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<title>Nature Reviews Molecular Cell Biology</title>
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<title>Boveri revisited: chromosomal instability, aneuploidy and tumorigenesis</title>
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<description>The mitotic checkpoint is a major cell cycle control mechanism that guards against chromosome missegregation and the subsequent production of aneuploid daughter cells. Most cancer cells are aneuploid and frequently missegregate chromosomes during mitosis. Indeed, aneuploidy is a common characteristic of tumours, and, for over </description>
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<p>
<b>Boveri revisited: chromosomal instability, aneuploidy and tumorigenesis</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 478 (2009). <a href="http://dx.doi.org/10.1038/nrm2718">doi:10.1038/nrm2718</a>
</p>
<p>Authors: Andrew J. Holland &amp; Don W. Cleveland</p>
<p>The mitotic checkpoint is a major cell cycle control mechanism that guards against chromosome missegregation and the subsequent production of aneuploid daughter cells. Most cancer cells are aneuploid and frequently missegregate chromosomes during mitosis. Indeed, aneuploidy is a common characteristic of tumours, and, for over </p>
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<dc:title>Boveri revisited: chromosomal instability, aneuploidy and tumorigenesis</dc:title>
<dc:creator>Andrew J. Holland</dc:creator>
<dc:creator>Don W. Cleveland</dc:creator>
<dc:identifier>doi:10.1038/nrm2718</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 478 (2009)</dc:source>
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<title>Collective cell migration in morphogenesis, regeneration and cancer</title>
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<description>The collective migration of cells as a cohesive group is a hallmark of the tissue remodelling events that underlie embryonic morphogenesis, wound repair and cancer invasion. In such migration, cells move as sheets, strands, clusters or ducts rather than individually, and use similar actin- and </description>
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<p>
<b>Collective cell migration in morphogenesis, regeneration and cancer</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 445 (2009). <a href="http://dx.doi.org/10.1038/nrm2720">doi:10.1038/nrm2720</a>
</p>
<p>Authors: Peter Friedl &amp; Darren Gilmour</p>
<p>The collective migration of cells as a cohesive group is a hallmark of the tissue remodelling events that underlie embryonic morphogenesis, wound repair and cancer invasion. In such migration, cells move as sheets, strands, clusters or ducts rather than individually, and use similar actin- and </p>
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<dc:title>Collective cell migration in morphogenesis, regeneration and cancer</dc:title>
<dc:creator>Peter Friedl</dc:creator>
<dc:creator>Darren Gilmour</dc:creator>
<dc:identifier>doi:10.1038/nrm2720</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 445 (2009)</dc:source>
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<title>In brief</title>
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<description>Membrane trafficking</description>
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<p>
<b>In brief</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 442 (2009). <a href="http://dx.doi.org/10.1038/nrm2722">doi:10.1038/nrm2722</a>
</p>
<p>Membrane trafficking</p>
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<dc:title>In brief</dc:title>
<dc:identifier>doi:10.1038/nrm2722</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 442 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
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<title>In brief</title>
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<description>Cytoskeleton</description>
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<p>
<b>In brief</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 441 (2009). <a href="http://dx.doi.org/10.1038/nrm2723">doi:10.1038/nrm2723</a>
</p>
<p>Cytoskeleton</p>
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<dc:title>In brief</dc:title>
<dc:identifier>doi:10.1038/nrm2723</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 441 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:volume>10</prism:volume>
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<title>From the editors</title>
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<description>Studying the movements of single cells has enabled great advances in our understanding of the general mechanisms that underlie cell migration. Effective cell migration requires the integration of localized and transient signals with changes in cellular architecture, cell adhesion and asymmetric polarization. As a result, </description>
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<p>
<b>From the editors</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 437 (2009). <a href="http://dx.doi.org/10.1038/nrm2725">doi:10.1038/nrm2725</a>
