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<title>A biomedical adventurers' guide to navigating between careers in academia and industry</title>
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<b>A biomedical adventurers' guide to navigating between careers in academia and industry</b>
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<p>Nature Reviews Molecular Cell Biology 10, 884 (2009). <a href="http://dx.doi.org/10.1038/nrm2796">doi:10.1038/nrm2796</a>
</p>
<p>Author: Giulio Superti-Furga</p>
<p>An explosion of scientific and technological advances has broadened the field of biomedicine. Traditional boundaries between the public and private research sectors are now blurred by multidisciplinary projects and the necessity for new and more efficient models of the translational process. This allows the adventurous </p>
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<description>Regulation of cell motility is important for the metastatic dissemination of tumour cells from their primary location to lymph or blood vessels. Transforming growth factor-β (TGFβ) signalling — which is mediated by Smad transcription factors — enhances cell motility and tumour progression. Erik Sahai and </description>
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<b>Cell migration: The benefit of being single</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 816 (2009). <a href="http://dx.doi.org/10.1038/nrm2798">doi:10.1038/nrm2798</a>
</p>
<p>Author: Iley Ozerlat</p>
<p>Regulation of cell motility is important for the metastatic dissemination of tumour cells from their primary location to lymph or blood vessels. Transforming growth factor-&#946; (TGF&#946;) signalling &#8212; which is mediated by Smad transcription factors &#8212; enhances cell motility and tumour progression. Erik Sahai and </p>
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<dc:title>Cell migration: The benefit of being single</dc:title>
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<dc:identifier>doi:10.1038/nrm2798</dc:identifier>
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<title>Growth versus development</title>
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<description>For most of the past century, scientists interested in plant growth and development generally fell into two different camps. Those interested in growth worked on plant hormones such as the small indolic molecule auxin, which regulates plant cell division and expansion. Meanwhile, plant developmental biologists </description>
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<p>
<b>Growth versus development</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 813 (2009). <a href="http://dx.doi.org/10.1038/nrm2800">doi:10.1038/nrm2800</a>
</p>
<p>Author: Mark Estelle</p>
<p>For most of the past century, scientists interested in plant growth and development generally fell into two different camps. Those interested in growth worked on plant hormones such as the small indolic molecule auxin, which regulates plant cell division and expansion. Meanwhile, plant developmental biologists </p>
]]></content:encoded>
<dc:title>Growth versus development</dc:title>
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<dc:identifier>doi:10.1038/nrm2800</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 813 (2009)</dc:source>
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<title>DNA damage response: Keeping telomerase at bay</title>
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<description>The enzyme telomerase maintains chromosome integrity by synthesizing telomeres at chromosome ends. What prevents telomerase from adding telomeres to double-stranded DNA breaks (DSBs)? In Nature Cell Biology, Svetlana Makovets and Elizabeth Blackburn now report that DNA damage signalling induces phosphorylation of the telomerase inhibitor </description>
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<p>
<b>DNA damage response: Keeping telomerase at bay</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 813 (2009). <a href="http://dx.doi.org/10.1038/nrm2801">doi:10.1038/nrm2801</a>
</p>
<p>Author: Emily J. Chenette</p>
<p>The enzyme telomerase maintains chromosome integrity by synthesizing telomeres at chromosome ends. What prevents telomerase from adding telomeres to double-stranded DNA breaks (DSBs)? In Nature Cell Biology, Svetlana Makovets and Elizabeth Blackburn now report that DNA damage signalling induces phosphorylation of the telomerase inhibitor </p>
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<dc:title>DNA damage response: Keeping telomerase at bay</dc:title>
