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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.
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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.
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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.
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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.
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Kristensen, Tom; Nissen-Meyer, Jon; Diep, Dzung Bao; Oppegård, Camilla; Nes, Ingolf & Kjos, Morten
(2013).
Genomic sequencing as a tool to identify bacteriocin receptors.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
-
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.
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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.
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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.
Vis sammendrag
Peptide bacteriocins kill bacteria by permeabilizing their membrane. Some peptide bacteriocins (referred to as two-peptide bacteriocins), such as lactococcin G, consist of two different peptides and both peptides must be present in order for the bacteriocin to kill the target bacteria. Circular dichroism (CD) studies indicate that the two peptides of two-peptide bacteriocins interact physically with each other and that they adopt an α-helical structure upon contact with target membranes. All two-peptide bacteriocins contain GxxxG-motifs which are known to mediate helix-helix interactions in membrane proteins. Many of the GxxxG-motifs in two-peptide bacteriocins are located in putative amphiphilic α-helical regions and may play an important role in peptide-peptide interactions. Lactococcin G contains three such GxxxG-motifs, two in the α-peptide (G7xxxG11 and G18xxxG22) and one in the β-peptide (G18xxxG22). In this study, site-directed mutagenesis combined with CD measurements were used to analyse the role of the three GxxxG-motifs. The results indicate that the G7xxxG11-motif in the α-peptide and G18xxxG22-motif in the β-peptide are important in helix-helix interactions between the two lactococcin G peptides and that the two peptides form a transmembrane helix-helix structure.
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Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen
(2008).
The Three-Dimensional Structure of the Two-Peptide Bacteriocin Lactococcin G.
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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.
Vis sammendrag
Curvacin A is a pediocin-like (class IIa) bacteriocin produced by Lactabacillus curvatus LTH 1174. The three-dimensional structure of curvacin A has been determined by NMR-spectroscopy. The structure reveals that curvacin A consists of two structural elements: a cationic -sheet like N-terminal half followed by a helix-hinge-helix motif. The helix-hinge-helix motif is made up of a short polar helix and a longer C-terminal hydrophobic helix separated by a hinge region. Site-directed in vitro mutagenesis has been carried out on curvacin A. Based on these results along with the NMR-structure, a model for insertion of curvacin A in target membranes has been proposed. In this model, the N-terminal -sheet like half and the short central polar helix are positioned in the membrane interface, whereas the longer hydrophobic C-terminal helix penetrates into the hydrophobic core of membranes. Three glycine residues in the C-terminal helix form a GxxxG-like motif that might mediate close contact with an interaction partner allowing helix-helix interactions.
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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.
Vis sammendrag
Lactic acid bacteria (LAB) produce antimicrobial peptides, generally termed bacteriocins. The bacteriocins are part of the innate defence system of the producing bacteria. Targeting the membrane of cells, the bacteriocins render the membrane permeable to ions and small molecules, thereby killing the cell. Curvacin A is a pediocin-like (class IIa) bacteriocin produced by Lactabacillus curvatus LTH 1174 (LMGT 2355). The three-dimensional structure of curvacin A has been determined by NMR-spectroscopy. The structure reveals that curvacin A consists of two structural elements: a cationic -sheet like N-terminal half followed by a helix-hinge-helix motif. The helix-hinge-helix motif is made up of a short polar helix and a longer C-terminal hydrophobic helix separated by a hinge region. Site-directed in vitro mutagenesis has been carried out on curvacin A. Based on these results along with the NMR-structure, a model for insertion of curvacin A in target membranes has been proposed. In this model, the N-terminal -sheet like half and the short central polar helix are positioned in the membrane interface, whereas the longer hydrophobic C-terminal helix penetrates into the hydrophobic core of membranes. Three glycine residues in the C-terminal helix form a GxxxG-like motif that might mediate close contact with an interaction partner allowing helix-helix interactions.
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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.
Vis sammendrag
Lactococcin G is an unmodified two peptide bacteriocin. The bacteriocin consists of the 39 amino acid -peptide (LcnGα) and the 35 amino acid -peptide (LcnG). Both peptides, and , are required in about equal amounts in order for the bacteriocin to permeabilize target-cell membranes and thereby exert its antimicrobial activity (Nissen-Meyer et al). The peptides are unstructured in water but becomes structured when in contact with membranes (Hauge et al).
