem. 2023 Aug 2;14(11):2277-2300. doi: 10.1039\/d3md00286a. PMID: 38020072; PMCID: PMC10650955.<\/div>\n<div><\/div>\n<\/div>\n<div>\n<div class=\"citation-text\">Jia Y, Schroeder B, Pfeifer Y, Fr\u00f6hlich C, Deng L, Arkona C, Kuropka B, Sticht J, Ataka K, Bergemann S, Wolber G, Nitsche C, Mielke M, Leiros HS, Werner G, Rademann J. Kinetics, Thermodynamics, and Structural Effects of Quinoline-2-Carboxylates, Zinc-Binding Inhibitors of New Delhi Metallo-\u03b2-lactamase-1 Re-sensitizing Multidrug-Resistant Bacteria for Carbapenems. J Med Chem. 2023 Sep 14;66(17):11761-11791. doi: 10.1021\/acs.jmedchem.3c00171. Epub 2023 Aug 16. PMID: 37585683.<\/div>\n<\/div>\n<h2><strong>2022<\/strong><\/h2>\n<div class=\"citation-text\">Maharajan AD, Hjerde E, Hansen H, Willassen NP. Quorum Sensing Controls the CRISPR and Type VI Secretion Systems in <i>Aliivibrio wodanis<\/i> 06\/09\/139. Front Vet Sci. 2022 Feb 8;9:799414. doi: 10.3389\/fvets.2022.799414. PMID: 35211539; PMCID: PMC8861277.<\/div>\n<div><\/div>\n<div class=\"citation-text\">Manikandan P, Sandhya S, Nadig K, Paul S, Srinivasan N, Rothweiler U, Singh M. Identification, functional characterization, assembly and structure of ToxIN type III toxin-antitoxin complex from E. coli. Nucleic Acids Res. 2022 Feb 22;50(3):1687-1700. doi: 10.1093\/nar\/gkab1264. PMID: 35018473; PMCID: PMC8860590.<\/div>\n<div><\/div>\n<div>Palica K, Vor\u00e1cov\u00e1 M, Skagseth S, Andersson Rasmussen A, Allander L, Hubert M, Sandegren L, Schr\u00f8der Leiros HK, Andersson H, Erd\u00e9lyi M. Metallo-\u03b2-Lactamase Inhibitor Phosphonamidate Monoesters. ACS Omega. 2022 Jan 25;7(5):4550-4562. doi: 10.1021\/acsomega.1c06527. PMID: 35155946; PMCID: PMC8830069.<\/div>\n<h2><strong>2021<\/strong><\/h2>\n<p>Barzowska A, Pucelik B, Pustelny K, Matsuda A, Martyniak A, St\u0119pniewski J, Maksymiuk A, Dawidowski M, Rothweiler U, Dulak J, Dubin G, Czarna A. DYRK1A Kinase Inhibitors Promote \u03b2-Cell Survival and Insulin Homeostasis. Cells. 2021 Aug 31;10(9):2263. doi: 10.3390\/cells10092263. PMID: 34571911; PMCID: PMC8467532.<\/p>\n<p>Stensen W, Rothweiler U, Engh RA, Stasko MR, Bederman I, Costa ACS, Fugelli A, Svendsen JSM. (2021)Novel DYRK1A Inhibitor Rescues Learning and Memory Deficits in a Mouse Model of Down Syndrome.<\/p>\n<p><span class=\"docsum-authors full-authors\">Lorenz R, Wu J, Herberg FW, Taylor SS, Engh RA. Drugging the Undruggable: How Isoquinolines and PKA Initiated the Era of Designed Protein Kinase Inhibitor Therapeutics. Biochemistry. 2021 Aug 9. doi: <a href=\"https:\/\/doi.org\/10.1021\/acs.biochem.1c00359\">10.1021\/acs.biochem.1c00359<\/a>. Online ahead of print. PMID: 34370450 <\/span><\/p>\n<p><span class=\"docsum-authors full-authors\">Fr\u00f6hlich C, Gama JA, Harms K, Hirvonen VHA, Lund BA, van der Kamp MW, Johnsen PJ, Samuelsen \u00d8, Leiros HS. (2021) <\/span>Cryptic \u03b2-Lactamase Evolution Is Driven by Low \u03b2-Lactam Concentrations. <span class=\"docsum-journal-citation full-journal-citation\">mSphere. 2021 Apr 28;6(2):e00108-21. doi: 10.1128\/mSphere.00108-21.<\/span><\/p>\n<p>Fr\u00f6hlich C, Chen JZ, Gholipour S, Erdogan AN, Tokuriki N. Evolution of \u03b2-lactamases and enzyme promiscuity. Protein Eng Des Sel. 2021 Feb 15;34:gzab013. doi: 10.1093\/protein\/gzab013. PMID: 34100551<\/p>\n<p>Alam KA, Gani OASBM, Engh RA. Inhibitor binding to mutants of protein kinase A with GGGxxG and GxGxxA glycine-rich loop motifs.\u00a0 <span class=\"docsum-journal-citation full-journal-citation\">J Mol Recognit. 2021 Apr;34(4):e2882. <a href=\"https:\/\/doi.org\/10.1002\/jmr.2882\">doi: 10.1002\/jmr.2882<\/a>. Epub 2020 Nov 15.<\/span> <span class=\"citation-part\">PMID: <span class=\"docsum-pmid\">33191558<\/span><\/span><\/p>\n<div class=\"citation-text\">Pan J, Lian K, Sarre A, Leiros HS, Williamson A. Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase. Sci Rep. 2021 Sep 21;11(1):18693. doi: 10.1038\/s41598-021-98155-w. PMID: 34548548; PMCID: PMC8455567.<\/div>\n<div><\/div>\n<div>\n<div class=\"citation-text\">Lund BA, Thomassen AM, Carlsen TJW, Leiros HKS. Biochemical and biophysical characterization of the OXA-48-like carbapenemase OXA-436. Acta Crystallogr F Struct Biol Commun. 2021 Sep 1;77(Pt 9):312-318. doi: 10.1107\/S2053230X21008645. Epub 2021 Aug 31. PMID: 34473108; PMCID: PMC8411929.<\/div>\n<\/div>\n<div>\n<div><\/div>\n<div class=\"citation-text\">Silk MR, Price JR, Mohanty B, Leiros HS, Lund BA, Thompson PE, Chalmers DK. Side-Chain Interactions in d\/l Peptide Nanotubes: Studies by Crystallography, NMR Spectroscopy and Molecular Dynamics. Chemistry. 2021 Oct 19;27(58):14489-14500. doi: 10.1002\/chem.202102106. Epub 2021 Sep 12. PMID: 34415083.<\/div>\n<div><\/div>\n<\/div>\n<div>\n<div class=\"citation-text\">Alexeeva M, Moen MN, Xu XM, Rasmussen A, Leiros I, Kirpekar F, Klungland A, Als\u00f8e L, Nilsen H, Bjelland S. Intrinsic Strand-Incision Activity of Human UNG: Implications for Nick Generation in Immunoglobulin Gene Diversification. Front Immunol. 2021 Dec 22;12:762032. doi: 10.3389\/fimmu.2021.762032. PMID: 35003074; PMCID: PMC8730318.<\/div>\n<div><\/div>\n<\/div>\n<div>Maharajan AD, Hansen H, Khider M, Willassen NP. Quorum sensing in <i>Aliivibrio wodanis<\/i> 06\/09\/139 and its role in controlling various phenotypic traits. PeerJ. 2021 Aug 24;9:e11980. doi: 10.7717\/peerj.11980. PMID: 34513327; PMCID: PMC8395575.<\/div>\n<div>\n<div><\/div>\n<\/div>\n<h2><strong>2020<\/strong><\/h2>\n<p><span lang=\"en-US\">Hj\u00f6rleifsson, J.G., Helland, R., Magn\u00fasd\u00f3ttir, M., \u00c1sgeirsson, B. (2020) High catalytic rate of the cold-active Vibrio alkaline phosphatase depends on a hydrogen bonding network involving large-loop at the dimeric interface. <\/span><i>FEBS Open Bio<\/i>. In press. https:\/\/ DOI: 10.1002\/2211-5463.13041<\/p>\n<p><span lang=\"en-US\">\u00c1sgeirsson, B., Mark\u00fasson, S., Hlynsd\u00f3ttir, S.S., Helland, R., Hj\u00f6rleifsson, J.G. (2020) X-ray crystal structure of <i>Vibrio<\/i> alkaline phosphatase with the non-competitive inhibitor cyclohexylamine <i>Biochem Biophys Rep<\/i>, <b>24<\/b>, 100830, <a href=\"https:\/\/doi.org\/10.1016\/j.bbrep.2020.100830\" target=\"_blank\" rel=\"noopener noreferrer\">https:\/\/doi.org\/10.1016\/j.bbrep.2020.100830<\/a>\u00a0 <\/span><\/p>\n<p><span lang=\"en-US\">Mazurkewich, S., Helland, R., MacKenzie, A., Eijsink, V.G.H., Pope, P.B., Br\u00e4nd\u00e9n,G., Larsbrink, J. (2020) Structural insights of the enzymes from the Chitin Utilization Locus of <i>Flavobacterium johnsoniae<\/i>. <\/span><i>Sci Rep<\/i> <b>10<\/b>, 13775. <a href=\"https:\/\/doi.org\/10.1038\/s41598-020-70749-w\" target=\"_blank\" rel=\"noopener noreferrer\">https:\/\/doi.org\/10.1038\/s41598-020-70749-w<\/a><\/p>\n<p><span lang=\"en-US\">Jadhav PV, Sinha VK, Chugh S, Kotyada C, Bachhav D,Singh R, Rothweiler U, Singh M, <\/span><span lang=\"en-US\">2.09 \u00c5 resolution structure of <i>E. coli<\/i> HigBA toxin-antitoxin complex reveals an ordered DNA-binding domain and intrinsic dynamics in antitoxin. <\/span><i><span lang=\"de\">Biochem J, <\/span><\/i><span lang=\"de\">2020<\/span><span lang=\"de\">, <b>477<\/b> 4001-4019.\u00a0<span class=\"identifier doi\"><span class=\"id-label\">DOI: <\/span> <a class=\"id-link\" href=\"https:\/\/doi.org\/10.1042\/bcj20200363\" target=\"_blank\" rel=\"noopener\"> 10.1042\/BCJ20200363 <\/a><\/span><\/span><\/p>\n<p>Samuelsen, \u00d8rjan; \u00c5strand, Ove Alexander H\u00f8gmoen; Fr\u00f8hlich, Christopher; Heikal, Adam; Skagseth, Susann; Carlsen, Trine Josefine Olsen; Leiros, Hanna-Kirsti S.; Bayer, Annette; Schnaars, Christian; Kildahl-andersen, Geir; Lauksund, Silje; Finke, Sarah; Huber, Sandra; Gj\u00f8en, Tor; Andresen, Adriana Magalhaes Santos; \u00d8kstad, Ole Andreas; Rongved, P\u00e5l. ZN148 Is a Modular Synthetic Metallo-beta-Lactamase Inhibitor That Reverses Carbapenem Resistance in Gram-Negative Pathogens In Vivo. <a href=\"https:\/\/aac.asm.org\/content\/early\/2020\/03\/11\/AAC.02415-19.long\">(data)<\/a> Antimicrobial Agents and Chemotherapy 2020. ISSN 0066-4804.s doi: <a href=\"http:\/\/dx.doi.org\/10.1128\/AAC.02415-19\" target=\"_blank\" rel=\"noopener\">10.1128\/AAC.02415-19<\/a>.<\/p>\n<p>Leiros, Hanna-Kirsti S.; Thomassen, Ane Molden; Samuelsen, \u00d8rjan; Flach, Carl-Fredrik; Kotsakis, Stathis D.; Larsson, Joakim. Structural insights into the enhanced carbapenemase efficiency of OXA-655 compared to OXA-10. <a href=\"https:\/\/febs.onlinelibrary.wiley.com\/doi\/full\/10.1002\/2211-5463.12935\">(fulltekst)<\/a> FEBS Open Bio 2020. ISSN 2211-5463.s doi: <a href=\"http:\/\/dx.doi.org\/doi:10.1002\/2211-5463.12935\" target=\"_blank\" rel=\"noopener\">doi:10.1002\/2211-5463.12935<\/a>.<\/p>\n<p>Fr\u00f8hlich, Christopher; S\u00f8rum, Vidar; Huber, Sandra; Samuelsen, \u00d8rjan; Berglund, Fanny; Kristiansson, Erik; Kotsakis, Stathis D.; Marathe, Nachiket P.; Larsson, Joakim; Leiros, Hanna-Kirsti S.. Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1. <a href=\"https:\/\/academic.oup.com\/jac\/article\/75\/9\/2554\/5848379\">(fulltekst)<\/a> Journal of Antimicrobial Chemotherapy 2020; Volum 75. ISSN 0305-7453.s 2554 &#8211; 2563.s doi: <a href=\"http:\/\/dx.doi.org\/doi:10.1093\/jac\/dkaa175\" target=\"_blank\" rel=\"noopener\">doi:10.1093\/jac\/dkaa175<\/a>.<\/p>\n<p>Williamson, Adele Kim; Leiros, Hanna-Kirsti S.. Structural insight into DNA joining: from conserved mechanisms to diverse scaffolds. <a href=\"https:\/\/academic.oup.com\/nar\/advance-article\/doi\/10.1093\/nar\/gkaa307\/5828915\">(data)<\/a> <a href=\"10.1093\/nar\/gkaa307\">(fulltekst)<\/a> Nucleic Acids Research 2020. ISSN 0305-1048.s 1 &#8211; .s doi: <a href=\"http:\/\/dx.doi.org\/doi: 10.1093\/nar\/gkaa307\" target=\"_blank\" rel=\"noopener\">doi: 10.1093\/nar\/gkaa307<\/a>.