Jon Nissen-Meyer

Bilde av Jon Nissen-Meyer
English version of this page
Telefon +47 22857351
Brukernavn
Besøksadresse Blindernveien 31 0371 Oslo
Postadresse Postboks 1066 Blindern 0316 Oslo

Research activities

In recent years, it has become evident that antimicrobial peptides (AMPs) are produced by nearly all organisms: prokaryotes, plants, and a variety of animals, both invertebrates and vertebrates, including humans. These peptides clearly represent an important defense against microorganisms.  There has been much interest in these peptides due to the potential of developing them into useful antimicrobial additives and drugs, and due to their general biological and biochemical importance. By studying these peptides, insight has been gained into host defense systems, membrane-protein interactions, and protein modification and secretion.

Our group – The Peptide Group – has largely studied AMPs produced by lactic acid bacteria (LAB), in part because theseAMPs are very potent and they are produced by "food grade" bacteria and might consequently be utilized as relatively safe agents for preventing growth of pathogenic/undesirable microorganisms. Our research is presently focused on elucidating:

  1. structure-function relationships of AMPs
  2. the mode-of-action of AMPs
  3. how AMP-producing cells protect themself from the toxic action of the AMPs they produce.

Moreover, using insight gained from these studies, research is also focused on the construction of new and more optimal peptide variants.

We have identified, isolated and or characterized – (3D) structurally, functionally (i.e. the mode-of-action) and genetically – more than 20 different AMPs.  By use of CD- and NMR-spectroscopy, X-ray crystallography, and site-directed in vitro mutagenesis, the 3D structure and mode-of-action of these peptides and their cognate immunity proteins (proteins that AMP-producing bacteria also produce in order to protect them self from being killed by their own AMP) have been studied. In order to identify genes encoding proteins involved in the mode-of-action of AMPs, we have recently successfully applied sequencing of the whole genomes of AMP-sensitive bacteria and of corresponding bacteria that have become AMP-resistant due to long-time AMP-exposure.

 

