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		<title>Biozentrum Basel</title>
		<link>http://www.biozentrum.unibas.ch/</link>
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			<title>Biozentrum Basel</title>
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		<lastBuildDate>Tue, 11 Jun 2013 08:55:00 +0200</lastBuildDate>
		
		
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			<title>Blueprint for blood vessel fusion discovered</title>
			<link>http://www.biozentrum.unibas.ch/news-events/news-details/article/blueprint-for-blood-vessel-fusion-discovered/</link>
			<description>The fusion of blood vessels during the formation of the vascular system follows a uniform process....</description>
			<content:encoded><![CDATA[In the initial stages of the formation of new blood vessels, the leading cells of two vessel sprouts, the so-called tip cells, come into contact with each other. In these stages, tip cells have the task of making contact with other tip cells, to properly connect with them and so to form a common tube to establish blood flow. The research group of Markus Affolter at the Biozentrum of the University of Basel has been able to examine how this process works in detail using a living organism, the zebrafish.
<h3>First fusion, then splitting</h3>
The scientists showed that the generation of new blood vessels is based on an underlying uniform architectural plan. All forms of blood vessels that develop via sprouting make connections according to this blueprint. During the formation process, the tip cells of both blood vessels split after they have built the connection.
<h3>Transformation makes the point of fusion indiscernible</h3>
Furthermore, the team of scientists observed that the cells are subsequently rearranged so that each tip cell becomes part of a normal blood vessel. These cells can then no longer be distinguished from the other blood vessel cells. „It is practically not possible to identify the fusion site after the fusion process has been completed, „ explained Affolter. „The former tip cells can now fulfil all the functions of a blood vessel cell and are thus multifunctionally used.“ The research group was also able to show that the molecule VE-cadherin gives a signal to the blood vessel indicating that a contact between two tip cells has been successful, thereby completing the contact phase.<br /><br />The zebrafish is a suitable model organism for such investigations. The developing embryo is almost transparent, which makes it possible to closely observe blood vessel generation within the living animal. It is the first time that such a cell splitting process and the transformation of the architecture of a blood vessel could be demonstrated during the formation of new vessel connections in a closed vascular system. Markus Affolter`s group would now like to more closely investigate in living zebrafish, how blood vessel tip cells recognize each other and connect, which additional molecules control the fusion process and how tumors in an organism attach to the already existing circulation.
<b>Original article:</b><br />Anna Lenard, Elin Ellertsdottir, Lukas Herwig, Alice Krudewig, Loic Sauteur, Heinz-Georg Belting, and Markus Affolter (2013):<link http://www.sciencedirect.com/science/article/pii/S1534580713002840 _blank link-external-new-window> In Vivo Analysis Reveals A Highly Stereotypic Morphogenetic Pathway of Vascular Anastomosis.</link> Developmental Cell; Published online June 10, 2013.
<b>Contact: </b><link http://www.biozentrum.unibas.ch/media/ - link-default>Communications</link>, Heike Sacher]]></content:encoded>
			<category>Related to Prof. Markus Affolter</category>
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			<pubDate>Tue, 11 Jun 2013 08:47:00 +0200</pubDate>
			