<\/p>\n<p>Muhammad, Zeeshan; Skagseth, Susann; Boomgaren, Marc; Akhter, Sundus; Fr\u00f8hlich, Christopher; Ismael, Aya; Christopeit, Tony; Bayer, Annette; Leiros, Hanna-Kirsti S.. Structural studies of triazole inhibitors with promising inhibitor effects against antibiotic resistance metallo-\u03b2-lactamases. Bioorganic &amp; Medicinal Chemistry 2020; Volum 28 (15). ISSN 0968-0896.s 115598 &#8211; .s doi: <a href=\"http:\/\/dx.doi.org\/https:\/\/doi.org\/10.1016\/j.bmc.2020.115598\" target=\"_blank\" rel=\"noopener\">https:\/\/doi.org\/10.1016\/j.bmc.2020.115598<\/a><\/p>\n<p>Gr\u00f8svik, Kristin; Tesfahun, Almaz Nigatu; Muruz\u00e1bal-Lecumberri, Izaskun; Haugland, Gyri Teien; Leiros, Ingar; Ruoff, Peter; Kval\u00f8y, Jan Terje; Kn\u00e6velsrud, Ingeborg; \u00c5nensen, Hilde; Alexeeva, Marina; Sato, Kousuke; Matsuda, Akira; Alseth, Ingrun; Klungland, Arne; Bjelland, Svein. The escherichia coli alkA gene is activated to alleviate mutagenesis by an oxidized deoxynucleoside. Frontiers in Microbiology 2020; Volum 11:263. ISSN 1664-302X.s 1 &#8211; 17.s doi: <a href=\"http:\/\/dx.doi.org\/10.3389\/fmicb.2020.00263\" target=\"_blank\" rel=\"noopener\">10.3389\/fmicb.2020.00263<\/a>.<\/p>\n<p>Berg, Kristel; Pedersen, Hege Lynum; Leiros, Ingar. Biochemical characterization of ferric uptake regulator (Fur) from Aliivibrio salmonicida. Mapping the DNA sequence specificity through binding studies and structural modelling. Biometals 2020. ISSN 0966-0844.s doi: <a href=\"http:\/\/dx.doi.org\/10.1007\/s10534-020-00240-6\" target=\"_blank\" rel=\"noopener\">10.1007\/s10534-020-00240-6<\/a>.<\/p>\n<p>Hillier, Heidi Therese; Altermark, Bj\u00f8rn; Leiros, Ingar. The crystal structure of the tetrameric DABA-aminotransferase EctB, a rate-limiting enzyme in the ectoine biosynthesis pathway. The FEBS Journal 2020. ISSN 1742-464X.s doi: <a href=\"http:\/\/dx.doi.org\/10.1111\/febs.15265\" target=\"_blank\" rel=\"noopener\">10.1111\/febs.15265<\/a>.<\/p>\n<p>Tarnowski, Krzysztof; Klimecka, Maria; Ciesielski, Arkadiusz; Goch, Grazyna; Kulik, Anna; Fedak, Halina; Poznanski, Jaroslaw; Lichocka, Malgorzata; Pierechod, Marcin Miroslaw; Engh, Richard Alan; Dadlez, Michal; Dobrowolska, Grazyna; Bucholc, Maria. Two SnRK2-Interacting Calcium Sensor Isoforms Negatively Regulate SnRK2 Activity by Different Mechanisms. Plant Physiology 2020 ;Volum 182.(2) s. 1142-1160. doi: https:\/\/doi.org\/10.1104\/pp.19.00900.<\/p>\n<h2><strong>2019<\/strong><\/h2>\n<p>Man Kumari Gurung, Bj\u00f8rn Altermark, Ronny Helland, Arne O Smal\u00e5s, Inger Lin U R\u00e6der, Features and structure of a cold active N-acetylneuraminate lyase, PLoS One 2019; Jun 11;14(6):e0217713.doi: 10.1371\/journal.pone.0217713<\/p>\n<p>Prandina, Anthony; Radix, Sylvie; Le Borgne, Marc; Jordheim, Lars Petter; Bousfiha, Zineb; Fr\u00f6hlich, Christopher; Leiros, Hanna-Kirsti S.; Samuelsen, \u00d8rjan; Fr\u00f8vold, Espen; Rongved, P\u00e5l; \u00c5strand, Ove Alexander H\u00f8gmoen. Synthesis and biological evaluation of new dipicolylamine zinc chelators as metallo-\u03b2-lactamase inhibitors. Tetrahedron 2019; Volum 75 (11). ISSN 0040-4020.s 1525 &#8211; 1540.s doi: <a href=\"http:\/\/dx.doi.org\/10.1016\/j.tet.2019.02.004\" target=\"_blank\" rel=\"noopener\">10.1016\/j.tet.2019.02.004<\/a>.<\/p>\n<p>Williamson, Adele Kim; Leiros, Hanna-Kirsti S.. Structural intermediates of a DNA-ligase complex illuminate the role of the catalytic metal ion and mechanism of phosphodiester bond formation. <a href=\"https:\/\/academic.oup.com\/nar\/article-lookup\/doi\/10.1093\/nar\/gkz596\">(data)<\/a> <a href=\"https:\/\/academic.oup.com\/nar\/article-lookup\/doi\/10.1093\/nar\/gkz596\">(fulltekst)<\/a> Nucleic Acids Research 2019; Volum 47 (14). ISSN 0305-1048.s 7147 &#8211; 7162.s doi: <a href=\"http:\/\/dx.doi.org\/10.1093\/nar\/gkz596\" target=\"_blank\" rel=\"noopener\">10.1093\/nar\/gkz596<\/a>.<\/p>\n<p>Fr\u00f8hlich, Christopher; S\u00f8rum, Vidar; Thomassen, Ane Molden; Johnsen, P\u00e5l Jarle; Leiros, Hanna-Kirsti S.; Samuelsen, \u00d8rjan. OXA-48-Mediated Ceftazidime-Avibactam Resisance Is Associated with Evolutionary Trade-Offs. mSphere 2019; Volum 4 (2). ISSN 2379-5042.s doi: <a href=\"http:\/\/dx.doi.org\/10.1128\/mSphere.00024-19\" target=\"_blank\" rel=\"noopener\">10.1128\/mSphere.00024-19<\/a>.<\/p>\n<p>Helland R, Bj\u00f8rkeng EK, Rothweiler U, Sydnes MO, Pampanin DM. The crystal structure of haemoglobin from Atlantic cod. <span class=\"jrnl\" title=\"Acta crystallographica. Section F, Structural biology communications\">Acta Crystallogr F Struct Biol Commun<\/span>. 2019.<\/p>\n<p>Haglund Hals\u00f8r MJ, Rothweiler U, Altermark B, Uttakleiv R\u00e6der IL. The crystal structure of the <span class=\"it\"><i>N<\/i><\/span>-acetylglucosamine 2-epimerase from <span class=\"it\"><i>Nostoc<\/i><\/span> sp. KVJ10 reveals the true dimer.\u00a0Acta Crystallographica Section D: Biological Crystallography 2019<\/p>\n<p>Berg, Kristel; Leiros, Ingar; Williamson, Adele Kim. Temperature adaptation of DNA ligases from psychrophilic organisms. Extremophiles 2019; Volum 23 (3). ISSN 1431-0651.s 305 &#8211; 317.s doi: <a href=\"http:\/\/dx.doi.org\/10.1007\/s00792-019-01082-y\" target=\"_blank\" rel=\"noopener\">10.1007\/s00792-019-01082-y<\/a>.<\/p>\n<p>Piotrowski, Yvonne; Berg, Kristel; Klebl, David P.; Leiros, Ingar; Larsen, Atle Noralf. Characterization of an intertidal zone metagenome oligoribonuclease and the role of the intermolecular disulfide bond for homodimer formation and nuclease activity. FEBS Open Bio 2019; Volum 9 (10). ISSN 2211-5463.s 1674 &#8211; 1688.s doi: <a href=\"http:\/\/dx.doi.org\/10.1002\/2211-5463.12720\" target=\"_blank\" rel=\"noopener\">10.1002\/2211-5463.12720<\/a>.<\/p>\n<div class=\"inline-authors\">\n<div class=\"authors\">\n<div class=\"authors-list\"><span class=\"citation-doi\">\u00a0<\/span><\/div>\n<\/div>\n<\/div>\n<h2><strong>2018<\/strong><\/h2>\n<p>Grgic, Miriam; Williamson, Adele Kim; Bjerga, Gro Elin Kj\u00e6reng; Altermark, Bj\u00f8rn; Leiros, Ingar. Biochemical characterization of ParI, an orphan C5-DNA methyltransferase from Psychrobacter arcticus 273-4. Protein Expression and Purification 2018; Volum 150. ISSN 1046-5928.s 100 &#8211; 108.s doi: <a href=\"http:\/\/dx.doi.org\/10.1016\/j.pep.2018.05.012\" target=\"_blank\" rel=\"noopener\">10.1016\/j.pep.2018.05.012<\/a>.<\/p>\n<p>Bjerga, Gro Elin Kj\u00e6reng; Larsen, \u00d8ivind; ARSIN, Hasan; Williamson, Adele Kim; Garcia-Moyano, Antonio; Leiros, Ingar; Puntervoll, P\u00e5l. Mutational analysis of the pro-peptide of a marine intracellular subtilisin protease supports its role in inhibition. Proteins: Structure, Function, and Bioinformatics 2018. ISSN 0887-3585.s 1 &#8211; 13.s doi: <a href=\"http:\/\/dx.doi.org\/10.1002\/prot.25528\" target=\"_blank\" rel=\"noopener\">10.1002\/prot.25528<\/a>.<\/p>\n<p>Jensen, Marianne Slang; Fredriksen, Lasse; Mackenzie, Alasdair; Pope, Phillip; Leiros, Ingar; Chylenski, Piotr; Williamson, Adele Kim; Christopeit, Tony; \u00d8stby, Heidi; Vaaje-Kolstad, Gustav; Eijsink, Vincent. Discovery and characterization of a thermostable two-domain GH6 endoglucanase from a compost metagenome. PLOS ONE 2018; Volum 13 (5). ISSN 1932-6203.s doi: <a href=\"http:\/\/dx.doi.org\/10.1371\/journal.pone.0197862\" target=\"_blank\" rel=\"noopener\">10.1371\/journal.pone.0197862<\/a>.<\/p>\n<p>Czarna A, Wang J, Zelencova D, Liu Y, Deng X, Choi HG, Zhang T, Zhou W, Chang JW, Kildalsen H, Seternes OM, Gray NS, Engh RA, Rothweiler U.\u00a0Novel scaffolds for Dual specificity tyrosine-phosphorylation-regulated kinase (DYRK1A) inhibitors.<span class=\"jrnl\">J Med Chem<\/span>. 2018 Sep 3;61(17):7560-7572. doi: 10.1021\/acs.jmedchem.7b01847. Epub 2018 Aug 23.PMID:30095246<\/p>\n<p>Thakkar BS, Svendsen JSM, Engh RA. Density Functional Studies on Secondary Amides: Role of Steric Factors in Cis\/Trans Isomerization. <span class=\"jrnl\" title=\"Molecules (Basel, Switzerland)\">Molecules<\/span>. 2018<\/p>\n<p>Thakkar, Balmukund; Engh, Richard Alan. Comparative conformational analyses and molecular dynamics studies of glycylglycine methyl ester and glycylglycine N -methylamide. RSC Advances 2018 ;Volum 8.(8) s. 4445-4453<\/p>\n<p>Ahkter, Sundus; Lund, Bjarte Aarmo; Ismael, Aya; Langer, Manuel; Isaksson, Johan; Christopeit, Tony; Leiros, Hanna-Kirsti S.; Bayer, Annette. A focused fragment library targeting the antibiotic resistance enzyme &#8211; Oxacillinase-48: Synthesis, structural evaluation and inhibitor design. European Journal of Medicinal Chemistry 2018; Volum 145. ISSN 0223-5234.s 634 &#8211; 648.s doi: <a href=\"http:\/\/dx.doi.org\/10.1016\/j.ejmech.2017.12.085\" target=\"_blank\" rel=\"noopener\">10.1016\/j.ejmech.2017.12.085<\/a>.<\/p>\n<p>Williamson, Adele Kim; Grgic, Miriam; Leiros, Hanna-Kirsti S.. DNA binding with a minimal scaffold: structure-function analysis of Lig E DNA ligases. Nucleic Acids Research 2018; Volum 46 (16). ISSN 0305-1048.s 8616 &#8211; 8629.s doi: <a href=\"http:\/\/dx.doi.org\/10.1093\/nar\/gky622\" target=\"_blank\" rel=\"noopener\">10.1093\/nar\/gky622<\/a>.<\/p>\n<p>Lund, Bjarte Aarmo; Thomassen, Ane Molden; Nesheim, Birgit Helene Berg; Carlsen, Trine Josefine Olsen; Isaksson, Johan; Christopeit, Tony; Leiros, Hanna-Kirsti S.. The biological assembly of OXA\u201048 reveals a dimer interface with high charge complementarity and very high affinity. The FEBS Journal 2018; Volum 285 (22). ISSN 1742-464X.s 4214 &#8211; 4228.s doi: <a href=\"http:\/\/dx.doi.org\/10.1111\/febs.14643\" target=\"_blank\" rel=\"noopener\">10.1111\/febs.14643<\/a>.