Emneord: Biokjemi, Mikrobiologi, Proteinstruktur

Publikasjoner

  • Ekblad, Bie; Nissen-Meyer, Jon & Kristensen, Tom (2017). Whole-genome sequencing of mutants with increased resistance against the two-peptide bacteriocin plantaricin JK reveals a putative receptor and potential docking site. PLOS ONE. ISSN 1932-6203. doi: 10.1371/journal.pone.0185279. Fulltekst i vitenarkiv
  • Boye, Erik; Skotland, Tore; Østerud, Bjarne & Nissen-Meyer, Jon (2017). Doping and drug testing. EMBO Reports. ISSN 1469-221X. 18(3), s. 351–354. doi: 10.15252/embr.201643540.
  • Kristiansen, Per Eugen; Persson, Cecilia; Fuochi, Virginia; Pedersen, Anders; Karlsson, Göran & Nissen-Meyer, Jon [Vis alle 7 forfattere av denne artikkelen] (2016). Nuclear Magnetic Resonance Structure and Mutational Analysis of the Lactococcin A Immunity Protein. Biochemistry. ISSN 0006-2960. 55(45), s. 6250–6257. doi: 10.1021/acs.biochem.6b00848.
  • Oppegård, Camilla; Kjos, Morten; Veening, Jan-Willem; Nissen-Meyer, Jon & Kristensen, Tom (2016). A putative amino acid transporter determines sensitivity to the two-peptide bacteriocin plantaricin JK. MicrobiologyOpen. ISSN 2045-8827. doi: 10.1002/mbo3.363. Fulltekst i vitenarkiv
  • Ekblad, Bie; Kyriakou, Panagiota K.; Oppegård, Camilla; Nissen-Meyer, Jon; Kaznessis, Yiannis N & Kristiansen, Per Eugen (2016). Structure-Function Analysis of the Two-Peptide Bacteriocin Plantaricin EF. Biochemistry. ISSN 0006-2960. 55(36), s. 5106–5116. doi: 10.1021/acs.biochem.6b00588.
  • Nissen-Meyer, Jon; Boye, Erik; Østerud, Bjarne & Skotland, Tore (2016). Another troubling doping case is questioning WADA’s credibility again: Borderline Analysis. Lab Times. ISSN 1864-2381. 2016-5, s. 16–19.
  • Nissen-Meyer, Jon; Boye, Erik; Østerud, Bjarne & Skotland, Tore (2016). EPO Testing in Doping Control Laboratories is Absolutely No Joke. Lab Times. ISSN 1864-2381. 2016-6, s. 28–29.
  • Oppegård, Camilla; Fimland, Gunnar; Anonsen, Jan Haug & Nissen-Meyer, Jon (2015). The pediocin PA-1 accessory protein ensures correct disulfide bond formation in the antimicrobial peptide pediocin PA-1. Biochemistry. ISSN 0006-2960. 54(19), s. 2967–2974. doi: 10.1021/acs.biochem.5b00164.
  • Nissen-Meyer, Jon; Boye, Erik; Østerud, Bjarne & Skotland, Tore (2015). Problems at a WADA-accredited anti-doping lab: Puzzling Discrepancy. Lab Times. ISSN 1864-2381. 2015-5, s. 18–23.
  • Ovchinnikov, Kirill V.; Kristiansen, Per Eugen; Uzelac, Gordana; Topisirovic, Ljubisa; Kojic, Milan & Nissen-Meyer, Jon [Vis alle 8 forfattere av denne artikkelen] (2014). Defining the Structure and Receptor Binding Domain of the Leaderless Bacteriocin LsbB. Journal of Biological Chemistry. ISSN 0021-9258. 289(34), s. 23838–23845. doi: 10.1074/jbc.M114.579698.
  • Kjos, Morten; Oppegård, Camilla; Diep, Dzung Bao; Nes, Ingolf; Veening, Jan-Willem & Nissen-Meyer, Jon [Vis alle 7 forfattere av denne artikkelen] (2014). Sensitivity to the two-peptide bacteriocin lactococcin G is dependent on UppP, an enzyme involved in cell-wall synthesis. Molecular Microbiology. ISSN 0950-382X. 92(6), s. 1177–1187. doi: 10.1111/mmi.12632.
