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self-organising map (som)  (RStudio)

 
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    RStudio self-organising map (som)
    Self Organising Map (Som), supplied by RStudio, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/self-organising+map+(som)/self+organising+map++som+/pm35367374-112-9-13
    Average 90 stars, based on 1 article reviews
    self-organising map (som) - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    Construct:

    Article Title: Transcriptomic characterisation of a common skin lesion in farmed chinook salmon.
    Article Snippet: Little is known about host responses of farmed Chinook salmon with skin lesions, despite the lesions being associated with increased water temperatures and elevated mortality rates.. To address this shortfall, a transcriptomic approach was used to characterise the molecular landscape of spot lesions, the most commonly reported lesion type in New Zealand Chinook salmon, versus healthy appearing skin in fish with and without spot lesions.. Many biological (gene ontology) pathways were enriched in lesion adjacent tissue, relative to control skin tissue, including proteolysis, fin regeneration, calcium ion binding, mitochondrial transport, actin cytoskeleton organisation, epithelium development, and tissue development.

    Expressing:

    Article Title: Transcriptomic characterisation of a common skin lesion in farmed chinook salmon.
    Article Snippet: Little is known about host responses of farmed Chinook salmon with skin lesions, despite the lesions being associated with increased water temperatures and elevated mortality rates.. To address this shortfall, a transcriptomic approach was used to characterise the molecular landscape of spot lesions, the most commonly reported lesion type in New Zealand Chinook salmon, versus healthy appearing skin in fish with and without spot lesions.. Many biological (gene ontology) pathways were enriched in lesion adjacent tissue, relative to control skin tissue, including proteolysis, fin regeneration, calcium ion binding, mitochondrial transport, actin cytoskeleton organisation, epithelium development, and tissue development.



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    A , Venn diagram analysis of the statistically differentially <t>regulated</t> <t>proteins:</t> 1) RT1 vs. baseline, 2) DT vs. baseline, 3) RT2 vs. baseline, 4) DT vs. RT1 (pre-DT) and 5) RT2 vs. DT (pre-RT2) ( FDR < 0.05, FC >|1.2|). The 6th comparison: RT2 vs. RT1 is not shown as it did not produce any statistically significantly different proteins. The figure illustrates the number of common overlapping and unique significant proteins across each comparison. There were 285 proteins that were significantly different in at least one of the pairwise comparisons highlighted in the Venn diagram. B , <t>SOM</t> profiling of 285 proteins identified in the Venn diagram above in the PRT group over the 30 weeks time-course of baseline, RT1, DT and RT2.
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    Image Search Results


    A , Venn diagram analysis of the statistically differentially regulated proteins: 1) RT1 vs. baseline, 2) DT vs. baseline, 3) RT2 vs. baseline, 4) DT vs. RT1 (pre-DT) and 5) RT2 vs. DT (pre-RT2) ( FDR < 0.05, FC >|1.2|). The 6th comparison: RT2 vs. RT1 is not shown as it did not produce any statistically significantly different proteins. The figure illustrates the number of common overlapping and unique significant proteins across each comparison. There were 285 proteins that were significantly different in at least one of the pairwise comparisons highlighted in the Venn diagram. B , SOM profiling of 285 proteins identified in the Venn diagram above in the PRT group over the 30 weeks time-course of baseline, RT1, DT and RT2.

    Journal: bioRxiv

    Article Title: Human skeletal muscle possesses both reversible proteomic signatures and a retained proteomic memory after repeated resistance training

    doi: 10.1101/2024.11.19.624068

    Figure Lengend Snippet: A , Venn diagram analysis of the statistically differentially regulated proteins: 1) RT1 vs. baseline, 2) DT vs. baseline, 3) RT2 vs. baseline, 4) DT vs. RT1 (pre-DT) and 5) RT2 vs. DT (pre-RT2) ( FDR < 0.05, FC >|1.2|). The 6th comparison: RT2 vs. RT1 is not shown as it did not produce any statistically significantly different proteins. The figure illustrates the number of common overlapping and unique significant proteins across each comparison. There were 285 proteins that were significantly different in at least one of the pairwise comparisons highlighted in the Venn diagram. B , SOM profiling of 285 proteins identified in the Venn diagram above in the PRT group over the 30 weeks time-course of baseline, RT1, DT and RT2.

    Article Snippet: To plot temporal changes in proteins across the intervention, we undertook Self Organising Map (SOM) profiling of the change in standardised mean protein content within each time-point using Partek Genomics Suite as previously described earlier ( Turner et al ., 2020 ).

    Techniques: Comparison

    A and B , Reactome pathway analysis together with Sankey-diagram illustrates that the retained proteins are enriched in cytokine signalling, biosynthesis, and folding, sorting and degradation pathways and functions. C , The 29 and 81 retained proteins (SOM) in GO have as a molecular function especially in calcium or calcium-dependent protein binding, actin filament binding and phospholipase inhibitor activity. D , CAPN2, CLIC1, MYH9 and CAPNS1 proteins increasing after RT1 and maintaining their levels after DT still above the baseline. N=17 in PRT and n=11 in CRT. * <0.05, ** <0.01 and *** <0.001 or exact FDR-value ( FDR < 0.10) vs. baseline. Data is presented as mean ± SEM.

    Journal: bioRxiv

    Article Title: Human skeletal muscle possesses both reversible proteomic signatures and a retained proteomic memory after repeated resistance training

    doi: 10.1101/2024.11.19.624068

    Figure Lengend Snippet: A and B , Reactome pathway analysis together with Sankey-diagram illustrates that the retained proteins are enriched in cytokine signalling, biosynthesis, and folding, sorting and degradation pathways and functions. C , The 29 and 81 retained proteins (SOM) in GO have as a molecular function especially in calcium or calcium-dependent protein binding, actin filament binding and phospholipase inhibitor activity. D , CAPN2, CLIC1, MYH9 and CAPNS1 proteins increasing after RT1 and maintaining their levels after DT still above the baseline. N=17 in PRT and n=11 in CRT. * <0.05, ** <0.01 and *** <0.001 or exact FDR-value ( FDR < 0.10) vs. baseline. Data is presented as mean ± SEM.

    Article Snippet: To plot temporal changes in proteins across the intervention, we undertook Self Organising Map (SOM) profiling of the change in standardised mean protein content within each time-point using Partek Genomics Suite as previously described earlier ( Turner et al ., 2020 ).

    Techniques: Protein Binding, Binding Assay, Activity Assay