<\/p>\n<p>Samuelsen, \u00d8rjan; Hansen, Frank; Aasn\u00e6s, Bettina; Hasman, Henrik; Lund, Bjarte Aarmo; Leiros, Hanna-Kirsti S.; Lilje, Berit; James Peter, Jessin Janice; Jakobsen, Lotte; Littauer, Pia; S\u00f8es, Lillian M; Holzknecht, Barbara J.; Andersen, Leif P; Stegger, Marc; Andersen, Paal S.; Hammerum, Anette M.. Dissemination and Characteristics of a Novel Plasmid-Encoded Carbapenem-Hydrolyzing Class D \u03b2-Lactamase, OXA-436, Found in Isolates from Four Patients at Six Different Hospitals in Denmark. Antimicrobial Agents and Chemotherapy 2018; Volum 62 (1). ISSN 0066-4804.s doi: <a href=\"http:\/\/dx.doi.org\/10.1128\/AAC.01260-17\" target=\"_blank\" rel=\"noopener\">10.1128\/AAC.01260-17<\/a>.<\/p>\n<p>Marcoccia, Francesca; Leiros, Hanna-Kirsti S.; Aschi, Massimiliano; Amicosante, Gianfranco; Perilli, Mariagrazia. Exploring the role of L209 residue in the active site of NDM-1 a metallo-\u03b2-lactamase. PLOS ONE 2018; Volum 13 (1). ISSN 1932-6203.s doi: <a href=\"http:\/\/dx.doi.org\/10.1371\/journal.pone.0189686\" target=\"_blank\" rel=\"noopener\">10.1371\/journal.pone.0189686<\/a>.<\/p>\n<h2><strong>2017<\/strong><\/h2>\n<p>Thakkar, Balmukund; Albrigtsen, Marte; Svendsen, John Sigurd Mj\u00f8en; Andersen, Jeanette Hammer; Engh, Richard Alan. Biofocussed chemoprospecting: An efficient approach for drug discovery. Chemical Biology and Drug Design 2017; Volum 90 (1). ISSN 1747-0277.s 128 &#8211; 140.s doi: <a href=\"http:\/\/dx.doi.org\/10.1111\/cbdd.12934\" target=\"_blank\" rel=\"noopener\">10.1111\/cbdd.12934<\/a>.<\/p>\n<p>Narayanan D, Gani OABSM, Gruber FXE, Engh RA. Data driven polypharmacological drug design for lung cancer: analyses for targeting ALK, MET, and EGFR.<span class=\"jrnl\">J Cheminform<\/span>. 2017 Jul 4;9(1):43. doi: 10.1186\/s13321-017-0229-8.<\/p>\n<p>Woywod C, Gruber FX, Engh RA, Fl\u00e5 T. Dynamical models of mutated chronic myelogenous leukemia cells for a post-imatinib treatment scenario: Response to dasatinib or nilotinib therapy. <span class=\"jrnl\">PLoS One<\/span>. 2017 Jul 5;12(7):e0179700. doi: 10.1371\/journal.pone.0179700. eCollection 2017.<\/p>\n<div class=\"supp\">\n<p>Tuveng TR, Rothweiler U, Udatha G, Vaaje-Kolstad G, Smal\u00e5s A, Eijsink VGH. Structure and function of a CE4 deacetylase isolated from a marine environment. <span class=\"jrnl\">PLoS One<\/span>. 2017 Nov 6;12(11):e0187544. doi: 10.1371\/journal.pone.0187544. eCollection 2017.<\/p>\n<\/div>\n<p>Thakkar BS, Svendsen JM, Engh RA. Cis\/Trans Isomerization in Secondary Amides: Reaction Paths, Nitrogen Inversion, and Relevance to Peptidic Systems. <span class=\"jrnl\" title=\"The journal of physical chemistry. A\">J Phys Chem A<\/span>. 2017<\/p>\n<p>Lund, Bjarte Aarmo; Thomassen, Ane Molden; Carlsen, Trine Josefine Olsen; Leiros, Hanna-Kirsti S.. Structure, activity and thermostability investigations of OXA-163, OXA-181 and OXA-245 using biochemical analysis, crystal structures and differential scanning calorimetry analysis. Acta Crystallographica. Section F : Structural Biology and Crystallization Communications 2017; Volum 73 (10). ISSN 1744-3091.s 579 &#8211; 587.s doi: <a href=\"http:\/\/dx.doi.org\/10.1107\/S2053230X17013838\" target=\"_blank\" rel=\"noopener\">10.1107\/S2053230X17013838<\/a>.<\/p>\n<p>Skagseth, Susann; Christopeit, Tony; Akhter, Sundus; Bayer, Annette; Samuelsen, \u00d8rjan; Leiros, Hanna-Kirsti S.. Structural insights into TMB-1 and the role of residues 119 and 228 in substrate and inhibitor binding. Antimicrobial Agents and Chemotherapy 2017; Volum 61:e02602-16 (8). ISSN 0066-4804.s 1 &#8211; 19.s doi: <a href=\"http:\/\/dx.doi.org\/10.1128\/AAC.02602-16\" target=\"_blank\" rel=\"noopener\">10.1128\/AAC.02602-16<\/a>.<\/p>\n<p>Skagseth, Susann; Akhter, Sundus; Paulsen, Marianne H.; Zeeshan, Muhammad; Lauksund, Silje; Samuelsen, \u00d8rjan; Leiros, Hanna-Kirsti S.; Bayer, Annette. Metallo-\u03b2-lactamase inhibitors by bioisosteric replacement: preparation, activity and binding. European Journal of Medicinal Chemistry 2017; Volum 135. ISSN 0223-5234.s 159 &#8211; 173.s doi: <a href=\"http:\/\/dx.doi.org\/10.1016\/j.ejmech.2017.04.035\" target=\"_blank\" rel=\"noopener\">10.1016\/j.ejmech.2017.04.035<\/a>.<\/p>\n<p><span class=\"authors-list-item \">Concetta De Santi<span class=\"comma\">,\u00a0<\/span><\/span><span class=\"authors-list-item \">Osman Absm Gani<span class=\"comma\">,\u00a0<\/span><\/span><span class=\"authors-list-item \">Ronny Helland<span class=\"comma\">,\u00a0<\/span><\/span><span class=\"authors-list-item \">Adele Williamson, <\/span>Structural insight into a CE15 esterase from the marine bacterial metagenome, Sci Rep 2017 <span class=\"citation-doi\">doi: 10.1038\/s41598-017-17677-4. <\/span><\/p>\n<h2><strong>2016<\/strong><\/h2>\n<p>Marit Seppola, Kathrine Ryvold Bakkemo, Helene Mikkelsen, Bj\u00f8rnar Myrnes , Ronny Helland, David M Irwin, Inge W Nilsen, Multiple specialised goose-type lysozymes potentially compensate for an exceptional lack of chicken-type lysozymes in Atlantic cod, Sci Rep 2016; Jun 21;6:28318. doi: 10.1038\/srep28318<\/p>\n<p>Rothweiler, Ulli; Stensen, Wenche; Brandsdal, Bj\u00f8rn Olav; Isaksson, Johan; Leeson, Frederick Alan; Engh, Richard Alan; Svendsen, John Sigurd Mj\u00f8en.\u00a0Probing the ATP-Binding Pocket of Protein Kinase DYRK1A with Benzothiazole Fragment Molecules. Journal of Medicinal Chemistry 2016; Volum 59 (21). ISSN 0022-2623.s 9814 &#8211; 9824.s doi:\u00a0<a href=\"http:\/\/dx.doi.org\/10.1021\/acs.jmedchem.6b01086\" target=\"_blank\" rel=\"noopener\">10.1021\/acs.jmedchem.6b01086<\/a>.<\/p>\n<p>Ivan, Taavi; Enkvist, Erki; Viira, Birgit; Manoharan, Ganesh babu; Raidaru, Gerda; Pflug, Alexander; Alam, Kazi Asraful; Zaccolo, Manuela; Engh, Richard Alan; Uri, Asko.\u00a0Bifunctional ligands for inhibition of tight-binding protein-protein interactions. Bioconjugate chemistry 2016; Volum 27 (8). ISSN 1043-1802.s 1900 &#8211; 1910.s doi:\u00a0<a href=\"http:\/\/dx.doi.org\/10.1021\/acs.bioconjchem.6b00293\" target=\"_blank\" rel=\"noopener\">10.1021\/acs.bioconjchem.6b00293<\/a><\/p>\n<p>Skagseth, Susann; Carlsen, Trine Josefine Olsen; Bjerga, Gro Elin Kj\u00e6reng; Spencer, James; Samuelsen, \u00d8rjan; Leiros, Hanna-Kirsti S.. Role of residues W228 and Y233 in the structure and activity of metallo-\u03b2-lactamase GIM-1. Antimicrobial Agents and Chemotherapy 2016; Volum 60 (2). ISSN 0066-4804.s 990 &#8211; 1002.s doi: <a href=\"http:\/\/dx.doi.org\/10.1128\/AAC.02017-15\" target=\"_blank\" rel=\"noopener\">10.1128\/AAC.02017-15<\/a>.<\/p>\n<p>Christopeit, Tony; Yang, Ke-Wu; Yang, Shao-Kang; Leiros, Hanna-Kirsti S.. The structure of the metallo-\u03b2-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor. Acta Crystallographica. Section F : Structural Biology and Crystallization Communications 2016; Volum 72 (11). ISSN 1744-3091.s 813 &#8211; 819.s doi: <a href=\"http:\/\/dx.doi.org\/10.1107\/S2053230X16016113\" target=\"_blank\" rel=\"noopener\">10.1107\/S2053230X16016113<\/a>.<\/p>\n<p>Christopeit, Tony; Leiros, Hanna-Kirsti S.. Fragment-based discovery of inhibitor scaffolds targeting the metallo-\u03b2-lactamases NDM-1 and VIM-2. Bioorganic &amp; Medicinal Chemistry Letters 2016; Volum 26 (8). ISSN 0960-894X.s 1973 &#8211; 1977.s doi: <a href=\"http:\/\/dx.doi.org\/10.1016\/j.bmcl.2016.03.004\" target=\"_blank\" rel=\"noopener\">10.1016\/j.bmcl.2016.03.004<\/a>.<\/p>\n<p>De Santi, Concetta; Leiros, Hanna-Kirsti S.; Di Scala, Alessia; de Pascale, Donatella; Altermark, Bj\u00f8rn; Willassen, Nils Peder. Biochemical characterization and structural analysis of a new cold-active and salt-tolerant esterase from the marine bacterium Thalassospira sp.. Extremophiles 2016; Volum 20 (3). ISSN 1431-0651.s 323 &#8211; 336.s doi: <a href=\"http:\/\/dx.doi.org\/10.1007\/s00792-016-0824-z\" target=\"_blank\" rel=\"noopener\">10.1007\/s00792-016-0824-z<\/a>.<\/p>\n<p>Christopeit, Tony; Albert, Anastasia; Leiros, Hanna-Kirsti S.. Discovery of a novel covalent non-\u03b2-lactam inhibitor of the metallo-\u03b2-lactamase NDM-1. Bioorganic &amp; Medicinal Chemistry 2016; Volum 24 (13). ISSN 0968-0896.s 2947 &#8211; 2953.s doi: <a href=\"http:\/\/dx.doi.org\/10.1016\/j.bmc.2016.04.064\" target=\"_blank\" rel=\"noopener\">10.1016\/j.bmc.2016.04.064<\/a>.<\/p>\n<p>Lund, Bjarte Aarmo; Christopeit, Tony; Guttormsen, Yngve; Bayer, Annette; Leiros, Hanna-Kirsti S.. Screening and Design of Inhibitor Scaffolds for the Antibiotic Resistance Oxacillinase-48 (OXA-48) through Surface Plasmon Resonance Screening. Journal of Medicinal Chemistry 2016; Volum 59 (11). ISSN 0022-2623.s 5542 &#8211; 5554.s doi: <a href=\"http:\/\/dx.doi.org\/10.1021\/acs.jmedchem.6b00660\" target=\"_blank\" rel=\"noopener\">10.1021\/acs.jmedchem.6b00660<\/a><\/p>\n<h2><strong>2015<\/strong><\/h2>\n<p>Laber, B.S., Hardegger, L.A., Asraful, A.K., Lund, B.A., Dumele, O., Harder, M., Kuhn, B., Engh, R.A., &amp; Diederich, F. (2015) Addressing the Glycine-Rich Loop of Protein Kinases by a Multi-Facetted Interaction Network: Inhibition of PKA and a PKB Mimic. <em>Chem. Eur. J<\/em>. doi:10.1002\/chem.201503552<\/p>\n<p>Bjerga, G.E.K, Williamson, A.K. (2015) Cold shock induction of recombinant Arctic environmental genes. <em>BMC Biotech<\/em> <strong>15<\/strong>, 78<\/p>\n<p>Hansen, H., Purohit, A.A., Leiros, H.K., Johansen, .JA., Kellermann, S.J., Bjelland, A.M., Willassen, N.P. (2015) The autoinducer synthases LuxI and AinS are responsible for temperature-dependent AHL production in the fish pathogen <em>Aliivibrio salmonicida<\/em>. <em>BMC Microbiol<\/em><strong> 15<\/strong>, 69<\/p>\n<p>Pedersen, H.L., \u00a0Johnson, K.A., McVey, C.E., Leiros,I., Moe, E. (2015) Crystal structure determination of uracil-DNA N-glycosylase (UNG) from <em>Deinococcus radiodurans<\/em> in complex with DNA.