3,367 research outputs found

    Flow Measurement Challenges for Carbon Capture, Utilisation and Storage

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    Carbon Capture, Utilisation and Storage (CCUS) is a key element in the United Kingdom Government strategy for reducing carbon dioxide (CO2) emissions. The UK aims to capture and store 10 million tonnes of CO2 each year by 2030. At each stage in the CCUS infrastructure, accurate measurement of the CO2 flow rate is required, over a range of temperatures, pressures, flow rates and fluid phases, where the flow measurement must be validated through a credible traceability chain. The traceability chain provides the underpinning confidence required to verify meter performance, financial and fiscal transactions, and environmental compliance. The UK equivalent of the EU Emissions Trading System (EU ETS) specifies a maximum uncertainty value for CO2 flow measurement. Accordingly, the provision of accurate and traceable flow measurement of CO2 is a prerequisite for an operational CCUS scheme. However, there are currently no CO2 flow measurement facilities, nationally or internationally, providing traceable flow calibrations of gas phase, liquid/dense phase and supercritical phase CO2 that replicate real-world CCUS conditions. This lack of traceable CO2 gas and liquid flow measurement facilities and associated flow measurement standards is a significant barrier to the successful implementation of CCUS projects worldwide. This paper presents an overview of the traceability chain required for CO2 flow measurement in the UK and globally. Current challenges are described along with potential solutions and opportunities for the flow measurement community

    State of the Science and the Intraductal Approach for Breast Cancer: Proceedings Summary of The Sixth International Symposium on the Intraductal Approach To Breast Cancer Santa Monica, California, 19–21 February 2009

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    Researchers are using the intraductal approach to advance breast cancer risk assessment, prevention, diagnosis, and treatment. Procedures and technologies that can access and interrogate the ductal-alveolar systems include nipple aspiration, ductal lavage and ductoscopy. Ductoscopic papillectomy, ductoscopic margin evaluation, and intraductal therapy are considered promising investigational and innovative treatments. These techniques are used to explore the biology of the normal breast; collect and analyze breast fluid and cells to identify biomarkers that can be used in breast cancer detection and risk assessment; and to identify new ways to find and administer therapeutic and/or preventive agents to the breast tissue. This report summarizes the latest research findings in these areas, presented at The 6th International Symposium on the Intraductal Approach to Breast Cancer in 2009

    Pericles and President Lincoln.

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    Detached from Atlantic Monthly, March 1863.https://scholarsjunction.msstate.edu/fvw-pamphlets/1641/thumbnail.jp

    Carvedilol inhibits the cardiostimulant and thermogenic effects of MDMA in humans : lost in translation

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    We greatly appreciate the comments offered by Drs Rolle, Takematsu, and Hoffman and the opportunity to put our work into a wider perspective. We share the view that our work does not reflect the clinical situation but rather provides a proof of mechanism study, which aims to help to translate preclinical findings (Sprague et al., 2005) into the clinic. As we noted in the discussion of our work (Hysek et al., 2012b) the primary goal of the study was to investigate the role of adrenoceptors in the mechanism of action of MDMA in humans. Therefore, the study provided only indirect support for the use of carvedilol in the treatment of stimulant toxicity in which carvedilol would be administered following the ingestion of Ecstasy or other stimulants. Furthermore, we noted the limitation that the MDMA-induced increase in body temperature in our study was moderate and we do not know whether carvedilol would also be effective in cases of severe hyperthermia following ecstasy use

    Stability, unfolding, and aggregation of the gamma D and gamma S human eye lens crystallins

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    Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2007.Includes bibliographical references (v. 2, leaves 189-208).The transparency of the human eye lens depends on the properties of the a- crystallin and py-crystallin families of proteins, which accumulate to very high concentrations in mature lens fiber cells. The 0- and y-crystallins are thought to be primarily structural proteins while a-crystallin possess an additional chaperone activity. Aggregation of partially unfolded or covalently damaged forms of these proteins results in cataract, which is the leading cause of blindness in the world. The biochemical basis of the very high crystallin stability, and the nature of the misfolded, modified, or aggregated states, are thus of considerable importance in understanding the etiology of loss of lens transparency. All vertebrate P- and y-crystallins are homologous and contain two highly symmetrical domains with a hydrophobic interface connected by an interdomain linker. The overall sequences, fold topology, and domain interfaces of vertebrate py-crystallins are highly conserved. The two domain 0- and y-crystallins are believed to have evolved by gene duplication and fusion from an ancestral single domain py-crystallin. This thesis is focused on stability and aggregation properties of human yD crystallin (yDwT) and human yS crystallin (ySwT), two of the most abundant proteins in the human lens.(cont.) Terminally differentiated fiber cells in the central nucleus of the lens are enucleated and devoid of organelles. The yD crystallins synthesized in utero must remain stable and soluble throughout life. The yS protein is more prevalent in the cortical regions of the lens, where protein degradation and synthesis do occur. Given the importance of long-term solubility for the crystallins, it seems likely that selection for the two-domain form is related to the need for very long-term stability. Comparison of the stabilities of the isolated domains and the intact protein indicated that the domain interface contributes a AGH20 of~ 4.2 kcal*mol-l to the stability of the complete yDwT two-domain protein. The differential stability observed for the yD isolated domains was not as distinct for the yS isolated domains. These results support the idea that selection for increased thermal stability was one of the factors leading to the evolution of two domain crystallins. A distinct hysteresis occurs during equilibrium unfolding and refolding, due to a kinetic barrier in the unfolding pathway. By extrapolating kinetic unfolding results from denaturing GuHCl concentrations to buffer, I show that the ti2 for the initial unfolding step is -19 years. The value extrapolated for the YSwT is not as long, though still significant. This supports the earlier conclusion that the domain interface is an important source of stability.(cont.) Previous studies had shown that upon dilution from denaturant partially folded intermediates of yD crystallin formed highly ordered fibrous aggregates that were not amyloid in nature. This aggregation reaction of yDwT polypeptide chains competing with productive refolding provided a model for cataractogenesis in vitro. The structurally homologous ySwT crystallin did not exhibit an off-pathway aggregation under the same conditions as yDwT. This suggested that the pathway of aggregation involved specific amino acids or sequences essential for association and was not a general feature of the y- crystallins. To investigate this disparity between two structurally similar crystallins, chimera proteins were created in an attempt to narrow down regions of the protein that promoted aggregation in DwTr or regions in ySwT that inhibited aggregation. The aggregation behavior upon refolding was analyzed for the chimeras and isolated single domains. Partitioning of refolding chains into the aggregation pathway was strongest for the full-length proteins that retained the yD interface. This result is consistent with a domain swapping mechanism for the off-pathway aggregation of the crystallins. This aggregation reaction may be coupled to the increased stability of the yD-protein, as a kind of evolutionary cost of the extremely stable and long-lived native state conformation.by Ishara Amenti Rakem Mills-Henry.Ph.D
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