المؤلفون: Brian S. Vad, Jan Skov Pedersen, Andreas Bøggild, Madhu Nagaraj, Mumdooh Ahmed, Jeppe Lyngsø, Anne Fillipsen, Daniel E. Otzen, Ümit Akbey

المصدر: Nagaraj, M, Ahmed, M, Lyngsø, J, Vad, B S, Bøggild, A, Fillipsen, A, Pedersen, J S, Otzen, D E & Akbey, Ü 2020, ' Predicted Loop Regions Promote Aggregation : A Study of Amyloidogenic Domains in the Functional Amyloid FapC ', Journal of Molecular Biology, vol. 432, no. 7, pp. 2232-2252 . https://doi.org/10.1016/j.jmb.2020.01.044

مصطلحات موضوعية: Amyloid, Mutant, Nucleation, Amyloidogenic Proteins, Fibril, polymorphism, Protein Aggregates, 03 medical and health sciences, 0302 clinical medicine, Bacterial Proteins, Structural Biology, Pseudomonas, fibrillation mechanism, Amino Acid Sequence, Molecular Biology, 030304 developmental biology, solid state NMR, 0303 health sciences, Small-angle X-ray scattering, Chemistry, SAXS, functional amyloid fibril FapC, Phenotype, Mutation, Biophysics, 030217 neurology & neurosurgery

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f0f60043b5fcda772fa980ff6e8364c
https://doi.org/10.1016/j.jmb.2020.01.044

المؤلفون: Guanghong eZeng, Brian S Vad, Morten S Dueholm, Gunna eChristiansen, Martin eNilsson, Tim eTolker-Nielsen, Per Halkjær Nielsen, Rikke Louise Meyer, Daniel E Otzen

المصدر: Frontiers in Microbiology, Vol 6 (2015)

مصطلحات موضوعية: Amyloid, Pseudomonas, Biofilm, AFM, force spectroscopy, Contact angle, Microbiology, QR1-502

وصف الملف: electronic resource

Relation: http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01099/full; https://doaj.org/toc/1664-302X

URL الوصول: https://doaj.org/article/a24b49f924aa4b228d62b1dca2797cbf

المؤلفون: Carina Lynggaard, Brian S. Vad, Maria Andreasen, Jan J. Enghild, Daniel E. Otzen, Gunna Christiansen, Casper Bøjer Rasmussen

المصدر: Protein Science. 28:633-642

مصطلحات موضوعية: Fibrillation, Genetics, 0303 health sciences, Amyloid, 030302 biochemistry & molecular biology, Mutant, Biofilm, Context (language use), Biology, Fibril, medicine.disease_cause, Biochemistry, 03 medical and health sciences, medicine, medicine.symptom, Molecular Biology, Escherichia coli, Gene, 030304 developmental biology

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::883c257dc51d0842cb8cc07c4d68ad66
https://doi.org/10.1002/pro.3566

المؤلفون: Rikke Louise Meyer, Gunna Christiansen, Guanghong Zeng, Per Halkjær Nielsen, Staffan Kjelleberg, Morten Simonsen Dueholm, Marcel Stenvang, Susana Geifman-Shochat, Brian S. Vad, Thomas Seviour, Daniel E. Otzen, Mads Toft Søndergaard

المساهمون: School of Biological Sciences, Singapore Centre for Environmental Life Sciences Engineering

المصدر: Stenvang, M R, Dueholm, M S, Vad, B S, Seviour, T, Zeng, G, Geifman-Shochat, S, Søndergaard, M T, Christiansen, G, Meyer, R L, Kjelleberg, S, Nielsen, P H & Otzen, D E 2016, ' Epigallocatechin gallate remodels overexpressed functional amyloids in pseudomonas aeruginosa and increases biofilm susceptibility to antibiotic treatment ', The Journal of Biological Chemistry, vol. 291, no. 51, pp. 26540-26553 . https://doi.org/10.1074/jbc.M116.739953
Stenvang, M, Dueholm, M S, Vad, B S, Seviour, T W, Zeng, G, Geifman-Shochat, S, Søndergaard, M T, Christiansen, G, Meyer, R L, Kjelleberg, S, Otzen, D E & Nielsen, P H 2016, ' Epigallocatechin Gallate Remodels overexpressed Functional Amyloids in Pseudomonas aeruginosa and Increases Biofilm Susceptibility to Antibiotic Treatment ', Journal of Biological Chemistry, vol. 291, no. 51, pp. 26540-26553 . https://doi.org/10.1074/jbc.M116.739953

