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Strongylocentrotus purpuratus

ABSTRACT: Gene expression in tissues from an immune challenged adult sea urchin (Strongylocentrotus purpuratus)

PROVIDER: PRJNA381801 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR5420081.fastq.gz	Fastqsanger.gz
	SRR5420082.fastq.gz	Fastqsanger.gz

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Response to elevated pCO2 in Strongylocentrotus purpuratus larvae

2013-01-01 | GSE37522 | GEO

Response to elevated pCO2 in Strongylocentrotus purpuratus larvae

Project description:Transcriptional profiling of purple sea urchin (Strongylocentrotus purpuratus) larvae cultured under three different seawater CO2 concentrations 400, 800, 1200 M-BM-5atm. The goal was to determine the effects of CO2, an important climate change variable, on global gene expression Larvae were cultured under three different seawater CO2 concentrations 400, 800, 1200 M-BM-5atm, each with four replicate cultures, and sampled at two developmental stages (gastrula and pluteus)

2013-01-01 | E-GEOD-37522 | biostudies-arrayexpress

Synergistic effects of temperature and pCO2 on growth, development and gene expression of Strongylocentrotus purpuratus larvae

Project description:Transcriptional profiling of purple sea urchin (Strongylocentrotus purpuratus) larvae cultured under four different seawater conditions: (i)13°C/400 µatm pCO2, (ii)13°C/1100 µatm pCO2, (iii)18°C/400 µatm pCO2 (iv)18°C/1100 µatm pCO2. The goal was to determine the effects of temperature and CO2, both important climate change variables, on gene expression

2013-01-01 | GSE39125 | GEO

Synergistic effects of temperature and pCO2 on growth, development and gene expression of Strongylocentrotus purpuratus larvae

Project description:Transcriptional profiling of purple sea urchin (Strongylocentrotus purpuratus) larvae cultured under four different seawater conditions: (i)13M-BM-0C/400 M-BM-5atm pCO2, (ii)13M-BM-0C/1100 M-BM-5atm pCO2, (iii)18M-BM-0C/400 M-BM-5atm pCO2 (iv)18M-BM-0C/1100 M-BM-5atm pCO2. The goal was to determine the effects of temperature and CO2, both important climate change variables, on gene expression Larvae were cultured under four different seawater conditions (ii)13M-BM-0C/1100 M-BM-5atm pCO2, (iii)18M-BM-0C/400 M-BM-5atm pCO2 (iv)18M-BM-0C/1100 M-BM-5atm pCO2, (i)13M-BM-0C/400 M-BM-5atm each with three replicate cultures for each condition and sampled at pluteus stage

2013-01-01 | E-GEOD-39125 | biostudies-arrayexpress

Strongylocentrotus purpuratus

Project description:Parental environments alter DNA methylation in offspring of the purple sea urchin, Strongylocentrotus purpuratus

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Strongylocentrotus purpuratus

Project description:Strongylocentrotus purpuratus RNAseq

| PRJNA322662 | ENA

Strongylocentrotus purpuratus

Project description:Strongylocentrotus purpuratus early transcriptome

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Strongylocentrotus purpuratus

Project description:Strongylocentrotus purpuratus developmental transcriptomes

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Strongylocentrotus purpuratus

Project description:Strongylocentrotus purpuratus Genomic Resources

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Phosphoproteomic Network Analysis in the Sea Urchin Strongylocentrotus purpuratus Reveals New Candidates in Egg Activation

Project description:Fertilization triggers a dynamic symphony of molecular transformations induced by a rapid rise in intracellular calcium. Most prominent are surface alterations, metabolic activation, cytoskeletal reorganization, and cell cycle reentry. While the activation process appears to be broadly evolutionarily conserved, and protein phosphorylation is known to play a key role, the signaling networks mediating the response to fertilization are not well described. To address this gap, we performed a time course phosphoproteomic analysis of egg activation in the sea urchin Strongylocentrotus purpuratus, a system that offers biochemical tractability coupled with exquisite synchronicity. By coupling large-scale phosphopeptide enrichment with unbiased quantitative mass spectrometry, we identified striking changes in global phosphoprotein patterns at 2- and 5- min post fertilization as compared to unfertilized eggs. Overall, we mapped 8796 distinct phosphosite modifications on 2833 phosphoproteins, of which 15% were differentially regulated in early egg activation. Activated kinases were identified by phosphosite mapping, while enrichment analyses revealed conserved signaling cascades not previously associated with egg activation. This work represents the most comprehensive study of signaling associated with egg activation to date, providing both novel mechanistic insights and a valuable resource for the broader research community.

2015-08-04 | PXD002239 | Pride

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