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<title><![CDATA[Quantitative analysis of chromatin compaction in living cells using FLIM-FRET]]></title>
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<p>FRET analysis of cell lines expressing fluorescently tagged histones on separate nucleosomes demonstrates that variations in chromosome compaction occur during mitosis.</p>
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<dc:title><![CDATA[Quantitative analysis of chromatin compaction in living cells using FLIM-FRET]]></dc:title>
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<title><![CDATA[Lte1 contributes to Bfa1 localization rather than stimulating nucleotide exchange by Tem1]]></title>
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<p>Reevaluation of Lte1&rsquo;s involvement in the mitotic exit network reveals that it is involved in localizing Bfa1 to the spindle pole body but does not function as a GEF for Tem1.</p>
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<dc:identifier>info:doi/10.1083/jcb.200905114</dc:identifier>
<dc:title><![CDATA[Lte1 contributes to Bfa1 localization rather than stimulating nucleotide exchange by Tem1]]></dc:title>
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<title><![CDATA[Capacity for stochastic self-renewal and differentiation in mammalian spermatogonial stem cells]]></title>
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<p>Spermatogonial stem cells have an innate ability to choose, with constant probability, between different fates independently of cues from the microenvironment.</p>
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<dc:date>Mon, 16 Nov 2009 10:11:50 PST</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200907047</dc:identifier>
<dc:title><![CDATA[Capacity for stochastic self-renewal and differentiation in mammalian spermatogonial stem cells]]></dc:title>
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<p>Increasing the size of the ER by lipid synthesis helps the cell deal with ER stress.</p>
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<dc:identifier>info:doi/10.1083/jcb.200907074</dc:identifier>
<dc:title><![CDATA[Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response]]></dc:title>
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<title><![CDATA[Adenovirus RID-{alpha} activates an autonomous cholesterol regulatory mechanism that rescues defects linked to Niemann-Pick disease type C]]></title>
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<p>Viral subversion of cholesterol homeostasis provides insights into sterol trafficking, autophagy, and lysosomal storage diseases.</p>
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<dc:title><![CDATA[Adenovirus RID-{alpha} activates an autonomous cholesterol regulatory mechanism that rescues defects linked to Niemann-Pick disease type C]]></dc:title>
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<title><![CDATA[The CEACAM1 N-terminal Ig domain mediates cis- and trans-binding and is essential for allosteric rearrangements of CEACAM1 microclusters]]></title>
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<p>Structural analyses reveal that oligomerization between cell adhesion molecules in the same membrane is influenced by their interactions across opposing membranes (see also in this issue the accompanying paper by M&uuml;ller et al.).</p>
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<dc:title><![CDATA[The CEACAM1 N-terminal Ig domain mediates cis- and trans-binding and is essential for allosteric rearrangements of CEACAM1 microclusters]]></dc:title>
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<title><![CDATA[Homophilic adhesion and CEACAM1-S regulate dimerization of CEACAM1-L and recruitment of SHP-2 and c-Src]]></title>
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<p>The monomer/dimer equilibrium of adhesion molecule CEACAM1-L is regulated by binding between opposing membranes, which in turn controls cytoplasmic enzyme binding and signaling (see also in this issue the accompanying paper by Klaile et al.).</p>
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<dc:identifier>info:doi/10.1083/jcb.200904150</dc:identifier>
<dc:title><![CDATA[Homophilic adhesion and CEACAM1-S regulate dimerization of CEACAM1-L and recruitment of SHP-2 and c-Src]]></dc:title>
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<title><![CDATA[Mammalian Rif1 contributes to replication stress survival and homology-directed repair]]></title>
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<p>Multifunctional protein Rif1 accumulates at stalled replication forks to facilitate DNA repair during S phase.</p>
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<dc:creator><![CDATA[Buonomo, S. B.C., Wu, Y., Ferguson, D., de Lange, T.]]></dc:creator>
<dc:date>Mon, 02 Nov 2009 10:42:11 PST</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200902039</dc:identifier>
