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<title>Nature Reviews Molecular Cell Biology</title>
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<title>Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/RauYDEYTR9I/nrm2777</link>
<description>Alternative splicing of mRNA precursors provides an important means of genetic control and is a crucial step in the expression of most genes. Alternative splicing markedly affects human development, and its misregulation underlies many human diseases. Although the mechanisms of alternative splicing have been studied </description>
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<p>
<b>Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 741 (2009). <a href="http://dx.doi.org/10.1038/nrm2777">doi:10.1038/nrm2777</a>
</p>
<p>Authors: Mo Chen &amp; James L. Manley</p>
<p>Alternative splicing of mRNA precursors provides an important means of genetic control and is a crucial step in the expression of most genes. Alternative splicing markedly affects human development, and its misregulation underlies many human diseases. Although the mechanisms of alternative splicing have been studied </p>
]]></content:encoded>
<dc:title>Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches</dc:title>
<dc:creator>Mo Chen</dc:creator>
<dc:creator>James L. Manley</dc:creator>
<dc:identifier>doi:10.1038/nrm2777</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 741 (2009)</dc:source>
<dc:date>2009-09-23</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
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<prism:doi>10.1038/nrm2777</prism:doi>
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<title>mRNA decay: Removing the tail</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/l0AbJ-jHQYY/nrm2781</link>
<description>MicroRNAs (miRNAs) function in post-transcriptional gene silencing by directly inhibiting mRNA translation or by inducing mRNA deadenylation, which promotes mRNA decay. Fabian et al., in a paper published in Molecular Cell, provide new insights into the mechanism by which miRNAs promote mRNA deadenylation </description>
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<p>
<b>mRNA decay: Removing the tail</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 736 (2009). <a href="http://dx.doi.org/10.1038/nrm2781">doi:10.1038/nrm2781</a>
</p>
<p>Author: Rachel David</p>
<p>MicroRNAs (miRNAs) function in post-transcriptional gene silencing by directly inhibiting mRNA translation or by inducing mRNA deadenylation, which promotes mRNA decay. Fabian et al., in a paper published in Molecular Cell, provide new insights into the mechanism by which miRNAs promote mRNA deadenylation </p>
]]></content:encoded>
<dc:title>mRNA decay: Removing the tail</dc:title>
<dc:creator>Rachel David</dc:creator>
<dc:identifier>doi:10.1038/nrm2781</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 736 (2009)</dc:source>
<dc:date>2009-10-01</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-10-01</prism:publicationDate>
<prism:doi>10.1038/nrm2781</prism:doi>
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<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Research Highlight</prism:section>
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<feedburner:origLink>http://dx.doi.org/10.1038/nrm2781</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2783">
<title>Chromatin: JAK2 goes nuclear</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/4IWeD4tuORs/nrm2783</link>
<description>Janus kinase 2 (JAK2) is a non-receptor tyrosine kinase known to initiate cytoplasmic signalling cascades that regulate various processes, including cell cycle progression, apoptosis, mitotic recombination, genetic instability and heterochromatin modifications. In Nature, Tony Kouzarides and colleagues now report an unprecedented role for JAK2 </description>
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<p>
<b>Chromatin: JAK2 goes nuclear</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 736 (2009). <a href="http://dx.doi.org/10.1038/nrm2783">doi:10.1038/nrm2783</a>
</p>
<p>Author: Kim Baumann</p>
<p>Janus kinase 2 (JAK2) is a non-receptor tyrosine kinase known to initiate cytoplasmic signalling cascades that regulate various processes, including cell cycle progression, apoptosis, mitotic recombination, genetic instability and heterochromatin modifications. In Nature, Tony Kouzarides and colleagues now report an unprecedented role for JAK2 </p>
]]></content:encoded>
<dc:title>Chromatin: JAK2 goes nuclear</dc:title>
<dc:creator>Kim Baumann</dc:creator>
<dc:identifier>doi:10.1038/nrm2783</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 736 (2009)</dc:source>
<dc:date>2009-10-08</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-10-08</prism:publicationDate>
<prism:doi>10.1038/nrm2783</prism:doi>
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<prism:section>Research Highlight</prism:section>
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<feedburner:origLink>http://dx.doi.org/10.1038/nrm2783</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2785">
<title>And the winner is...</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/_jrzULUt4V0/nrm2785</link>
<description>This year's Albert Lasker Basic Medical Research Award goes to John Gurdon and Shinya Yamanaka for their discoveries on nuclear reprogramming. This process instructs fully differentiated adult cells to revert to early embryonic stem (ES) cells, which, when transplanted into an egg, can restart </description>
<content:encoded><![CDATA[

