Hydra vulgaris AEP
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA428595 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR6443010_1.fastq.gz | Fastqsanger.gz | |||
| SRR6443010_2.fastq.gz | Fastqsanger.gz | |||
| SRR6443020_1.fastq.gz | Fastqsanger.gz | |||
| SRR6443020_2.fastq.gz | Fastqsanger.gz | |||
| SRR6443030_1.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 78 |
Similar Datasets
Project description:Hydra vulgaris strain:Zurich Raw sequence reads
| PRJNA587737 | ENA
Project description:Morus alba L. Raw protein sequence reads and sequence
2024-02-08 | PXD049451 |
Project description:To understand the emergent properties of neural circuits, it would be ideal to record the activity of every neuron in a behaving animal and decode how it relates to behavior. We have achieved this with the cnidarian Hydra vulgaris, using calcium imaging of genetically engineered animals to measure the activity of essentially all of its neurons. Although the nervous system of Hydra is traditionally described as a simple nerve net, we surprisingly find instead a series of functional networks that are anatomically non-overlapping and are associated with specific behaviors. Three major functional networks extend through the entire animal and are activated selectively during longitudinal contractions, elongations in response to light, and radial contractions, whereas an additional network is located near the hypostome and is active during nodding. These results demonstrate the functional sophistication of apparently simple nerve nets, and the potential of Hydra and other basal metazoans as a model system for neural circuit studies.
| S-EPMC5423359 | biostudies-literature
Project description:This study aimed to identify the total proteome of Hydra vulgaris, a freshwater polyp, belongs to the cnidarians family with feature of not having a visual eye, while being sensitive to light. Proteins were identified using a combination of gel electrophoresis and data-independent nanoflow liquid chromatography mass spectrometry resulting in the identification of more than 5,200 proteins from all cellular components
2022-02-28 | PXD005828 | Pride
Project description:Recent body of evidence demonstrates that extracellular vesicles (EVs) represent the first language of cell-cell communication emerged during evolution. In aquatic environments, transferring signals between cells by EVs offer protection against degradation, allowing delivering of chemical information in high local concentrations to the target cells. The packaging of multiple signals, including those of hydrophobic nature, ensures target cells to receive the same EV-conveyed messages, and the coordination of a variety of physiological processes across cells of a single organisms, or at the population level, i.e. mediating the population´s response to changing environmental conditions. Here, we purified EVs from the medium of the freshwater invertebrate Hydra vulgaris, and the molecular profiling by proteomic and transcriptomic analyses revealed multiple markers of the exosome EV subtype. Moreover, positive and negative regulators of the Wnt/β-catenin signaling pathway, the major developmental pathway acting in body axial patterning, were identified. Functional analysis on amputated polyps revealed EV ability to interfere with both head and foot regeneration, suggesting an active role in setting up tissue gradients and oro-aboral polarity through delivery of short and long-distance signals. Our results open the path to unravel EV biogenesis and function in all cnidarian species, tracing back the origin of the cell-cell, cross-species or cross-kingdom communication in aquatic ecosystems
2022-02-17 | PXD027774 | Pride
Project description:Catalase, an antioxidant and hydroperoxidase enzyme protects the cellular environment from harmful effects of hydrogen peroxide by facilitating its degradation to oxygen and water. Molecular information on a cnidarian catalase and/or peroxidase is, however, limited. In this work an apparent full length cDNA sequence coding for a catalase (HvCatalase) was isolated from Hydra vulgaris using 3'- and 5'- (RLM) RACE approaches. The 1859 bp HvCatalase cDNA included an open reading frame of 1518 bp encoding a putative protein of 505 amino acids with a predicted molecular mass of 57.44 kDa. The deduced amino acid sequence of HvCatalase contained several highly conserved motifs including the heme-ligand signature sequence RLFSYGDTH and the active site signature FXRERIPERVVHAKGXGA. A comparative analysis showed the presence of conserved catalytic amino acids [His(71), Asn(145), and Tyr(354)] in HvCatalase as well. Homology modeling indicated the presence of the conserved features of mammalian catalase fold. Hydrae exposed to thermal, starvation, metal and oxidative stress responded by regulating its catalase mRNA transcription. These results indicated that the HvCatalase gene is involved in the cellular stress response and (anti)oxidative processes triggered by stressor and contaminant exposure.
| S-EPMC3387816 | biostudies-literature
Project description:Analysis of gene expression in MyD88-Knockdown-Hydra vulgaris (AEP)
| PRJNA147961 | ENA