</p>
<p>Studying the movements of single cells has enabled great advances in our understanding of the general mechanisms that underlie cell migration. Effective cell migration requires the integration of localized and transient signals with changes in cellular architecture, cell adhesion and asymmetric polarization. As a result, </p>
]]></content:encoded>
<dc:title>From the editors</dc:title>
<dc:identifier>doi:10.1038/nrm2725</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 437 (2009)</dc:source>
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<title>Bio-art: the ethics behind the aesthetics</title>
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<description>Bio-art represents a crossover of art and the biological sciences, with living matter, such as genes, cells or animals, as its new media. Such manipulations of life require collaborations with scientists and considerable financial backing. Herein, I consider bio-art that goes 'under the skin' &#8212; </description>
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<p>
<b>Bio-art: the ethics behind the aesthetics</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 496 (2009). <a href="http://dx.doi.org/10.1038/nrm2699">doi:10.1038/nrm2699</a>
</p>
<p>Author: Frances Stracey</p>
<p>Bio-art represents a crossover of art and the biological sciences, with living matter, such as genes, cells or animals, as its new media. Such manipulations of life require collaborations with scientists and considerable financial backing. Herein, I consider bio-art that goes 'under the skin' &#8212; </p>
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<dc:title>Bio-art: the ethics behind the aesthetics</dc:title>
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<dc:identifier>doi:10.1038/nrm2699</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 496 (2009)</dc:source>
<dc:date>2009-05-20</dc:date>
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<item rdf:about="http://dx.doi.org/10.1038/nrm2710">
<title>Seeing red</title>
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<description>The power of fluorescent proteins in biological research was acknowledged in 2008, when the Nobel Prize in Chemistry was awarded to the scientists who discovered and pioneered the use of jellyfish green fluorescent protein (GFP). One of these Nobel laureates, Roger Tsien, is in the </description>
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<p>
<b>Seeing red</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 440 (2009). <a href="http://dx.doi.org/10.1038/nrm2710">doi:10.1038/nrm2710</a>
</p>
<p>Author: Katharine H. Wrighton</p>
<p>The power of fluorescent proteins in biological research was acknowledged in 2008, when the Nobel Prize in Chemistry was awarded to the scientists who discovered and pioneered the use of jellyfish green fluorescent protein (GFP). One of these Nobel laureates, Roger Tsien, is in the </p>
]]></content:encoded>
<dc:title>Seeing red</dc:title>
<dc:creator>Katharine H. Wrighton</dc:creator>
<dc:identifier>doi:10.1038/nrm2710</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 440 (2009)</dc:source>
<dc:date>2009-05-28</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
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<title>Membrane trafficking: Lipid sorting and clustering</title>
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<description>Intracellular trafficking ensures the proper delivery of proteins and lipids to different parts of the cell. However, the process by which lipids are sorted and enriched at the plasma membrane remains unclear. Klemm et al. now provide new insights into this process by showing </description>
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<p>
<b>Membrane trafficking: Lipid sorting and clustering</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 442 (2009). <a href="http://dx.doi.org/10.1038/nrm2711">doi:10.1038/nrm2711</a>
</p>
<p>Author: Alicia Chung</p>
<p>Intracellular trafficking ensures the proper delivery of proteins and lipids to different parts of the cell. However, the process by which lipids are sorted and enriched at the plasma membrane remains unclear. Klemm et al. now provide new insights into this process by showing </p>
]]></content:encoded>
<dc:title>Membrane trafficking: Lipid sorting and clustering</dc:title>
<dc:creator>Alicia Chung</dc:creator>
<dc:identifier>doi:10.1038/nrm2711</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 442 (2009)</dc:source>
<dc:date>2009-05-28</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
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<item rdf:about="http://dx.doi.org/10.1038/nrm2714">
<title>Apoptosis: Death by ubiquitylation</title>
<link>http://dx.doi.org/10.1038/nrm2714</link>
<description>The extrinsic pathway of apoptosis is initiated when certain tumour necrosis factor superfamily ligands, such as APO2L (also known as TNFSF10 or TRAIL), activate cell surface death receptors. The ligand&#8211;receptor complex interacts with FAS-associated death domain protein, an adaptor protein that recruits caspase 8</description>