<p>
<b>And the winner is...</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 736 (2009). <a href="http://dx.doi.org/10.1038/nrm2785">doi:10.1038/nrm2785</a>
</p>
<p>Author: Kim Baumann</p>
<p>This year's Albert Lasker Basic Medical Research Award goes to John Gurdon and Shinya Yamanaka for their discoveries on nuclear reprogramming. This process instructs fully differentiated adult cells to revert to early embryonic stem (ES) cells, which, when transplanted into an egg, can restart </p>
]]></content:encoded>
<dc:title>And the winner is...</dc:title>
<dc:creator>Kim Baumann</dc:creator>
<dc:identifier>doi:10.1038/nrm2785</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 736 (2009)</dc:source>
<dc:date>2009-10-08</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-10-08</prism:publicationDate>
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<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>736</prism:startingPage>
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<feedburner:origLink>http://dx.doi.org/10.1038/nrm2785</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2788">
<title>Apoptosis: Watching caspase 2 get active</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/6J0oAYjgY-M/nrm2788</link>
<description>In the mitochondrial apoptosis pathway, cellular stress induces mitochondrial outer membrane permeabilization (MOMP). This results in the release of proteins from the mitochondrial intermembrane space that activate caspase cysteine proteases. So-called initiator caspases cleave and activate downstream caspases, which subsequently cleave other cellular substrates to </description>
<content:encoded><![CDATA[

<p>
<b>Apoptosis: Watching caspase 2 get active</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 739 (2009). <a href="http://dx.doi.org/10.1038/nrm2788">doi:10.1038/nrm2788</a>
</p>
<p>Author: Katharine H. Wrighton</p>
<p>In the mitochondrial apoptosis pathway, cellular stress induces mitochondrial outer membrane permeabilization (MOMP). This results in the release of proteins from the mitochondrial intermembrane space that activate caspase cysteine proteases. So-called initiator caspases cleave and activate downstream caspases, which subsequently cleave other cellular substrates to </p>
]]></content:encoded>
<dc:title>Apoptosis: Watching caspase 2 get active</dc:title>
<dc:creator>Katharine H. Wrighton</dc:creator>
<dc:identifier>doi:10.1038/nrm2788</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 739 (2009)</dc:source>
<dc:date>2009-10-14</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-10-14</prism:publicationDate>
<prism:doi>10.1038/nrm2788</prism:doi>
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<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Research Highlight</prism:section>
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<feedburner:origLink>http://dx.doi.org/10.1038/nrm2788</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2790">
<title>Autophagy: Autophagy takes an alternative route</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/9whYG2KTYa0/nrm2790</link>
<description>Autophagy-related protein 5 (ATG5) and ATG7 are thought to be essential for mammalian autophagy (also known as macroautophagy) — the lysosomal breakdown of organelles, proteins and other components of the cytoplasm to sustain metabolism during starvation and metabolic stress. Now, a study in Nature</description>
<content:encoded><![CDATA[

<p>
<b>Autophagy: Autophagy takes an alternative route</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 735 (2009). <a href="http://dx.doi.org/10.1038/nrm2790">doi:10.1038/nrm2790</a>
</p>
<p>Author: Francesca Cesari</p>
<p>Autophagy-related protein 5 (ATG5) and ATG7 are thought to be essential for mammalian autophagy (also known as macroautophagy) &#8212; the lysosomal breakdown of organelles, proteins and other components of the cytoplasm to sustain metabolism during starvation and metabolic stress. Now, a study in Nature</p>
]]></content:encoded>
<dc:title>Autophagy: Autophagy takes an alternative route</dc:title>
<dc:creator>Francesca Cesari</dc:creator>
<dc:identifier>doi:10.1038/nrm2790</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 735 (2009)</dc:source>
<dc:date>2009-10-14</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-10-14</prism:publicationDate>
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<prism:number>11</prism:number>
<prism:section>Research Highlight</prism:section>
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<item rdf:about="http://dx.doi.org/10.1038/nrm2791">
<title>Chromosome biology: Small RNAs find the centre</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/lXDJQDCSXkE/nrm2791</link>
<description>The list of biological processes that are controlled by chromatin structure or small RNAs has expanded rapidly in recent years, and a few examples are emerging in which these two modes of regulation are connected. Research presented in three companion papers now links an RNA </description>
<content:encoded><![CDATA[