مصطلحات موضوعية: 0301 basic medicine, Amyloid, 030106 microbiology, macromolecular substances, Epigallocatechin gallate, Fibril, medicine.disease_cause, complex mixtures, Biochemistry, Catechin, Microbiology, 03 medical and health sciences, chemistry.chemical_compound, Pyocyanin, Bacterial Proteins, Drug Resistance, Bacterial, medicine, Humans, Pseudomonas Infections, heterocyclic compounds, Benzothiazoles, Molecular Biology, Chemistry, Pseudomonas aeruginosa, Biofilm, food and beverages, Gene Expression Regulation, Bacterial, Cell Biology, Science::Biological sciences [DRNTU], Thiazoles, Quorum sensing, 030104 developmental biology, Biofilms, Protein Structure and Folding, Tobramycin, Thioflavin, sense organs

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fee2de00cc6cc58821d4b4031b75634
https://doi.org/10.1074/jbc.m116.739953

المؤلفون: Rosa Bartucci, Manuela Pantusa, Ove Lillelund, Daniel E. Otzen, Lars Kjær, Brian S. Vad

المصدر: Pantusa, M, Vad, B, Lillelund, O, Kjær, L, Otzen, D & Bartucci, R 2016, ' Alpha-synuclein and familial variants affect the chain order and the thermotropic phase behavior of anionic lipid vesicles ', B B A-Proteins and Proteomics, vol. 1864, pp. 1206-1214 . https://doi.org/10.1016/j.bbapap.2016.05.003

مصطلحات موضوعية: Protein Conformation, alpha-Helical, 0301 basic medicine, Protein Folding, Circular dichroism, Lipid Bilayers, Biophysics, Gene Expression, Plasma protein binding, Biochemistry, Thermotropic crystal, Phase Transition, Analytical Chemistry, Structure-Activity Relationship, 03 medical and health sciences, Humans, Protein Interaction Domains and Motifs, Lipid bilayer, Molecular Biology, Chemistry, Vesicle, Bilayer, Phosphatidylglycerols, Recombinant Proteins, Solutions, Crystallography, 030104 developmental biology, Membrane, Amino Acid Substitution, Mutation, Phosphatidylcholines, alpha-Synuclein, Thermodynamics, Protein Conformation, beta-Strand, Protein folding, Protein Binding

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d2bf38487ee3c115db68991dfe1645a
https://doi.org/10.1016/j.bbapap.2016.05.003

المؤلفون: Daniel E. Otzen, Troels Skrydstrup, Brian S. Vad, Claudia U. Hjørringgaard, Julie L. H. Madsen

المصدر: Madsen, J L H, Hjørringgaard, C U, Vad, B S, Otzen, D & Skrydstrup, T 2016, ' Incorporation of β-Silicon-β3-Amino Acids in the Antimicrobial Peptide Alamethicin Provides a 20-Fold Increase in Membrane Permeabilization ', Chemistry: A European Journal, vol. 22, no. 24, pp. 8358-8367 . https://doi.org/10.1002/chem.201600445

مصطلحات موضوعية: Silicon, Cell Membrane Permeability, Peptidomimetic, Peptide, 010402 general chemistry, 01 natural sciences, Protein Structure, Secondary, Catalysis, chemistry.chemical_compound, Anti-Infective Agents, Alamethicin, Amino Acids, Solid-Phase Synthesis Techniques, chemistry.chemical_classification, 010405 organic chemistry, Circular Dichroism, Organic Chemistry, General Chemistry, Antimicrobial, Combinatorial chemistry, 0104 chemical sciences, Amino acid, Membrane, chemistry, Membrane protein, Liposomes, Lipophilicity, Antimicrobial Cationic Peptides

