Zobrazeno 1 - 10 of 61 pro vyhledávání: '"Camilla Christiansen"'
1
The carbohydrate-binding module family 20 - diversity, structure, and function
Autor: Birte Svensson, Camilla Christiansen, Maher Abou Hachem, Anders Viksø-Nielsen, Andreas Blennow, Štefan Janeček
Publikováno v: FEBS Journal. 276:5006-5029
Starch-active enzymes often possess starch-binding domains (SBDs) mediating attachment to starch granules and other high molecular weight substrates. SBDs are divided into nine carbohydrate-binding module (CBM) families, and CBM20 is the earliest-ass
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::aa3037ddf7c435806186b35c9cdc16ac
https://doi.org/10.1111/j.1742-4658.2009.07221.x
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2
An enzyme family reunion — similarities, differences and eccentricities in actions on α-glucans
Autor: Birte Svensson, Andreas Blennow, Sophie Bozonnet, Morten M. Nielsen, Nushin Aghajari, Richard Haser, Camilla Christiansen, Eun-Seong Seo, Kenji Fukuda, Maher Abou Hachem
Publikováno v: Biologia. 63:967-979
α-Glucans in general, including starch, glycogen and their derived oligosaccharides are processed by a host of more or less closely related enzymes that represent wide diversity in structure, mechanism, specificity and biological role. Sophisticated
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3de2bcc002b2d425c8b4aa07dc9ec8a6
https://doi.org/10.2478/s11756-008-0164-2
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3
The carbohydrate-binding module family 20--diversity, structure, and function
Autor: Camilla, Christiansen, Maher, Abou Hachem, Stefan, Janecek, Anders, Viksø-Nielsen, Andreas, Blennow, Birte, Svensson
Publikováno v: The FEBS journal. 276(18)
Starch-active enzymes often possess starch-binding domains (SBDs) mediating attachment to starch granules and other high molecular weight substrates. SBDs are divided into nine carbohydrate-binding module (CBM) families, and CBM20 is the earliest-ass
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dc95a54e1eca740c590d8f674afba652
https://pubmed.ncbi.nlm.nih.gov/19682075
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5
Construction of two Lolium perenne BAC libraries and identification of BACs containing candidate genes for disease resistance and forage quality
Autor: Camilla Christiansen, Iain Donnison, Thomas Lübberstedt, Torben Asp, Mingliang Xu, Mervyn O. Humphreys, Ann Thomas, Kerrie Farrar
Publikováno v: Farrar, K, Asp, T, Lübberstedt, T, Xu, M, Thomas, A M, Christiansen, C, Humpfryes, M O & Donnison, I S 2007, ' Construction of two Lolium perenne BAC libraries and identification of BACs containing candidate genes for disease resistance and forage quality ', Molecular Breeding, vol. 19, no. 1, pp. 15-23 . https://doi.org/10.1007/s11032-006-9036-z
Two BAC libraries were constructed for the forage and turf grass species Lolium perenne L. The libraries consisted of 98,304 and 101,376 BAC clones for L. perenne genotypes LTS18 and NV#20F1-30, respectively. The estimated average insert size of both
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16adf6e49c879cf4c50e2eaa4de5338d
https://pure.au.dk/portal/da/publications/construction-of-two-lolium-perenne-bac-libraries-and-identification-of-bacs-containing-candidate-genes-for-disease-resistance-and-forage-quality(b4433bb0-b057-11db-bd61-000ea68e967b).html
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6
Fluorometric polyethyleneglycol-peptide hybrid substrates for quantitative assay of protein disulfide isomerase
Autor: Phaedria M. St. Hilaire, Camilla Christiansen, Jakob R. Winther
Publikováno v: Analytical biochemistry. 333(1)
In eukaryotic cells the enzyme protein disulfide isomerase (PDI) is responsible for the formation and reshuffling of disulfide bonds in secretory proteins. The reaction carried out by PDI involves interaction with a highly complex mixture of polypept
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b14b4a5e002ce3de93f5c81bc27a704
https://pubmed.ncbi.nlm.nih.gov/15351291
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