  • Sand, Sverre; Nissen-Meyer, Jon; Sand, Olav & Haug, Trude M (2013). Plantaricin A, a cationic peptide produced by Lactobacillus plantarum, permeabilizes eukaryotic cell membranes by a mechanism dependent on negative surface charge linked to glycosylated membrane proteins. Biochimica et Biophysica Acta - Biomembranes. ISSN 0005-2736. 1828(2), s. 249–259. doi: 10.1016/j.bbamem.2012.11.001.
  • Nissen-Meyer, Jon; Boye, Erik; Østerud, Bjarne & Skotland, Tore (2013). WADA-accredited doping analyses cannot always be trusted. Lab Times. ISSN 1864-2381. 2013-1, s. 18–23.
  • Haugen, Helen Sophie; Fimland, Gunnar & Nissen-Meyer, Jon (2011). Mutational Analysis of Residues in the Helical Region of the Class IIa Bacteriocin Pediocin PA-1. Applied and Environmental Microbiology. ISSN 0099-2240. 77(6), s. 1966–1972. doi: 10.1128/AEM.02488-10.
  • Sand, Sverre; Oppegård, Camilla; Ohara, S.; Iijima, Toshio; Naderi, Soheil & Blomhoff, Heidi Kiil [Vis alle 8 forfattere av denne artikkelen] (2010). Plantaricin A, a peptide pheromone produced by Lactobacillus plantarum, permeabilizes the cell membrane of both normal and cancerous lymphocytes and neuronal cells. Peptides. ISSN 0196-9781. 31(7), s. 1237–1244. doi: 10.1016/j.peptides.2010.04.010.
  • Oppegård, Camilla; Rogne, Per Anders; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2010). Structure analysis of the two-peptide bacteriocin lactococcin G by introducing D-amino acid residues. Microbiology (Reading). ISSN 1350-0872. 156, s. 1883–1889. doi: 10.1099/mic.0.038430-0.
  • Oppegård, Camilla; Emanuelsen, Linda; Thorbek, Lisbeth; Fimland, Gunnar & Nissen-Meyer, Jon (2010). The Lactococcin G Immunity Protein Recognizes Specific Regions in Both Peptides Constituting the Two-Peptide Bacteriocin Lactococcin G. Applied and Environmental Microbiology. ISSN 0099-2240. 76(4), s. 1267–1273. doi: 10.1128/AEM.02600-09.
  • Nissen-Meyer, Jon; Oppegård, Camilla; Rogne, Per Anders; Haugen, Helen Sophie & Kristiansen, Per Eugen (2010). Structure and mode-of-action of the two-peptide (class-IIb) bacteriocins. Probiotics and Antimicrobial Proteins. ISSN 1867-1306. 2, s. 52–60. doi: 10.1007/s12602-009-9021-z.
  • Nissen-Meyer, Jon; Rogne, Per Anders; Oppegård, Camilla; Haugen, Helen Sophie & Kristiansen, Per Eugen (2009). Structure-function relationships of the non-lanthionine-containing peptide (class II) bacteriocin produced by gram-positive bacteria. Current Pharmaceutical Biotechnology. ISSN 1389-2010. 10(1), s. 19–37.
  • Rogne, Per Anders; Haugen, Mads Christofer; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2009). Three-dimensional structure of the two-peptide bacteriocin plantaricin JK. Peptides. ISSN 0196-9781. 30(9), s. 1613–1621. doi: 10.1016/j.peptides.2009.06.010.
  • Haugen, Helen Sophie; Kristiansen, Per Eugen; Fimland, Gunnar & Nissen-Meyer, Jon (2008). Mutational Analysis of the Class IIa Bacteriocin Curvacin A and Its Orientation in Target Cell Membranes. Applied and Environmental Microbiology. ISSN 0099-2240. 74(21), s. 6766–6773. doi: 10.1128/AEM.01068-08.
  • Fimland, N; Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2008). Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin plantaricin EF. Biochimica et Biophysica Acta - Proteins and Proteomics. ISSN 1570-9639. 1784(11), s. 1711–1719. doi: 10.1016/j.bbapap.2008.05.003.
  • Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2008). Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin lactococcin G. Biochimica et Biophysica Acta - Proteins and Proteomics. ISSN 1570-9639. 1784. doi: 10.1016/j.bbapap.2007.12.002.
  • Oppegård, Camilla; Schmidt, Juliane; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2008). Mutational analysis of putative helix-helix interacting GxxxG-Motifs and tryptophan residues in the two-peptide bacteriocin lactococcin G. Biochemistry. ISSN 0006-2960. 47, s. 5242–5249. doi: 10.1021/bi800289w.
  • Fimland, Gunnar & Nissen-Meyer, Jon (2007). Genetically Modified Bacteriocins. I Riley, Margaret A & Gillor, Osnat (Red.), Research and Applications in Bacteriocins. Cromwell Press, Horizon Bioscience. ISSN 978-1-904933-23-6. s. 42–66.
  • Oppegård, Camilla; Fimland, Gunnar; Thorbæk, Lisbeth & Nissen-Meyer, Jon (2007). Analysis of the two-peptide bacteriocin lactococcin G and enterocin 1071 by site-directed mutagenesis. Applied and Environmental Microbiology. ISSN 0099-2240. 73(9), s. 2931–2938. doi: 10.1128/AEM.02718-06.
  • Oppegård, Camilla; Rogne, Per Anders; Emanuelsen, Linda; Kristiansen, Per Eugen; Fimland, Gunnar & Nissen-Meyer, Jon (2007). The Two-Peptide Class II Bacteriocins: Structure, Production, and Mode of Action. Journal of Molecular Microbiology and Biotechnology. ISSN 1464-1801. 13, s. 210–219. doi: 10.1159/000104750.
  • Sand, Sverre; Haug, Trude M; Nissen-Meyer, Jon & Sand, Olav (2007). The bacterial peptide pheromone plantaricin a permeabilizes cancerous, but not normal, rat pituitary cells and differentiates between the outer and inner membrane leaflet. Journal of Membrane Biology. ISSN 0022-2631. 216(2-3), s. 61–71. doi: 10.1007/s00232-007-9030-3.
  • Fimland, Gunnar; Pirneskoski, J; Kaewsrichan, J; Jutila, A; Kristiansen, Per Eugen & Kinnunen, P K [Vis alle 7 forfattere av denne artikkelen] (2006). Mutational analysis and membrane-interactions of the beta-sheet-like N-terminal domain of the pediocin-like antimicrobial peptide sakacin P. Biochimica et Biophysica Acta - Proteins and Proteomics. ISSN 1570-9639. 1764(6), s. 1132–1140.
  • Zhao, H; Sood, R; Jutila, A; Bose, S; Fimland, Gunnar & Nissen-Meyer, Jon [Vis alle 7 forfattere av denne artikkelen] (2006). Interaction of the antimicrobial peptide pheromone plantaricin A with model membranes: implications for a novel mechanism of action. Biochimica et Biophysica Acta - Biomembranes. ISSN 0005-2736. 1758(9), s. 1461–1474.
  • Spilsberg, Bjorn; Rise, Frode; Petersen, Dirk & Nissen-Meyer, Jon (2006). Thymidine secretion by hybridoma and myeloma cells. Biochemical and Biophysical Research Communications - BBRC. ISSN 0006-291X. 342, s. 221–226.
  • Fimland, Gunnar; Johnsen, Line; Dalhus, Bjørn & Nissen-Meyer, Jon (2005). The pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: Biosynthesis, structure and mode of action. Journal of Peptide Science. ISSN 1075-2617. 11, s. 688–696. doi: 10.1002/psc.699.
  • Haugen, Helen Sophie; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2005). Three-Dimensional Structure in Lipid Micelles of the Pediocin-like Antimicrobial Peptide Curvacin A. Biochemistry. ISSN 0006-2960. 44(49), s. 16149–16157 . doi: 10.1021/bi051215u.