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efb980e156c3e508d8529b15f88e880c
https://doi.org/10.1002/chem.201600445

المؤلفون: Gunna Christiansen, Line Friis Bakmann Christensen, Daniel E. Otzen, Brian S. Vad, Janni Nielsen, Kirstine Friis Jensen

المصدر: ACS Omega
Christensen, L F B, Jensen, K F, Nielsen, J, Vad, B S, Christiansen, G & Otzen, D E 2019, ' Reducing the Amyloidogenicity of Functional Amyloid Protein FapC Increases Its Ability To Inhibit α-Synuclein Fibrillation ', ACS Omega, vol. 4, no. 2, pp. 4029-4039 . https://doi.org/10.1021/acsomega.8b03590
ACS Omega, Vol 4, Iss 2, Pp 4029-4039 (2019)

مصطلحات موضوعية: Amyloid, General Chemical Engineering, BIOGENESIS, macromolecular substances, Fibril, CLASSIFICATION, Article, lcsh:Chemistry, Fibril formation, PARKINSONS-DISEASE, FILAMENTS, medicine, BRAIN, INNERVATION, Fibrillation, Chemistry, BIOFILM FORMATION, Biofilm, General Chemistry, AGGREGATION, Cell biology, CURLI, lcsh:QD1-999, Bacterial virulence, GASTROINTESTINAL-TRACT, α synuclein, medicine.symptom, Biogenesis

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8b7aa29f20783394b40ed7baa825953
https://pubmed.ncbi.nlm.nih.gov/31459612

المؤلفون: Casper B, Rasmussen, Gunna, Christiansen, Brian S, Vad, Carina, Lynggaard, Jan J, Enghild, Maria, Andreasen, Daniel, Otzen

المصدر: Protein science : a publication of the Protein Society. 28(3)

مصطلحات موضوعية: Models, Molecular, Amyloid, Kinetics, Protein Aggregates, Pseudomonas, Full‐Length Papers, Humans, Amyloidogenic Proteins, Pseudomonas Infections, Amino Acid Sequence

URL الوصول: https://explore.openaire.eu/search/publication?articleId=pmid________::27b55ffe69f6215970d6da76efd2a7ef
https://pubmed.ncbi.nlm.nih.gov/30592554

المؤلفون: Tim Tolker-Nielsen, Gunna Christiansen, Kell K. Andersen, Daniel E. Otzen, Lars Kjær, Brian S. Vad

المصدر: Andersen, K K, Vad, B S, Kjaer, L, Tolker-Nielsen, T, Christiansen, G & Otzen, D E 2018, ' Pseudomonas aeruginosa rhamnolipid induces fibrillation of human α-synuclein and modulates its effect on biofilm formation ', FEBS Letters, vol. 592, no. 9, pp. 1484-1496 . https://doi.org/10.1002/1873-3468.13038

مصطلحات موضوعية: 0301 basic medicine, Amyloid, Biophysics, Fibril, medicine.disease_cause, Biochemistry, Permeability, 03 medical and health sciences, chemistry.chemical_compound, Protein Aggregates, Structural Biology, Genetics, medicine, Humans, Molecular Biology, Micelles, Fibrillation, Pseudomonas aeruginosa, Biofilm, Rhamnolipid, Cell Biology, Kinetics, 030104 developmental biology, Membrane, chemistry, Biofilms, alpha-Synuclein, α synuclein, Protein Conformation, beta-Strand, medicine.symptom, Glycolipids

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b8fdfb8004d1ca03265e9b90f5b1bbf
https://pure.au.dk/portal/da/publications/pseudomonas-aeruginosa-rhamnolipid-induces-fibrillation-of-human-synuclein-and-modulates-its-effect-on-biofilm-formation(40d02970-b47b-4b98-b4c8-22811d2e0290).html

المؤلفون: Gunna Christiansen, Poul Larsen, Andreas Bøggild, Per Halkjær Nielsen, Marcel Stenvang, Daniel E. Otzen, Kai Finster, Morten Simonsen Dueholm, Brian S. Vad