<em> Acta cryst D<\/em>, In press<\/p>\n<p>Hjerde, E., Karlsen, C., S\u00f8rum, H., Parkhill, J., Willassen, N.P., Thomson, N.R.( 2015) Co-cultivation and transcriptome sequencing of two co-existing fish pathogens <em>Moritella viscosa<\/em> and <em>Aliivibrio wodanis<\/em>. <em>BMC Genomics<\/em> <strong>16<\/strong>, 447<\/p>\n<p>Lysvand, H., Helland, R., Hagen, L., Slupphaug, G., Iversen, O.J. (2015) Psoriasis pathogenesis &#8211; Pso p27 constitutes a compact structure forming large aggregates. <em>Biochem Biophys Rep<\/em> <strong>2<\/strong>, 132-136<\/p>\n<p>Gani, O.G., Thakkar, B., Narayanan, D., Alam, K.A., Kyomuhendo, P., Rothweiler, U., Tello-Franco, V., Engh, R.A. (2015) Assessing protein kinase target similarity: comparing sequence, structure, and cheminformatics approaches. <i>Biochim Biophys Acta Prot Pro<\/i>t Volum 1854.(10) s. 1605-1616.<\/p>\n<p>Sarre, A., \u00d6kvist, M., Klar, T., Hall, D.R., Smal\u00e5s, A.O., McSweeney, S., Timmins, J., Moe, E. (2015) Structural and functional characterization of two unusual endonuclease III enzymes from <i>Deinococcus radiodurans<\/i>. <i>J Struct Biol<\/i> In press<\/p>\n<p>Martin, E., Knapp, S., Engh, R.A., Moebitz, H., Varin, T., Roux, B., Meiler,.J., Berdini, V., Baumann, A., Vieth, M. (2015) Perspective on computational and structural aspects of kinase discovery from IPK2014. <i>Biochim Biophys Acta- Proteins and Proteomics 2015 ;Volum 1854.(10) s. 1595-1604.<\/i><\/p>\n<p>Thode, S.K., Kahlke, T., Robertsen, E.M., Hansen, H., Haugen, P. (2015) The immediate global responses of <em>Aliivibrio salmonicida<\/em> to iron limitations. <em>BMC Microbiology<\/em>, <strong>15<\/strong>, 9<\/p>\n<p>Alexeeva, M., \u00c5berg, E., Engh, R.A., Rothweiler, U. (2015) The structure of a dual-specificity tyrosine phosphorylation-regulated kinase 1A\u2013PKC412 complex reveals disulfide-bridge formation with the anomalous catalytic loop HRD(HCD) cysteine. <i>Acta Cryst<\/i>. <strong>D71, <\/strong>1207-1215.<\/p>\n<p>Rothweiler, U., Eriksson, J., Stensen, W., Leeson, F., Engh, R.A., Svendsen, J.S. (2015) Luciferin and derivatives as a DYRK selective scaffold for the design of protein kinase inhibitors. <i>Eur J Med Chem<\/i> <strong>94<\/strong>, 140-148.<\/p>\n<p>Niiranen, L., Lian, K., Johnson, K.A., Moe, E. (2015) Crystal structure of the DNA polymerase III beta subunit (beta-clamp) from the extremophile <em>Deinococcus radiodurans<\/em> .<em>BMC Struct Bio<\/em>l <strong>15<\/strong>, 5<\/p>\n<p>Lian, K., Leiros, H.K., Moe, E. (2015) MutT from the fish pathogen <em>Aliivibrio salmonicida<\/em> is a cold active nucleotide pool sanitization enzyme with an unexpected high thermostability. <em>FEBS Open Bio<\/em> <strong>5<\/strong>, 107-116<\/p>\n<p>Leiros, H.K., Edvardsen, K.S., Bjerga, G.E., Samuelsen, \u00d8. (2015) Structural and biochemical characterization of VIM-26 show that Leu224 has implications for the substrate specificity of VIM metallo-b-lactamases <em>FEBS J<\/em>, 1031-1042<\/p>\n<p>Kashulin, A., S\u00f8rum, H., Hjerde, H., Willassen, N.P. (2015) IS elements in <em>Aliivibrio salmonicida<\/em> LFI1238: Occurrence, variability and impact on adaptability. <em>Gene<\/em> <strong>554<\/strong>, 40-49<\/p>\n<p>Kristiansen, A., Grgic, M., Altermark, B., Leiros, I. (2015) Properties and distribution of a Metallo-\u03b2-Lactamase (ALI-1) from the fish pathogen <em>Aliivibrio salmonicida<\/em> LFI1238. <em>J Antimicrob Chemother<\/em>. <strong>70<\/strong>, 766-722<\/p>\n<h2><strong>2014<\/strong><\/h2>\n<p>Sarre, A., \u00d6kvist, M., Klar, T., Moe, E., Timmins, J. (2014) Expression, purification and crystallization of two endonuclease III enzymes from <em>Deinococcus radiodurans<\/em>. <em>Acta Cryst<\/em> <strong>F70<\/strong>, 1688-1692<\/p>\n<p>Hansen, H., Bjelland, A.M., Ronessen, M., Robertsen, E.M., Willassen, N.P. (2014). LitR is a repressor of syp genes and has a temperature-sensitive regulatory effect on biofilm formation and colony morphology in <em>Vibrio (Aliivibrio) salmonicida<\/em>. <em>Appl Environ Microbio<\/em>l. <strong>80<\/strong> (17), 5530-5541<\/p>\n<p>Berg, T.O., Gurung, M., Smal\u00e5s, A.O., Altermark, B., R\u00e6der, I.L.U. (2014) Characterization of the N-acetylneuraminic acid synthase (NeuB) from the psychrophilic fish pathogen <em>Moritella viscosa<\/em>. <em>Carbohyd Res<\/em> <strong>402c<\/strong>, 133-145<\/p>\n<p>Williamson, A., Rothweiler, U., Leiros, H.K.S. (2014) Enzyme-Adenylate Structure of a Bacterial ATP-Dependent DNA Ligase With a Minimized DNA-Binding Surface. <em>Acta Cryst<\/em><strong> D 70<\/strong>, 3043-3056<\/p>\n<p>Cavanagh, J.P., Hjerde, E., Holden, M.T., Kahlke, T., Klingenberg, C., Fl\u00e6gstad, T., Parkhill, J., Bentley, S.D., Sollid, J.U. (2014) Whole-genome sequencing reveals clonal expansion of multiresistant <em>Staphylococcus haemolyticus<\/em> in European hospitals. <em>J Antimicrob Chemother<\/em>.<strong>69<\/strong> (11), 2920-2927<\/p>\n<p>Leiros, H.-K.S., Skagseth, S., Edvardsen, K.S.W., Lorentzen, M.S., Bjerga, G.E.K., Leiros, I., Samuelsen, \u00d8. (2014) His224 alters the R2 drug binding site and Phe218 influences the catalytic efficiency in the metallo-\u03b2-lactamase VIM-7. <em>Antimicrob Agents Chemother<\/em>\u00a0<strong>58<\/strong>, 4826 &#8211; 4836<\/p>\n<p>Assefa, N.G., Niiranen, L., Johnson, K., Leiros, H.-K.S., Smal\u00e5s, A.O., Willassen, N.P., \u00a0Moe, E. (2014) Structural and biophysical analysis of interactions between cod and human uracil-DNA N-glycosylase (UNG) and UNG inhibitor (Ugi) <em>Acta Cryst\u00a0<strong>\u00a0D70<\/strong> (8), 2093-2100<\/em><\/p>\n<p>Williamson, A.K, Pedersen, H.L. (2014) Recombinant expression and purification of an ATP-dependent DNA ligase from <em>Aliivibrio salmonicida<\/em>. <em>Prot Expres Purif<\/em>\u00a0<strong>97<\/strong>, 29-36<\/p>\n<p>Forsberg, Z., Mackenzie, A.K., S\u00f8rlie,M., R\u00f8hr,\u00c5.K., Helland,R., Arvai, A.S., Vaaje-Kolstad,G., Eijsink, V.G.H. (2014) Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases (2014) <em>PNAS<\/em> <strong>111<\/strong>(23):8446-8451<\/p>\n<p>Lund, B.AA., Leiros,, H.K.S,. Bjerga, G.E.K. (2014) A high-throughput, restriction-free cloning and screening strategy based on ccdB-gene replacement<em> Microbial Cell Factories<\/em>. In press<\/p>\n<p>Kashulin, A., S\u00f8rum, H (2014) A novel in vivo model for rapid evaluation of <em>Aliivibrio salmonicida<\/em> infectivity in Atlantic salmon. <em>Aquaculture<\/em>, <strong>420-421<\/strong>, 112-118<\/p>\n<p>Bjerga, G.E.K., Hjerde, E., De Santi, C., Williamson, A.K., Smal\u00e5s, A.O., Willassen, N.P., Altermark, A. (2014) High quality draft genome sequence of <em>Streptomyces sp<\/em>. strain AW19M42 isolated from a sea squirt in Northern Norway. <em>Stand. Genomic Sci<\/em>. <strong>9<\/strong>, 3<\/p>\n<p>Sivertsen, A., Isaksson, J., Leiros, H.K., Svenson, J., Svendsen, J.S., Brandsdal, B.O. (2014) Synthetic cationic antimicrobial peptides bind with their hydrophobic parts to drug site II of human serum albumin.<em> BMC Struct Biol<\/em> <strong>14<\/strong> (1), 4<\/p>\n<p>Johnson, K.A., Ve, T., Larsen, \u00d8., Pedersen, R.B., Lillehaug, J.R., Jensen, H.B., Helland, R., Karlsen, O.A. (2014) CorA is a copper repressible surface-associated copper(I)-binding protein produced in <em>Methylomicrobium album<\/em> BG8 <em>PLoS ONE<\/em> <strong>9<\/strong>(2), e87750<\/p>\n<h2><strong>2013<\/strong><\/h2>\n<p>Liang, Z., Demko, V., Wilson, R.C., Johnson, K.A., Ahmad, R., Perroud, P.F., Quatrano, R., Zhao, S., Shalchian-Tabrizi, K., Otegui, M.S., Olsen, O.A., Johansen, W. (2013) The catalytic domain CysPc of the DEK1 calpain is functionally conserved in land plants <em>Plant J<\/em>. <strong>75 <\/strong>(5), 742-754<\/p>\n<p>Bj\u00f8rkeng, E., Hjerde, E., Pedersen, T., Sundsfjord, A., Hegstad, K. (2013) ICESluvan; a 94-kb mosaic Integrative Conjugative Element conferring interspecies transfer of VanB-type glycopeptide resistance, a novel bacitracin resistance locus and a toxin-antitoxin stabilisation system. <em>J Bact <\/em><strong>195<\/strong>(23), 5381-5390<\/p>\n<p>Hjerde E, Pierechod MM, Williamson AK, Bjerga GE, Willassen NP, Smal\u00e5s AO, Altermark B. (2013) Draft Genome Sequence of the <em>Actinomycete Rhodococcus<\/em> sp. Strain AW25M09, Isolated from the Hadsel Fjord, Northern Norway. <em>Genome Announc<\/em>. <strong>1 <\/strong>(2), e0005513.<\/p>\n<p>Sivertsen, A., Brandsdal, B.O., Svendsen, J.S.,\u00a0 Andersen, J.H., Svenson, J. (2013) Short cationic antimicrobial peptides bind to human alpha-1 acid glycoprotein with no implications for the in vitro bioactivity.<em> J Mol Rec<\/em> <strong>26<\/strong> (10), 461-469<\/p>\n<p>Leiros, H.K.S., Flydal, M.I., Martinez, A. (2013) Structural and thermodynamic insight into phenylalanine hydroxylase from the human pathogen <em>Legionella pneumophila.<\/em> <em>FEBS OpenBio<\/em> <strong>3<\/strong>, 370-378<\/p>\n<p>Gani, O.A.B.S.M., Narayanan, D.,\u00a0 Engh, R.A. (2013) Evaluating the predictivity of virtual screening for Abl kinase inhibitors to hinder drug resistance <em>Chem Biol Drug Des<\/em> <strong>82 <\/strong>(5), 506-519<\/p>\n<p>Purohit, A.A., Johansen, J.A., Hansen, H., Leiros, H.K., Kashulin, A., Karlsen, C., Smal\u00e5s, A., Haugen, P., Willassen, N.P. (2013) Presence of acyl-homoserine lactones in 57 members of the Vibrionaceae family.