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<dc:identifier>doi:10.1038/nrm2801</dc:identifier>
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<title>Plant cell biology: To die for</title>
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<description>On pathogen infection, plants initiate a rapid cell death programme — known as hypersensitive cell death — at the site of infection to prevent pathogens from spreading to healthy tissues. How cell death is executed and whether plants share cell death mechanisms with animals remains </description>
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<p>
<b>Plant cell biology: To die for</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 815 (2009). <a href="http://dx.doi.org/10.1038/nrm2802">doi:10.1038/nrm2802</a>
</p>
<p>Author: Kim Baumann</p>
<p>On pathogen infection, plants initiate a rapid cell death programme &#8212; known as hypersensitive cell death &#8212; at the site of infection to prevent pathogens from spreading to healthy tissues. How cell death is executed and whether plants share cell death mechanisms with animals remains </p>
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<dc:title>Plant cell biology: To die for</dc:title>
<dc:creator>Kim Baumann</dc:creator>
<dc:identifier>doi:10.1038/nrm2802</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 815 (2009)</dc:source>
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<title>Tissue remodelling through branching morphogenesis</title>
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<description>Branched structures are evident at all levels of organization in living organisms. Many organs, such as the vascular system, lung, kidney and mammary gland, are heavily branched. In each of these cases, equally fascinating questions have been put forward, including those that address the cellular </description>
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<p>
<b>Tissue remodelling through branching morphogenesis</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 831 (2009). <a href="http://dx.doi.org/10.1038/nrm2797">doi:10.1038/nrm2797</a>
</p>
<p>Authors: Markus Affolter, Rolf Zeller &amp; Emmanuel Caussinus</p>
<p>Branched structures are evident at all levels of organization in living organisms. Many organs, such as the vascular system, lung, kidney and mammary gland, are heavily branched. In each of these cases, equally fascinating questions have been put forward, including those that address the cellular </p>
]]></content:encoded>
<dc:title>Tissue remodelling through branching morphogenesis</dc:title>
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<dc:identifier>doi:10.1038/nrm2797</dc:identifier>
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<title>Integrins: masters and slaves of endocytic transport</title>
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<description>Since it has become clear that adhesion receptors are trafficked through the endosomal pathway and that this can influence their function, much effort has been invested in obtaining detailed descriptions of the molecular machinery responsible for internalizing and recycling integrins. New findings indicate that integrin </description>
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<p>
<b>Integrins: masters and slaves of endocytic transport</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 843 (2009). <a href="http://dx.doi.org/10.1038/nrm2799">doi:10.1038/nrm2799</a>
</p>
<p>Authors: Patrick T. Caswell, Suryakiran Vadrevu &amp; Jim C. Norman</p>
<p>Since it has become clear that adhesion receptors are trafficked through the endosomal pathway and that this can influence their function, much effort has been invested in obtaining detailed descriptions of the molecular machinery responsible for internalizing and recycling integrins. New findings indicate that integrin </p>
]]></content:encoded>
<dc:title>Integrins: masters and slaves of endocytic transport</dc:title>
<dc:creator>Patrick T. Caswell</dc:creator>
<dc:creator>Suryakiran Vadrevu</dc:creator>
<dc:creator>Jim C. Norman</dc:creator>
<dc:identifier>doi:10.1038/nrm2799</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 843 (2009)</dc:source>
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<title>Circadian rhythms: Calibrating the clock</title>
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<description>Mammalian circadian rhythms, which govern activities such as sleeping and eating, are regulated by a light-controlled master clock in the brain. Mammals also have clocks in their peripheral organs, which are regulated by nutrient availability through an unknown molecular mechanism. Now, Lamia et al. </description>
<content:encoded><![CDATA[