المصدر: Dueholm, M S, Larsen, P, Finster, K, Stenvang, M R, Christiansen, G, Vad, B S, Bøggild, A, Otzen, D E & Nielsen, P H 2015, ' The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids ', Journal of Biological Chemistry, vol. 290, no. 33, pp. 20590-20600 . https://doi.org/10.1074/jbc.M115.654780
Dueholm, M S, Larsen, P, Finster, K, Stenvang, M R, Christiansen, G, Vad, B S, Bøggild, A, Otzen, D E & Halkjær Nielsen, P 2015, ' The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids ', Journal of Biological Chemistry, vol. 290, pp. 20590-26600 . https://doi.org/10.1074/jbc.M115.654780

مصطلحات موضوعية: Amyloid, Proteases, medicine.diagnostic_test, Proteolysis, Cell Biology, Methanosarcinales, Biology, biology.organism_classification, Microbiology, Biochemistry, Cell wall, Microscopy, Electron, Transmission, Tandem Mass Spectrometry, mental disorders, Biophysics, Extracellular, medicine, Extreme environment, Protein folding, Molecular Biology, Archaea

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bdcc273235335ded00d7413af004b37
https://doi.org/10.1074/jbc.m115.654780

المؤلفون: Brian S. Vad, Heidi F. Christoffersen, Erik Nielsen, Troels Skrydstrup, Jakob Nielsen, Sara K. Hansen, Daniel E. Otzen, Thomas Vosegaard

المصدر: Frahm, H, Hansen, S K, Vad, B S, Nielsen, E H, Nielsen, J T, Vosegaard, T, Skrydstrup, T & Otzen, D E 2015, ' The natural, peptaibolic peptide SPF-5506-A4 adopts a β-bend spiral structure, shows low hemolytic activity and targets membranes through formation of large pores ', B B A-Proteins and Proteomics, vol. 1854, no. 8, pp. 882-889 . https://doi.org/10.1016/j.bbapap.2015.03.003

مصطلحات موضوعية: Cell Membrane Permeability, Biophysics, Peptaibol, Peptide, Gram-Positive Bacteria, Hemolysis, Biochemistry, Protein Structure, Secondary, Bacterial cell structure, Analytical Chemistry, chemistry.chemical_compound, Escherichia coli, Membrane activity, Peptide synthesis, Humans, Molecular Biology, chemistry.chemical_classification, Cell growth, Vesicle, Erythrocyte Membrane, Membrane, Models, Chemical, chemistry, Oligopeptides

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c37ec52a419ba03b2e0664384e884c2
https://doi.org/10.1016/j.bbapap.2015.03.003

المؤلفون: Brian S. Vad, Yuichi Yoshimura, Cristine Betzer, Jørn Døvling Kaspersen, Frans A. A. Mulder, Camilla Bertel Andersen, Poul Henning Jensen, Gunna Christiansen, Nikolai Lorenzen, Daniel E. Otzen, Jan Skov Pedersen, Søren B. Nielsen

المصدر: Lorenzen, N, Nielsen, S B, Yoshimura, Y, Vad, B S, Andersen, C B, Betzer, C, Kaspersen, J D, Christiansen, G, Pedersen, J S, Jensen, P H, Mulder, F A A & Otzen, D E 2014, ' How epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro ', Journal of Biological Chemistry, vol. 289, no. 31, pp. 21299-21310 . https://doi.org/10.1074/jbc.M114.554667

مصطلحات موضوعية: Cell Membrane Permeability, In Vitro Techniques, Epigallocatechin gallate, complex mixtures, Biochemistry, Oligomer, Catechin, Protein Structure, Secondary, chemistry.chemical_compound, Biopolymers, Microscopy, Electron, Transmission, medicine, heterocyclic compounds, Cytotoxicity, Nuclear Magnetic Resonance, Biomolecular, Molecular Biology, Alpha-synuclein, Microscopy, Confocal, Calorimetry, Differential Scanning, Chemistry, Circular Dichroism, Vesicle, food and beverages, Cell Biology, Small molecule, Monomer, Mechanism of action, Protein Structure and Folding, alpha-Synuclein, medicine.symptom