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<p>
<b>Apoptosis: Death by ubiquitylation</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 441 (2009). <a href="http://dx.doi.org/10.1038/nrm2714">doi:10.1038/nrm2714</a>
</p>
<p>Author: Katharine H Wrighton</p>
<p>The extrinsic pathway of apoptosis is initiated when certain tumour necrosis factor superfamily ligands, such as APO2L (also known as TNFSF10 or TRAIL), activate cell surface death receptors. The ligand&#8211;receptor complex interacts with FAS-associated death domain protein, an adaptor protein that recruits caspase 8</p>
]]></content:encoded>
<dc:title>Apoptosis: Death by ubiquitylation</dc:title>
<dc:creator>Katharine H Wrighton</dc:creator>
<dc:identifier>doi:10.1038/nrm2714</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 441 (2009)</dc:source>
<dc:date>2009-06-03</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
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<item rdf:about="http://dx.doi.org/10.1038/nrm2715">
<title>Gene expression: UV-induced coupling</title>
<link>http://dx.doi.org/10.1038/nrm2715</link>
<description>Alternative splicing (AS) is thought to be a key response to DNA damage because many apoptotic genes are alternatively spliced, but the underlying mechanism is unknown. A new study by Kornblihtt and colleagues reports that ultraviolet (UV) irradiation triggers co-transcriptional AS, through the hyperphosphorylation of </description>
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<p>
<b>Gene expression: UV-induced coupling</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 440 (2009). <a href="http://dx.doi.org/10.1038/nrm2715">doi:10.1038/nrm2715</a>
</p>
<p>Author: Arianne Heinrichs</p>
<p>Alternative splicing (AS) is thought to be a key response to DNA damage because many apoptotic genes are alternatively spliced, but the underlying mechanism is unknown. A new study by Kornblihtt and colleagues reports that ultraviolet (UV) irradiation triggers co-transcriptional AS, through the hyperphosphorylation of </p>
]]></content:encoded>
<dc:title>Gene expression: UV-induced coupling</dc:title>
<dc:creator>Arianne Heinrichs</dc:creator>
<dc:identifier>doi:10.1038/nrm2715</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 440 (2009)</dc:source>
<dc:date>2009-06-03</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-06-03</prism:publicationDate>
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<prism:number>7</prism:number>
<prism:section>Research Highlight</prism:section>
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<title>Dynamics and diversity in autophagy mechanisms: lessons from yeast</title>
<link>http://dx.doi.org/10.1038/nrm2708</link>
<description>Autophagy is a fundamental function of eukaryotic cells and is well conserved from yeast to humans. The most remarkable feature of autophagy is the synthesis of double membrane-bound compartments that sequester materials to be degraded in lytic compartments, a process that seems to be mechanistically </description>
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<p>
<b>Dynamics and diversity in autophagy mechanisms: lessons from yeast</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 458 (2009). <a href="http://dx.doi.org/10.1038/nrm2708">doi:10.1038/nrm2708</a>
</p>
<p>Authors: Hitoshi Nakatogawa, Kuninori Suzuki, Yoshiaki Kamada &amp; Yoshinori Ohsumi</p>
<p>Autophagy is a fundamental function of eukaryotic cells and is well conserved from yeast to humans. The most remarkable feature of autophagy is the synthesis of double membrane-bound compartments that sequester materials to be degraded in lytic compartments, a process that seems to be mechanistically </p>
]]></content:encoded>
<dc:title>Dynamics and diversity in autophagy mechanisms: lessons from yeast</dc:title>
<dc:creator>Hitoshi Nakatogawa</dc:creator>
<dc:creator>Kuninori Suzuki</dc:creator>
<dc:creator>Yoshiaki Kamada</dc:creator>
<dc:creator>Yoshinori Ohsumi</dc:creator>
<dc:identifier>doi:10.1038/nrm2708</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 458 (2009)</dc:source>
<dc:date>2009-06-03</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-06-03</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
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<prism:startingPage>458</prism:startingPage>
<prism:endingPage>467</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nrm2712">
<title>Clearing the way for mitosis: is cohesin a target?</title>
<link>http://dx.doi.org/10.1038/nrm2712</link>
<description>In interphase, chromosomes are associated with proteins and RNAs that participate in many processes, such as DNA replication, transcription, recombination and repair of DNA damage. These components (for example, cohesin) might have to be removed during mitosis, as they might become obstacles that inhibit chromosome </description>
<content:encoded><![CDATA[

<p>