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			<title>Michael N. Hall elected SAMS Member</title>
			<link>http://www.biozentrum.unibas.ch/news-events/news-details/article/michael-n-hall-elected-sams-member/</link>
			<description>The Swiss Academy of Medical Sciences (SAMS) has honored Prof. Michael N. Hall from the Biozentrum...</description>
			<content:encoded><![CDATA[In their last meeting, the SAMS (German: SAMW) Senate appointed Prof. Michael N. Hall to be an individual member for his extraordinary scientific achievements. In choosing Hall, the SAMS has honored his outstanding research on cell growth and carcinogenesis. As a young assistant professor, he discovered a key molecular switch - the protein «Target of Rapamycin» (TOR). It controls cell growth and size, the production of proteins and regulates metabolism and energy balance within cells. Hall’s scientific studies have contributed greatly to the understanding of the function and significance of TOR and shown that the protein kinase is causally involved in the development of serious diseases such as cancer, diabetes and cardiovascular disease. Hall’s discoveries are among the major breakthroughs in understanding the cellular processes of life.
Michael N. Hall is a Swiss-American dual citizen and has been carrying out research at the Biozentrum of the University of Basel for over 25 years and, since 1992, is a Professor of Biochemistry. He has published his findings in over 160 scientific journal articles. During his scientific career, Hall has received numerous awards including the Clöetta Prize for Biomedical Research (2003), the Louis-Jeantet Prize for Medicine (2009) and the Marcel Benoist Prize (2012). He is a member of highly respected scientific associations and serves as an editor for international journals.&nbsp; In addition, he directs the «Basel Signaling Alliance» Center of Excellence at the University of Basel. 
The Swiss Academy of Medical Sciences was founded in 1943 with the goal of supporting high quality medicine in all its facets, promoting young talents in medical research as well as the efficient implementation of scientifically validated knowledge into practice. The SAMS individual membership is a distinction for outstanding scientific achievements in medicine. The welcoming ceremony will take place in a closed circle on November 28th at the SAMS Senate meeting.
<b>Contact:</b> <link 118>Communications</link>, Katrin Bühler]]></content:encoded>
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			<pubDate>Mon, 10 Jun 2013 12:04:00 +0200</pubDate>
			
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			<title>EMBO Memberships for Christoph Dehio and Peter Scheiffele </title>
			<link>http://www.biozentrum.unibas.ch/news-events/news-details/article/embo-memberships-for-peter-scheiffele-and-christoph-dehio/</link>
			<description>Prof. Christoph Dehio and Prof. Peter Scheiffele from the Biozentrum of the University of Basel...</description>
			<content:encoded><![CDATA[Since the foundation of the Biozentrum a total of 25 scientists, including Christoph Dehio and Peter Scheiffele, have been recognized for their achievements with an EMBO Membership. This year, a total of 52 new EMBO Members, including 16 female scientists, from 15 countries were elected. Amongst the new members are 4 Swiss scientists. The European research network EMBO was founded in 1964 with the goal of furthering biological sciences in Europe. Each year, EMBO elects new members on the basis of their outstanding scientific achievements and supports the career of the researchers. Today EMBO has 1600 members. “They are the basis for the excellent international reputation of EMBO. We welcome this group of exceptional scientists and look forward to their fresh input and ideas”. With these words, the EMBO Director Maria Leptin greeted the newly-appointed members.
<h3>EMBO Member - Christoph Dehio</h3>
Christoph Dehio is Professor for Infection Biology at the Biozentrum since 2000. In 2006, he was awarded the Senior Scientist Prize of the German Society for Hygiene and Microbiology and from 2005 to 2010 was an «International Research Scholar» of the renowned Howard Hughes Medical Institute. Since 2010, he is a member of the German National Academy of Sciences, Leopoldina. Dehio investigates the type IV secretion systems of pathogenic bacteria. With this apparatus, the pathogens inject effector proteins into host cells to selectively alter cellular functions. This favors pathogen persistence in the host resulting in chronic infection. With a systems biology approach, Dehio studies the pathogen-host interactions at the molecular level, providing the basis for the development of novel anti-infective agents. 
<h3>EMBO Member - Peter Scheiffele</h3>
The neurobiologist Peter Scheiffele was appointed as Professor at the Biozentrum in 2008. For his research, he received several awards, including the «Searle Scholar Award» in 2002 and in 2004 the «John Merck Scholar Award».&nbsp; Scheiffele investigates the mechanisms of formation and elimination of neuronal connections - the synapses. He discovered critical functions of synaptic adhesion complexes in synapse formation during brain development. His findings also contribute to the understanding of neurodevelopmental disorders and his laboratory is developing novel mechanism-based interventions for autism. 
<b>Contact:</b> Communications, <link 118>Katrin Bühler</link>]]></content:encoded>
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			<category>Related to Prof. Christoph Dehio</category>
			<category>Related to Prof. Peter Scheiffele</category>
			
