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Capital market

A capital market is a financial market in which long-term debt or equity-backed securities are bought and sold. Capital markets channel the wealth of savers to those who can put it to long-term productive use, such as companies or governments making long-term investments. Financial regulators like Securities and Exchange Board of India, Bank of England and the U. S. Securities and Exchange Commission oversee capital markets to protect investors against fraud, among other duties. Modern capital markets are invariably hosted on computer-based electronic trading platforms; as an example, in the United States, any American citizen with an internet connection can create an account with TreasuryDirect and use it to buy bonds in the primary market, though sales to individuals form only a tiny fraction of the total volume of bonds sold. Various private companies provide browser-based platforms that allow individuals to buy shares and sometimes bonds in the secondary markets. There are many thousands of such systems, most serving only small parts of the overall capital markets.

Entities hosting the systems include stock exchanges, investment banks, government departments. Physically, the systems are hosted all over the world, though they tend to be concentrated in financial centres like London, New York, Hong Kong. A capital market can be either a secondary market. In primary market, new stock or bond issues are sold to investors via a mechanism known as underwriting; the main entities seeking to raise long-term funds on the primary capital markets are governments and business enterprises. Governments issue only bonds, whereas companies issue both equity and bonds; the main entities purchasing the bonds or stock include pension funds, hedge funds, sovereign wealth funds, less wealthy individuals and investment banks trading on their own behalf. In the secondary market, existing securities are sold and bought among investors or traders on an exchange, over-the-counter, or elsewhere; the existence of secondary markets increases the willingness of investors in primary markets, as they know they are to be able to swiftly cash out their investments if the need arises.

A second important division falls between the bond markets. The money markets are used for the raising of short-term finance, sometimes for loans that are expected to be paid back as early as overnight. In contrast, the "capital markets" are used for the raising of long-term finance, such as the purchase of shares/equities, or for loans that are not expected to be paid back for at least a year. Funds borrowed from money markets are used for general operating expenses, to provide liquid assets for brief periods. For example, a company may have inbound payments from customers that have not yet cleared, but need immediate cash to pay its employees; when a company borrows from the primary capital markets the purpose is to invest in additional physical capital goods, which will be used to help increase its income. It can take many months or years before the investment generates sufficient return to pay back its cost, hence the finance is long term. Together, money markets and capital markets form the financial markets, as the term is narrowly understood.

The capital market is concerned with long-term finance. In the widest sense, it consists of a series of channels through which the savings of the community are made available for industrial and commercial enterprises and public authorities. Regular bank lending is not classed as a capital market transaction when loans are extended for a period longer than a year. First, regular bank loans are not securitized. Second, lending from banks is more regulated than capital market lending. Third, bank depositors tend to be more risk-averse than capital market investors; these three differences all act to limit institutional lending as a source of finance. Two additional differences, this time favoring lending by banks, are that banks are more accessible for small and medium-sized companies, that they have the ability to create money as they lend. In the 20th century, most company finance apart from share issues was raised by bank loans, but since about 1980 there has been an ongoing trend for disintermediation, where large and creditworthy companies have found they have to pay out less interest if they borrow directly from capital markets rather than from banks.

The tendency for companies to borrow from capital markets instead of banks has been strong in the United States. According to the Financial Times, capital markets overtook bank lending as the leading source of long-term finance in 2009, which reflects the risk aversion and bank regulation in the wake of the 2008 financial crisis. Compared to in the United States, companies in the European Union have a greater reliance on bank lending for funding. Efforts to enable companies to raise more funding through capital markets are being coordinated through the EU's Capital Markets Union initiative; when a government wants to raise long-term finance it will sell bonds in the capital markets. In the 20th and early 21st centuries, many governments would use investment banks to organize the sale of their bonds; the leading bank would underwrite the bonds, would head up

Aksay customs outpost

The Aksay customs outpost is an earthen fortification construction situated in the Aksay, Rostov region of Russia. It is located on the territory of the former Don Noble estate at the mouth of Small Log Beam; the Czar's outpost was built on this territory, followed by a customs post. The fortress was built in the second half of the 18th century; the building was run by the military-historical Museum of Aksay. The complex is part of Dmitryi Rostovskiy fortress; the fortress was built according to the redoubt project standards of the time. The trenches and open space for the Casemates were built and surrounded by brick walls. Logs and beams were used to construct the walls, which were covered with several layers of rammed and dried clay extracted from the banks of the river. Ventilation channels were added to the ceilings; the walls were 10 meters thick and provided protection against shelling. The erection was completed in the year 1763; the final version took the form of a hill-like shape with the dimensions of 15x10 meters.

