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Bo Nilson

Researcher at Lund University

Publications -  57
Citations -  1835

Bo Nilson is an academic researcher from Lund University. The author has contributed to research in topics: Bacteremia & Infective endocarditis. The author has an hindex of 20, co-authored 47 publications receiving 1560 citations. Previous affiliations of Bo Nilson include Claude Bernard University Lyon 1.

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Protein L from Peptostreptococcus magnus binds to the kappa light chain variable domain.

TL;DR: Although it is possible, from comparative amino acid sequence data, to identify certain VL-framework region residues that account for the selective binding of protein L by kappa I, kappa III, and kappa IV proteins, this interaction is essentially dependent upon the tertiary structural integrity of the kappa chain VL domain.
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Lactobacillus apinorum sp. nov., Lactobacillus mellifer sp. nov., Lactobacillus mellis sp. nov., Lactobacillus melliventris sp. nov., Lactobacillus kimbladii sp. nov., Lactobacillus helsingborgensis sp. nov. and Lactobacillus kullabergensis sp. nov., isolated from the honey stomach of the honeybee Apis mellifera

TL;DR: A symbiotic lactic acid bacterial microbiota in the honey stomach of the honeybee Apis mellifera was found to be composed of several phylotypes of Bifidobacterium and Lactobacillus, and the phylotypes isolated represent seven novel species.
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Purification of antibodies using protein L-binding framework structures in the light chain variable domain.

TL;DR: It is demonstrated that it is possible to engineer antibodies and antibody fragments (Fab, Fv) with protein L-binding framework regions, which can then be utilized in aprotein L-based purification protocol.
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Improvement of retroviral retargeting by using amino acid spacers between an additional binding domain and the N terminus of Moloney murine leukemia virus SU.

TL;DR: It is hypothesized that conformational rearrangements of envelope glycoproteins were not optimally triggered following binding, and to overcome these postbinding blocks, a set of chimeric MoMLV-derived envelopes targeted to the Ram-1 phosphate transporter are generated in which the interdomain spacing was varied.
Journal Article

Targeting of retroviral vectors through protease-substrate interactions.

TL;DR: Proteolytic activation of receptor-targeted vectors can provide the basis for a novel two-step targeting strategy that may facilitate efficient targeted in vivo delivery of therapeutic genes.