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d81e8a034fcf12ed438572e43d823f8
https://doi.org/10.1074/jbc.m114.554667

المؤلفون: Kristian Juul-Madsen, Stig Hill Christiansen, Xianwei Zhang, Kenneth A. Howard, Michael Lykke Hvam, Manja A. Behrens, Jan Skov Pedersen, Babak Jalilian, Brian S. Vad, Thomas Vorup-Jensen, Ida Lysgaard Thygesen, Daniel E. Otzen

المصدر: Christiansen, S H, Zhang, X, Juul-Madsen, K, Hvam, M L, Vad, B S, Behrens, M A, Thygesen, I L, Jalilian, B, Pedersen, J S, Howard, K, Otzen, D & Vorup-Jensen, T 2017, ' The random co-polymer glatiramer acetate rapidly kills primary human leukocytes through sialic-acid-dependent cell membrane damage ', Biochimica et Biophysica Acta. Biomembranes, bind 1859, s. 425–437 . https://doi.org/10.1016/j.bbamem.2017.01.001
Christiansen, S H, Zhang, X, Juul-Madsen, K, Hvam, M L, Vad, B S, Behrens, M A, Thygesen, I L, Jalilian, B, Pedersen, J S, Howard, K, Otzen, D E & Vorup-Jensen, T 2017, ' The random co-polymer glatiramer acetate rapidly kills primary human leukocytes through sialic-acid-dependent cell membrane damage ', B B A-Biomembranes, vol. 1859, no. 3, pp. 425-437 . https://doi.org/10.1016/j.bbamem.2017.01.001

مصطلحات موضوعية: 0301 basic medicine, Cationic co-polymers, Multiple Sclerosis, Polymers, medicine.medical_treatment, T-Lymphocytes, Biophysics, Apoptosis, Biology, Biochemistry, Monocytes, Cathelicidin, Cell membrane, 03 medical and health sciences, chemistry.chemical_compound, X-Ray Diffraction, Cathelicidins, Neuraminic acid, Scattering, Small Angle, medicine, Cytotoxic T cell, Humans, Cytotoxicity, Cells, Cultured, chemistry.chemical_classification, Liposome, Cell Membrane, Cell Biology, Glatiramer Acetate, Flow Cytometry, Sialic acid, Amino acid, 030104 developmental biology, medicine.anatomical_structure, chemistry, Liposomes, Neuraminic Acids, Immunotherapy, Glatiramoids, Antimicrobial Cationic Peptides

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d32141dd5af50467d0c3af97a22cb8bc
https://orbit.dtu.dk/en/publications/682bf468-b92a-4415-8944-b550c55f5ee2

المؤلفون: Jan J. Enghild, Kell K. Andersen, Brian S. Vad, Carsten Scavenius, Daniel E. Otzen

المصدر: Andersen, K K, Vad, B S, Scavenius, C, Enghild, J J & Otzen, D E 2017, ' Human lysozyme peptidase resistance is perturbed by the anionic glycolipid biosurfactant rhamnolipid produced by the opportunistic pathogen Pseudomonas aeruginosa ', Biochemistry, vol. 56, no. 1, pp. 260–270 . https://doi.org/10.1021/acs.biochem.6b01009

مصطلحات موضوعية: Anions, Models, Molecular, 0301 basic medicine, Virulence Factors, Proteolysis, Static Electricity, Virulence, Biology, medicine.disease_cause, Biochemistry, Mass Spectrometry, Bacterial cell structure, Microbiology, 03 medical and health sciences, chemistry.chemical_compound, Bacterial Proteins, Protein Domains, medicine, Humans, Secretion, Pancreatic Elastase, medicine.diagnostic_test, Pseudomonas aeruginosa, Circular Dichroism, Elastase, Rhamnolipid, 030104 developmental biology, chemistry, Biofilms, Electrophoresis, Polyacrylamide Gel, Muramidase, Glycolipids, Lysozyme, Peptide Hydrolases, Protein Binding

