Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Brian S. Vad"'
Autor:
Brian S. Vad, Jan Skov Pedersen, Andreas Bøggild, Madhu Nagaraj, Mumdooh Ahmed, Jeppe Lyngsø, Anne Fillipsen, Daniel E. Otzen, Ümit Akbey
Publikováno v:
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
Protein fibrillation is traditionally associated with misfolding, loss of functional phenotype, and gain of toxicity in neurodegenerative diseases. However, many organisms exploit fibrils in the form of functional amyloids (FA), as seen in bacteria,
Autor:
Guanghong eZeng, Brian S Vad, Morten S Dueholm, Gunna eChristiansen, Martin eNilsson, Tim eTolker-Nielsen, Per Halkjær Nielsen, Rikke Louise Meyer, Daniel E Otzen
Publikováno v:
Frontiers in Microbiology, Vol 6 (2015)
The success of Pseudomonas species as opportunistic pathogens derives in great part from their ability to form stable biofilms that offer protection against chemical and mechanical attack. The extracellular matrix of biofilms contains numerous biomol
Externí odkaz:
https://doaj.org/article/a24b49f924aa4b228d62b1dca2797cbf
Autor:
Carina Lynggaard, Brian S. Vad, Maria Andreasen, Jan J. Enghild, Daniel E. Otzen, Gunna Christiansen, Casper Bøjer Rasmussen
Publikováno v:
Protein Science. 28:633-642
Functional amyloid (FA) is widespread in bacteria and serves multiple purposes such as strengthening of biofilm and contact with eukaryotic hosts. Unlike pathological amyloid, FA has been subjected to evolutionary optimization which is likely to be r
Autor:
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
Publikováno v:
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
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
Epigallocatechin-3-gallate (EGCG) is the major polyphenol in green tea. It has antimicrobial properties and disrupts the ordered structure of amyloid fibrils involved in human disease. The antimicrobial effect of EGCG against the opportunistic pathog
Autor:
Gunna Christiansen, Line Friis Bakmann Christensen, Daniel E. Otzen, Brian S. Vad, Janni Nielsen, Kirstine Friis Jensen
Publikováno v:
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)
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)
Functional amyloid (FA) proteins have evolved to assemble into fibrils with a characteristic cross-β structure, which stabilizes biofilms and contributes to bacterial virulence. Some of the most studied bacterial FAs are the curli protein CsgA, expr
Autor:
Casper B, Rasmussen, Gunna, Christiansen, Brian S, Vad, Carina, Lynggaard, Jan J, Enghild, Maria, Andreasen, Daniel, Otzen
Publikováno v:
Protein science : a publication of the Protein Society. 28(3)
Functional amyloid (FA) is widespread in bacteria and serves multiple purposes such as strengthening of biofilm and contact with eukaryotic hosts. Unlike pathological amyloid, FA has been subjected to evolutionary optimization which is likely to be r
Publikováno v:
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
Alpha-synuclein (aSN) is a presynaptic protein with a pathological role in Parkinson's disease (PD). The mutants A30P, E46K and A53T are involved in PD early-onset forms. aSN is natively unfolded but can self-assemble to oligomers and fibrils and bin
Autor:
Daniel E. Otzen, Troels Skrydstrup, Brian S. Vad, Claudia U. Hjørringgaard, Julie L. H. Madsen
Publikováno v:
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
Incorporation of silicon-containing amino acids in peptides is known to endow the peptide with desirable properties such as improved proteolytic stability and increased lipophilicity. In the presented study, we demonstrate that incorporation of β-si
Autor:
Tim Tolker-Nielsen, Gunna Christiansen, Kell K. Andersen, Daniel E. Otzen, Lars Kjær, Brian S. Vad
Publikováno v:
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
The Parkinson's disease-associated protein α-synuclein (αSN) is natively unfolded but its structure can be modulated by membranes and surfactants. The opportunistic pathogen Pseudomonas aeruginosa (PA) produces and secretes the biosurfactant rhamno
Externí odkaz:
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
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
Autor:
Gunna Christiansen, Poul Larsen, Andreas Bøggild, Per Halkjær Nielsen, Marcel Stenvang, Daniel E. Otzen, Kai Finster, Morten Simonsen Dueholm, Brian S. Vad
Publikováno v:
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
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
Archaea are renowned for their ability to thrive in extreme environments, although they can be found in virtually all habitats. Their adaptive success is linked to their unique cell envelopes that are extremely resistant to chemical and thermal denat