<b>Clearing the way for mitosis: is cohesin a target?</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 489 (2009). <a href="http://dx.doi.org/10.1038/nrm2712">doi:10.1038/nrm2712</a>
</p>
<p>Author: Mitsuhiro Yanagida</p>
<p>In interphase, chromosomes are associated with proteins and RNAs that participate in many processes, such as DNA replication, transcription, recombination and repair of DNA damage. These components (for example, cohesin) might have to be removed during mitosis, as they might become obstacles that inhibit chromosome </p>
]]></content:encoded>
<dc:title>Clearing the way for mitosis: is cohesin a target?</dc:title>
<dc:creator>Mitsuhiro Yanagida</dc:creator>
<dc:identifier>doi:10.1038/nrm2712</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 489 (2009)</dc:source>
<dc:date>2009-06-03</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-06-03</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Perspectives</prism:section>
<prism:startingPage>489</prism:startingPage>
<prism:endingPage>496</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nrm2716">
<title>Gene expression: Complex interactions</title>
<link>http://dx.doi.org/10.1038/nrm2716</link>
<description>Transcription factors (TFs) and their DNA-binding sites are crucial components of gene regulatory networks that control myriad cellular processes. However, the DNA-binding specificities of only a few TFs have been sufficiently characterized to enable the prediction of the sequences that they can and cannot bind </description>
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<p>
<b>Gene expression: Complex interactions</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 444 (2009). <a href="http://dx.doi.org/10.1038/nrm2716">doi:10.1038/nrm2716</a>
</p>
<p>Author: Francesca Cesari</p>
<p>Transcription factors (TFs) and their DNA-binding sites are crucial components of gene regulatory networks that control myriad cellular processes. However, the DNA-binding specificities of only a few TFs have been sufficiently characterized to enable the prediction of the sequences that they can and cannot bind </p>
]]></content:encoded>
<dc:title>Gene expression: Complex interactions</dc:title>
<dc:creator>Francesca Cesari</dc:creator>
<dc:identifier>doi:10.1038/nrm2716</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 444 (2009)</dc:source>
<dc:date>2009-06-10</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-06-10</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>444</prism:startingPage>
<prism:endingPage>444</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nrm2719">
<title>Protein degradation: Assembly from the base</title>
<link>http://dx.doi.org/10.1038/nrm2719</link>
<description>The 26S proteasome comprises the 20S proteolytic core particle (CP) and the 19S regulatory particle (RP), which consists of a lid subcomplex and a base subcomplex. Whereas the mechanisms underlying CP assembly are well established, little is known about how the RP forms. Several groups </description>
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<p>
<b>Protein degradation: Assembly from the base</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 442 (2009). <a href="http://dx.doi.org/10.1038/nrm2719">doi:10.1038/nrm2719</a>
</p>
<p>Author: Arianne Heinrichs</p>
<p>The 26S proteasome comprises the 20S proteolytic core particle (CP) and the 19S regulatory particle (RP), which consists of a lid subcomplex and a base subcomplex. Whereas the mechanisms underlying CP assembly are well established, little is known about how the RP forms. Several groups </p>
]]></content:encoded>
<dc:title>Protein degradation: Assembly from the base</dc:title>
<dc:creator>Arianne Heinrichs</dc:creator>
<dc:identifier>doi:10.1038/nrm2719</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 442 (2009)</dc:source>
<dc:date>2009-06-10</dc:date>
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<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>442</prism:startingPage>
<prism:endingPage>443</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2717">
<title>Proximal events in Wnt signal transduction</title>
<link>http://dx.doi.org/10.1038/nrm2717</link>
<description>The Wnt family of secreted ligands act through many receptors to stimulate distinct intracellular signalling pathways in embryonic development, in adults and in disease processes. Binding of Wnt to the Frizzled family of receptors and to low density lipoprotein receptor-related protein 5 (LRP5) or LRP6 </description>
<content:encoded><![CDATA[

<p>
<b>Proximal events in Wnt signal transduction</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 468 (2009). <a href="http://dx.doi.org/10.1038/nrm2717">doi:10.1038/nrm2717</a>
</p>
<p>Authors: Stephane Angers &amp; Randall T. Moon</p>
<p>The Wnt family of secreted ligands act through many receptors to stimulate distinct intracellular signalling pathways in embryonic development, in adults and in disease processes. Binding of Wnt to the Frizzled family of receptors and to low density lipoprotein receptor-related protein 5 (LRP5) or LRP6 </p>