<em> J Appl Microbiol<\/em> <strong>115 <\/strong>(3), 835-847<\/p>\n<p>Gurung, M.K., R\u00e6der, I.L., Altermark, B., Smal\u00e5s, A.O. (2013) Characterization of the sialic acid synthase from <em>Aliivibrio salmonicida<\/em> suggests a novel pathway for bacterial synthesis of 7-O-acetylated sialic acids. <em>Glycobiology<\/em> <strong>23 <\/strong>(7), 806-819<\/p>\n<p>Cazam\u00e9a-Catalan, D., Magnanou, E., Helland, R., Besseau, L., Boeuf, G., Falc\u00f3n, J., J\u00f8rgensen, E.H. (2013) Unique arylalkylamine N-acetyltransferase-2 polymorphism in Salmonids and profound variations in thermal stability and catalytic efficiency\u00a0conferred by two residues.<em> J Exp Biol<\/em> <strong>216<\/strong>, 1938-1948<\/p>\n<p>Harmsen, R.A.G., Sivertsen, A., Michetti, D., Brandsdal, B.O., Sydnes, L.K., Haug, B.E. (2013) Synthesis and docking of novel piperidine renin inhibitors. <em>Monatsh Chem<\/em>\u00a0<strong>144<\/strong>, 479-494<\/p>\n<p>Borra, P.S., Samuelsen, O., Spencer, J., Walsh, T.R., Lorentzen, M.S., Leiros, H.K. (2013) Crystal structures of <em>Pseudomonas aeruginosa<\/em> GIM-1: active site plasticity in metallo-\u03b2-lactamases. <em>Antimicrob Agents Chemother<\/em> <strong>57<\/strong>(2), 848-854<\/p>\n<p>Fu, J., Leiros, H.K., de Pascale, D., Johnson, K.A., Blencke, H.M., Landfald, B. (2012) Functional and structural studies of a novel cold-adapted esterase from an Arctic intertidal metagenomic library. <em>Appl Microbiol Biotechnol<\/em> <strong>97<\/strong>(9), 3965-3978<\/p>\n<h2><strong>2012<\/strong><\/h2>\n<p>Karstad, R., Isaksen, G., Wynendaele, E., Guttormsen, Y., De Spiegeleer, B., Brandsdal, B.O., Svendsen, J.S., Svenson, J. (2012) Targeting the S1 and S3 subsite of trypsin with unnatural cationic amino acids generates antimicrobial peptides with potential for oral administration. <em>J Med Chem<\/em>. <strong>55<\/strong>(14), 6294-6305<\/p>\n<p>Ahmad, R., Hansen, G.\u00c5., Hansen, H., Hjerde, E., Pedersen, H.L., Paulsen, S.M., Nyrud, M.L.J., Willassen, N.P., Haugen, P. (2012) Prediction, microarray and Northern blot analyses identify new intergenic small RNAs in <em>Aliivibrio salmonicida<\/em>. <em>J. Mol. Micro. Biotech.<\/em> <strong>22<\/strong>(6), 352-360<\/p>\n<p>Kahlke, T., Steinar Thorvaldsen, S. (2012) Molecular characterization of cold adaptation of membrane proteins in the Vibrionaceae core-genome. <em>PLoS ONE<\/em>. <strong>7<\/strong>(12), e51761<\/p>\n<p>Hanssen, K.\u00d8., Andersen, J.H., Stiberg, T, Engh, R.A., Svenson, J., Genevi\u00e8re, A.M., Hansen, E. (2012) Antitumoral and Mechanistic Studies of Ianthelline Isolated from the Arctic Sponge Stryphnus fortis. <em>Anticancer Res<\/em> <strong>32 <\/strong>(10), 4287-4297<\/p>\n<p>\u00c5berg, E., Lund, B.A., Pflug, A., Gani, O., Rothweiler, U., de Oliveira, T.M., Engh, R.A (2012) Structural origins of AGC protein kinase inhibitor selectivities: PKA as a drug discovery tool. <em>Biol Chem<\/em>. <strong>393<\/strong> (10), 1121-1129<\/p>\n<p>Lagos, L.X., Iliev, D.B., Helland, R., Rosemblatt, M., J\u00f8rgensen, J.B. (2012) CD40L &#8211; a costimulatory molecule involved in the maturation of antigen presenting cells in Atlantic salmon (<em>Salmo salar<\/em>) <em>Dev Comp Immunol<\/em>. <strong>38<\/strong>, 416-430<\/p>\n<p>Ve, T., Mathisen, K., Helland, R., Karlsen, O.A., Fjellbirkeland, A., R\u00f8hr, \u00c5.K., Andersson, K.K., Pedersen, R.B., Lillehaug, J.R., Jensen, H.B. (2012) The <em>Methylococcus capsulatus<\/em> (Bath) secreted protein, MopE*, binds both reduced and oxidized copper. <em>PLoS ONE<\/em>. <strong>7<\/strong>, e43146<\/p>\n<p>Lindell, K., Fahlgren, A., Hjerde, E., Willassen, N.P., F\u00e4llman, M., Milton, D.L. (2012) Lipopolysaccharide O-antigen prevents phagocytosis of Vibrio anguillarum by rainbow trout (Oncorhynchus mykiss) skin epithelial cells. <em>PLoS One <\/em><strong>7<\/strong>(5, e37678<\/p>\n<p>Fu, J., Leiros, H.K., de Pascale, D., Johnson, K.A., Blencke, H.M., Landfald, B. (2012) Functional and structural studies of a novel cold-adapted esterase from an Arctic intertidal metagenomic library. <em>Appl Microbiol Biotechnol<\/em> In press<\/p>\n<p>Leiros, H.K.S., Fed\u00f8y, A.E., Leiros, I., Steen, I.H. (2012) The complex structures of Isocitrate dehydrogenase from <em>Clostridium thermocellum<\/em> and <em>Desulfotalea psychrophila<\/em>, suggest a new active site locking mechanism. <em>FEBS Open Bio<\/em>. <strong>2<\/strong>, 159-171<\/p>\n<p>Cazam\u00e9a-Catalan, D., Magnanou, E., Helland, R., Vanegas, G., Besseau, L., Boeuf, G., Paulin, C.H., J\u00f8rgensen, E.H., Falc\u00f3n, J. (2012) Functional diversity of Teleost arylalkylamine N-acetyltransferase-2: Is the timezyme evolution driven by habitat temperature? <em>Mol Ecol<\/em>. <strong>21<\/strong>, 5027-5041.<\/p>\n<p>Pflug, A., Johnson, K.A., Engh, R.A. (2012) Anomalous dispersion analysis of inhibitor flexibility &#8211; A case study of the kinase inhibitor H-89. Acta Cryst <strong>F68<\/strong>, 873-877<\/p>\n<p>Leiros, H.K.S., Borra, P.S., Brandsdal, B.O., Edvardsen, K.S.W., Spencer, J., Walsh, T.R., Samuelsen, \u00d8. (2012) Crystal Structure of the Mobile Metallo-b-Lactamase AIM-1 from <em>Pseudomonas aeruginosa<\/em>: Insights into Antibiotic Binding and the role of Gln157. <em>Antimicrob Agents Chemoter<\/em>. <strong>56<\/strong>, 4341-4353<\/p>\n<p>Kahlke, T., Goesmann, A., Hjerde, E., Willassen, N.P., Haugen, P. (2012) Unique core genomes of the bacterial family vibrionaceae: Insights into niche adaptation and speciation. <em>BMC Genomics<\/em>, <strong>13<\/strong> (1), 179<\/p>\n<p>Bjelland, A.M., S\u00f8rum, H., Tegegne, D.A., Winther-Larsen, H.C., Willassen, N.P., Hansen, H. (2012) LitR of Vibrio salmonicida Is a Salinity-Sensitive Quorum-Sensing Regulator of Phenotypes Involved in Host Interactions and Virulence. <em>Infect immune,<\/em> <strong>80<\/strong> (5), 1681-1689<\/p>\n<p>Bjornsdottir, B., Hjerde, E., Bragason,\u00a0B.T., Gudmundsdottir, T., Willassen,\u00a0N.P., Gudmundsdottir, B.K. (2012) Identification of type VI secretion systems in <em>Moritella viscosa<\/em>. <em>Vet. Microbiol<\/em>. <strong>158<\/strong>, 436-442.<\/p>\n<p>Moe, E., Hall, D.R., Leiros, I., Monsen, V.T., Timmins, J., McSweeney, S. (2012) Structure\/function studies of an unusual 3-methyladenine DNA glycosylase II (AlkA) from Deinococcus radiodurans. <em>Acta Cryst<\/em> <strong>D68<\/strong>, 703-712.<\/p>\n<p>Hansen GA, Ahmad R, Hjerde E, Fenton CG, Willassen NP, Haugen P. (2012) Expression profiling reveals Spot 42 small RNA as a key regulator in the central metabolism of <em>Aliivibrio salmonicida<\/em>. <em>BMC Genomics<\/em>. <strong>13<\/strong>, 37-49.<\/p>\n<p>McManus, H.A., Lewis, L.A., Fu\u010d\u00edkov\u00e1, K., Haugen, P. (2012). Invasion of protein coding genes by green algal ribosomal group I introns. <em>Molecular Phylogenetics and Evolution<\/em>. <strong>62<\/strong>(1), 109-116.<\/p>\n<p>Assefa, N.G., Niiranen, L., Willassen, N.P., Smal\u00e5s, A.O., Moe, E (2012) Thermal Unfolding Studies of Cold Adapted Uracil-DNA N-Glycosylase (UNG) From Atlantic Cod (<em>Gadus morhua<\/em>). A Comparative Study with Human UNG. <em>Comp Biochem Physiol B<\/em>, <strong>161<\/strong>(1),60-68.<\/p>\n<p>Karlsen C, S\u00f8rum H, Willassen NP, \u00c5sakk K (2012) Moritella viscosa bypasses Atlantic salmon epidermal keratocyte clearing activity and might use skin surfaces as a port of infection. <em>Vet Microbiol<\/em>. <strong>154<\/strong>(3-4), 353-362.<\/p>\n<p>Gruber FX, Ernst T, Porkka K, Engh RA, Mikkola I, Maier J, Lange T, Hochhaus A. (2012) Dynamics of the emergence of dasatinib and nilotinib resistance in imatinib-resistant CML patients. <em>Leukemia<\/em> <strong>26<\/strong>, 172-177.<\/p>\n<h2><strong>2011<\/strong><\/h2>\n<p>Weber B., Lindell K., Elqquaidi S., Hjerde E., Willassen N. P. and Milton D. L. The phosphotransferase VanU represses expression of four qrr genes antagonizing VanO-mediated quorum-sensing regulation in <em>Vibrio anguillarum<\/em>. <em>Microbiology<\/em>, <strong>157<\/strong>, 3324-3339.<\/p>\n<p>Karlsen C, Espelid S, Willassen NP, Paulsen SM (2011) Identification and cloning of immunogenic <em>Aliivibrio salmonicida<\/em> Pal-like protein present in profiled outer membrane and secreted subproteome. <em>Dis Aquat Org<\/em> <strong>93, <\/strong>215-223.<\/p>\n<p>Pflug, A., de Oliveira, T.M., Bossemeyer, D., Engh, R.A. (2011) &#8220;<em>Mutants of protein kinase A that mimic the ATP-binding site of Aurora kinase<\/em>&#8220;. <em>Biochem J<\/em>. <strong>440<\/strong>, 85-93.<\/p>\n<p>Rothweiler, U., \u00c5berg, E., Johnson, K.A., Hansen, T.E., J\u00f8rgensen, J.B., and Engh, R.A. (2011) &#8220;<em>p38\u03b1 MAP Kinase Dimers with Swapped Activation Segments and a Novel Catalytic Loop Conformation<\/em>&#8220;. <em>J Mol Biol<\/em> <strong>411<\/strong>, 474-48.<\/p>\n<p>Borra, P.S., Leiros, H.K., Ahmad, R., Spencer, J., Leiros, I., Walsh, T.R., Sundsfjord, A., Samuelsen, O. (2011) &#8220;<em>Structural and computational investigations of VIM-7: Insights into the substrate specificity of VIM\u00a0 metallo-beta-lactamases<\/em>&#8221; <em>J Mol Biol<\/em> <strong>411<\/strong>, 174-189.<\/p>\n<p>Oliveira, T.M., Ahmad, R., Engh, R.A (2011) &#8220;<em>Vx680 binding interactions with the glycine rich loop aromat of Aurora A<\/em>&#8220;. <em>J. Phys. Chem. A<\/em> <strong>115<\/strong>, 3895-3904.<\/p>\n<p>M.E. Prime, M.E., Courtney, S.M., Brookfield, F.A.,\u00a0 Marston, R.W.,\u00a0 Walker, V.,\u00a0 Warne, J.,\u00a0 Boyd, A.E.,\u00a0 Kairies, N.A.,\u00a0 von der Saal, W., Limberg,\u00a0 A., Georges, G.,\u00a0 Engh, R.A.,\u00a0 Goller, B.,\u00a0 Rueger, P.,\u00a0 Rueth, M. (2011) &#8220;<em>Phthalazinone pyrazoles as potent, selective and orally bioavailable inhibitors of Aurora-A kinase<\/em>&#8220;. <em>J. Med. Chem<\/em>\u00a0\u00a0<strong>54<\/strong>, 312-319<\/p>\n<p>von Bubnoff, N., Gorantla, S.P., Engh, R.A., de Oliveira, T., Th\u00f6ne, S., \u00c5berg, E., Peschel, C., Duyster, J. (2011) <em>&#8220;The low frequency of clinical resistance to PDGFR inhibitors in myeloid neoplasms with abnormalities of PDGFRA might be related to the limited repertoire of possible PDGFRA kinase domain mutations in vitro. &#8221; Oncogene,<\/em> <strong>30<\/strong>, 933-943.