Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Magnus Hallas-Møller"'
Autor:
Corinna Probst, Magnus Hallas-Møller, Johan Ø Ipsen, Jacob T Brooks, Karsten Andersen, Mireille Haon, Jean-Guy Berrin, Helle J Martens, Connie B Nichols, Katja S Johansen, J Andrew Alspaugh
Publikováno v:
PLoS Pathogens, Vol 19, Iss 4, p e1010946 (2023)
Fungi often adapt to environmental stress by altering their size, shape, or rate of cell division. These morphological changes require reorganization of the cell wall, a structural feature external to the cell membrane composed of highly interconnect
Externí odkaz:
https://doaj.org/article/5b53086b515f485db0cf1679cf628b5d
Autor:
Magnus Hallas-Møller, Katja S Johansen
Publikováno v:
eLife, Vol 11 (2022)
How does a protein at the cell wall determine if a newly encountered fungus is safe to fuse with?
Externí odkaz:
https://doaj.org/article/bb6e933205d647f8859c1ef8cd9c6ce5
Autor:
Corinna Probst, Magnus Hallas-Møller, Johan Ø. Ipsen, Jacob T. Brooks, Karsten Andersen, Mireille Haon, Jean-Guy Berrin, Helle J. Martens, Connie B. Nichols, Katja S. Johansen, J. Andrew Alspaugh
Fungi often adapt to environmental stress by altering their size, shape, or rate of cell division. These morphological changes require reorganization of the cell wall, a structural feature external to the cell membrane composed of highly interconnect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::11e1cc318d21c8e4e0e2b88069fec67e
https://doi.org/10.1101/2022.10.25.513642
https://doi.org/10.1101/2022.10.25.513642
Publikováno v:
Ipsen, J, Hallas-Møller, M, Brander, S, Leggio, L L & Johansen, K S 2021, ' Lytic polysaccharide monooxygenases and other histidine-brace copper proteins : structure, oxygen activation and biotechnological applications ', Biochemical Society Transactions, vol. 49, no. 1, pp. 531-540 . https://doi.org/10.1042/BST20201031
Biochemical Society Transactions
Biochemical Society Transactions
Lytic polysaccharide monooxygenases (LPMOs) are mononuclear copper enzymes that catalyse the oxidative cleavage of glycosidic bonds. They are characterised by two histidine residues that coordinate copper in a configuration termed the Cu-histidine br
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b989ae0d052a3df466075e6a7ccd3fc9
https://curis.ku.dk/ws/files/259098245/bst_2020_1031c.pdf
https://curis.ku.dk/ws/files/259098245/bst_2020_1031c.pdf
Publikováno v:
Applied Microbiology and Biotechnology. 102:8477-8491
Cereals are vulnerable substrates for fungal growth and subsequent mycotoxin contamination. One of the major fungal genera to colonize the ecosystem of stored grain is Penicillium, especially species in the series of Viridicata and Verrucosa. Culturi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50aff2452d0c030b0c957c63e821e5c3
https://doi.org/10.1007/s00253-018-9213-0
https://doi.org/10.1007/s00253-018-9213-0
Publikováno v:
Planta Medica. 81:S1-S381
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::af2ab2a4cf3e862bb8ce3df0035069f9
https://doi.org/10.1055/s-0036-1596698
https://doi.org/10.1055/s-0036-1596698
Publikováno v:
Journal of agricultural and food chemistry. 64(22)
Moniliformin is a mycotoxin produced by several cereal associated Fusaria. Here, we show for the first time that moniliformin can be produced by the cereal fungus, Penicillium melanoconidium (4 out of 4 strains), but not in the related species in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc22e813b9d4b2bf2b290dd3da238741
https://pubmed.ncbi.nlm.nih.gov/27195914
https://pubmed.ncbi.nlm.nih.gov/27195914