  • Johnsen, Line; Fimland, Gunnar & Nissen-Meyer, Jon (2005). The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum. Journal of Biological Chemistry. ISSN 0021-9258. 280.
  • Johnsen, Line; Dalhus, Bjørn; Leiros, Ingar & Nissen-Meyer, Jon (2005). 1.6-Å Crystal Structure of EntA-im: A bacterial immunity protein conferring immunity to the antimicrobial activity of the pediocin-like bacteriocin enterocin A. Journal of Biological Chemistry. ISSN 0021-9258. 280, s. 19045–19050.
  • Kristiansen, Per Eugen; Fimland, Gunnar; Mantzilas, Dimitrios & Nissen-Meyer, Jon (2005). Structure and mode of action of the membrane-permeabilizing antimicrobial peptide pheromone plantaricin A. Journal of Biological Chemistry. ISSN 0021-9258. 280, s. 22945–22950.
  • Lüders, Torben; Birkemo, Gunn Alice; Andersen, Øivind; Nissen-Meyer, Jon & Nes, Ingolf F. (2005). Proline conformation-dependent antimicrobioal activity of a proline-rich histone H1N-terminal peptide fragment isolated from the skin mucus of Atlantic Salmon. Antimicrobial Agents and Chemotherapy. ISSN 0066-4804. 49(6), s. 2399–2406.
  • Lüders, Torben; Birkemo, Gunn Alice; Nissen-Meyer, Jon; Andersen, Øivind & Nes, Ingolf (2005). Proline conformation-dependent antimicrobial activity of a proline-rich histone H1 N-terminal peptide fragment isolated from the skin mucus of Atlantic salmon. Antimicrobial Agents and Chemotherapy. ISSN 0066-4804. 49(6), s. 2399–2406. doi: 10.1128/AAC.49.6.2399-2406.2005.
  • Johnsen, Line; Fimland, Gunnar; Mantzilas, Dimitrios & Nissen-Meyer, Jon (2004). Structure-function analysis of immunity proteins of pediocin-like bacteriocins: C-terminal parts of immunity proteins are involved in specific recognition of cognate bacteriocins. Applied and Environmental Microbiology. ISSN 0099-2240. 70, s. 2647–2652.
  • Birkemo, Gunn Alice; Mantzilas, Dimitrios; Lüders, Torben; Nes, Ingolf & Nissen-Meyer, Jon (2004). Identification and structural analysis of the antimicrobial domain in hipposin, a 51-mer antimicrobial peptide isolated from Atlantic halibut. Biochimica et Biophysica Acta - Proteins and Proteomics. ISSN 1570-9639. 1699, s. 221–227.
  • Kaewsrichan, J; Douglas, CWI; Nissen-Meyer, Jon; Fimland, Gunnar & Teanpaisan, R (2004). Characterization of a bacteriocin produced by Prevotella nigrescens ATCC 25261. Letters in Applied Microbiology. ISSN 0266-8254. 39, s. 451–458.
  • Birkemo, Gunn Alice; Mantzilas, Dimitris; Lüders, Torben; Nes, Ingolf F. & Nissen-Meyer, Jon (2004). Identification and structural analysis of the antimicrobial domain in hipposin, a 51-mer antimicrobial peptide isolated from Atlantic halibut. ?. 1699(01.feb), s. 221–227.
  • Birkemo, Gunn Alice; Lüders, Torben; Andersen, Øivind; Nes, Ingolf F. & Nissen-Meyer, Jon (2003). Hipposin, a histone-derived antimicrobial peptide in Atlantic halibut (Hippoglossus hippoglossus L.). Biochimica et Biophysica Acta. ISSN 0006-3002. 1646, s. 207–215.
  • Dalhus, Bjørn; Johnsen, Line & Nissen-Meyer, Jon (2003). Crystallization and preliminary X-ray data investigation of the bacterial enterocin A immunity protein at 1.65Å resolution. Acta Crystallographica Section D: Biological Crystallography. ISSN 0907-4449. D59, s. 1291–1293.