]]></content:encoded>
<dc:title>Proximal events in Wnt signal transduction</dc:title>
<dc:creator>Stephane Angers</dc:creator>
<dc:creator>Randall T. Moon</dc:creator>
<dc:identifier>doi:10.1038/nrm2717</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 468 (2009)</dc:source>
<dc:date>2009-06-17</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-06-17</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Review</prism:section>
<prism:startingPage>468</prism:startingPage>
<prism:endingPage>477</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2721">
<title>Cell signalling: A fertility network</title>
<link>http://dx.doi.org/10.1038/nrm2721</link>
<description>Mammalian fertility depends on luteinizing hormone (LH)-induced changes in ovarian follicular growth. A new study now reveals some of the signalling components that effect these changes.As oocytes mature and follicles grow, the somatic granulosa cells (GCs) in the ovarian follicle terminally differentiate into luteal </description>
<content:encoded><![CDATA[

<p>
<b>Cell signalling: A fertility network</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 443 (2009). <a href="http://dx.doi.org/10.1038/nrm2721">doi:10.1038/nrm2721</a>
</p>
<p>Author: Simon Bishop</p>
<p>Mammalian fertility depends on luteinizing hormone (LH)-induced changes in ovarian follicular growth. A new study now reveals some of the signalling components that effect these changes.As oocytes mature and follicles grow, the somatic granulosa cells (GCs) in the ovarian follicle terminally differentiate into luteal </p>
]]></content:encoded>
<dc:title>Cell signalling: A fertility network</dc:title>
<dc:creator>Simon Bishop</dc:creator>
<dc:identifier>doi:10.1038/nrm2721</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 443 (2009)</dc:source>
<dc:date>2009-06-17</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-06-17</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>443</prism:startingPage>
<prism:endingPage>443</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2724">
<title>Cell signalling: An activating inhibitor?</title>
<link>http://dx.doi.org/10.1038/nrm2724</link>
<description>Members of the AGC family of protein kinases, including the Akt (also known as protein kinase B (PKB)) proteins and PKC, have important functions in normal and pathological cellular processes. Studies on their mode of activation have shown that 'priming' phosphorylation events in the </description>
<content:encoded><![CDATA[

<p>
<b>Cell signalling: An activating inhibitor?</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 439 (2009). <a href="http://dx.doi.org/10.1038/nrm2724">doi:10.1038/nrm2724</a>
</p>
<p>Author: Emily J. Chenette</p>
<p>Members of the AGC family of protein kinases, including the Akt (also known as protein kinase B (PKB)) proteins and PKC, have important functions in normal and pathological cellular processes. Studies on their mode of activation have shown that 'priming' phosphorylation events in the </p>
]]></content:encoded>
<dc:title>Cell signalling: An activating inhibitor?</dc:title>
<dc:creator>Emily J. Chenette</dc:creator>
<dc:identifier>doi:10.1038/nrm2724</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 439 (2009)</dc:source>
<dc:date>2009-06-17</dc:date>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:publicationDate>2009-06-17</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>439</prism:startingPage>
<prism:endingPage>439</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nrm2709">
<title>Building on the shoulders of giants</title>
<link>http://dx.doi.org/10.1038/nrm2709</link>
<description>Major breakthroughs in science often originate from fundamental biological discoveries or significant technological or methodological advances. For those of us working with model organisms, methods that allow and facilitate the manipulation of genomes transform the field by enabling the creation of animals, tissues or cells </description>
<content:encoded><![CDATA[

<p>
<b>Building on the shoulders of giants</b>
</p>
<p>Nature Reviews Molecular Cell Biology 10, 444 (2009). <a href="http://dx.doi.org/10.1038/nrm2709">doi:10.1038/nrm2709</a>
</p>
<p>Author: Norbert Perrimon</p>
<p>Major breakthroughs in science often originate from fundamental biological discoveries or significant technological or methodological advances. For those of us working with model organisms, methods that allow and facilitate the manipulation of genomes transform the field by enabling the creation of animals, tissues or cells </p>
]]></content:encoded>
<dc:title>Building on the shoulders of giants</dc:title>
<dc:creator>Norbert Perrimon</dc:creator>
<dc:identifier>doi:10.1038/nrm2709</dc:identifier>
<dc:source>Nature Reviews Molecular Cell Biology 10, 444 (2009)</dc:source>
<prism:publicationName>Nature Reviews Molecular Cell Biology</prism:publicationName>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Research Highlight</prism:section>
<prism:startingPage>444</prism:startingPage>
<prism:endingPage>444</prism:endingPage>
</item>
</rdf:RDF>
