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Sökning: WFRF:(Gellerfors M)

  • Resultat 1-22 av 22
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  • Broms, Jacob, et al. (författare)
  • Prehospital tracheal intubations by anaesthetist-staffed critical care teams: a prospective observational multicentre study
  • 2023
  • Ingår i: BRITISH JOURNAL OF ANAESTHESIA. - 0007-0912 .- 1471-6771. ; 131:6, s. 1102-1111
  • Tidskriftsartikel (refereegranskat)abstract
    • Background: Prehospital tracheal intubation is a potentially lifesaving intervention, but is associated with prolonged time on-scene. Some services strongly advocate performing the procedure outside of the ambulance or aircraft, while others also perform the procedure inside the vehicle. This study was designed as a non-inferiority trial registering the rate of successful tracheal intubation and incidence of complications performed by a critical care team either inside or outside an ambulance or helicopter.Methods: This observational multicentre study was performed between March 2020 and September 2021 and involved 12 anaesthetiststaffed critical care teams providing emergency medical services by helicopter in Denmark, Norway, and Sweden. The primary outcome was first-pass successful tracheal intubations.Results: Of the 422 drug-assisted tracheal intubations examined, 240 (57%) took place in the cabin of the ambulance or helicopter. The rate of first-pass success was 89.2% for intubations in-cabin vs 86.3% outside. This difference of 2.9% (confidence interval -2.4% to 8.2%) (two sided 10%, including 0, but not the non-inferiority limit D=-4.5) fulfils our criteria for non-inferiority, but not significant superiority. These results withstand after performing a propensity score analysis. The mean on-scene time associated with the helicopter in-cabin procedures (27 min) was significantly shorter than for outside the cabin (32 min, P=0.004).Conclusions: Both in-cabin and outside the cabin, prehospital tracheal intubation by anaesthetists was performed with a high success rate. The mean on-scene time was shorter in the in-cabin helicopter cohort.
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  • Fagerqvist, Therese, et al. (författare)
  • Monoclonal antibodies selective for α-synuclein oligomers/protofibrils recognize brain pathology in Lewy body disorders and α-synuclein transgenic mice with the disease-causing A30P mutation
  • 2013
  • Ingår i: Journal of Neurochemistry. - : Wiley-Blackwell. - 0022-3042 .- 1471-4159. ; 126:1, s. 131-144
  • Tidskriftsartikel (refereegranskat)abstract
    • Inclusions of intraneuronal alpha-synuclein (-synuclein) can be detected in brains of patients with Parkinson's disease and dementia with Lewy bodies. The aggregation of -synuclein is a central feature of the disease pathogenesis. Among the different -synuclein species, large oligomers/protofibrils have particular neurotoxic properties and should therefore be suitable as both therapeutic and diagnostic targets. Two monoclonal antibodies, mAb38F and mAb38E2, with high affinity and strong selectivity for large -synuclein oligomers were generated. These antibodies, which do not bind amyloid-beta or tau, recognize Lewy body pathology in brains from patients with Parkinson's disease and dementia with Lewy bodies and detect pathology earlier in -synuclein transgenic mice than linear epitope antibodies. An oligomer-selective sandwich ELISA, based on mAb38F, was set up to analyze brain extracts of the transgenic mice. The overall levels of -synuclein oligomers/protofibrils were found to increase with age in these mice, although the levels displayed a large interindividual variation. Upon subcellular fractionation, higher levels of -synuclein oligomers/protofibrils could be detected in the endoplasmic reticulum around the age when behavioral disturbances develop. In summary, our novel oligomer-selective -synuclein antibodies recognize relevant pathology and should be important tools to further explore the pathogenic mechanisms in Lewy body disorders. Moreover, they could be potential candidates both for immunotherapy and as reagents in an assay to assess a potential disease biomarker.
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  • Gellerfors, M (författare)
  • [Proton pump inhibitors and non-prescription]
  • 2010
  • Ingår i: Tidsskrift for den Norske laegeforening : tidsskrift for praktisk medicin, ny raekke. - : Norwegian Medical Association. - 0807-7096. ; 130:1, s. 14-
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)
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  • Magnusson, Kristina, et al. (författare)
  • Specific Uptake of an Amyloid-beta Protofibril-Binding Antibody-Tracer in A beta PP Transgenic Mouse Brain
  • 2013
  • Ingår i: Journal of Alzheimer's Disease. - 1387-2877 .- 1875-8908. ; 37:1, s. 29-40
  • Tidskriftsartikel (refereegranskat)abstract
    • Evidence suggests that amyloid-beta (A beta) protofibrils/oligomers are pathogenic agents in Alzheimer's disease (AD). Unfortunately, techniques enabling quantitative estimates of these species in patients or patient samples are still rather limited. Here we describe the in vitro and ex vivo characteristics of a new antibody-based radioactive ligand, [I-125]mAb158, which binds to A beta protofibrils with high affinity. [I-125]mAb158 was specifically taken up in brain of transgenic mice expressing amyloid-beta protein precursor (A beta PP) as shown ex vivo. This was in contrast to [I-125]mAb-Ly128 which does not bind to A beta. The uptake of intraperitoneally-administered [I-125]mAb158 into the brain was age- and time-dependent, and saturable in A beta PP transgenic mice with modest A beta deposition. Brain uptake was also found in young A beta PP transgenic mice that were devoid of A beta deposits, suggesting that [I-125]mAb158 targets soluble A beta protofibrils. The radioligand was diffusely located in the parenchyma, sometimes around senile plaques and only occasionally colocalized with cerebral amyloid angiopathy. A refined iodine-124-labeled version of mAb158 with much improved blood-brain barrier passage and a shorter plasma half-life might be useful for PET imaging of A beta protofibrils.
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