			
			<pubDate>Wed, 22 May 2013 09:25:00 +0200</pubDate>
			
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			<title>Become a Marathon Runner with the Protein PGC-1α</title>
			<link>http://www.biozentrum.unibas.ch/news-events/news-details/article/become-a-marathon-runner-with-the-protein-pgc-1a/</link>
			<description>Even with a greater muscle mass, a sprinter cannot win a marathon.  His specially-trained and...</description>
			<content:encoded><![CDATA[<div>Marathon runners complete a special training program to improve their endurance capacity. Accordingly, their muscles are able to sustain the provision of energy using aerobic, hence oxygen consuming processes. Untrained athletes and also bodybuilders reach however, in a much earlier stage, a condition where their muscles produce energy without oxygen. This results in the production of lactate in the muscles. At the same time, the muscles begin to fatigue and the legs become heavy.
<h3>Less Lactate with Endurance Training</h3>
The reason for this difference: the muscles switch their metabolism during endurance training. Importantly, amongst others, the production of the protein PGC-1α is stimulated. Mice with a permanently increased PGC-1α develop the same high endurance muscles as those in trained athletes. Handschin and his team were now able to show in these mice that PGC-1α prevents the formation and accumulation of lactate in the muscles. For this, the researchers have had to train the mice for an hour on the treadmill. After a few minutes, the lactic acid rates increased in the untrained mice, followed by performance degradation and exhaustion. Mice with a high PGC-1α, however, maintained their performance levels until the end of the training. Their lactate levels remained low despite a high training load. &quot;As it turned out,&quot; said Handschin &quot;PGC-1α changed the composition of an enzyme complex. This reduced the formation of lactate. Also, the remaining lactate in the muscle is converted and used immediately as energy substrate.&quot;
<h3>Sport Therapy for Diabetics</h3>
Also in human skeletal muscle, PGC-1α controls the balance between the formation and degradation of lactate. Disturbances in lactate metabolism are common in obese and diabetic patients. The stimulation of PGC-1α&nbsp;production by endurance exercise activity is therefore an important approach to improve the metabolism in these patients. This could help prevent the resulting damage and progressive physical limitations to the body caused by metabolic diseases.</div>
<h3>Original article:</h3>
Serge Summermatter, Gesa Santos, Joaquín Pérez-Schindler, and Christoph Handschin (2013). <link http://www.pnas.org/content/early/2013/05/01/1212976110.abstract _blank>Skeletal muscle PGC-1α controls whole-body lactate homeostasis through estrogen-related receptor α-dependent activation of LDH B and repression of LDH A.</link> PNAS; Published online May 6, 2013
<b>Contact: </b><link 118>Communications</link>, Katrin Bühler]]></content:encoded>
			<category>Bionews</category>
			<category>Related to Prof. Christoph Handschin</category>
			
			
			<pubDate>Wed, 08 May 2013 20:27:00 +0200</pubDate>
			
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			<title>Cleaning service out-of-order – Muscle weakness results </title>
			<link>http://www.biozentrum.unibas.ch/news-events/news-details/article/cleaning-service-out-of-order-muscle-weakness-results/</link>
			<description>The protein complex mTORC1 promotes muscle growth. However, should this complex remain constantly...</description>
			<content:encoded><![CDATA[Similarly to parts in a machine, individual components of a cell wear out with time. For a cell to remain healthy, malfunctioning components and waste products must be regularly disposed of or recycled. A cellular self-cleaning process, called autophagy, is responsible for this. However, the capacity for self-renewal decreases with age and participates in a wide range of age-related diseases such as cancer, heart disease and muscle weakness. In this process, the growth regulator, mTORC1, plays a primary role. The exact relationship has now been discovered by Markus Rüegg’s team from the Biozentrum of the University of Basel, together with scientists from the Department of Biomedicine.
<h3>Muscle weakness due to overactive growth regulator</h3>
Until recently, it was assumed that the protein complex mTORC1 in the skeletal muscle plays a key role in growth regulation but not in the process of autophagy. Rüegg and his team of scientists have been able to refute this widely accepted assumption. In the current study, they investigated the cellular processes in skeletal muscle of mice, in which mTORC1 was permanently activated. Particularly in aging mice, the scientists observed a progressive myopathy, which could be ascribed to impaired autophagy. Interestingly, the researchers could reverse the symptoms by administering rapamycin. The muscle function of the mice returned to normal. Rapamycin is a substance that inhibits mTORC1, thereby promoting cell self-cleaning.
<h3>Counteracting muscle breakdown</h3>
According to these findings, mTORC1 plays a major role in tightly coordinating the mechanism of autophagy, maintaining the balance between muscle growth and breakdown. The scientists suspect that an overactive mTORC1 complex may also contribute to the development of the&nbsp; age-related muscle weakness seen in man. Therefore, a closer examination of the mTORC1 regulation system in the context of aging may provide new therapeutic approaches for the counteracting of the muscle weakness.
<h3>Original article:</h3>
Perrine Castets, Shuo Lin, Nathalie Rion, Sabrina Di Fulvio, Klaas Romanino, Maitea Guridi, Stephan Frank, Lionel A. Tintignac, Michael Sinnreich and Markus A. Rüegg (2013). <link http://www.cell.com/cell-metabolism/abstract/S1550-4131(13)00119-8 _blank>Sustained activation of mTORC1 in skeletal muscle inhibits constitutive and starvation-induced autophagy and causes a severe, late-onset myopathy.</link> Cell Metabolism; Published online April 18, 2013
<b>Contact:</b> <link 118>Communications</link>, Katrin Bühler]]></content:encoded>
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			<category>Related to Prof. Markus Rüegg</category>
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			<pubDate>Sun, 21 Apr 2013 17:07:00 +0200</pubDate>
			