<dc:title><![CDATA[Mammalian Rif1 contributes to replication stress survival and homology-directed repair]]></dc:title>
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<title><![CDATA[Ase1/Prc1-dependent spindle elongation corrects merotely during anaphase in fission yeast]]></title>
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<p>The tug of war that ensues when a kinetochore binds microtubules from both spindle poles is resolved by Ase1/Prc1.</p>
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<dc:creator><![CDATA[Courtheoux, T., Gay, G., Gachet, Y., Tournier, S.]]></dc:creator>
<dc:date>Mon, 02 Nov 2009 10:42:11 PST</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200902093</dc:identifier>
<dc:title><![CDATA[Ase1/Prc1-dependent spindle elongation corrects merotely during anaphase in fission yeast]]></dc:title>
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<prism:number>3</prism:number>
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<title><![CDATA[Membrane proteins Bqt3 and -4 anchor telomeres to the nuclear envelope to ensure chromosomal bouquet formation]]></title>
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<p>A screen identifies two more bouquet proteins required for meiotic telomere clustering: Bqt4 anchors the telomeres, whereas Bqt3 protects Bqt4 from degradation.</p>
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<dc:creator><![CDATA[Chikashige, Y., Yamane, M., Okamasa, K., Tsutsumi, C., Kojidani, T., Sato, M., Haraguchi, T., Hiraoka, Y.]]></dc:creator>
<dc:date>Mon, 02 Nov 2009 10:42:11 PST</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200902122</dc:identifier>
<dc:title><![CDATA[Membrane proteins Bqt3 and -4 anchor telomeres to the nuclear envelope to ensure chromosomal bouquet formation]]></dc:title>
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<prism:number>3</prism:number>
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<title><![CDATA[MCL-1-dependent leukemia cells are more sensitive to chemotherapy than BCL-2-dependent counterparts]]></title>
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<p>Cancer-expressed anti-apoptotic protein BCL-2 is stable, whereas MCL-1 undergoes proteasome-dependent degradation in response to chemotherapeutic agents.</p>
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<dc:creator><![CDATA[Brunelle, J. K., Ryan, J., Yecies, D., Opferman, J. T., Letai, A.]]></dc:creator>
<dc:date>Mon, 02 Nov 2009 10:42:11 PST</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200904049</dc:identifier>
<dc:title><![CDATA[MCL-1-dependent leukemia cells are more sensitive to chemotherapy than BCL-2-dependent counterparts]]></dc:title>
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<title><![CDATA[Cohesin SMC1{beta} protects telomeres in meiocytes]]></title>
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<p>Telomeres fail to attach to the nuclear envelope and lose structural integrity in cells lacking SMC1&beta;.</p>
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<dc:date>Mon, 19 Oct 2009 10:02:31 PDT</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200808016</dc:identifier>
<dc:title><![CDATA[Cohesin SMC1{beta} protects telomeres in meiocytes]]></dc:title>
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<title><![CDATA[Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD]]></title>
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<p>Loss of ubiquilin or erasin activates ER stress, increases accumulation of polyubiquitinated proteins, and shortens lifespan in worms.</p>
]]></description>
<dc:creator><![CDATA[Lim, P. J., Danner, R., Liang, J., Doong, H., Harman, C., Srinivasan, D., Rothenberg, C., Wang, H., Ye, Y., Fang, S., Monteiro, M. J.]]></dc:creator>
<dc:date>Mon, 19 Oct 2009 10:02:31 PDT</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200903024</dc:identifier>
<dc:title><![CDATA[Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD]]></dc:title>
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<title><![CDATA[Temporal regulation of Drosophila IAP1 determines caspase functions in sensory organ development]]></title>
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<p>Caspase activation is regulated by the turnover of E3 ubiquitin ligase, DIAP1, and depends on cell type and maturity.</p>
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<dc:creator><![CDATA[Koto, A., Kuranaga, E., Miura, M.]]></dc:creator>
<dc:date>Mon, 19 Oct 2009 10:02:31 PDT</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200905110</dc:identifier>
<dc:title><![CDATA[Temporal regulation of Drosophila IAP1 determines caspase functions in sensory organ development]]></dc:title>
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<title><![CDATA[Pex3 peroxisome biogenesis proteins function in peroxisome inheritance as class V myosin receptors]]></title>
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<p>Pex3 links peroxisome formation and inheritance. By binding to class V myosin, biogenesis protein Pex3 also directs the organelles into daughter cells.</p>
