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| [1.] Dsa/Fragment 017 01 - Diskussion Zuletzt bearbeitet: 2016-08-02 12:33:35 WiseWoman | Dsa, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Wikipedia Protein kinase 2007 |
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| Untersuchte Arbeit: Seite: 17, Zeilen: 1-16, 23-24 |
Quelle: Wikipedia Protein kinase 2007 Seite(n): 1 (online source), Zeilen: - |
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| 1.2. Protein kinase
A protein kinase is a kinase enzyme that modifies other proteins by chemically adding phosphate groups to them (phosphorylation). This usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins. Up to 30% of all proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction, the transmission of signals within the cell. The human genome contains about 500 protein kinase genes; they constitute about 2% of all eukaryotic genes. The chemical activity of a kinase involves removing a phosphate group from ATP and covalently attaching it to one of three amino acids that have a free hydroxyl group. Because protein kinases have profound effects on a cell, their activity is highly regulated. Kinases are turned on or off by phosphorylation (sometimes by the kinase itself - cis-phosphorylation/autophosphorylation), by binding of activator proteins or inhibitor proteins, or small molecules, or by controlling their location in the cell relative to their substrates. Disregulated kinase activity is a frequent cause of disease, particularly cancer, where kinases regulate many aspects that control cell growth, movement and death. [...] Drugs which inhibit specific kinases are being developed to treat several diseases, and some are currently in clinical use. |
Protein kinase
A protein kinase is a kinase enzyme that modifies other proteins by chemically adding phosphate groups to them (phosphorylation). This class of protein is further separated into subsets such as PKC alpha, PKC beta, and PKC gamma, each with specific functions. Phosphorylation usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins. Up to 30% of all proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction, the transmission of signals within the cell. The human genome contains about 500 protein kinase genes; they constitute about 2% of all eukaryotic genes. The chemical activity of a kinase involves removing a phosphate group from ATP and covalently attaching it to one of three amino acids that have a free hydroxyl group. Most kinases act on both serine and threonine, others act on tyrosine, and a number (dual specificity kinases) act on all three. Because protein kinases have profound effects on a cell, their activity is highly regulated. Kinases are turned on or off by phosphorylation (sometimes by the kinase itself - cis-phosphorylation/autophosphorylation), by binding of activator proteins or inhibitor proteins, or small molecules, or by controlling their location in the cell relative to their substrates. Disregulated kinase activity is a frequent cause of disease, particularly cancer, where kinases regulate many aspects that control cell growth, movement and death. Drugs which inhibit specific kinases are being developed to treat several diseases, and some are currently in clinical use, including Gleevec (imatinib) and Iressa (gefitinib). |
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| [2.] Dsa/Fragment 017 16 - Diskussion Zuletzt bearbeitet: 2016-08-02 19:33:58 WiseWoman | Dsa, Fragment, Gesichtet, Kinexus 2006, KomplettPlagiat, SMWFragment, Schutzlevel sysop |
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| Untersuchte Arbeit: Seite: 17, Zeilen: 16-23, 25-45 |
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| Approximately fifty of the hundred or so known genes that have been directly linked to induction of cancer (i.e. oncogenes) encode protein kinases. The remainder of the oncogenes specify proteins that either activate kinases or are phosphorylated by kinases. Although the findings are less direct, aberrant cell signalling through protein kinases has also been associated with cardiovascular disease, diabetes, inflammation, arthritis and other immune disorders, and neurological disorders such as Alzheimer's disease. Over 400 human diseases have been connected to protein kinases. [...]
With the sequencing of the complete human genome, it is now possible to identify all the related genes within distinct families. It is most efficient if a company can develop expertise around a single family of highly similar proteins. Lessons learned from one family member are most rapidly transferable to related proteins. Protein kinases are the largest family of related genes identified so far that encode enzymes with measurable catalytic activities that are suitable to screen for inhibitory drugs. Protein kinases are amongst the most meticulously investigated enzymes by researchers. There is a wealth of data about these enzymes that already serves as a solid foundation from which to build. The primary structures of over 500 human protein kinases are already known and the three-dimensional structures of many different protein kinases have been elucidated. Extensive artificial mutagenesis of several protein kinases has been performed to establish detailed structure-function relationships. After the proteases, protein kinases represent the most attractive candidates for molecular modelling studies to design new drugs. It is estimated that over 25% of the drug discovery efforts in pharmaceutical and biotech companies are focused on protein kinase inhibitors. These drugs have demonstrated applications for treatment of a wide range of diseases including cancer, inflammation, diabetes, congestive heart failure, and neurological damage. Over 60 protein kinase inhibitors are currently in advanced clinical trials, and three are now available in the market place (Herceptin, Gleevec, and Ireesa). The pharmaceutical industry has clearly come to fully recognize the therapeutic potential of protein kinase inhibitors. |
Approximately fifty of the hundred or so known genes that have been directly linked to induction of cancer (i.e. oncogenes) encode protein kinases. The remainder of the oncogenes specify proteins that either activate kinases or are phosphorylated by kinases. Although the findings are less direct, aberrant cell signalling through protein kinases has also been associated with cardiovascular disease, diabetes, inflammation, arthritis and other immune disorders, and neurological disorders such as Alzheimer's disease. Over 400 human diseases have been connected to protein kinases.
[...] With the sequencing of the complete human genome, it is now possible to identify all the related genes within distinct families. It is most efficient if a company can develop expertise around a single family of highly similar proteins. Lessons learned from one family member is most rapidly transferable to related proteins. Protein kinases are the largest family of related genes identified so far that encode enzymes with measurable catalytic activities that are suitable to screen for inhibitory drugs. Protein kinases are amongst the most meticulously investigated enzymes by researchers. There is a wealth of data about these enzymes that already serves as a solid foundation from which to build. The primary structures of over 510 human protein kinases are already known and the three-dimensional structures of many different protein kinases have been elucidated. Extensive artificial mutagenesis of several protein kinases has been performed to establish detailed structure-function relationships. After the proteases, protein kinases represent the most attractive candidates for molecular modelling studies to design new drugs. [...] It is estimated that over 25% of the drug discovery efforts in pharmaceutical and biotech companies are focused on protein kinase inhibitors. These drugs have demonstrated applications for treatment of a wide range of diseases including cancer, inflammation, diabetes, congestive heart failure, and neurological damage. Over 60 protein kinase inhibitors are currently in advanced clinical trials, and three are now available in the market place (Herceptin, Gleevec, and Ireesa). The pharmaceutical industry has clearly come to fully recognize the therapeutic potential of protein kinase inhibitors. |
No source is given. |
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