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| 2. |
- Fagevik Olsén, Monika, 1964, et al.
(författare)
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Effects of high-intensity high-frequency transcutaneous electric nerve stimulation in primary dysmenorrhea - a randomised cross-over pilot study
- 2020
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Ingår i: European Journal of Physiotherapy. - : Informa UK Limited. - 2167-9169 .- 2167-9177. ; 22:5, s. 248-252
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Tidskriftsartikel (refereegranskat)abstract
- Background: Many women are affected by primary dysmenorrhoea. Transcutaneous Electric Nerve Stimulation (TENS) can be an alternative to analgesics. In one trial, high-intensity, high-frequency TENS was shown to be effective but there is need for more trials. Objectives: To study the effects of high-intensity, high-frequency TENS for primary dysmenorrhoea. Design: Randomised controlled pilot study with cross over design. Methods: Sixteen women with primary dysmenorrhoea participated. Pain, limitation in physical function, other symptoms related to the menstrual period and use of analgesics were registered at baseline, treatment versus control period followed by a wash-out period. Treatment consisted of high-intensity (40 mA) high-frequency (80 Hz) TENS stimulation in sessions of 60 s. Results: The results revealed no significant difference in pain intensity, limitations in physical function, consumption of analgesics and associated symptoms between the groups but a significant lower limitation in physical function during the wash-out period in comparison to the treatment period within the whole group. Conclusion: No significant effect of TENS was seen in contrast to previous studies. The effect is therefore questionable, but results must be interpreted with care, as this was a pilot study and the use of the equipment was not monitored and therefore unknown.
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| 3. |
- Jemt, Anders, 1985-, et al.
(författare)
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An automated approach to prepare tissue-derived spatially barcoded RNA-sequencing libraries.
- 2016
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Ingår i: Scientific Reports. - : Nature Publishing Group. - 2045-2322. ; 6
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Tidskriftsartikel (refereegranskat)abstract
- Sequencing the nucleic acid content of individual cells or specific biological samples is becoming increasingly common. This drives the need for robust, scalable and automated library preparation protocols. Furthermore, an increased understanding of tissue heterogeneity has lead to the development of several unique sequencing protocols that aim to retain or infer spatial context. In this study, a protocol for retaining spatial information of transcripts has been adapted to run on a robotic workstation. The method spatial transcriptomics is evaluated in terms of robustness and variability through the preparation of reference RNA, as well as through preparation and sequencing of six replicate sections of a gingival tissue biopsy from a patient with periodontitis. The results are reduced technical variability between replicates and a higher throughput, processing four times more samples with less than a third of the hands on time, compared to the standard protocol.
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| 4. |
- Johnson, Kenneth A, et al.
(författare)
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The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis.
- 2006
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Ingår i: EMBO J. - : Wiley. - 0261-4189 .- 1460-2075. ; 25:9, s. 1977-86
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Tidskriftsartikel (refereegranskat)abstract
- Presequence protease PreP is a novel protease that degrades targeting peptides as well as other unstructured peptides in both mitochondria and chloroplasts. The first structure of PreP from Arabidopsis thaliana refined at 2.1 Angstroms resolution shows how the 995-residue polypeptide forms a unique proteolytic chamber of more than 10,000 Angstroms(3) in which the active site resides. Although there is no visible opening to the chamber, a peptide is bound to the active site. The closed conformation places previously unidentified residues from the C-terminal domain at the active site, separated by almost 800 residues in sequence to active site residues located in the N-terminal domain. Based on the structure, a novel mechanism for proteolysis is proposed involving hinge-bending motions that cause the protease to open and close in response to substrate binding. In support of this model, cysteine double mutants designed to keep the chamber covalently locked show no activity under oxidizing conditions. The manner in which substrates are processed inside the chamber is reminiscent of the proteasome; therefore, we refer to this protein as a peptidasome.
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| 5. |
- Kvastad, Linda, et al.