<\/p>\n<p>Kancha, RK; von Bubnoff, N.; Bartosch, N; Peschel, C.; Engh, Richard Alan; Duyster, J.. Irreversible inhibitors overcome lapatinib resistance due to ERBB2 kinase domain mutations. Onkologie (Basel) 2011 ;Volum 34. s. 118.<\/p>\n<p>Kancha, Rama Krishna; von Bubnoff, Nikolas; Bartosch, Natalie; Peschel, Christian; Engh, Richard Alan; Duyster, Justus. Differential sensitivity of ERBB2 kinase domain mutations towards lapatinib. PLOS ONE 2011 ;Volum 6(10):e26760.<\/p>\n<h2><strong>2010<\/strong><\/h2>\n<p>Pedersen HL, Hjerde E, Paulsen SM, Hansen H, Olsen L, Thode SK, Dos Santos MT, Paulssen RH, Willassen NP, Haugen P. (2010) Global responses of Aliivibrio salmonicida to hydrogen peroxide as revealed by microarray analysis. <em>Marine Genomics<\/em>, <strong>3<\/strong>, 193-200.<\/p>\n<p>Janowski, S., Kormeier, B., T\u00f6pel, T., Hippe, K., Hofest\u00e4dt, R,. Willassen, N.P., Friesen, R., Rubert, S., Borck, D., Haugen, P., Chen, M (2010) <em>&#8220;Modeling of cell-cell communication processes with Petri nets using the example of quorum sensing&#8221; In Silico Biology.<\/em> <strong>10<\/strong>, 0003.<\/p>\n<p>Kn\u00e6velsrud, I., Moen, M.N., Gr\u00f8svik, K., Haugland, G.T., Birkeland, N.K., Klungland, A., Leiros, I., Bjelland, S. (2010) <em>&#8220;The Hyperthermophilic Euryarchaeon Archaeoglobus fulgidus Repairs Uracil by Single Nucleotide Replacement. &#8221; J Bacteriol.<\/em><strong> 192<\/strong> (21), 5755-5766<\/p>\n<p>Byeon, I.J., Dao, K.K., Jung, J., Keen, J., Leiros, I., D\u00f8skeland, S.O., Martinez, A. &amp; Gronenborn, A.M. (2010) <em>&#8220;Allosteric communication between cAMP binding sites in the RI subunit of protein kinase A revealed by NMR. &#8221; J Biol Chem.<\/em> <strong>285<\/strong>(18), 14062-14070<\/p>\n<p>Pflug, A., Rogozina, J., Lavogina, D., Enkvist, E., Uri, A., Engh, R.A., Bossemeyer, D. (2010) <em>&#8220;Diversity of Bisubstrate Binding Modes of Adenosine Analogue-Oligoarginine Conjugates in Protein Kinase A and Implications for Protein Substrate Interactions.&#8221; J Mol Biol.<\/em> <strong>403<\/strong> (1), 66-77<\/p>\n<p>Karstad, R., Isaksen, G., Brandsdal, B.O., Svendsen, J.S., Svenson, J. (2010) <em>&#8220;Unnatural Amino Acid Side Chains as S1, S1&#8242;, and S2&#8242; Probes Yield Cationic Antimicrobial Peptides with Stability toward Chymotryptic Degradation&#8221; J Med Chem B<\/em>. <strong>53<\/strong> (15), 5558-5566<\/p>\n<p>Mereghetti, P., Riccardi, L., Fantucci, P., Brandsdal, B.O., De Gioia, L. and Papaleo, E. (2010) <em>&#8220;Near Native-State Free Energy Landscape of Psychrophilic and Mesophilic Enzymes: Probing the Folding Funnel Model&#8221; J Phys Chem B<\/em>. <strong>114<\/strong> (22), 7609-7619<\/p>\n<p>Kyomyhendo, P., Myrnes, B., Brandsdal, B.O., Smal\u00e5s, A.O., Nilsen, I.W., Helland, R. (2010) <em>&#8220;Thermodynamics and structure of a salmon cold-active goose-type lysozyme.&#8221; Comp Biochem Biophys B. <\/em>. <strong>156<\/strong>, 254-263<\/p>\n<p>Gani, O. A.B.S.M. and Engh, R.A. (2010) <em>&#8220;Protein kinase inhibition of clinically important staurosporine analogues&#8221;. Natural Product Reports.<\/em> <strong>27<\/strong> (4), 489-498.<\/p>\n<p>Leiros, H.-K.S., Brandsdal, B.O. &amp; McSweeney, S.M. (2010). <em>&#8220;Biophysical characterization and mutational analysis of the antibiotic resistance protein NimA from Deinococcus radiodurans.&#8221; Biochim Biophys Acta-Proteins and Proteomics.<\/em> <strong>1804<\/strong> (4), 967-976<\/p>\n<p>R\u00e6der, I.L.U., Moe, E., Willassen, N.P., Smal\u00e5s, A.O., Leiros, I. (2010) <em>&#8220;Structure of uracil-DNA N-glycosylase (UNG) from Vibrio cholerae: mapping temperature adaptation through structural and mutational analysis. &#8221; Acta Cryst. <\/em><strong>F66<\/strong>, 130-136.<\/p>\n<p>Pedersen, H.L., Ahmad, R., Riise E.K., Leiros, H.-K.L., Hauglid, S., Espelid, S., Brandsdal, B.O., Leiros, I, Willassen, N.P., Haugen, P. (2010). <em>&#8220;Experimental and Computational Characterisation of the Ferric Uptake Regulator from Aliivibrio salmonicida (Vibrio salmonicida) &#8220;. The Journal of Microbiology.<\/em> <strong>48<\/strong>, 174-183.<\/p>\n<h2><strong>2009<\/strong><\/h2>\n<p>von Bubnoff N, Engh RA, Aberg E, S\u00e4nger J, Peschel C and Duyster J. (2009) <em>&#8220;FMS-like tyrosine kinase 3 internal tandem duplication tyrosine kinase inhibitors display a nonoverlapping profile of resistance mutations in vitro&#8221;, Cancer Res<\/em>. <strong>69<\/strong>, 3032-41.<\/p>\n<p>von Bubnoff, N; Gorantla, SP; Engh, Richard Alan; de Oliveira, Taian\u00e1 Maia; Thoene, S; \u00c5berg, espen; Peschel, C; Duyster, J. Sorafenib and Nilotinib Are Candidates to Overcome Imatinib Resistance in Myeloproliferation with FIP1L1-PDGFRA. Blood 2009 ;Volum 114.(22) s. 1138-1138.<\/p>\n<p>Pflug, A., de Oliveira T.M., Bossemeyer D. and Engh, R.A. (2009) <em>&#8220;Mutants of protein kinase A with Aurora kinase inhibitor specificity&#8221;<\/em>, <em>Acta Biochemica Polonica<\/em> <strong>S1<\/strong>, 66-67.<\/p>\n<p>Helland, R., Larsen, R.L., Finstad, S., Kyomuhendo, P., Larsen, A.N. (2009) <em>&#8220;Crystal structures of g-type lysozyme from Atlantic cod shed new light on substrate binding and the catalytic mechanism.&#8221;<\/em> <em>Cell Mol Life Sci.<\/em> <strong>66<\/strong> ,2585-2598.<\/p>\n<p>Svenson,J., Karstad, K., Flaten, G.E., Brandsdal, B.O., Brandl, M. and Svendsen, J.S. (2009) <em>&#8220;Altered Activity and Physicochemical Properties of Short Cationic Antimicrobial Peptides by Incorporation of Arginine Analogues.&#8221;<\/em> Mol Pharmaceutics, <strong>6<\/strong>, 996-1005.<\/p>\n<p>Knaevelsrud, I., Slupphaug, G., Leiros, I., Matsuda, A., Ruoff, P., Bjelland, S. (2009) <em>&#8220;Opposite-base dependent excision of 5-formyluracil from DNA by hSMUG1.&#8221;<\/em> <em>Int J Radiat Biol<\/em> <strong>85<\/strong> ,413-420.<\/p>\n<p>Robertson, A.B., Klungland, A., Rognes, T., Leiros, I.(2009) &#8220;<em>DNA repair in mammalian cells: Base excision repair: the long and short of it.<\/em>&#8221; <em>Cell Mol Life Sci.<\/em> <strong>66<\/strong> ,981-93.<\/p>\n<p>Pedersen, H.L., Willassen, N.P., Leiros, I. (2009) &#8220;<em>The first crystal structure of a cold-adapted superoxide dismutase (SOD). Biochemical and structural characterisation of iron SOD from Vibrio salmonicida<\/em>.&#8221; <em>Acta Cryst<\/em>, <strong>F65<\/strong>, 84-92.<\/p>\n<p>Hjerde, E., Lorentzen, M.S., Holden, M.T., Seeger, K., Paulsen, S., Bason, N., Churcher, C., Harris, D., Norbertczak, H., Quail, M.A., Sanders, S., Thurston, S., Parkhill, J., Willassen, N.P., Thomson, N.R. (2009) <em>The Genome Sequence Of The Fish Pathogen Aliivibrio salmonicida Strain LFI1238 shows extensive evidence of gene decay<\/em>, <em>BMC Genomics,<\/em> <strong>9<\/strong>, 616<\/p>\n<p>Ahmad, R., Brandsdal, B.O., Michaud-Soret, I. and Willassen, N.P. (2009) &#8220;<em>Ferric uptake regulator protein: Binding free energy calculations and per-residue free energy decomposition.<\/em>&#8221; <em>Proteins,<\/em> <strong>75<\/strong> 373-386.<\/p>\n<p>Ahmad, R., Hjerde, E., Hansen, G.\u00c5., Haugen, P. &amp; Willassen, N.P. (2009) &#8220;<em>Prediction and experimental testing of Fur regulons in vibrios.<\/em>&#8221; <em>J. Mol. Microbiol. Biotechnol.<\/em> <strong>16<\/strong> 159-168.<\/p>\n<p>Helland, R., Larsen, R.L. and Asgeirsson, B. (2009) &#8220;<em>The 1.4 \u00c5 crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase.<\/em>&#8221; <em>BBA-Proteins and Proteomics,<\/em><strong>1794<\/strong>, 297-308.<\/p>\n<p>Szlachcic,A., Zakrzewska, M., Krowarsch, D., Vibeke Os, V., Helland, R., Smal\u00e5s, A.O. and Otlewski, J. (2009) \u201c<em>Structure of a highly stable mutant of human fibroblast growth factor 1<\/em>\u201d. <em>Acta Cryst D<\/em>,<strong> 65<\/strong>, 67-73.<\/p>\n<h2><strong>2008<\/strong><\/h2>\n<p>Engh, R. (2008) Protein kinase inhibitors highlight the complexities of drug target noncovalent interactions, <em>Biotechnol. &amp; Biotechnol. Eq.<\/em>, <strong>22<\/strong>, 773-777.<\/p>\n<p>Bjelic, S., Brandsdal, B.O. and \u00c5qvist, J. (2008) &#8220;<em>Cold-Adaptation of Enzyme Reaction Rates.<\/em>&#8221; <em>Biochemistry <\/em><strong>47<\/strong>(38), 10049-10057.<\/p>\n<p>Karlsen, C., Paulsen, S.M., Tunsj\u00f8, H.S., Krinner, S., S\u00f8rum, H., Haugen, P., Willassen, N.P. (2008) <em>\u201dMotility and flagellin gene expression in the fish pathogen Vibrio salmonicida: Effects of salinity and temperature.\u201d<\/em><em> Microb Pathog.<\/em> <strong>45<\/strong>(4), 258-264.<\/p>\n<p>Strandskog, G., Skj\u00e6veland, I., Ellingsen, T., J\u00f8rgensen, J.B.(2008) &#8220;<em>Double-stranded RNA- and CpG DNA-induced immune responses in Atlantic salmon: Comparison and synergies<\/em>&#8220;. <em>Vaccine<\/em>. <strong>26<\/strong>(36), 4704-4715.<\/p>\n<p>Skj\u00e6veland, I., Iliev, D.B., Zou, J., J\u00f8rgensen, T., J\u00f8rgensen, J.B. (2008) &#8220;<em>A TLR9 homolog that is up-regulated by IFN-gamma in Atlantic salmon (Salmo salar)<\/em>&#8220;. <em>Dev Comp Immunol<\/em>. <strong>32<\/strong>(6), 603-607.<\/p>\n<p>Koutsioulis, D., Wang, E., Tzanodaskalaki, M., Nikiforaki,, D., Deli, A., Feller, G., Heikinheimo, P., Bouriotis V.. (2008), &#8220;<em>Directed evolution on the cold adapted properties of TAB5 alkaline phosphatase.<\/em>&#8221; <em>Protein Eng Des Sel.