The three dimensional structure of the two peptides have been determined in a membrane mimicking environment using NMR (figure 1). The structures of the two peptides are α-helical and contains helix-helix interaction motifs.
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Rise, Frode; Krengel, Ute; Gørbitz, Carl Henrik; Nissen-Meyer, Jon; Kristiansen, Per Eugen & Davies, William
(2007).
THE UNIVERSITY OF OSLO BIOMOLECULAR STRUCTURE PLATFORM.
Vis sammendrag
In-depth understanding of the mode of action of proteins and other biomolecules relies to a large extent on knowledge of their three-dimensional structures. Such knowledge is necessary for understanding bio-recognition and response processes, and is required for rational design of specific pharmacological reagents. Consequently it is essential for research in the molecular biosciences to determine the structures of biomolecules. We have applied for funding. with a grant proposal to EMBIO, to establish and manage a “Biomolecular Structure Platform” at the University of Oslo. The intention of the platform is to make methods for structure determination of biomolecules available to a larger group of the biomedical and biological communities. Moreover, it is also aimed to provide assistance in large-scale production and purification of proteins for structural studies. The principle objectives and purposes of the “Biomolecular Structure-Platform” are to:
1. Establish and develop methods for large-scale production and purification of isotope labeled proteins and peptides for structural analysis.
2. Determine the structure of proteins under investigation by the contributing groups, and thereby gain detailed insight into how these proteins function at a molecular level.
3. Serve other research groups that need assistance in production and purification of 13C, 15N and Se-Met labeled proteins and peptides.
4. Provide assistance to other research groups that wish to analyze the structure of proteins, peptides and other biomolecules by NMR-spectroscopy and X-ray crystallography, mainly in the context of collaborative research.
5. Strengthen the expertise in both three-dimensional structure- and function- analysis of biological macromolecules by performing a variety of experiments and employing different structure determination tools and also by educating Ph.D.- and Master- degree students in structure determination and analysis.
6. Strengthen the expertise in large-scale production and purification of proteins by educating Ph.D.- and Master- degree students in relevant techniques.
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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.
Vis sammendrag
Antimicrobial peptides and proteins, generally referred to as bacteriocins, are produced by numerous strains of bacteria. Plantaricin A (PlnA) is a 26-mer peptide pheromone that induces bacteriocin production in the strain from which it is released, Lactobacillus plantarum C11. Although pheromone activity is the prime biological function of PlnA, the peptide also has membrane-permeabilizing strain-specific antibacterial activity.
The pheromone activity of PlnA depends on its binding to specific receptors, preceded by a non-chiral interaction with the target cell membrane. The latter mechanism is presumably responsible for the membrane-permeabilizing effect on sensitive strains.
We have studied the effect of PlnA on the GH4 cell line using the patch clamp techniques. This neoplastic cell line is derived from a rat anterior pituitary tumor, and is commonly used as a model system for anterior pituitary cells. Whole-cell current clamp recordings revealed massive membrane permeabilization within 5 s after exposure to 10-100 µM PlnA. The membrane depolarized to abut 0 mV and the membrane resistance decreased to a mere fraction of the initial value after less than 1 min. Recordings from outside-out patches during exposure to 10 µM PlnA showed that the induced membrane current reversed at 0 mV, indicating an unspecific conductance increase. The D-form of the peptide, composed of only D-amino acids, was as effective as the L-form, indicating that PlnA exerts its membrane-permeabilizing effect through a non-chiral mechanism. Recordings from inside-out patches during exposure of the internal leaflet of the cell membrane to 1 mM PlnA showed both unaltered membrane conductance and BK channel activity. These results suggest that the peptide does not interfere with the membrane integrity when the inner leaflet is exposed. Surprisingly, the normal counterparts of the GH4 cell line, primary cell cultures of rat anterior pituitary, were insensitive to the peptide. Even at a concentration of 1 mM, PlnA had no detectable effects on the membrane conductance of normal anterior pituitary cells in any of the patch clamp configurations. Thus, the peptide seems to differentiate not only between membrane leaflets, but also between plasma membranes. This characteristic makes the membrane permeabilizing effects of PlnA particularly intriguing.
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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.
-
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.
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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.
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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.