Exceeding the range of any ship's guns, 36 guns and howitzers were at the disposal of the defenders. Some of these guns are present in the museum. Cavalry units could be accommodated underground; the military-strategic importance of the Aksay fortress was its geographical position at the crossroads of eight trade routes. In the period of the Russo-Turkish wars, the fortress helped to defend Azov, which belonged to Russia following the Constantinople peace treaty in 1700. In the middle of the eighteenth century the tsar's customs outpost and a small settlement called Ust-Aksaisk sheltered under the garrison off the fortress

Jin Soo Kim

Jin Soo Kim is an installation artist who lives and works in Chicago, Illinois. Jin Soo Kim is a South Korean installation artist recognized for her work exploring immigrant cultural identity and labor. Kim's upbringing in post-war Korea and observation of traditional gender inequality motivated her to live a different life based on deep interests in arts since adolescence. In 1974, Kim received her B. S. from Seoul National University and left for Los Angeles, U. S. Having studied at Western Illinois University while working as a nurse, she earned an MFA in 1983 from the School of the Art Institute of Chicago, where she has been a professor of sculpture since 1990. Though her art was not exhibited in the 1980s because it differed so from the popular styles, she began exhibiting at the Chicago Cultural Center and the Museum of Contemporary Art, Chicago. Kim began to exhibit commercially, she focuses on installation art, whose ephemerality has engaged her. One of her best known works is Stratiformis, a piece of public art in Catalano Square, completed in 1996.

A large work that uses disassembled knitting machines, it signifies the local labor history of the area. She is known for her Body and Shadow, which re-purposes machine made textiles into a work made by hand, representing the tension between pre-industrial Korean society and Western consumerism. Kim has received several fellowships, including Illinois Arts Council Fellowships and a National Endowment for the Arts Fellowship. Kim has shown her work worldwide, including at the Chicago Cultural Center.

Northeim (district)

Northeim is a district in Lower Saxony, Germany. It is bounded by the districts of Holzminden, Goslar and Göttingen, the state of Hesse. In medieval times the area had been part of the Duchy of Brunswick-Lüneburg; the majority of it belonged to Hanover and Prussia. In 1885 the Prussian government created districts in the newly acquired provinces. In 1884 the districts of Einbeck and Uslar were established. Northeim and Uslar were merged in 1932, they were again merged with Einbeck in 1974; the district's area was further enlarged in 1977, when some municipalities of neighbouring districts joined the Northeim district. The district is located in the Weserbergland mountains; the Weser forms the western border of the district. Another river, the Leine, runs through the district from south to north, it is joined by the River Rhume which flows through the town of Northeim and the River Ilme which flows through the town of Einbeck. Metropolitan region Hannover-Braunschweig-Göttingen-Wolfsburg Media related to Landkreis Northeim at Wikimedia Commons Official website

Diphosphomevalonate decarboxylase

Diphosphomevalonate decarboxylase, most referred to in scientific literature as mevalonate diphosphate decarboxylase, is an enzyme that catalyzes the chemical reaction ATP + -5-diphosphomevalonate ⇌ ADP + phosphate + isopentenyl diphosphate + CO2This enzyme converts mevalonate 5-diphosphate to isopentenyl diphosphate through ATP dependent decarboxylation. The two substrates of this enzyme are ATP and mevalonate 5-diphosphate, whereas its 4 products are ADP, isopentenyl diphosphate, CO2. Mevalonate diphosphate decarboxylase catalyzes the final step in the mevalonate pathway; the mevalonate pathway is responsible for the biosynthesis of isoprenoids from acetate. This pathway plays a key role in multiple cellular processes by synthesizing sterol isoprenoids, such as cholesterol, non-sterol isoprenoids, such as dolichol, heme A, tRNA isopentenyltransferase, ubiquinone; this enzyme belongs to the family of lyases the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is ATP:-5-diphosphomevalonate carboxy-lyase.

