Integrating Biological Data into Ocean Observing Systems: The Future Role of OBIS

Abstract

The future data needs of ocean science and ocean resource management will require a more seamless and accessible coupling of biological data with physical oceanographic processes. This bio-physical data framework will be built through the active integration of data from an extensive variety of sensors, observers, platforms and data archives across a wide range of space and time scales. This necessary synthesis of raw biological data into useful information and potentially new understanding is dependent on both new developments in ocean exploration as well as developments in information systems and informatics. The Ocean Biogeographic Information System (OBIS) is poised to play a significant and expanding role in the evolving ocean observation system [1] and [2].

Identification of poliovirions and subviral particles by capillary electrophoresis

“…The virus is purified with anion-exchange chromatography using an in-house-made column containing ecteola (epichlorohydrin triethanolamine) as stationary phase [24] (height, 10 cm and diameter, 1 cm). The poliovirions are eluted from the column with 15 mL phosphate buffer, pH 7.2, at room temperature.…”

RIP kinase 3 in necroptosis: does it take two or more to kill?

“…9,17 These findings suggested that the RIP homotypic interaction motif (RHIM)-dependent formation of a RIPK1/RIPK3 heterodimer is critical for the induction of necroptosis. RHIM-dependent oligomerization of RIPK1 and RIPK3 was recently proposed to form a functional amyloid signaling complex triggering necroptosis.…”

“…[13][14][15][16] The activation of RIPK3 and recruitment of MLKL are thought to require the formation of a high-molecular weight signaling complex, termed the necrosome, which also contains RIPK1, caspase-8 and FADD. 9 However, the stoichiometry of the necrosome complex and the mechanisms regulating its formation and activation remain only partly understood. FADD and caspase-8 negatively regulate necroptosis as inhibition of caspase-8 activity as well as knockdown or knockout of FADD or caspase-8 sensitize RIPK3-expressing cells to necroptosis.…”

“…FADD and caspase-8 negatively regulate necroptosis as inhibition of caspase-8 activity as well as knockdown or knockout of FADD or caspase-8 sensitize RIPK3-expressing cells to necroptosis. 9 Studies based mainly on small molecule inhibitors of RIPK1, termed necrostatins, showed that inhibition of RIPK1 kinase activity blocks necroptosis in response to most stimuli, leading to the conclusion that RIPK1 kinase activity is essential for necroptosis.…”

“…[1][2][3][4][5][6][7][8] Necroptosis is induced by multiple pathways, such as death receptors of the tumor necrosis factor receptor (TNFR) superfamily, TRIFdependent Toll-like receptor (TLR) signaling, and type I and type II interferon receptors. 9 Necroptotic cell death is executed by RIPK3-mediated recruitment and phosphorylation of mixed lineage kinase domain-like protein (MLKL), [10][11][12] which seems to kill cells by a mechanism dependent on its translocation to the plasma membrane. [13][14][15][16] The activation of RIPK3 and recruitment of MLKL are thought to require the formation of a high-molecular weight signaling complex, termed the necrosome, which also contains RIPK1, caspase-8 and FADD.…”