WorldCat Identities

Kragelund, Birthe B.

Overview
Works: 19 works in 21 publications in 2 languages and 37 library holdings
Publication Timeline
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Most widely held works by Birthe B Kragelund
CNDs skriftserie. Om studiestarterne 2002 på nanoteknologistudiet på Københavns Universitet( )

in Danish and held by 2 WorldCat member libraries worldwide

CNDs skriftserie. Studieforløbsundersøgelser i naturvidenskab : en antologi( )

in Danish and held by 2 WorldCat member libraries worldwide

CNDs skriftserie. Kammeratlæring på førstekursus i mekanik( )

in Danish and held by 2 WorldCat member libraries worldwide

CNDs skriftserie( )

in Danish and held by 2 WorldCat member libraries worldwide

CNDs skriftserie. Projekt Rum til Bedre Læring( )

in Danish and held by 2 WorldCat member libraries worldwide

Universitetsstuderendes tilgang til eksperimentelt udstyr : kønslige og faglige aspekter : universitetspædagogisk undersøgelse( Book )

1 edition published in 2003 in Danish and held by 2 WorldCat member libraries worldwide

CNDs skriftserie. Studieårgangene 1999-2000 på geografi( )

in Danish and held by 2 WorldCat member libraries worldwide

Functional Characterization of a Conserved Archaeal Viral Operon Revealing Single-Stranded DNA Binding, Annealing and Nuclease Activities( )

1 edition published in 2015 in English and held by 1 WorldCat member library worldwide

Abstract: The majority of archaeal viral genes are of unknown function hindering our understanding of the virus life cycle and viral interactions with their host. Here, we first describe functional characterization of ORF131b ( gp17 ) and ORF436 ( gp18 ) of Sulfolobus islandicus rod-shaped virus 2 (SIRV2), both encoding proteins of unknown function and forming an operon with ORF207 ( gp19 ). SIRV2 gp17 was found to be a single-stranded DNA (ssDNA) binding protein different in structure from all previously characterized ssDNA binding proteins. Mutagenesis of a few conserved basic residues suggested a U-shaped binding path for ssDNA. The recombinant gp18 showed an ssDNA annealing activity often associated with helicases and recombinases. To gain insight into the biological role of the entire operon, we characterized SIRV2 gp19 and showed it to possess a 5′ → 3′ ssDNA exonuclease activity, in addition to the previously demonstrated ssDNA endonuclease activity. Further, in vitro pull-down assay demonstrated interactions between gp17 and gp18 and between gp18 and gp19 with the former being mediated by the intrinsically disordered C-terminus of gp17. The strand-displacement replication mode proposed previously for rudiviruses and the close interaction among the ssDNA binding, annealing and nuclease proteins strongly point to a role of the gene operon in genome maturation and/or DNA recombination that may function in viral DNA replication/repair. Graphical abstract: Highlights: A SIRV2 operon of unknown function is conserved in archaeal linear viruses. The encoded three proteins exhibit ssDNA binding, annealing and nuclease activities. The three proteins interact with one another. This operon may be involved in virus genome maturation and/or DNA recombination. Contributing to a better understanding of archaeal viruses and ssDNA metabolism
Residue 146 regulates prolactin receptor folding, basal activity and ligand-responsiveness: Potential implications in breast tumorigenesis( )

1 edition published in 2015 in English and held by 1 WorldCat member library worldwide

Highlights: A gain-of-function mutation at position 146 disentangled in the prolactin receptor. Structural integrity was altered in a mutation-specific manner. Structural alteration paralleled increased basal activity and ligand-insensitivity. Mutant expression did not affect two representative breast cancer cell lines. Abstract: PRLR I146L is the first identified gain-of-function variant of the prolactin receptor (PRLR) that was proposed to be associated with benign breast tumorigenesis. Structural investigations suggested this hydrophobic core position in the extracellular D2 domain to be linked to receptor dimerization. Here, we used a mutational approach to address how the conservative I-to-L substitution induced constitutive activity. Using cell-based assays of different I146-PRLR variants in combination with spectroscopic/nuclear magnetic resonance analyses we found that chemical manipulation of position 146 profoundly altered folding, PRL-responsiveness, and ligand-independent activity of the receptor in a mutation-specific manner. Together, these data further add to the critical role of position 146, showing it to also be crucial to structural integrity thereby imposing on the biological PRLR properties. When stably introduced in MCF-7 (luminal) and MDA-MB231 (mesenchymal) breast cancer cells, the most potent of the PRL-insensitive mutants (PRLR I146D) had minimal impact on cell proliferation and cell differentiation status
 
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Audience Level
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  Kids General Special  
Audience level: 0.97 (from 0.88 for Functional ... to 0.98 for CNDs skrif ...)

Languages
Danish (19)

English (2)