<p>
<b>Circadian rhythms: Calibrating the clock</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 816 (2009). <a href="http://dx.doi.org/10.1038/nrm2806">doi:10.1038/nrm2806</a>
</p>
<p>Author: Rachel David</p>
<p>Mammalian circadian rhythms, which govern activities such as sleeping and eating, are regulated by a light-controlled master clock in the brain. Mammals also have clocks in their peripheral organs, which are regulated by nutrient availability through an unknown molecular mechanism. Now, Lamia et al. </p>
]]></content:encoded>
<dc:title>Circadian rhythms: Calibrating the clock</dc:title>
<dc:creator>Rachel David</dc:creator>
<dc:identifier>doi:10.1038/nrm2806</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 816 (2009)</dc:source>
<dc:date>2009-11-11</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
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<title>Microscopy: And then there was light</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/ZWNGF_piXNQ/nrm2808</link>
<description>Fluorescence microscopy is limited by the fact that many light-absorbing chromophores do not emit a detectable level of fluorescence and are not easily tagged with fluorophores in a physiological context. Min and colleagues now show how non-fluorescent molecules can be imaged using a technique known </description>
<content:encoded><![CDATA[

<p>
<b>Microscopy: And then there was light</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 814 (2009). <a href="http://dx.doi.org/10.1038/nrm2808">doi:10.1038/nrm2808</a>
</p>
<p>Author: Katharine H. Wrighton</p>
<p>Fluorescence microscopy is limited by the fact that many light-absorbing chromophores do not emit a detectable level of fluorescence and are not easily tagged with fluorophores in a physiological context. Min and colleagues now show how non-fluorescent molecules can be imaged using a technique known </p>
]]></content:encoded>
<dc:title>Microscopy: And then there was light</dc:title>
<dc:creator>Katharine H. Wrighton</dc:creator>
<dc:identifier>doi:10.1038/nrm2808</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 814 (2009)</dc:source>
<dc:date>2009-11-11</dc:date>
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<title>Fine-tuning of GPCR activity by receptor-interacting proteins</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/EGJh-zpDxpI/nrm2803</link>
<description>G protein-coupled receptors (GPCRs) mediate physiological responses to various ligands, such as hormones, neurotransmitters and sensory stimuli. The signalling and trafficking properties of GPCRs are often highly malleable depending on the cellular context. Such fine-tuning of GPCR function can be attributed in many cases to </description>
<content:encoded><![CDATA[

<p>
<b>Fine-tuning of GPCR activity by receptor-interacting proteins</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 819 (2009). <a href="http://dx.doi.org/10.1038/nrm2803">doi:10.1038/nrm2803</a>
</p>
<p>Authors: Stefanie L. Ritter &amp; Randy A. Hall</p>
<p>G protein-coupled receptors (GPCRs) mediate physiological responses to various ligands, such as hormones, neurotransmitters and sensory stimuli. The signalling and trafficking properties of GPCRs are often highly malleable depending on the cellular context. Such fine-tuning of GPCR function can be attributed in many cases to </p>
]]></content:encoded>
<dc:title>Fine-tuning of GPCR activity by receptor-interacting proteins</dc:title>
<dc:creator>Stefanie L. Ritter</dc:creator>
<dc:creator>Randy A. Hall</dc:creator>
<dc:identifier>doi:10.1038/nrm2803</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 819 (2009)</dc:source>
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<title>Regulators of the cytoplasmic dynein motor</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/L4XQqcuFNII/nrm2804</link>
<description>Eukaryotic cells use cytoskeletal motor proteins to transport many different intracellular cargos. Numerous kinesins and myosins have evolved to cope with the various transport needs that have arisen during eukaryotic evolution. Surprisingly, a single cytoplasmic dynein (a minus end-directed microtubule motor) carries out similarly diverse </description>
<content:encoded><![CDATA[

<p>
<b>Regulators of the cytoplasmic dynein motor</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 854 (2009). <a href="http://dx.doi.org/10.1038/nrm2804">doi:10.1038/nrm2804</a>
</p>
<p>Authors: Julia R. Kardon &amp; Ronald D. Vale</p>
<p>Eukaryotic cells use cytoskeletal motor proteins to transport many different intracellular cargos. Numerous kinesins and myosins have evolved to cope with the various transport needs that have arisen during eukaryotic evolution. Surprisingly, a single cytoplasmic dynein (a minus end-directed microtubule motor) carries out similarly diverse </p>
]]></content:encoded>
<dc:title>Regulators of the cytoplasmic dynein motor</dc:title>
<dc:creator>Julia R. Kardon</dc:creator>
<dc:creator>Ronald D. Vale</dc:creator>
<dc:identifier>doi:10.1038/nrm2804</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 854 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2804</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2804</prism:url>
<prism:volume>10</prism:volume>
<prism:number>12</prism:number>
<prism:section>Review</prism:section>
<prism:startingPage>854</prism:startingPage>
<prism:endingPage>865</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2804</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2805">
<title>Exploring protein fitness landscapes by directed evolution</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/cCxA0Ij_QDg/nrm2805</link>
<description>Directed evolution circumvents our profound ignorance of how a protein's sequence encodes its function by using iterative rounds of random mutation and artificial selection to discover new and useful proteins. Proteins can be tunedto adapt to new functions or environments by simple adaptive walks involving </description>
<content:encoded><![CDATA[