Se alle arbeider i Cristin

  • Nissen-Meyer, Jon; Skotland, Tore; Østerud, Bjarne & Boye, Erik (2019). Improving scientific practice in sports-associated drug testing. The FEBS Journal. ISSN 1742-464X. s. 1–6. doi: 10.1111/febs.14920.
  • Kristensen, Tom; Nissen-Meyer, Jon; Oppegård, Camilla; Ekblad, Bie; Kjos, Morten & Diep, Dzung Bao [Vis alle 7 forfattere av denne artikkelen] (2015). Whole genome sequencing as a tool to elucidate the mechanism of action of AMPs.
  • Kristensen, Tom; Kjos, Morten; Oppegård, Camilla; Diep, Dzung Bao; Nes, Ingolf & Nissen-Meyer, Jon (2014). Identification of bacteriocin resistance-inducing mutations by whole genome sequencing without a reference genome: The putative receptor of plantaricin JK.
  • Oppegård, Camilla; Kjos, Morten; Diep, Dzung Bao; Nes, Ingolf; Veening, Jan-Willem & Nissen-Meyer, Jon [Vis alle 7 forfattere av denne artikkelen] (2014). Genome sequencing of lactococcin G-resistant strains identified UppP, an enzyme involved in cell wall synthesis, as a putative bacteriocin receptor.
  • Ekblad, Bie; Jørgenrud, Benedicte Marie; Kristiansen, Per Eugen; Nissen-Meyer, Jon & Oppegård, Camilla (2013). Structure-Function Analysis of the Two-Peptide Bacteriocin Plantaricin EF by the use of NMR and In Vitro Site-Directed Mutagenesis.
  • Kristensen, Tom; Nissen-Meyer, Jon; Diep, Dzung Bao; Oppegård, Camilla; Nes, Ingolf & Kjos, Morten (2013). Genomic sequencing as a tool to identify bacteriocin receptors.
  • Nissen-Meyer, Jon; Kristensen, Tom; Diep, Dzung Bao & Nes, Ingolf (2012). Bakteriosiner: En gruppe antimikrobielle peptider med et stort potensial til å bekjempe patogene bakterier. NBS-nytt. ISSN 0801-3535. 3.
  • Sand, Sverre L.; Nissen-Meyer, Jon; Sand, Olav & Haug, Trude M (2011). The cationic peptide plantaricin A produced by Lactobacillus plantarum permeabilizes eukaryotic cell membranes by a mechanism dependent on negative surface charge linked to glycosylated membrane proteins. Acta Physiologica. ISSN 1748-1708. 202.
  • Oppegård, Camilla & Nissen-Meyer, Jon (2011). Immunity against two-peptide bacteriocins.
  • Oppegård, Camilla; Emanulesen, Linda; Thorbek, Lisbeth; Fimland, Gunnar & Nissen-Meyer, Jon (2010). The lactococcin G immunity protein recognizes specific regions in both peptides constituting the two-peptide bacteriocin lactococcin G.
  • Oppegård, Camilla; Rogne, Per Anders; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2010). Structure-analysis of the two-peptide bacteriocin lactococcin G by introducing D-amino acid residues.
  • Oppegård, Camilla; Emanuelsen, Linda; Thorbek, Lisbeth; Fimland, Gunnar & Nissen-Meyer, Jon (2010). The lactococcin G immunity protein recognizes specific regions in both peptides constituting the two-peptide bacteriocin lactococcin G. The FEBS Journal. ISSN 1742-464X. 277, s. 242–242.
  • Oppegård, Camilla; Rogne, Per Anders; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2009). Structure-analysis of the two-peptide bacteriocin lactococcin G by introducing D-amino acid residues.
  • Oppegård, Camilla; Emanuelsen, Linda; Thorbek, Lisbeth; Fimland, Gunnar & Nissen-Meyer, Jon (2009). The two-peptide bacteriocin lactococcin G is recognised by its cognate immunity protein indirectly through a cellular component.
  • Oppegård, Camilla; Rogne, Per Anders; Schmidt, Juliane; Kristiansen, Per Eugen; Emanuelsen, Linda & Nissen-Meyer, Jon (2008). Structural and Functional Model of the Membrane-Permeabilizing Two-Peptide Bacteriocin Lactococcin G and its Cognate Immunity Protein.
  • Sand, Sverre L.; Ohara, S.; Oppegård, Camilla; Iijima, Toshio; Blomhoff, Heidi Kiil & Nissen-Meyer, Jon [Vis alle 7 forfattere av denne artikkelen] (2008). BOTH NORMAL AND CANCEROUS LYMPHOCYTES AND NEURONS ARE PERMEABILIZED BY PLANTARICIN A, A PEPTIDE PRODUCED BY LACTOBACILLUS PLANTARUM. Acta Physiologica. ISSN 1748-1708. 193.
  • Haugen, Helen Sophie; Fimland, Gunnar; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2008). Structure and Position in Membranes of the Bacteriocin Curvacin A Based on NMR-structure and Mutagenesis Studies.