<\/em> <strong>21<\/strong>, 319-327.<\/p>\n<p>Kapp,U. Macedo,S., Hall, D., Leiros,I., S. McSweeney, S. and Mitchell, E. (2008) &#8220;<em>Crystal structure of Deinococcus radiodurans tunicamycin resistance protein (TmrD): a phosphotransferase.<\/em>&#8221; <em>Acta Cryst F,<\/em>, <strong>64<\/strong>, 479-486.<\/p>\n<p>Leiros, H.-K. S., Tedesco, C. and McSweeney, S. (2008) &#8220;<em>High resolution crystal structure of the antibiotic resistance protein NimA from Deinococcus radiodurans.<\/em>&#8221; <em>Acta Cryst F.<\/em>, <strong>64<\/strong>, 442-447.<\/p>\n<p>Helland, R, Fjellbirkeland, A, Karlsen, OA, Ve, T, Lillehaug, JR &amp; Jensen, HB (2008). &#8220;<em>An oxidized tryptophan facilitates copper binding in Methylococcus capsulatus-secreted protein MopE<\/em>.&#8221; <em>J. Biol. Chem.<\/em>, <strong>283<\/strong>, 13897-13904.<\/p>\n<p>Niiranen, L., Altermark, B., Brandsdal, B.O., Leiros, H.K.S., Helland, R., Smal\u00e5s, A.O. and Willassen, N.P. (2008) &#8220;<em>Effects of salt on kinetics and thermodynamic stability of endonuclease I from Vibrio salmonicida and Vibrio cholerae.<\/em>&#8221; <em>FEBS J.<\/em>, <strong>275<\/strong>, 1593-1605.<\/p>\n<p>Kyomohendo, P., Nilsen, I.W., Brandsdal, B.O. &amp; Smal\u00e5s, A.O. (2008) &#8220;<em>Inhibition of marine g-type lysozymes by invertebrate inhibitor of lysozyme.<\/em>&#8221; <em>J. Mol. Mod.<\/em>,<strong> 14 <\/strong>, 777-788.<\/p>\n<p>Svenson, J., Stensen, W., Brandsdal, B.O., Haug, B.E., Monrad, J. &amp; Svendsen, J.S. (2008) &#8220;<em>Antimicrobial peptides with stability towards tryptic degradation.<\/em>&#8220;<em> Biochemistry.<\/em>, <strong>47<\/strong> ,3777-3788.<\/p>\n<p>Olufsen, M., Papaleo, E., Smal\u00e5s, A.O. &amp; Brandsdal, B.O. (2008). &#8220;<em>Ion pairs and their role in modulating stability of cold- and warm-active uracil DNA glycosylase.<\/em>&#8220;<em> Proteins.<\/em> <strong>71 <\/strong>, 1219-1230.<\/p>\n<p>Olufsen, M., Smal\u00e5s, A.O. &amp; Brandsdal, B.O. (2008) &#8220;<em>Electrostatic interactions play an essential role in DNA repair and cold-adaptation of Uracil DNA glycosylase.<\/em>&#8220;<em> J. Mol. Mod.<\/em>, <strong>14 <\/strong>, 201-213.<\/p>\n<p>Altermark, B., Helland, R., Moe, E., Willassen, N.P. &amp; Smal\u00e5s, A.O. (2008) &#8220;<em>Environmental adaptation of endonuclease I from Vibrio salmonicida.<\/em>&#8220;<em> Acta Cryst D.<\/em>, <strong>64<\/strong>, 368-376.<\/p>\n<h2><strong>2007<\/strong><\/h2>\n<p>Timmins, J., Leiros, I. &amp; McSweeney, S. (2007) &#8220;<em>Crystal structure and mutational study of RecOR provide insight into its mode of DNA binding.<\/em>&#8221; <em>EMBO Journal.<\/em>, <strong>26<\/strong>, 3260-3271<\/p>\n<p>Solstad, T., Stenvik, J. &amp; J\u00f8rgensen, T.\u00d8. (2007) &#8220;<em>mRNA expression patterns of the BPI\/LBP molecule in the Atlantic cod (Gadus morhua L.).<\/em>&#8220;<em> Fish &amp; Shellfish Immunology<\/em>, <strong>23<\/strong>, 260-271.<\/p>\n<p>Fed\u00f8y, A.-E., Yang, N., Martinez, A., Leiros, H.-K.S. &amp; Steen, I.H. (2007). &#8220;<em>Structural and functional properties of isocitrate dehydrogenase from the psychrophilic bacterium Desulfotalea psychrophila.<\/em>&#8221; <em>J. Mol Biol.<\/em>, <strong>372<\/strong>, 130-49.<\/p>\n<p>Leiros, H-K., Pey, A., Innselset, M., Moe, E., Leiros, I., Steen, IH. &amp; Martinez, A. (2007) &#8220;<em>Structure of phenylalanine hydroxylase from Colwellia psychrerythraea 34H, a monomeric cold active enzyme with local flexibility around the active site and high overall stability.<\/em>&#8221; <em>J. Biol. Chem.<\/em>, <strong>282<\/strong>, 21973-21986.<\/p>\n<p>Svenson, J., Brandsdal, B.O., Stensen, W. &amp; Svendsen, J.S. (2007) &#8220;<em>Albumin binding of short cationic antimicrobial micropeptides and its influence on the in vitro bactericidal effect.<\/em>&#8221; <em>J. Med. Chem.<\/em>, <strong>50<\/strong>, 3334-3339.<\/p>\n<p>Thorvaldsen, S., Hjerde, E., Fenton, C. and Willassen, N.P. (2007)&#8221;<em>Molecular characterization of cold adaptation based on ortholog protein sequences from Vibrionaceae species.<\/em>&#8221; <em>Extremophiles,<\/em> <strong>11<\/strong>, 719-732.<\/p>\n<p>S\u00e6lensminde, G., Halskau jr., \u00d8., Helland, R., Willassen, N.P., and Jonassen, I. (2007) &#8220;<em>Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins.<\/em>&#8221; <em>Extremophiles<\/em> <strong>11<\/strong>, 585-596.<\/p>\n<p>Olufsen, M., Brandsdal, B.O. and Smal\u00e5s, A.O. (2007) &#8220;<em>Comparative unfolding studies of psychrophilic and mesophilic uracil DNA glycosylase: MD simulations show reduced thermal stability of the cold-adapted enzyme.<\/em>&#8220;<em> J. Mol. Graph. Mod. <\/em><strong>26<\/strong>, 124-134.<\/p>\n<p>Papaleo, E., Olufsen, M., de Gioia, L. and Brandsdal, B.O. (2007). &#8220;<em>Optimization of electrostatics as a strategy for cold-adaptation: A case study of cold- and warm- active elastases.<\/em>&#8220;<em> J. Mol. Graph. Mod.<\/em><strong> 26<\/strong>, 93-103.<\/p>\n<p>Stokke R, Madern D, Fedoy AE, Karlsen S, Birkeland NK, &amp; Steen IH. (2007) &#8220;<em>Biochemical characterization of isocitrate dehydrogenase from Methylococcus capsulatus reveals a unique NAD(+)-dependent homotetrameric enzyme.<\/em>&#8221; <em>Arch. Microbiol.<\/em> <strong>187,<\/strong> 361-370.<\/p>\n<p>Altermark, B., Torvaldsen S., Moe, E., Smal\u00e5s, A.O., &amp; Willassen, N.P. (2007). &#8220;<em>Sequence comparison and environmental adaptation of a bacterial endonuclease<\/em>.&#8221;<em> Comput. Biol. Chem.<\/em> <strong>31<\/strong>, 163-172.<\/p>\n<p>Smith Tunsj\u00f8, H., Paulsen, S.M., Mikkelsen, H., L&#8217;Ab\u00e9e-Lund, T., Skjerve, E. and S\u00f8rum, Henning. (2007) &#8220;<em>Adaptive response to environmental changes in the fish pathogen Moritella viscose.<\/em>&#8221; <em>Res. Microbiol.<\/em> <strong>158<\/strong>, 244-250.<\/p>\n<p>Hansen, T.E. &amp; J\u00f8rgensen, J.B. (2007) &#8220;<em>Cloning and characterisation of p38 MAP kinase from Atlantic salmon. A kinase important for regulating salmon TNF-2 and IL-1\u03b2 expression.<\/em>&#8221; <em>Molecular Immunology.<\/em> <strong>44<\/strong>,3137-3146.<\/p>\n<p>Stokke, R., Karlstr\u00f6m, M., Yang, N., Leiros, I., Ladenstein, R., Birkeland, N-K. &amp; Steen, IH. (2007) &#8220;<em>Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers.<\/em>&#8221; <em>Extremophiles.<\/em> <strong>11<\/strong>, 481-493.<\/p>\n<p>Leiros, I., Nabong, MP., Gr\u00f8svik, K., Ringvoll, J., Haugland, GT., Uldal, L., Reite, K., Olsbu, IK., Kn\u00e6velsrud, I., Moe, E., Andersen, OA., Birkeland, N-K., Ruoff, P., Klungland, A. &amp; Bjelland, S. (2007) &#8220;<em>Structural basis for enzymatic excision of N1-methyladenine and N3-methylcytosine from DNA.<\/em>&#8221; <em>EMBO J.<\/em> <strong>26<\/strong>, 2206-2217.<\/p>\n<p>Leiros, H.K.S. &amp; McSweeney, S. (2007) &#8220;<em>The crystal structure of DR2241 from Deinococcus radiodurans at 1.9 \u00c5 resolution reveals a multi-domain protein with structural similarity to chelatases but also with two additional novel domains.<\/em>&#8220;<em> J. Struct. Biol.<\/em>,<strong> 159<\/strong>, 92-102.<\/p>\n<p>Wang, E., Koutsioulis, D., Leiros, H-K. S, Andersen, O.A., Hough, E., &amp; Heikinheimo, P. (2007) &#8220;<em>The Crystal Structure of Alkaline Phosphatase from the Antarctic strain TAB5<\/em>.&#8221; <em>J. Mol. Biol.<\/em><strong> 366<\/strong>, 1318-1331.<\/p>\n<p>Niiranen L., Espelid, S., Karlsen, C.R., Mustonen, M., Paulsen, S.M., Heikinheimo, P. and Willassen, N.P. (2007) &#8220;<em>Comparative expression study to increase the solubility of cold adapted Vibrio proteins in Escherichia coli.<\/em>&#8220;<em> Protein Expression and purification,<\/em><strong> 52<\/strong>, 210-218.<\/p>\n<p>Altermark, B., Niiranen, L., Willassen, N.P., Smal\u00e5s, A.O., and Moe, E. (2007). &#8220;<em>Comparative studies of endonuclease I from cold adapted Vibrio salmonicida and mesophilic Vibrio cholerae.<\/em>&#8221; <em>FEBS Journal.<\/em><strong> 274<\/strong>, 252-263.<\/p>\n<p>Riise, E. K., Lorentzen, M. S., Helland, R., Smal\u00e5s, A.O., Leiros, H-K. and Willassen, N. P. (2007) &#8220;<em>The first crystal structure of a cold active catalase from Vibrio salmonicida at 1.96 \u00c5 reveals structural aspects of cold adaptation<\/em>&#8220;<em> Acta Cryst D.<\/em><strong> D63<\/strong>, 135-148.<\/p>\n<p>R\u00e6der, I.L.U, Paulsen, S.M., Smal\u00e5s, A.O. and Willassen, N.P. (2007). &#8220;<em>Effect of fish skin mucus on the soluble proteome of Vibrio salmonicida analysed by 2-D gel electrophoresis and tandem mass spectrometry.<\/em>&#8220;<em>Microbial Pathogenesis.<\/em> <strong>42<\/strong>, 37-46.<\/p>\n<h2><strong>2006<\/strong><\/h2>\n<p>Leiros, I., Wang, E., Rasmussen, T., Oksanen, E., Repo, H., Petersen, S.B., Heikinheimo, P. &amp; Hough, E. (2006) &#8220;<em>The 2.1\u00c5 crystal structure of Aerococcus viridans L-lactate oxidase (LOX).<\/em>&#8221; <em>Acta Cryst F.<\/em><strong> 62<\/strong>, 1185-1190.<\/p>\n<p>Altermark, B., Smal\u00e5s, A.O., Willassen, N.P. and Helland, R. (2006). &#8220;<em>The structure of Vibrio cholerae extracellular endonuclease I reveals the presence of a buried chloride ion.<\/em>&#8220;<em> Acta Cryst. D<\/em>, <strong>D62<\/strong>, 1387-91<\/p>\n<p>S\u00f8rmo, C.G., Leiros, I., Brembu, T., Winge, P., Kristensen, R., Os, V. and Bones, A.M. (2006). &#8220;<em>The crystal structure of Arabidopsis thaliana RAC7\/ROP9, a plant specific Rho GTPase.<\/em>&#8220;<em>Phytochemistry<\/em>, <strong>67<\/strong>, 2332-40<\/p>\n<p>Adekoya, O. A, Willassen, N.P. and Sylte, I. (2006)&#8221;<em> Molecular insight into pseudolysin inhibition using the MM-PBSA and LIE methods.