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e56db6b2e902ee7f60c7d2d07e4ce32
https://pure.au.dk/portal/da/publications/human-lysozyme-peptidase-resistance-is-perturbed-by-the-anionic-glycolipid-biosurfactant-rhamnolipid-produced-by-the-opportunistic-pathogen-pseudomonas-aeruginosa(09ee6f4e-1916-4096-a8c7-9a44c2f07268).html

المؤلفون: Tanja Schneider, Frederik Teilfeldt Hansen, Hans-Georg Sahl, Daniel E. Otzen, Søren Neve, Kent D. Nørgaard, Daniel H. Knudsen, Carina Lynggaard, Reinhard Wimmer, Line Anker Nielsen, Hans-Henrik Kristensen, Brian S. Vad, Jesper S. Oeemig, Dorthe Sandvang

المصدر: Journal of Biological Chemistry. 287:42361-42372

مصطلحات موضوعية: chemistry.chemical_classification, Fungal protein, Lipid II, Membrane lipids, Vesicle, Antimicrobial peptides, Cell Biology, Biology, Biochemistry, Amino acid, Beta defensin, chemistry, Molecular Biology, Defensin

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::99adb1853469121f1eb7e9a2af59d084
https://doi.org/10.1074/jbc.m112.382028

المؤلفون: Brian S. Vad, Daniel E. Otzen, Kell K. Andersen, Sahar Omer

المصدر: Andersen, K K, Vad, B, Omer, S & Otzen, D E 2016, ' Concatemers of Outer Membrane Protein A Take Detours in the Folding Landscape ', Biochemistry, vol. 55, no. 51, pp. 7123–7140 . https://doi.org/10.1021/acs.biochem.6b01153

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Protein Folding, Concatemer, Biochemistry, Micelle, Protein Structure, Secondary, 03 medical and health sciences, chemistry.chemical_compound, Surface-Active Agents, Native state, Escherichia coli, Denaturation (biochemistry), Maltose, Guanidine, Micelles, Protein Unfolding, Chemistry, Escherichia coli Proteins, Lipids, Transmembrane protein, Crystallography, Kinetics, 030104 developmental biology, Membrane, Spectrometry, Fluorescence, Membrane protein, Biophysics, Thermodynamics, bacteria, Electrophoresis, Polyacrylamide Gel, Bacterial outer membrane, Algorithms, Bacterial Outer Membrane Proteins

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbfb49d9dfece07c73523817b218715c
https://pure.au.dk/portal/da/publications/concatemers-of-outer-membrane-protein-a-take-detours-in-the-folding-landscape(935c750e-4da6-45c5-8e84-1748188411eb).html

المؤلفون: Martin Nilsson, Daniel E. Otzen, Gunna Christiansen, Per Halkjær Nielsen, Tim Tolker-Nielsen, Rikke Louise Meyer, Morten Simonsen Dueholm, Brian S. Vad, Guanghong Zeng

المصدر: Frontiers in Microbiology, Vol 6 (2015)
Zeng, G, Vad, B S, Dueholm, M S, Christiansen, G, Nilsson, M, Tolker-Nielsen, T, Nielsen, P H, Meyer, R L & Otzen, D 2015, ' Functional bacterial amyloid increases Pseudomonas biofilm hydrophobicity and stiffness ', Frontiers in Microbiology, vol. 6, 1099 . https://doi.org/10.3389/fmicb.2015.01099
Zeng, G, Vad, B S, Dueholm, M S, Christiansen, G, Nilsson, M, Tolker-Nielsen, T, Nielsen, P H, Meyer, R L & Otzen, D E 2015, ' Functional bacterial amyloid increases Pseudomonas biofilm hydrophobicity and stiffness ', Frontiers in Microbiology, vol. 6, pp. 1099 . https://doi.org/10.3389/fmicb.2015.01099
Frontiers in Microbiology

