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Bodil Jönsson

Researcher at Sahlgrenska University Hospital

Publications -  83
Citations -  2489

Bodil Jönsson is an academic researcher from Sahlgrenska University Hospital. The author has contributed to research in topics: Mycobacterium abscessus & Nontuberculous mycobacteria. The author has an hindex of 19, co-authored 81 publications receiving 2179 citations. Previous affiliations of Bodil Jönsson include Lund University & University of Gothenburg.

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Emergence and spread of a human-transmissible multidrug-resistant nontuberculous mycobacterium.

Josephine M. Bryant, +90 more
- 11 Nov 2016 - 
TL;DR: Using whole-genome analysis of a global collection of clinical isolates, it is shown that the majority of M. abscessus infections are acquired through transmission, potentially via fomites and aerosols, of recently emerged dominant circulating clones that have spread globally.

Emergence and spread of a human-transmissible multidrug-resistant nontuberculous mycobacterium

TL;DR: In this paper, the authors used whole-genome analysis of a global collection of clinical isolates to show that the majority of M. abscessus infections are acquired through transmission, potentially via fomites and aerosols, of recently emerged dominant circulating clones.
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A large Escherichia coli O157 outbreak in Sweden associated with locally produced lettuce.

TL;DR: The epidemiological investigations implicated lettuce as the most likely source of the outbreak, with an OR of 13.0 and handling of fresh greens from farm to table must be improved to minimize the risk of contamination.
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Molecular Epidemiology of Mycobacterium abscessus, with Focus on Cystic Fibrosis

TL;DR: It is shown that most patients colonized by M. abscessus in the airways have unique strains, indicating that these strains derive from the environment and that patient-to-patient transmission rarely occurs.
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Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis

TL;DR: Ferrochelatase seems to have a structurally conserved core region that is common to the enzyme from bacteria, plants and mammals, and it is proposed that porphyrin binds in the identified cleft; this cleft also includes the metal-binding site of the enzyme.