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			<title>The Credit for the New Biozentrum Construction is  Approved</title>
			<link>http://www.biozentrum.unibas.ch/news-events/news-details/article/the-credit-for-the-new-biozentrum-construction-is-approved/</link>
			<description>The Basel-Land parliament has approved the 158-million loan for the construction of the new...</description>
			<content:encoded><![CDATA[After the decision was made by the Basel-City parliament, yesterday the Basel-Land parliament voted to approve the loan of 158.2 million francs to the University of Basel. The new building for the Biozentrum University of Basel has therefore made a further step forward.
The Basel-Land parliament endorsed the credit with an overwhelming majority. Speakers of different groups spoke of a proactive business development plan, important both for the region and the state.
The new building of the Biozentrum will replace the existing, non-contemporary, 42-year old one. In 2010, Zürich architects Andreas Ilg and Marcel Santer emerged as winners of the architectural competition for the new prototype entitled “chroma&quot;.]]></content:encoded>
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			<pubDate>Fri, 12 Apr 2013 12:27:00 +0200</pubDate>
			
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			<title>Using molecules to feel molecules</title>
			<link>http://www.biozentrum.unibas.ch/news-events/news-details/article/using-molecules-to-feel-molecules/</link>
			<description>The research group of Prof. Roderick Lim has developed a new method to gain deeper insights into...</description>
			<content:encoded><![CDATA[The function of proteins depends on their form. Roderick Lim, Argovia Professor of Nanobiology at the Biozentrum and the Swiss Nanoscience Institute at the University of Basel, has been investigating the nuclear pore complex, which regulates the transport of molecules between the cytoplasm and nucleus, for many years.&nbsp; His newly developed method enabled his lab to resolve the form-function relationship of key proteins inside the nuclear pore complex.
<h3>Molecules on nanoscale &quot;highway&quot;</h3>
Based on their findings, Lim and his co-workers explain that the nuclear pore complex resembles a nanoscale &quot;highway&quot;, where there exist slow and fast lanes. This explanation is capable of resolving the biological problem of how the proteins inside the nuclear pore complex select and promote the fast transport of specific molecules between the cytoplasm and nucleus.
The breakthrough came with the realization that non-interacting molecules are the most natural probes that “feel” conformational changes in interfacial layers using a routine technique - surface plasmon resonance (SPR). With the new SPR method, the Lim group could circumvent physical limitations, which previously made SPR structural measurements difficult. This enabled Lim to successfully measure conformational changes and binding properties in situ for the first time.
<h3>Engineering of&nbsp;nanopores</h3>
Surface plasmon resonance (SPR) is routinely applied to assess protein-protein interactions and binding affinities, as well as in drug and proteomic research. Since protein and/or polymer coated surfaces are found everywhere in biology and technology, resolving such binding-associated conformational changes is of important benefit for understanding their function. In addition, Lim’s findings provide the basis for designing molecular, selective channels and nanopores for scientific and medical research.
<h3></h3>
<h3>Original Article:</h3>
Schoch, R. L. and&nbsp; Lim, R. Y. H. (2013) <link http://pubs.acs.org/doi/abs/10.1021/la3049289 _blank>Non-Interacting molecules as innate structural probes in surface plasmon resonance.</link> Langmuir;&nbsp;Published online February 25, 2013
Schoch, R. L., Kapinos, L. E. and Lim, R. Y. H. (2012) <link http://www.pnas.org/content/early/2012/09/27/1208440109.abstract _blank>Nuclear transport receptor binding avidity triggers a self-healing collapse transition in FG-nucleoporin molecular brushes.</link>&nbsp;PNAS;&nbsp;Published online October 4, 2012
<b>Contact:</b> <link 118>Communications</link>
]]></content:encoded>
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			<pubDate>Mon, 08 Apr 2013 12:26:00 +0200</pubDate>
			