<p>
<b>Chromosome biology: Small RNAs find the centre</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 738 (2009). <a href="http://dx.doi.org/10.1038/nrm2791">doi:10.1038/nrm2791</a>
</p>
<p>Author: Mary Muers</p>
<p>The list of biological processes that are controlled by chromatin structure or small RNAs has expanded rapidly in recent years, and a few examples are emerging in which these two modes of regulation are connected. Research presented in three companion papers now links an RNA </p>
]]></content:encoded>
<dc:title>Chromosome biology: Small RNAs find the centre</dc:title>
<dc:creator>Mary Muers</dc:creator>
<dc:identifier>doi:10.1038/nrm2791</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 738 (2009)</dc:source>
<dc:date>2009-10-14</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-10-14</prism:publicationDate>
<prism:doi>10.1038/nrm2791</prism:doi>
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<prism:number>11</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>738</prism:startingPage>
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<title>Building ubiquitin chains: E2 enzymes at work</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/gbiXFr3MhFs/nrm2780</link>
<description>The modification of proteins with ubiquitin chains can change their localization, activity and/or stability. Although ubiquitylation requires the concerted action of ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s), it is the E2s that have recently emerged as key mediators of chain assembly. </description>
<content:encoded><![CDATA[

<p>
<b>Building ubiquitin chains: E2 enzymes at work</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 755 (2009). <a href="http://dx.doi.org/10.1038/nrm2780">doi:10.1038/nrm2780</a>
</p>
<p>Authors: Yihong Ye &amp; Michael Rape</p>
<p>The modification of proteins with ubiquitin chains can change their localization, activity and/or stability. Although ubiquitylation requires the concerted action of ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s), it is the E2s that have recently emerged as key mediators of chain assembly. </p>
]]></content:encoded>
<dc:title>Building ubiquitin chains: E2 enzymes at work</dc:title>
<dc:creator>Yihong Ye</dc:creator>
<dc:creator>Michael Rape</dc:creator>
<dc:identifier>doi:10.1038/nrm2780</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 755 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2780</prism:doi>
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<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Review</prism:section>
<prism:startingPage>755</prism:startingPage>
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<title>Traffic control: regulation of kinesin motors</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/1tFHXQhMn7E/nrm2782</link>
<description>Kinesins are a family of molecular motors that use the energy of ATP hydrolysis to move along the surface of, or destabilize, microtubule filaments. Much progress has been made in understanding the mechanics and functions of the kinesin motors that play important parts in cell </description>
<content:encoded><![CDATA[

<p>
<b>Traffic control: regulation of kinesin motors</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 765 (2009). <a href="http://dx.doi.org/10.1038/nrm2782">doi:10.1038/nrm2782</a>
</p>
<p>Authors: Kristen J. Verhey &amp; Jennetta W. Hammond</p>
<p>Kinesins are a family of molecular motors that use the energy of ATP hydrolysis to move along the surface of, or destabilize, microtubule filaments. Much progress has been made in understanding the mechanics and functions of the kinesin motors that play important parts in cell </p>
]]></content:encoded>
<dc:title>Traffic control: regulation of kinesin motors</dc:title>
<dc:creator>Kristen J. Verhey</dc:creator>
<dc:creator>Jennetta W. Hammond</dc:creator>
<dc:identifier>doi:10.1038/nrm2782</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 765 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2782</prism:doi>
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<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Review</prism:section>
<prism:startingPage>765</prism:startingPage>
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<title>Biased segregation of DNA and centrosomes — moving together or drifting apart?</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/qq1YZivT-2A/nrm2784</link>
<description>Old and newly synthesized centrosomes have different microtubule nucleating abilities and they contribute to cell polarity when they migrate to opposite poles during cell division. The asymmetric localization of epigenetic marks and kinetochore proteins could lead to the differential recognition of sister chromatids and the </description>
<content:encoded><![CDATA[

<p>
<b>Biased segregation of DNA and centrosomes &#8212; moving together or drifting apart?</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 804 (2009). <a href="http://dx.doi.org/10.1038/nrm2784">doi:10.1038/nrm2784</a>
</p>
<p>Authors: Shahragim Tajbakhsh &amp; Cayetano Gonzalez</p>
<p>Old and newly synthesized centrosomes have different microtubule nucleating abilities and they contribute to cell polarity when they migrate to opposite poles during cell division. The asymmetric localization of epigenetic marks and kinetochore proteins could lead to the differential recognition of sister chromatids and the </p>
]]></content:encoded>
<dc:title>Biased segregation of DNA and centrosomes — moving together or drifting apart?</dc:title>
<dc:creator>Shahragim Tajbakhsh</dc:creator>
<dc:creator>Cayetano Gonzalez</dc:creator>
<dc:identifier>doi:10.1038/nrm2784</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 804 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2784</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2784</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Perspectives</prism:section>
<prism:startingPage>804</prism:startingPage>
<prism:endingPage>810</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2784</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2786">
<title>Non-muscle myosin II takes centre stage in cell adhesion and migration</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/mmNoVfz_gWc/nrm2786</link>
<description>Non-muscle myosin II (NM II) is an actin-binding protein that has actin cross-linking and contractile properties and is regulated by the phosphorylation of its light and heavy chains. The three mammalian NM II isoforms have both overlapping and unique properties. Owing to its position downstream </description>
<content:encoded><![CDATA[