  • Haugen, Helen Sophie; Fimland, Gunnar; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2008). Structure and Position in Membranes of the Bacteriocin Curvacin A Based on NMR-structure and Mutagenesis Studies.
  • Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2008). The Three-Dimensional Structure of the Two-Peptide Bacteriocin Lactococcin G.
  • Oppegård, Camilla; Schmidt, Juliane; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2008). Analysis of the GxxxG motifs in the two-peptide bacteriocin lactococcin G by use of site-directed mutagenesis.
  • Oppegård, Camilla; Rogne, Per Anders; Schmidt, Juliane; Kristiansen, Per Eugen; Emanuelsen, Linda & Nissen-Meyer, Jon (2008). Structural and Functional Model of the Membrane-Permeabilizing Two-Peptide Bacteriocin Lactococcin G and its Cognate Immunity Protein.
  • Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2007). NMR-analysis of the 3-D structure of the two-peptide bacteriocin Lactococcin G.
  • Rise, Frode; Krengel, Ute; Gørbitz, Carl Henrik; Nissen-Meyer, Jon; Kristiansen, Per Eugen & Davies, William (2007). THE UNIVERSITY OF OSLO BIOMOLECULAR STRUCTURE PLATFORM.
  • Sand, Sverre Larsstuvold; Haug, Trude M; Fimland, Gunnar; Nissen-Meyer, Jon & Sand, Olav (2006). Membrane-permeabilizing effects of the bacterial peptide Plantaricin A on rat anterior pituitary cells. Acta Physiologica. ISSN 1748-1708. 187.
  • Sand, Sverre L.; Haug, Trude M; Nissen-Meyer, Jon & Sand, Olav (2006). Clonal rat anterior pituitary cells (GH4 cells) are permeabilized by plantaricin A, a peptide pheromone produced by Lactobacillus plantarum. SFN Abstract Viewer/Itinerary Planner.
  • Kristiansen, Per Eugen; Sand, Sverre; Haug, Trude M; Sand, Olav; Fimland, Gunnar & Zhao, Hongxia [Vis alle 10 forfattere av denne artikkelen] (2006). Structure and Mode of Action of the Membrane-Permeabilizing Antimicrobial Peptide Pheromone Plantaricin A.
  • Fimland, Gunnar; Johnsen, Line; Dalhus, Bjørn; Haugen, Helen Sofie; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2006). Analysing the mode of action of pediocin-like bacteriocins and their immunity proteins by determining their NMR- and crystal-structures, and by genetic modifications.
  • Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). NMR-analysis of the 3-D structure of the two-peptide bacteriocin Lactococcin G.
  • Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). NMR-analysis of the 3-D structure of the two-peptide bacteriocin Lactococcin G.
  • Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). NMR-analysis of the 3-D structure of the two-peptide bacteriocin lactococcin G.
  • Kristiansen, Per Eugen; Fimland, Gunnar & Nissen-Meyer, Jon (2006). The NMR structure and mode of action of the membrane-permeabilizing antimicrobial peptide pheromone plantaricin A.
  • Oppegård, Camilla; Fimland, Gunnar; Emanuelsen, Linda & Nissen-Meyer, Jon (2006). Analysis of the two-peptide bacteriocins lactococcin G and enterocin 1071 by the use of in vitro site directed mutagenesis.
  • Johnsen, Line; Fimland, Gunnar; Dalhus, Bjørn; Leiros, Ingar; Mantzilas, Dimitris & Nissen-Meyer, Jon (2006). The crystal structure (1.6 Å) of a pediocin-like immunity protein and the identification of a region in pediocin-like immunity proteins that specifically recognizes the C-terminal domain of the cognate bacteriocins.
  • Haugen, Helen Sofie; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). The three-dimensional NMR structure of th epediocin-like bacteriocin (antimicrobial peptide) curvacin A.
  • Haugen, Helen Sofie; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). The three-dimensional NMR structure of th epediocin-like bacteriocin (antimicrobial peptide) curvacin A.
  • Haugen, Helen Sofie; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). The three-dimensional NMR structure of the pediocin-like bacteriocin (antimicrobial peptide) curvacin A.
  • Oppegård, Camilla; Fimland, Gunnar; Emanuelsen, Linda & Nissen-Meyer, Jon (2006). Analysis of the two-peptide bacteriocins lactococcin G and enterocin 1071 by the use of in vitro site directed mutagenesis.