Vis sammendrag
Lactococcin G is a bacteriocin that consists of two peptides, the peptide with 39 residues and the peptide with 35 residues. Both peptides are required in about equal amounts in order for the bacteriocin to permeabilize target-cell membranes and thereby exert its antimicrobial activity. As determined by CD-spectroscopy, the two peptides interact with each other and become structured – adopting a partial amphiphilic -helical conformation – when exposed to membrane-like entities.[1] In this study, NMR-spectroscopy has been used to analyse the 3-D structure of the lactococcin G peptides seperatly upon exposure to dodecylphosphocoline micelles. The interactions between the two peptides will be the scope of further investigation. 15N labelled peptides were obtained using a fusion protein based over-expression system in E. coli.
The peptides were assigned using 15N-HSQC-TOCSY and 15N-HSQC-NOESY in combination with 2D-TOCSY and NOESY spectra. The structures were calculated using both NOE-distance restraints and dihedral-angle restraints calculated on the basis of the chemical shift values [2] , using CYANA [3].
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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.
Vis sammendrag
Lactococcin G is an unmodified two peptide bacteriocin, the name bacteriocin stems from its potential to kill bacteria. The bacteriocin consists of the 39 amino acid -peptide (LcnGα) and the 35 amino acid -peptide (LcnG) (figure 2). Both peptides, and , are required in about equal amounts in order for the bacteriocin to permeabilize target-cell membranes and thereby exert its antimicrobial activity (Nissen-Meyer et al). The peptides are unstructured in water but becomes structured when in contact with membranes (Hauge et al). In this project, the three dimensional structure of the two peptides will be determined in a membrane mimicking environment using NMR.
-
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.
Vis sammendrag
Lactococcin G is an unmodified two peptide bacteriocin. The bacteriocin consists of the 39 amino acid -peptide (LcnGα) and the 35 amino acid -peptide (LcnG) (figure 4). Both peptides, and , are required in about equal amounts in order for the bacteriocin to permeabilize target-cell membranes and thereby exert its antimicrobial activity (Nissen-Meyer et al). The peptides are unstructured in water but becomes structured when in contact with membranes (Hauge et al). In this project, the three dimensional structure of the two peptides will be determined in a membrane mimicking environment using NMR.
-
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.
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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.
-
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.
-
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.
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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.
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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.
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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.
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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.
-
Kristiansen, Per Eugen; Fimland, Gunnar & Nissen-Meyer, Jon
(2005).
Structure and mode of action of the membrane permeabilizing antimicrobial peptide pheromone plantaricin A.
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Fimland, Gunnar; Johnsen, Line; Dalhus, Bjørn; Uteng, Marianne; Muhle-Goll, Claudia & Nissen-Meyer, Jon
(2005).
Structure function analysis of membrane-permeabilizing antimicrobial peptides (AMPs).
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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.
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Birkemo, Gunn Alice; Lüders, Torben; Andersen, Øivind; Nes, Ingolf F. & Nissen-Meyer, Jon
(2004).
Hipposin, a histone-derived antimicrobial peptide in Atlantic halibu.
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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.
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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.
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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.
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Nissen-Meyer, Jon
(2004).
Peptide bacteriocins (antimicrobial peptides) produced by gram positive bacteria: Synthesis, structure and mode of action.
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Nissen-Meyer, Jon
(2004).
Peptide bacteriocins (antimicrobial peptides) produced by gram positive bacteria: Synthesis, structure, and mode of action.
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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.
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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.
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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.
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Birkemo, Gunn Alice; Lüders, Torben; Andersen, Øivind; Nes, Ingolf & Nissen-Meyer, Jon
(2004).
Hipposin, a histone-derived antimicrobial peptide in Atlantic halibut.
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Kaewsrichan, Jasadee; Fimland, Gunnar & Nissen-Meyer, Jon
(2004).
Site directed mutagenesis of the highly conserved YGNGV-motif in pediocin-like bacteriocins.
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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.
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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.
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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.
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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.
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Lüders, Torben; Birkemo, Gunn Alice; Andersen, Øivind; Nissen-Meyer, Jon & Nes, Ingolf F.
(2003).
Proline conformation-dependant antimicrobial activity of a proline-rich histone H1 N-terminal peptide fragment isolated from the skin mucos of Atlantic salmon.