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			<title>Nobel Prize Laureate Elizabeth Blackburn at the Biozentrum</title>
			<link>http://www.biozentrum.unibas.ch/news-events/news-details/article/nobel-prize-laureate-elizabeth-blackburn-at-the-biozentrum/</link>
			<description>In 2007, the Time magazine named Elizabeth Blackburn one of the 100 “Most Influential People in the...</description>
			<content:encoded><![CDATA[Prof. Elizabeth Blackburn has investigated the genetic mechanisms of aging for 30 years. For her groundbreaking discoveries, she was awarded the Nobel Prize for Physiology or Medicine in 2009. On 22nd April, 2013, Elizabeth Blackburn gave a public presentation as part of the “Biozentrum Lectures” series.
The Nobel Prize laureate is the Morris Herzstein Professor in Biology and Physiology at the University of California, San Francisco. Already in the 1970’s, Blackburn discovered a structure at the ends of the chromosomes which served as a kind of protective cap, the so called telomeres. With each cell division, however, these ends become shorter. When the telomeres become too short, age-related illnesses such as cancer, diabetes and cardiovascular diseases can result. In 1984, Blackburn and Carol Greider found an enzyme, which they named telomerase. It can replenish the shortened end of the chromosomes, thus delaying aging in man. Disorders in telomerase activity, such as those caused by mutations, weaken the body’s ability to repair itself.
Blackburn graduated in 1975 at the University of Cambridge, in England from the Lab of the Nobel Prize laureate Fred Sanger and subsequently continued her research as a postdoc at Yale University. In 1990, she moved to the Department of Microbiology and Immunology at the University of California, San Francisco, which she headed from 1993 until 1999. For her pioneering research work, she has been honored with many awards including the «Albert Lasker Award for Basic Medical Research» (2006) and the «L’Oreal-UNESCO for Woman in Science» (2008). Blackburn has also taken on leadership positions in various scientific societies and is currently President of the «American Association for Cancer Research».
The public Biozentrum Lecture held by Prof. Elizabeth Blackburn will take place at 4.00 pm, on 22nd April, 2013, in Lecture Theater 1 at the Pharmazentrum, Klingelbergstrasse 50.]]></content:encoded>
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			<pubDate>Mon, 08 Apr 2013 08:52:00 +0200</pubDate>
			