  • Haugen, Helen Sofie; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). The three-dimensional NMR structure of the pediocin-like bacteriocin (antimicrobial peptide) curvacin A.
  • Fimland, Gunnar; Johnsen, Line; Dalhus, Bjørn; Uteng, Marianne; Muhle-Goll, Claudia & Nissen-Meyer, Jon (2005). Structure function analysis of membrane-permeabilizing antimicrobial peptides (AMPs).
  • Fimland, Gunnar; Johnsen, Line; Dalhus, Bjørn; Uteng, Marianne; Muhle-Goll, Claudia & Nissen-Meyer, Jon (2005). Structure function analysis of pediocin-like bacteriocins and immunity proteins.
  • Kristiansen, Per Eugen; Fimland, Gunnar & Nissen-Meyer, Jon (2005). Structure and mode of action of the membrane permeabilizing antimicrobial peptide pheromone plantaricin A.
  • Kristiansen, Per eugen; Fimland, Gunnar; Nissen-Meyer, Jon; Borowik, T; Lindstrom, F & Bokvist, M [Vis alle 7 forfattere av denne artikkelen] (2004). Mode of action of antimicrobial sakacin P peptides with biological membranes studied by calorimetry, circular dichroism and biological MAS NMR. Biophysical Journal. ISSN 0006-3495. 86, s. 339A–339A.
  • Birkemo, Gunn Alice; Lüders, Torben; Andersen, Øivind; Nes, Ingolf F. & Nissen-Meyer, Jon (2004). Hipposin, a histone-derived antimicrobial peptide in Atlantic halibu.
  • Bråthe, Anders; Gundersen, Lise-Lotte; Rise, Frode; Malterud, Karl Egil; Nissen-Meyer, Jon & Spilsberg, Bjørn (2004). Antioxidant and Cytotoxic Properties of Some 6-Substituted Purines.
  • Kristiansen, Per Eugen; Nissen-Meyer, Jon & Fimland, Gunnar (2004). Mode of action of antimicrobial sakacin P peptides with biological membranes studied by calorimetry, circular dichroism and biological MAS NMR.
  • Nissen-Meyer, Jon (2004). Peptide bacteriocins (antimicrobial peptides) produced by gram positive bacteria: Synthesis, structure, and mode of action.
  • Nissen-Meyer, Jon (2004). Peptide bacteriocins (antimicrobial peptides) produced by gram positive bacteria: Synthesis, structure and mode of action.
  • Johnsen, Line; Fimland, Gunnar; Dalhus, Bjørn & Nissen-Meyer, Jon (2004). The C-terminal domain of pediocin-like antimicrobial peptides is involved in determining the antimicrobial spectrum and in specifying recognition of the C-terminal part of the cognate immunity protein.
  • Fimland, Gunnar; Johnsen, Line; Dalhus, Bjørn & Nissen-Meyer, Jon (2004). Structure-function analysis of the pediocin-like antimicrobial peptides: Their three-dimensional structure, orientation in membranes, and domain functions.
  • Fimland, Gunnar; Uteng, Marianne; Johnsen, Line & Nissen-Meyer, Jon (2004). Pediocin-like antimicrobial peptides (class IIa bacteriocins): Their three dimmensional structure and orientation in membranes.
  • Fimland, Gunnar; Zhao, Hongxia; Mantzilas, Dimitrios; Kinnunen, Paavo & Nissen-Meyer, Jon (2004). Analyses of inetactions of antimicrobial peptides (plantaricin A and sakacin P) with liposomes and phospholipid monolayers using fluorescence spectrometry and a membrane monolayer technique.
  • Johnsen, Line; Fimland, Gunnar; Mantzilas, Dimitrios & Nissen-Meyer, Jon (2004). Structure-function analysis of immunity proteins of pediocin-like bacteriocins: The C-terminal part of the immunity proteins is involved in specific recognition of cognate becteriocins.
  • Kristiansen, Per Eugen; Nissen-Meyer, Jon; Fimland, Gunnar & Haugen, Helen Sofie (2004). Optimizing the conditions for NMR structural analysis of the antimicrobial peptide Curvacin A, A bactericine produced by Lactobacillus Curvatus.
  • Kaewsrichan, Jasadee; Fimland, Gunnar & Nissen-Meyer, Jon (2004). Site directed mutagenesis of the highly conserved YGNGV-motif in pediocin-like bacteriocins.
  • Haugen, Helen sofie; Kristiansen, Per Eugen; Fimland, Gunnar & Nissen-Meyer, Jon (2004). Optimising the coditions for NMR structural analysis of the antimicrobial peptide curvacin A, a bacteriocin produced by Lactobacillus curvatus.
  • Birkemo, Gunn Alice; Lüders, Torben; Andersen, Øivind; Nes, Ingolf & Nissen-Meyer, Jon (2004). Hipposin, a histone-derived antimicrobial peptide in Atlantic halibut.

Se alle arbeider i Cristin

Publisert 4. nov. 2010 14:45 - Sist endret 28. sep. 2021 11:30