<p>
<b>Non-muscle myosin II takes centre stage in cell adhesion and migration</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 778 (2009). <a href="http://dx.doi.org/10.1038/nrm2786">doi:10.1038/nrm2786</a>
</p>
<p>Authors: Miguel Vicente-Manzanares, Xuefei Ma, Robert S. Adelstein &amp; Alan Rick Horwitz</p>
<p>Non-muscle myosin II (NM II) is an actin-binding protein that has actin cross-linking and contractile properties and is regulated by the phosphorylation of its light and heavy chains. The three mammalian NM II isoforms have both overlapping and unique properties. Owing to its position downstream </p>
]]></content:encoded>
<dc:title>Non-muscle myosin II takes centre stage in cell adhesion and migration</dc:title>
<dc:creator>Miguel Vicente-Manzanares</dc:creator>
<dc:creator>Xuefei Ma</dc:creator>
<dc:creator>Robert S. Adelstein</dc:creator>
<dc:creator>Alan Rick Horwitz</dc:creator>
<dc:identifier>doi:10.1038/nrm2786</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 778 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2786</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2786</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Review</prism:section>
<prism:startingPage>778</prism:startingPage>
<prism:endingPage>790</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2786</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2787">
<title>Evolution of biomolecular networks — lessons from metabolic and protein interactions</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/ugZ-8-Imv3o/nrm2787</link>
<description>Despite only becoming popular at the beginning of this decade, biomolecular networks are now frameworks that facilitate many discoveries in molecular biology. The nodes of these networks are usually proteins (specifically enzymes in metabolic networks), whereas the links (or edges) are their interactions with other </description>
<content:encoded><![CDATA[

<p>
<b>Evolution of biomolecular networks &#8212; lessons from metabolic and protein interactions</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 791 (2009). <a href="http://dx.doi.org/10.1038/nrm2787">doi:10.1038/nrm2787</a>
</p>
<p>Authors: Takuji Yamada &amp; Peer Bork</p>
<p>Despite only becoming popular at the beginning of this decade, biomolecular networks are now frameworks that facilitate many discoveries in molecular biology. The nodes of these networks are usually proteins (specifically enzymes in metabolic networks), whereas the links (or edges) are their interactions with other </p>
]]></content:encoded>
<dc:title>Evolution of biomolecular networks — lessons from metabolic and protein interactions</dc:title>
<dc:creator>Takuji Yamada</dc:creator>
<dc:creator>Peer Bork</dc:creator>
<dc:identifier>doi:10.1038/nrm2787</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 791 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2787</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2787</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Review</prism:section>
<prism:startingPage>791</prism:startingPage>
<prism:endingPage>803</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nrm2792">
<title>Cell signalling: A new MAP for miRNAs</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/U0j9ytqrUhs/nrm2792</link>
<description>Mature microRNAs (miRNAs) result from the cleavage of precursor miRNAs by the miRNA-generating complex, which in humans consists of Dicer and the HIV TAR RNA-binding protein (TRBP). Some mature miRNAs promote cell growth, whereas others suppress it. Qinghua Liu and colleagues now show that the </description>
<content:encoded><![CDATA[

<p>
<b>Cell signalling: A new MAP for miRNAs</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 734 (2009). <a href="http://dx.doi.org/10.1038/nrm2792">doi:10.1038/nrm2792</a>
</p>
<p>Author: Katharine H. Wrighton</p>
<p>Mature microRNAs (miRNAs) result from the cleavage of precursor miRNAs by the miRNA-generating complex, which in humans consists of Dicer and the HIV TAR RNA-binding protein (TRBP). Some mature miRNAs promote cell growth, whereas others suppress it. Qinghua Liu and colleagues now show that the </p>
]]></content:encoded>
<dc:title>Cell signalling: A new MAP for miRNAs</dc:title>
<dc:creator>Katharine H. Wrighton</dc:creator>
<dc:identifier>doi:10.1038/nrm2792</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 734 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2792</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2792</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>734</prism:startingPage>
<prism:endingPage>734</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2792</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2793">
<title>In brief</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/C6n9zb52WaI/nrm2793</link>
<description>Transcription</description>
<content:encoded><![CDATA[