(författare)
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The spatial landscape of transcriptomes and genomes in pediatric brain tumors
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Annan publikation (övrigt vetenskapligt/konstnärligt)abstract
- Treatment of pediatric brain tumors is continually being improved; still, there is a great need for new treatment options. Here we explore the spatial transcriptomic and genomic landscape in a cohort of pediatric brain tumors using a new generation of unbiased methodologies. We demonstrate the gene expression patterns of the essential cancer-related gene programs of epithelial-to-mesenchymal transition (EMT), the reverse process mesenchymal-to-epithelial transition (MET), and tumor microenvironment (TME) observations through microglia. Furthermore, we identify the gene expression of SPP1 by microglia in the TME as a potential prognostic mRNA marker - in pediatric brain tumor relapse patients.
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| 7. |
- Salmén, Fredrik, et al.
(författare)
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Barcoded solid-phase RNA capture for Spatial Transcriptomics profiling in mammalian tissue sections
- 2018
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Ingår i: Nature Protocols. - : Nature Publishing Group. - 1754-2189 .- 1750-2799. ; 13:11, s. 2501-2534
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Tidskriftsartikel (refereegranskat)abstract
- Spatial resolution of gene expression enables gene expression events to be pinpointed to a specific location in biological tissue. Spatially resolved gene expression in tissue sections is traditionally analyzed using immunohistochemistry (IHC) or in situ hybridization (ISH). These technologies are invaluable tools for pathologists and molecular biologists; however, their throughput is limited to the analysis of only a few genes at a time. Recent advances in RNA sequencing (RNA-seq) have made it possible to obtain unbiased high-throughput gene expression data in bulk. Spatial Transcriptomics combines the benefits of traditional spatially resolved technologies with the massive throughput of RNA-seq. Here, we present a protocol describing how to apply the Spatial Transcriptomics technology to mammalian tissue. This protocol combines histological staining and spatially resolved RNA-seq data from intact tissue sections. Once suitable tissue-specific conditions have been established, library construction and sequencing can be completed in similar to 5-6 d. Data processing takes a few hours, with the exact timing dependent on the sequencing depth. Our method requires no special instruments and can be performed in any laboratory with access to a cryostat, microscope and next-generation sequencing.
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| 10. |
- Ståhl, Annelie, et al.
(författare)
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Two Novel Targeting Peptide Degrading Proteases, PrePs, in Mitochondria and Chloroplasts, so Similar and Still Different
- 2005
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Ingår i: Journal of Molecular Biology. - : Elsevier BV. - 0022-2836 .- 1089-8638. ; 349:4, s. 847-860
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Tidskriftsartikel (refereegranskat)abstract
- Two novel metalloproteases from Arabidopsis thaliana, termed AtPrePI and AtPrePII, were recently identified and shown to degrade targeting peptides in mitochondria and chloroplasts using an ambiguous targeting peptide. AtPrePI and AtPrePII are classified as dually targeted proteins as they are targeted to both mitochondria and chloroplasts. Both proteases harbour an inverted metal binding motif and belong to the pitrilysin subfamily A. Here we have investigated the subsite specificity of AtPrePI and AtPrePII by studying their proteolytic activity against the mitochondrial F1β pre-sequence, peptides derived from the F1β pre-sequence as well as non-mitochondrial peptides and proteins. The degradation products were analysed, identified by MALDI-TOF spectrometry and superimposed on the 3D structure of the F1β pre-sequence. AtPrePI and AtPrePII cleaved peptides that are in the range of 10 to 65 amino acid residues, whereas folded or longer unfolded peptides and small proteins were not degraded. Both proteases showed preference for basic amino acids in the P1 position and small, uncharged amino acids or serine residues in the P′1P′1position. Interestingly, both AtPrePI and AtPrePII cleaved almost exclusively towards the ends of the α-helical elements of the F1β pre-sequence. However, AtPrePI showed a preference for the N-terminal amphiphilic α-helix and positively charged amino acid residues and degraded the F1β pre-sequence into 10–16 amino acid fragments, whereas AtPrePII did not show any positional preference and degraded the F1β pre-sequence into 10–23 amino acid fragments. In conclusion, despite the high sequence identity between AtPrePI and AtPrePII and similarities in cleavage specificities, cleavage site recognition differs for both proteases and is context and structure dependent.
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