مصطلحات موضوعية: Microbiology (medical), Amyloid, Operon, lcsh:QR1-502, Young's modulus, force spectroscopy, Microbiology, lcsh:Microbiology, Extracellular matrix, Pseudomonas, mental disorders, Contact angle, Original Research, chemistry.chemical_classification, biology, Atomic force microscopy, Biomolecule, Biofilm, Force spectroscopy, biochemical phenomena, metabolism, and nutrition, biology.organism_classification, chemistry, Chaperone (protein), biology.protein, Biophysics, AFM

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d2848437d91df516e8404ddc5a9f67a
http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01099/full

المؤلفون: Søren B. Nielsen, Vijay S. Balakrishnan, Daniel E. Otzen, Brian S. Vad

المصدر: Vad, B S, Balakrishnan, V S, Nielsen, S B & Otzen, D 2015, ' Phospholipid Ether Linkages Significantly Modulate the Membrane Affinity of the Antimicrobial Peptide Novicidin ', Journal of Membrane Biology, pp. 487-496 . https://doi.org/10.1007/s00232-015-9792-y

مصطلحات موضوعية: Physiology, Vesicle, Lipid Bilayers, Biophysics, Phospholipid, Ether, Isothermal titration calorimetry, Cell Biology, Random coil, chemistry.chemical_compound, Kinetics, Ether lipid, Membrane, chemistry, Organic chemistry, Thermodynamics, Lipid bilayer phase behavior, Dimyristoylphosphatidylcholine, Unilamellar Liposomes, Antimicrobial Cationic Peptides, Protein Binding

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa380817866fe954ca22701b72c39d5e
https://pure.au.dk/portal/da/publications/phospholipid-ether-linkages-significantly-modulate-the-membrane-affinity-of-the-antimicrobial-peptide-novicidin(c7c28083-ed5b-46ec-a93a-46baf1f36b2e).html

المؤلفون: Marcel Stenvang, Per Halkjær Nielsen, Morten Simonsen Dueholm, Brian S. Vad, Daniel E. Otzen, Kell K. Andersen

المصدر: Andersen, K K, Vad, B S, Stenvang, M R, Dueholm, M S, Nielsen, P H & Otzen, D 2015, ' Stabilization and de-stabilization of (membrane-)proteins by microbial glycolipid and lipopeptide biosurfactants-in-vivo relevance and industrial applications ', Biophysical Journal, vol. 108, no. 2, pp. 521a-522a . https://doi.org/10.1016/j.bpj.2014.11.2860

مصطلحات موضوعية: chemistry.chemical_classification, Proteases, Globular protein, Biophysics, Rhamnolipid, Biology, chemistry.chemical_compound, Protein structure, chemistry, Membrane protein, Biochemistry, Denaturation (biochemistry), Lysozyme, Bacterial outer membrane

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6acf3c3ea33b955fbb610af322cffae7
https://vbn.aau.dk/da/publications/f1b1d61d-b983-4656-aac8-8a9452f273dc

المؤلفون: Tina Mygind, Marcel Stenvang, Morten Hyldgaard, Rikke Louise Meyer, Brian S. Vad, Daniel E. Otzen

المصدر: Hyldgaard, M, Mygind, T, Vad, B S, Stenvang, M, Otzen, D & Meyer, R L 2014, ' The Antimicrobial Mechanism of Action of Epsilon-Poly-L-Lysine ', Applied and Environmental Microbiology, vol. 80, no. 24, pp. 7758-7770 . https://doi.org/10.1128/AEM.02204-14

مصطلحات موضوعية: Ecology, Listeria, Vesicle, Cell Membrane, Biological membrane, Biological Transport, Biology, Cell morphology, Applied Microbiology and Biotechnology, Anti-Bacterial Agents, Cell membrane, chemistry.chemical_compound, Membrane, medicine.anatomical_structure, chemistry, Biochemistry, Polylysine, medicine, Food Microbiology, Escherichia coli, Lipid bilayer, Bacterial outer membrane, Food Science, Biotechnology

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5db9111a2ddffc47f7dc2ef6a50ef633
https://pure.au.dk/portal/da/publications/the-antimicrobial-mechanism-of-action-of-epsilonpolyllysine(6691e6b5-f4df-4f44-98bb-1b8f6327c057).html