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Träfflista för sökning "WFRF:(Ekström Simon) "

Sökning: WFRF:(Ekström Simon)

  • Resultat 1-10 av 145
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2.
  • Kondo, Y., et al. (författare)
  • First observation of 28 O
  • 2023
  • Ingår i: Nature. - 0028-0836 .- 1476-4687. ; 620:7976, s. 965-970
  • Tidskriftsartikel (refereegranskat)abstract
    • Subjecting a physical system to extreme conditions is one of the means often used to obtain a better understanding and deeper insight into its organization and structure. In the case of the atomic nucleus, one such approach is to investigate isotopes that have very different neutron-to-proton (N/Z) ratios than in stable nuclei. Light, neutron-rich isotopes exhibit the most asymmetric N/Z ratios and those lying beyond the limits of binding, which undergo spontaneous neutron emission and exist only as very short-lived resonances (about 10−21s), provide the most stringent tests of modern nuclear-structure theories. Here we report on the first observation of 28O and 27O through their decay into 24O and four and three neutrons, respectively. The 28O nucleus is of particular interest as, with the Z = 8 and N = 20 magic numbers1,2, it is expected in the standard shell-model picture of nuclear structure to be one of a relatively small number of so-called ‘doubly magic’ nuclei. Both 27O and 28O were found to exist as narrow, low-lying resonances and their decay energies are compared here to the results of sophisticated theoretical modelling, including a large-scale shell-model calculation and a newly developed statistical approach. In both cases, the underlying nuclear interactions were derived from effective field theories of quantum chromodynamics. Finally, it is shown that the cross-section for the production of 28O from a 29F beam is consistent with it not exhibiting a closed N = 20 shell structure.
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3.
  • McGinn, Steven, et al. (författare)
  • New Technologies for DNA analysis-A review of the READNA Project.
  • 2016
  • Ingår i: New Biotechnology. - : Elsevier BV. - 1876-4347 .- 1871-6784.
  • Forskningsöversikt (refereegranskat)abstract
    • The REvolutionary Approaches and Devices for Nucleic Acid analysis (READNA) project received funding from the European Commission for 4 1/2 years. The objectives of the project revolved around technological developments in nucleic acid analysis. The project partners have discovered, created and developed a huge body of insights into nucleic acid analysis, ranging from improvements and implementation of current technologies to the most promising sequencing technologies that constitute a 3(rd) and 4(th) generation of sequencing methods with nanopores and in situ sequencing, respectively.
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5.
  • Adler, Belinda, et al. (författare)
  • Miniaturized and Automated High-Throughput Verification of Proteins in the ISET Platform with MALDI MS
  • 2012
  • Ingår i: Analytical Chemistry. - : American Chemical Society (ACS). - 0003-2700 .- 1520-6882. ; 84:20, s. 8663-8669
  • Tidskriftsartikel (refereegranskat)abstract
    • A major bottleneck in high-throughput protein production is the validation step, which is why parallel and automated sample processing methods are highly desirable. Also, a miniaturized sample preparation format is preferred, as the reduction of reagent volumes significantly decreases the analysis cost per sample. We have developed an automated and miniaturized protein sequence verification protocol for recombinant proteins utilizing peptide mass fingerprinting and MS/MS analysis. The integrated selective enrichment target (ISET) platform, previously developed in our group, with its dual functionality, being both a sample preparation platform and a MALDI target plate, is employed. All steps including immobilized metal ion affinity chromatography of protein on cobalt-loaded beads, tryptic digestion, and MALDI MS analysis are performed in an array format, without any sample transfers, on the same ISET chip. The automated configuration reduced the sample preparation time significantly. Starting with crude lysate, a full plate of 48 purified, digested samples prepared for MALDI-MS can be generated in 4 h, with only 30 min of operator involvement. This paper demonstrates the utility of the method by parallel analysis of 45 His-tagged human recombinant proteins.
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6.
  • Adler, Belinda, et al. (författare)
  • Optimizing nanovial outlet designs for improved solid-phase extraction in the integrated selective enrichment target-ISET.
  • 2012
  • Ingår i: Electrophoresis. - : Wiley. - 0173-0835. ; 33:21, s. 3143-3150
  • Tidskriftsartikel (refereegranskat)abstract
    • The integrated selective enrichment target is a microfluidic platform for SPE sample preparation with integrated nanocolumns, which simultaneously offers direct MALDI MS read-out. Here, we present a study on the importance of different nanocolumn outlet hole geometries and hole areas in relation to MS signal intensity and reproducibility. A design solution that provides the flow characteristics required for robust sample preparation using automated liquid handling is reported.
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7.
  • Adler, Belinda, et al. (författare)
  • Porous silicon immunoaffinity microarrays
  • 2018. - 2
  • Ingår i: Handbook of Porous Silicon : Second Edition - Second Edition. - Cham : Springer International Publishing. - 9783319713793 - 9783319713816 ; 2-2, s. 1355-1367
  • Bokkapitel (refereegranskat)abstract
    • Porous silicon with immobilized recognition biomolecules is an attractive platform for many microfluidic chip-based bioanalytical applications. We review the progress in the field since its earliest developments in the 1990s. An improved assay for early detection of prostate cancer has reached clinical evaluation, but there are also exciting developments in both aptamer-based biosensing and mass spectrometry-based biosensing.
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9.
  • Ahmad Tajudin, Asilah, et al. (författare)
  • MALDI-target integrated platform for affinity-captured protein digestion.
  • 2014
  • Ingår i: Analytica Chimica Acta. - : Elsevier BV. - 1873-4324 .- 0003-2670. ; 807:Jan 7, s. 1-8
  • Tidskriftsartikel (refereegranskat)abstract
    • To address immunocapture of proteins in large cohorts of clinical samples high throughput sample processing is required. Here a method using the proteomic sample platform, ISET (integrated selective enrichment target) that integrates highly specific immunoaffinity capture of protein biomarker, digestion and sample cleanup with a direct interface to mass spectrometry is presented. The robustness of the on-ISET protein digestion protocol was validated by MALDI MS analysis of model proteins, ranging from 40fmol to 1pmol per nanovial. On-ISET digestion and MALDI MS/MS analysis of immunoaffinity captured disease-associated biomarker PSA (prostate specific antigen) from human seminal plasma are presented.
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