<p>
<b>Exploring protein fitness landscapes by directed evolution</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 866 (2009). <a href="http://dx.doi.org/10.1038/nrm2805">doi:10.1038/nrm2805</a>
</p>
<p>Authors: Philip A. Romero &amp; Frances H. Arnold</p>
<p>Directed evolution circumvents our profound ignorance of how a protein's sequence encodes its function by using iterative rounds of random mutation and artificial selection to discover new and useful proteins. Proteins can be tunedto adapt to new functions or environments by simple adaptive walks involving </p>
]]></content:encoded>
<dc:title>Exploring protein fitness landscapes by directed evolution</dc:title>
<dc:creator>Philip A. Romero</dc:creator>
<dc:creator>Frances H. Arnold</dc:creator>
<dc:identifier>doi:10.1038/nrm2805</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 866 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2805</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2805</prism:url>
<prism:volume>10</prism:volume>
<prism:number>12</prism:number>
<prism:section>Review</prism:section>
<prism:startingPage>866</prism:startingPage>
<prism:endingPage>876</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2805</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2807">
<title>The mechanisms of kinesin motor motility: lessons from the monomeric motor KIF1A</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/_PjXAtycV_0/nrm2807</link>
<description>Most kinesins move processively along microtubules by using energy derived from ATP hydrolysis. Almost all of the intermediate structures of this ATPase reaction cycle have been solved for the monomeric kinesin 3 family motor KIF1A. Based on this structural information, we propose a common mechanism </description>
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<p>
<b>The mechanisms of kinesin motor motility: lessons from the monomeric motor KIF1A</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 877 (2009). <a href="http://dx.doi.org/10.1038/nrm2807">doi:10.1038/nrm2807</a>
</p>
<p>Authors: Nobutaka Hirokawa, Ryo Nitta &amp; Yasushi Okada</p>
<p>Most kinesins move processively along microtubules by using energy derived from ATP hydrolysis. Almost all of the intermediate structures of this ATPase reaction cycle have been solved for the monomeric kinesin 3 family motor KIF1A. Based on this structural information, we propose a common mechanism </p>
]]></content:encoded>
<dc:title>The mechanisms of kinesin motor motility: lessons from the monomeric motor KIF1A</dc:title>
<dc:creator>Nobutaka Hirokawa</dc:creator>
<dc:creator>Ryo Nitta</dc:creator>
<dc:creator>Yasushi Okada</dc:creator>
<dc:identifier>doi:10.1038/nrm2807</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 877 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2807</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2807</prism:url>
<prism:volume>10</prism:volume>
<prism:number>12</prism:number>
<prism:section>Perspectives</prism:section>
<prism:startingPage>877</prism:startingPage>
<prism:endingPage>884</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2807</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2809">
<title>In brief</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/N0ZJOQV_YiI/nrm2809</link>
<description>Stem cells</description>
<content:encoded><![CDATA[

<p>
<b>In brief</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 814 (2009). <a href="http://dx.doi.org/10.1038/nrm2809">doi:10.1038/nrm2809</a>
</p>
<p>Stem cells</p>
]]></content:encoded>
<dc:title>In brief</dc:title>
<dc:identifier>doi:10.1038/nrm2809</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 814 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2809</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2809</prism:url>
<prism:volume>10</prism:volume>
<prism:number>12</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>814</prism:startingPage>
<prism:endingPage>814</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2809</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2810">
<title>DNA replication: Cohesin on the fork</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/OSPw5KjYqqg/nrm2810</link>
<description>Sister chromatid cohesion ensures proper chromosome segregation and is mediated by the cohesin complex forming a ring around sister chromatids. How DNA replication forks go through cohesin-associated obstructions to achieve genome replication remains unclear. Prasad Jallepalli and colleagues now report that fork advancement depends on </description>
<content:encoded><![CDATA[

<p>
<b>DNA replication: Cohesin on the fork</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 814 (2009). <a href="http://dx.doi.org/10.1038/nrm2810">doi:10.1038/nrm2810</a>
</p>
<p>Author: Kim Baumann</p>
<p>Sister chromatid cohesion ensures proper chromosome segregation and is mediated by the cohesin complex forming a ring around sister chromatids. How DNA replication forks go through cohesin-associated obstructions to achieve genome replication remains unclear. Prasad Jallepalli and colleagues now report that fork advancement depends on </p>
]]></content:encoded>
<dc:title>DNA replication: Cohesin on the fork</dc:title>
<dc:creator>Kim Baumann</dc:creator>
<dc:identifier>doi:10.1038/nrm2810</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 814 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2810</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2810</prism:url>
<prism:volume>10</prism:volume>
<prism:number>12</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>814</prism:startingPage>
<prism:endingPage>814</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2810</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2811">
<title>Membrane trafficking: IFT proteins play a new game</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/XDWZC-7mQvg/nrm2811</link>
<description>Primary cilia are present on most eukaryotic cells, where they function as sensory organelles to relay information from the external environment into the cell. Cilia are assembled by means of intraflagellar transport (IFT) — a process carried out by multimeric IFT particles and molecular motors. </description>
<content:encoded><![CDATA[

