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Hydra vulgaris, the fresh-water polyp, [3] is a small freshwater hydroid with length from 10 mm to 30 mm and width about 1 mm. [4] Description.
Hydra (/ ˈ h aɪ d r ə / HY-drə) is a genus of small freshwater hydrozoans of the phylum Cnidaria.They are native to the temperate and tropical regions. [2] [3] The genus was named by Linnaeus in 1758 after the Hydra, which was the many-headed beast of myth defeated by Heracles, as when the animal has a part severed, it will regenerate much like the mythical hydra's heads.
As an example, we will discuss the interaction between a host, Hydra vulgaris, and the main colonizer of its epithelial cell surfaces, Curvibacter spp. Those bacteria produce 3-oxo-HSL quorum sensing molecules. [17] However, the oxidoreductase activity of the polyp Hydra is able to modify the 3-oxo-HSL into their 3-hydroxy-HSL counterparts. [17]
Hydra oligactis; Hydra viridissima; Hydra vulgaris; T. Transgenic hydra This page was last edited on 27 September 2021, at 19:27 (UTC). Text is available under ...
Hydra viridissima is a species of cnidarian which is commonly found in still or slow-moving freshwater [2] in the Northern temperate zone. Hydra viridissima is commonly called green hydra due to its coloration, which is due to the symbiotic green algae Chlorella vulgaris which live within its body. [ 3 ]
H. vulgaris may refer to: Hippuris vulgaris, the common mare's tail, a common aquatic plant species found in Eurasia; Hydra vulgaris, a small freshwater hydroid species; Hydrocotyle vulgaris, the marsh pennywort, a small creeping perennial herb species native to North Africa, Europe, Florida and west to the Caspian region
The fresh-water polyp Hydra vulgaris and the jellyfish Cassiopea are among the most primitive organisms in which sleep-like states have been observed. [8] [9] Observing sleep states in jellyfish provides evidence that sleep states do not require that an animal have a brain or central nervous system. [10]
Gal4 is a modular protein consisting broadly of a DNA-binding domain and an activation domain. The UAS to which GAL4 binds is CGG-N 11-CCG, where N can be any base. [6] Although GAL4 is a yeast protein not normally present in other organisms it has been shown to work as a transcription activator in a variety of organisms such as Drosophila, [7] and human cells, highlighting that the same ...