Other names in common use include pyrophosphomevalonate decarboxylase, mevalonate-5-pyrophosphate decarboxylase, pyrophosphomevalonic acid decarboxylase, 5-pyrophosphomevalonate decarboxylase, mevalonate 5-diphosphate decarboxylase, ATP:-5-diphosphomevalonate carboxy-lyase. Mevalonate diphosphate decarboxylase recognizes and binds two substrates: ATP and mevalonate 5-diphosphate. After binding, the enzyme performs three types of reactions that can be separated into two main stages. First, phosphorylation occurs; this creates a reactive intermediate, which in the second stage undergoes concerted dephosphorylation and decarboxylation. Many enzyme residues in the active site play important roles in this concerted mechanism. A serine residue deprotonates the hydroxyl on MVAPP and facilitates the oxygen to attack a phosphate from ATP; as a result, intermediate 1, 3-phosphoMVAPP, now has a much better leaving group, which helps to produce intermediate 2. This third intermediate is a transient beta carboxy carbonium intermediate and provides an "electron sink" that helps drives the decarboxylation reaction.

The exact enzyme apparatus of mevalonate diphosphate decarboxylase is not understood. Structures of both the yeast and human mevalonate diphosphate decarboxylase have been solved with X-ray crystallography, but scientists have experienced difficulties in obtaining structures of bound metabolites. Scientists have classified mevalonate diphosphate decarboxylase as an enzyme in the GHMP kinase family. Both mevalonate kinase and mevalonate diphosphate decarboxylase evolved from a common ancestor since they have a similar fold and catalyze phosphorylation of similar substrates. Due to these commonalities, both enzymes are studied comparatively, in reference to inhibitors. Though there is limited information, some important residues have been identified and are highlighted in the active site structure and mechanism. Due to the difficulty of obtaining crystal structures of bound substrates, a sulfate ion and water molecules were used to better understand the residues role in substrate binding; when investigating the human form of mevalonate diphosphate decarboxylase, the following specific residues were identified: arginine-161, serine-127, aspartate-305, asparagine-17.

Arg-161 interacts with the C1 carbonyl of MVAPP, Asn-17 is important for hydrogen bonding with this same arginine residue. Asp-305 is positioned about 4 Å from the C3 hydroxyl on MVAPP and acts as a general base catalyst in the active site. Ser-127 aids in orientation of the phosphoryl chain for the phosphate transfer to MVAPP. Mevalonate diphosphate decarboxylase has a phosphate-binding loop where amino acid residues provide key interactions that stabilize the nucleotide triphosphoryl moiety; the residues from the P-loop are conserved across enzymes in the GHMP kinase family and include Ala-105, Ser-106, Ser-107 and Ala-108. Many different organisms utilize the mevalonate pathway and mevalonate diphosphate decarboxylase, but for different purposes. In gram positive bacteria, isopentenyl diphosphate, the end product of mevalonate diphosphate decarboxylase, is an essential intermediate in peptidoglycan and polyisoprenoid biosynethesis. Therefore, targeting the mevalonate pathway, mevalonate diphosphate decarboxylase, could be a potential antimicrobial drug.

The mevalonate pathway is used in higher order eukaryotes and plants. Mevalonate diphosphate decarboxylase is present in the liver of mammals where the majority of mevalonate is converted to cholesterol; some of the cholesterol is converted to steroid hormones, bile acids, vitamin D. Mevalonate is converted into many other important intermediates in mammalian cells: dolichols, ubiquinones, tRNA isopentenyltransferase, franesylated and geranylgeranylated proteins; the main point of regulation in cholesterol and nonsterol isoprene biosynethsis is HMGCoA reductase, the third enzyme in the mevalonate pathway. Coronary artery disease is the leading cause of death in the US general population. Hypercholesterolemia or high cholesterol is considered a major risk factor in coronary artery disease. Therefore, major efforts are focused toward understanding regulation and developing inhibitors of cholester

Cooma Back Creek

The Cooma Back Creek, a mostly–perennial river, part of the Murrumbidgee catchment within the Murray–Darling basin, is located in the Monaro region of New South Wales, Australia. The Cooma Back Creek rises below Two Tree Hill, south southeast of North Brother and south by east of Middle Brother, part of the Great Dividing Range, flows north and north by east, joined by one minor tributary before reaching its confluence with the Cooma Creek in the town of Cooma; the Cooma Back Creek descends 157 metres over its 16-kilometre course. The Snowy Mountains Highway crosses Cooma Back Creek in Cooma. Upper Murrumbidgee Demonstration Reach "Map". 1.22MB "Murrumbidgee and Lake George catchments". Office of Environment and Heritage. Government of New South Wales