<\/em>&#8220;<em> J. Struct. Biol. <\/em><strong>153<\/strong>, 129-44.<\/p>\n<p>Lorentzen, M.S., Moe, E., Jouve, H. and Willassen, N.P. (2006). &#8220;<em>Cold adapted features of Vibrio salmonicida catalase. Characterisation and comparison to the mesophilic counterpart from Proteus mirabilis.<\/em>&#8220;<em>Extremophiles<\/em>, <strong>10<\/strong>, 427-440<\/p>\n<p>Brandsdal, B.O., Smal\u00e5s, A.O. and \u00c5qvist, J. (2006) &#8220;<em>Free energy calculations show that acidic P1 variants undergo large pKa shifts upon binding to trypsin. <\/em>&#8220;<em> Proteins.<\/em>Proteins. <strong>64<\/strong>, 740-748.<\/p>\n<p>Hajjar, E., Korkmaz, B., Gauthier, F., Brandsdal, B.O, Witko-Sarsat, V. and Reuter, N. (2006) &#8220;<em>Inspection of the binding sites of proteinase3 and design of a highly specific substrate.<\/em>&#8220;<em> J. Med. Chem.<\/em><strong>49<\/strong>, 1248-1260.<\/p>\n<p>Mekonnen, S.M., Olufsen, M., Smal\u00e5s, A.O. and Brandsdal, B.O. (2006) &#8220;<em>Predicting proteinase specificities from free energy calculations.<\/em>&#8220;<em> J. Mol. Gra. Mod. <\/em><strong>25<\/strong>, 176-185<\/p>\n<p>Moe, E. Leiros, I., Smal\u00e5s, A.O. &amp; McSweeney, S. (2006) &#8220;<em>The crystal structure of mismatch specific URAClL-DNA glycosylase (MUG) from Deinococcus radiodurans revels a noveal catalytic residue and broad substrate specificity.<\/em>&#8220;<em> J. Biol. Chem.<\/em>, <strong>281<\/strong>, 569-577.<\/p>\n<p>Riise, E.K., Lorentzen, M.S., Helland, R. and Willassen, N.P. (2006) &#8220;<em>Crystallisation and preliminary X-ray diffraction analysis of a cold adapted catalase from Vibrio salmonicida.<\/em>\u201d. <em>Acta Cryst. <\/em><strong>F62<\/strong>, 77-79.<\/p>\n<p>Adekoya, O. A, Helland, R., Willassen, N. P and Sylte, I. (2006) &#8220;<em>Comparative sequence and structure analysis reveal features of cold adaptation of an enzyme in the thermolysin family. <\/em>&#8221; <em>Proteins.<\/em>, <strong>62<\/strong>,435-449.<\/p>\n<p>Helland, R., Larsen, A.N., Smal\u00e5s, A.O. and Willassen, N.P. (2006) <em>The 1.8 \u00c5 crystal structure of a Proteinase K like enzyme from a psychrotroph Serratia species.<\/em>&#8220;<em> FEBS J.<\/em>, <strong>273<\/strong>, 61-71.<\/p>\n<p>Larsen, A.N., Moe, E., Helland, R., Gjellesvik, D.R. and Willassen, N.P. (2006) &#8220;<em>Characterization of a recombinantly expressed proteinase K like enzyme from a psychrotrophic Serratia sp.<\/em>&#8220;<em> FEBS J.<\/em>, <strong>273<\/strong>, 47-60.<\/p>\n<p>Alml\u00f6f, M., \u00c5qvist, J., Smal\u00e5s, A.O. &amp; Brandsdal, B.O. (2006) &#8220;<em>Probing the effect of point mutations at protein-protein interfaces.<\/em>&#8221; <em>Biophys. J.<\/em>, <strong>90<\/strong>, 433-442.<\/p>\n<h2><strong>2005<\/strong><\/h2>\n<p>Thorvaldsen, S., Fl\u00e5, T., and Willassen, N.P. (2005) &#8220;<em>Extracting molecular diversity between populations through sequence alignments. Biological and Medical Data Analysis. <\/em>&#8221; In Lecture Notes in Computer Science, Subseries: Lecture Notes in Bioinformatics, Vol. 3745, p317 \u2013 328. Oliveira, J.L.; Maojo, V.; Martin-Sanchez, F.; Sousa Pereira, A. (Eds.) <strong>\u00a0<\/strong><\/p>\n<p>Braun, F.N., Paulsen, S., Sear, R.P. and Warren, P.B (2005) &#8220;<em>Miscibility gap in the microbial fitness landscape.<\/em>&#8221; <em>Phys. Rev. Lett.<\/em>, <strong>94<\/strong>, 178105.<\/p>\n<p>Adekoya, O. A, Willassen, N. P and Sylte, I. (2005) &#8220;<em>The protein-protein interaction between SMPI and Thermolysin studied by molecular dynamics and MM\/PBSA calculations.<\/em>&#8221; <em>J. Biomol. Struct. Dyn.<\/em>, <strong>22<\/strong>, 521-531.<\/p>\n<p>Krowarsch, D., Zakrzewska, M., Smal\u00e5s, AO., and Otlewski, J. (2005) &#8220;<em>Structure-Function Relationships in Serine Protease\u2013Bovine Pancreatic Trypsin Inhibitor Interaction<\/em>&#8221; <em>Protein &amp; Peptide Letter<\/em>, <strong>12<\/strong>, 403-407.<\/p>\n<p>Leiros, I., Moe, E., Smal\u00e5s, A.O. and McSweeney, S. (2005) &#8220;<em>The crystal structure of Uracil-DNA N-Glycosylase (UNG) from Deinococcus radiodurans.<\/em>&#8220;<em> Acta Cryst. D61.<\/em> <strong>61<\/strong>, 1049-1056.<\/p>\n<p>Zavialov, A.V., Tischebko, V.M., Fooks, L.F., Brandsdal, B.O., \u00c5qvist, J., Zav&#8217;yalov, V.P., MacIntyre, S. and Knight S.D. (2005) &#8220;<em>Resolving the energy paradox of chaperone\/usher-mediated fibre assembly.<\/em>&#8220;<em> Biochemical J.<\/em> <strong>389<\/strong>, 685-694.<\/p>\n<p>Olufsen, M., Smal\u00e5s, A.O., Moe, E. and Brandsdal, B.O. (2005) &#8220;<em>Increased flexibility as a strategy for cold-adaptation: A comparative MD study of cold-and warm-active Uracil DNA glycosylase&#8221;<\/em> <em>J. Biol. Chem.<\/em><strong>280<\/strong>, 18042-18048.<\/p>\n<h2><strong>2004<\/strong><\/h2>\n<p>Leiros, I., McSweeney, S. and Hough, E.(2004) &#8220;<em>The reaction mechanism of Phospholipase D from Streptomyces sp. Strain PMF. Snapshots along the reaction pathway reveal a pentacoordinate reaction intermediate and an unexpected final product.<\/em>.&#8221; <em>J. Mol. Biol.<\/em>, <strong>339<\/strong>, 805-820.<\/p>\n<p>Czapinska, H., Helland, R., Smal\u00e5s, A.O. and Otlewski, J. (2004) &#8220;<em>Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants<\/em>.&#8221; <em>J. Mol. Biol.<\/em>, <strong>344<\/strong>, 1005-1020.<\/p>\n<p>Moe, E., Leiros, I., Riise, E.K, Olufsen, M., Lanes, O., Smal\u00e5s, A. O. &amp; Willassen, N. P. (2004). &#8220;<em>Optimisation of electrostatic surface potential as strategies for cold adaptation of Uracil DNA glycosylase (UNG) from cod (Gadus morhua)<\/em>.&#8221; <em>J. Mol. Biol.<\/em>,<strong> 343<\/strong>, 1221-1230.<\/p>\n<p>Leiros, H.-K. S., Brandsdal, B.O. Andersen, O.A., Helland, R.,\u00a0 Os, V., Otlewski, J., Leiros, I., Willassen, N.P. &amp; Smal\u00e5s, A.O. (2004) &#8220;<em>Trypsin specificity as elucidated by LIE calculations, X-ray structures, and association constant measurements<\/em>&#8220;. <em>Protein Science<\/em><strong>, 13<\/strong>, 1056-1070.<\/p>\n<p>Stenvik, J., Solstad,T.,\u00a0 Leiros,I.&amp; .J\u00f8rgensen, T.\u00d8. (2004). &#8220;<em>Cloning and analysis of the BPI\/LBP gene of the Atlantic cod (Gadus morhua)<\/em>&#8221; <em>Journal of Developmental and Comparative Immunology<\/em>, Vol.<strong>28<\/strong>, 307-325<\/p>\n<p>Solem, S.T., Brandsdal, B.O , Smal\u00e5s, A.O. &amp; J\u00f8rgensen, T.\u00d8. (2004) &#8221; <em>The primary structure and specificity determining residues displayed by recombinant salmon antibody domains<\/em>&#8221; <em>Mol. Immunology, Vol.<\/em> <strong>40<\/strong>:1335-1348.<\/p>\n<h2><strong>2003<\/strong><\/h2>\n<p>Andersen OA, Stokka AJ, Flatmark T, Hough E. (2003) &#8220;<em>2.0 \u00c5 resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding.<\/em>&#8221; <em>J Mol Biol<\/em>. <strong>333<\/strong>(4), 747-757.<\/p>\n<p>Leiros, I., Moe, E., Lanes, O., Smal\u00e5s, A.O., &amp; Willassen, N.P. (2003). &#8220;<em>The crystal structure of uracil-DNA-glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features<\/em>&#8220;. <em>Acta Cryst<\/em>. <strong>D59<\/strong>, 1357-1365.<\/p>\n<p>Heikinheimo, P., Helland, R., Leiros, H.K., Leiros,I., Karlsen, S., Evjen, G., Ravelli, R., Schoehn, G., Ruigrok, R., Tollersrud, .O.K., McSweeney, S. and Hough., E. (2003). &#8220;<em>The Structure of Bovine Lysosomal alpha-Mannosidase Suggests a Novel Mechanism for Low-pH Activation<\/em>&#8221; <em>J. Mol. Biol.<\/em> <strong>327<\/strong>(3), 631-644.<\/p>\n<p>Heikinheimo, P., R. Helland, Leiros, H.K., Leiros, I., Karlsen, S., Evjen, G., Ravelli, R., Schoehn, G., Ruigrok, R., Tollersrud, .O.K., McSweeney, S. and Hough., E. (2003). &#8220;<em>Structure of the Bovine Lysosomal a-mannosidase, the Enzyme Involved in the Lysosomal Storage Disease a-Mannosidosis<\/em>&#8221; <em>ESRF Highlights 2002<\/em>: 12-13.<\/p>\n<p>Helland, R., Czapinska, H., Leiros, I., Olufsen, M., Otlewski, J. &amp; Smal\u00e5s, A.O. (2003) &#8220;<em>Structural Consequences of Accomodation of Four Non-cognate Amino Acid Residues in the S1 Pocket of Bovine Trypsin and Chymotrypsin<\/em>&#8221; <em>J. Mol. Biol.<\/em> 333, 845-861.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>2026 Skogvold ACA, Leiros I, Engh RA, Erlandsen H. Biochemical characterization and mutational analysis of the tetrameric DABA transaminase EctB from the Arctic bacterium Marinobacter sp. CK1. FEBS J. 2026 Jun;293(12):3545-3564. doi: 10.1111\/febs.70441. Epub 2026 Feb 6. PMID: 41652856. 2025 Skogvold ACA, Brakestad HT, Erlandsen H, Leiros I. Crystal structure and biochemical analysis of the <a class=\"read-more\" href=\"https:\/\/site.uit.no\/norstruct\/publications\/\">Read More<\/a><\/p>\n","protected":false},"author":893,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-9","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/site.uit.no\/norstruct\/wp-json\/wp\/v2\/pages\/9","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/site.uit.no\/norstruct\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/site.uit.no\/norstruct\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/site.uit.no\/norstruct\/wp-json\/wp\/v2\/users\/893"}],"replies":[{"embeddable":true,"href":"https:\/\/site.uit.no\/norstruct\/wp-json\/wp\/v2\/comments?post=9"}],"version-history":[{"count":3,"href":"https:\/\/site.uit.no\/norstruct\/wp-json\/wp\/v2\/pages\/9\/revisions"}],"predecessor-version":[{"id":439,"href":"https:\/\/site.uit.no\/norstruct\/wp-json\/wp\/v2\/pages\/9\/revisions\/439"}],"wp:attachment":[{"href":"https:\/\/site.uit.no\/norstruct\/wp-json\/wp\/v2\/media?parent=9"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}