<p>
<b>Membrane trafficking: IFT proteins play a new game</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 812 (2009). <a href="http://dx.doi.org/10.1038/nrm2811">doi:10.1038/nrm2811</a>
</p>
<p>Author: Francesca Cesari</p>
<p>Primary cilia are present on most eukaryotic cells, where they function as sensory organelles to relay information from the external environment into the cell. Cilia are assembled by means of intraflagellar transport (IFT) &#8212; a process carried out by multimeric IFT particles and molecular motors. </p>
]]></content:encoded>
<dc:title>Membrane trafficking: IFT proteins play a new game</dc:title>
<dc:creator>Francesca Cesari</dc:creator>
<dc:identifier>doi:10.1038/nrm2811</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 812 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2811</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2811</prism:url>
<prism:volume>10</prism:volume>
<prism:number>12</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>812</prism:startingPage>
<prism:endingPage>812</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2811</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2812">
<title>In brief</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/sN_A6tmyeHE/nrm2812</link>
<description>Reprogramming</description>
<content:encoded><![CDATA[

<p>
<b>In brief</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 817 (2009). <a href="http://dx.doi.org/10.1038/nrm2812">doi:10.1038/nrm2812</a>
</p>
<p>Reprogramming</p>
]]></content:encoded>
<dc:title>In brief</dc:title>
<dc:identifier>doi:10.1038/nrm2812</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 817 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2812</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2812</prism:url>
<prism:volume>10</prism:volume>
<prism:number>12</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>817</prism:startingPage>
<prism:endingPage>817</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2812</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2813">
<title>Structure watch</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/nezwMHI_m-I/nrm2813</link>
<description>On the DNA–RNA pivotThe RNA-induced silencing complex (RISC) mediates RNA cleavage by forming a complex with DNA and nascent RNA. The catalytic residues for RNA cleavage lie in the PIWI domain of the RISC component Argonaute (Ago). Now, Wang et al. define the </description>
<content:encoded><![CDATA[

<p>
<b>Structure watch</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 816 (2009). <a href="http://dx.doi.org/10.1038/nrm2813">doi:10.1038/nrm2813</a>
</p>
<p>On the DNA&#8211;RNA pivotThe RNA-induced silencing complex (RISC) mediates RNA cleavage by forming a complex with DNA and nascent RNA. The catalytic residues for RNA cleavage lie in the PIWI domain of the RISC component Argonaute (Ago). Now, Wang et al. define the </p>
]]></content:encoded>
<dc:title>Structure watch</dc:title>
<dc:identifier>doi:10.1038/nrm2813</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 816 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2813</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2813</prism:url>
<prism:volume>10</prism:volume>
<prism:number>12</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>816</prism:startingPage>
<prism:endingPage>816</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2813</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2814">
<title>From the editors</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/FDT7dJrqEBw/nrm2814</link>
<description>This year p53 celebrates 30 years of research. We mark this occasion with a Poster highlighting some of the key discoveries that have led to our current understanding of p53 as a tumour suppressor that regulates many important biological activities, and is itself regulated by </description>
<content:encoded><![CDATA[

<p>
<b>From the editors</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 811 (2009). <a href="http://dx.doi.org/10.1038/nrm2814">doi:10.1038/nrm2814</a>
</p>
<p>This year p53 celebrates 30 years of research. We mark this occasion with a Poster highlighting some of the key discoveries that have led to our current understanding of p53 as a tumour suppressor that regulates many important biological activities, and is itself regulated by </p>
]]></content:encoded>
<dc:title>From the editors</dc:title>
<dc:identifier>doi:10.1038/nrm2814</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 811 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2814</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2814</prism:url>
<prism:volume>10</prism:volume>
<prism:number>12</prism:number>
<prism:section>From The Editors</prism:section>
<prism:startingPage>811</prism:startingPage>
<prism:endingPage>811</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2814</feedburner:origLink></item>
</rdf:RDF>