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			<title>Symposium: Frontiers in Structural Biology and Biophysics</title>
			<link>http://www.biozentrum.unibas.ch/news-events/news-details/article/symposium-frontiers-in-structural-biology-and-biophysics/</link>
			<description>On 22nd March 2013, the Biozentrum of the University of Basel will hold a scientific symposium on...</description>
			<content:encoded><![CDATA[The understanding of biological functions depends ultimately on an accurate description of biomolecular interactions with regard to atomic structure, physical forces and their resulting dynamics. Researchers in Structural Biology and Biophysics employ a wide variety of cutting-edge techniques to study macromolecules on a molecular level. At the one-day symposium “Frontiers in Structural Biology and Biophysics” a large number of outstanding scientists will present their newest research.
The speakers include the renowned structural biologist Stephen Fesik (Vanderbilt University, USA) and the world’s most-cited chemist Ad Bax (National Institutes of Health Bethesda, USA). Stephen Fesik’s research focuses on the discovery of cancer drugs and the determination of the three-dimensional structures of protein-drug complexes. He developed “SAR by NMR”, an approach to determine structure-activity relationships by NMR which is widely used in target-directed drug research. Ad Bax is known for his revolutionary advances in the use of NMR spectroscopy to reveal the structure and dynamics of large biomolecules. In addition to the many talks of the symposium, attendees will have the exceptional opportunity to discuss with these leading scientists. The symposium also honors the outstanding, life-time work of Anna and Joachim Seelig at the Biozentrum.
The symposium will take place on March 22nd, 2013, between 8:45 h and 18:30 h in the Lecture Hall 1 of the Pharmazentrum. All those interested to attend this special event are kindly asked to register via the online registration form. The participation is free.
<link http://www.biozentrum.unibas.ch/symposium-structural-biology-2013/ _blank>More information and registration</link>
<b>Contact:</b> <link 113>Communications</link> ]]></content:encoded>
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			<category>Related to Prof. Stephan Grzesiek</category>
			
			
			<pubDate>Mon, 11 Mar 2013 09:28:00 +0100</pubDate>
			
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			<title>New Insights into the Signaling Network of the Vital Protein mTOR</title>
			<link>http://www.biozentrum.unibas.ch/news-events/news-details/article/new-insights-into-the-signaling-network-of-the-vital-protein-mtor/</link>
			<description>Many diseases are caused by malfunction of the mTOR signaling network. Accurate knowledge of...</description>
			<content:encoded><![CDATA[The protein mammalian target of rapamycin (mTOR) controls fundamentally important processes such as cell growth and metabolism. As the core component of two complexes, mTORC1 and mTORC2, it stimulates the production of proteins and fats, and ensures that cells have an adequate energy supply. Dysregulation of the finely-tuned mTOR signaling network is causally involved in the development of serious diseases such as cancer, cardiovascular diseases and diabetes. The search for previously unknown mTOR-regulated proteins could provide new approaches to treat these diseases.
<h3>Novel mTOR Target Proteins Identified</h3>
Because of the central role of mTOR in the cell, scientists suspect that many of the proteins and processes it controls remain to be discovered. By means of a very advanced technology, the so-called quantitative phosphoproteomics, the research group of Hall has now been able to identify more than 300 new mTOR target proteins which perform a wide range of tasks. 
Detailed investigations showed that the mTORC1 stimulates, amongst others, the formation of nucleotides and thus controls the growth and proliferation of cells. Nucleotides are the building blocks of the genetic material and are manufactured in several steps from simple molecules. The first steps in the biosynthesis of nucleotides are mediated by the CAD enzyme. mTORC1 enhances the association of multiple CAD enzymes to form oligomers and thereby stimulates CAD activity and the production of nucleotides.
<h3>Many Details Unknown</h3>
Although we now understand well how mTOR acts, the current results show that there are still many details which are unknown. The comprehensive investigation of the mTOR-controlled signaling pathways and the effects of regulation deficiencies are enourmously important for the understanding of disease processes and the development of new therapeutic approaches. With their research, Hall and his team add another important piece to the mTOR puzzle.
<h3>Original article:</h3>
Aaron M. Robitaille, Stefan Christen, Mitsugu Shimobayashi, Marion Cornu, Luca L. Fava, Suzette Moes, Cristina Prescianotto-Baschong, Uwe Sauer, Paul Jenoe and Michael N. Hall (2013). <link http://www.sciencemag.org/content/early/2013/02/20/science.1228771.full?sid=de24600c-7d2f-4058-8a9a-29dcca5c151a _blank>Quantitative Phosphoproteomics Reveal mTORC1 Activates <i>de</i> <i>Novo</i> Pyrimidine Synthesis</link>. Science; Published online February 21, 2013]]></content:encoded>
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			<pubDate>Fri, 22 Feb 2013 08:52:00 +0100</pubDate>
			
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