<p>
<b>In brief</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 737 (2009). <a href="http://dx.doi.org/10.1038/nrm2793">doi:10.1038/nrm2793</a>
</p>
<p>Transcription</p>
]]></content:encoded>
<dc:title>In brief</dc:title>
<dc:identifier>doi:10.1038/nrm2793</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 737 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2793</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2793</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>737</prism:startingPage>
<prism:endingPage>737</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2793</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2794">
<title>Stem cells: iPS cells strike a cord</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/0C-S6asyVLE/nrm2794</link>
<description>Induced pluripotent stem (iPS) cells — somatic and adult stem cells that are reprogrammed to a pluripotent state by the transient expression of various transcription factors — offer great promise for future regenerative therapies. Two studies, published in Cell Stem Cell, now report the </description>
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<p>
<b>Stem cells: iPS cells strike a cord</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 738 (2009). <a href="http://dx.doi.org/10.1038/nrm2794">doi:10.1038/nrm2794</a>
</p>
<p>Author: Kim Baumann</p>
<p>Induced pluripotent stem (iPS) cells &#8212; somatic and adult stem cells that are reprogrammed to a pluripotent state by the transient expression of various transcription factors &#8212; offer great promise for future regenerative therapies. Two studies, published in Cell Stem Cell, now report the </p>
]]></content:encoded>
<dc:title>Stem cells: iPS cells strike a cord</dc:title>
<dc:creator>Kim Baumann</dc:creator>
<dc:identifier>doi:10.1038/nrm2794</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 738 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2794</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2794</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>738</prism:startingPage>
<prism:endingPage>738</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2794</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2795">
<title>From the editors</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/DbGxvFj5gy0/nrm2795</link>
<description>The past month was particularly exciting for molecular and cell biologists. First, Elizabeth H. Blackburn, Carol W. Greider and Jack W. Szostak were awarded the Nobel Prize in Physiology or Medicine for the discovery of “how chromosomes are protected by telomeres and the enzyme telomerase”. </description>
<content:encoded><![CDATA[

<p>
<b>From the editors</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 733 (2009). <a href="http://dx.doi.org/10.1038/nrm2795">doi:10.1038/nrm2795</a>
</p>
<p>The past month was particularly exciting for molecular and cell biologists. First, Elizabeth H. Blackburn, Carol W. Greider and Jack W. Szostak were awarded the Nobel Prize in Physiology or Medicine for the discovery of &#8220;how chromosomes are protected by telomeres and the enzyme telomerase&#8221;. </p>
]]></content:encoded>
<dc:title>From the editors</dc:title>
<dc:identifier>doi:10.1038/nrm2795</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 733 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2795</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2795</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>From The Editors</prism:section>
<prism:startingPage>733</prism:startingPage>
<prism:endingPage>733</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/nrm2795</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2789">
<title>35 years later, mRNA caps still matter</title>
<link>http://feeds.nature.com/~r/nrm/rss/current/~3/rRd-Nhjmvz0/nrm2789</link>
<description>Whereas some important discoveries shine sudden and unexpected light on a research area, other seminal advances result from the contributions of several groups, and the realization of their impact comes years after the initial breakthrough. The discovery of the mRNA cap offers one example of </description>
<content:encoded><![CDATA[

<p>
<b>35 years later, mRNA caps still matter</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 735 (2009). <a href="http://dx.doi.org/10.1038/nrm2789">doi:10.1038/nrm2789</a>
</p>
<p>Author: Anne-Claude Gingras</p>
<p>Whereas some important discoveries shine sudden and unexpected light on a research area, other seminal advances result from the contributions of several groups, and the realization of their impact comes years after the initial breakthrough. The discovery of the mRNA cap offers one example of </p>
]]></content:encoded>
<dc:title>35 years later, mRNA caps still matter</dc:title>
<dc:creator>Anne-Claude Gingras</dc:creator>
<dc:identifier>doi:10.1038/nrm2789</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 735 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:doi>10.1038/nrm2789</prism:doi>
<prism:url>http://dx.doi.org/10.1038/nrm2789</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>735</prism:startingPage>
<prism:endingPage>735</prism:endingPage>
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