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<dc:date>Mon, 19 Oct 2009 10:02:31 PDT</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200902117</dc:identifier>
<dc:title><![CDATA[Pex3 peroxisome biogenesis proteins function in peroxisome inheritance as class V myosin receptors]]></dc:title>
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<title><![CDATA[AP-1 and KIF13A coordinate endosomal sorting and positioning during melanosome biogenesis]]></title>
<link>http://jcb.rupress.org/cgi/content/short/187/2/247?rss=1</link>
<description><![CDATA[
<p>The clathrin adaptor protein AP-1 and the motor KIF13A work together to deliver cargo into maturing melanosomes.</p>
]]></description>
<dc:creator><![CDATA[Delevoye, C., Hurbain, I., Tenza, D., Sibarita, J.-B., Uzan-Gafsou, S., Ohno, H., Geerts, W. J.C., Verkleij, A. J., Salamero, J., Marks, M. S., Raposo, G.]]></dc:creator>
<dc:date>Mon, 19 Oct 2009 10:02:31 PDT</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200907122</dc:identifier>
<dc:title><![CDATA[AP-1 and KIF13A coordinate endosomal sorting and positioning during melanosome biogenesis]]></dc:title>
<dc:publisher>The Rockefeller University Press</dc:publisher>
<prism:object>hw_mjid:jcb;187/2/247</prism:object>
<prism:number>2</prism:number>
<prism:volume>187</prism:volume>
<prism:endingPage>264</prism:endingPage>
<prism:publicationDate>2009-10-19</prism:publicationDate>
<prism:startingPage>247</prism:startingPage>
<prism:section>Articles</prism:section>
</item>

<item rdf:about="http://jcb.rupress.org/cgi/content/short/187/2/265?rss=1">
<title><![CDATA[Spred2 interaction with the late endosomal protein NBR1 down-regulates fibroblast growth factor receptor signaling]]></title>
<link>http://jcb.rupress.org/cgi/content/short/187/2/265?rss=1</link>
<description><![CDATA[
<p>Neighbor of BRCA1 (NBR1) suppresses growth factor responses by redirecting activated receptors to lysosomes for degradation.</p>
]]></description>
<dc:creator><![CDATA[Mardakheh, F. K., Yekezare, M., Machesky, L. M., Heath, J. K.]]></dc:creator>
<dc:date>Mon, 19 Oct 2009 10:02:31 PDT</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200905118</dc:identifier>
<dc:title><![CDATA[Spred2 interaction with the late endosomal protein NBR1 down-regulates fibroblast growth factor receptor signaling]]></dc:title>
<dc:publisher>The Rockefeller University Press</dc:publisher>
<prism:object>hw_mjid:jcb;187/2/265</prism:object>
<prism:number>2</prism:number>
<prism:volume>187</prism:volume>
<prism:endingPage>277</prism:endingPage>
<prism:publicationDate>2009-10-19</prism:publicationDate>
<prism:startingPage>265</prism:startingPage>
<prism:section>Articles</prism:section>
</item>

<item rdf:about="http://jcb.rupress.org/cgi/content/short/187/2/279?rss=1">
<title><![CDATA[PIKfyve regulates CaV1.2 degradation and prevents excitotoxic cell death]]></title>
<link>http://jcb.rupress.org/cgi/content/short/187/2/279?rss=1</link>
<description><![CDATA[
<p>Neuronal Ca levels are regulated by glutamate receptor activation, which recruits PIKfyve to voltage-gated Ca channels, prompting their degradation.</p>
]]></description>
<dc:creator><![CDATA[Tsuruta, F., Green, E. M., Rousset, M., Dolmetsch, R. E.]]></dc:creator>
<dc:date>Mon, 19 Oct 2009 10:02:31 PDT</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200903028</dc:identifier>
<dc:title><![CDATA[PIKfyve regulates CaV1.2 degradation and prevents excitotoxic cell death]]></dc:title>
<dc:publisher>The Rockefeller University Press</dc:publisher>
<prism:object>hw_mjid:jcb;187/2/279</prism:object>
<prism:number>2</prism:number>
<prism:volume>187</prism:volume>
<prism:endingPage>294</prism:endingPage>
<prism:publicationDate>2009-10-19</prism:publicationDate>
<prism:startingPage>279</prism:startingPage>
<prism:section>Articles</prism:section>
</item>

<item rdf:about="http://jcb.rupress.org/cgi/content/short/187/2/295?rss=1">
<title><![CDATA[Postsynaptic regulation of synaptic plasticity by synaptotagmin 4 requires both C2 domains]]></title>
<link>http://jcb.rupress.org/cgi/content/short/187/2/295?rss=1</link>
<description><![CDATA[
<p>Analogous to synaptotagmin 1, a calcium-sensitive regulator of presynaptic vesicle fusion, synaptotagmin 4 needs both of its calcium-binding sites to regulate synaptic plasticity via postsynaptic retrograde signaling.</p>
]]></description>
<dc:creator><![CDATA[Barber, C. F., Jorquera, R. A., Melom, J. E., Littleton, J. T.]]></dc:creator>
<dc:date>Mon, 19 Oct 2009 10:02:31 PDT</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200903098</dc:identifier>
<dc:title><![CDATA[Postsynaptic regulation of synaptic plasticity by synaptotagmin 4 requires both C2 domains]]></dc:title>
<dc:publisher>The Rockefeller University Press</dc:publisher>
<prism:object>hw_mjid:jcb;187/2/295</prism:object>
<prism:number>2</prism:number>
<prism:volume>187</prism:volume>
<prism:endingPage>310</prism:endingPage>
<prism:publicationDate>2009-10-19</prism:publicationDate>
<prism:startingPage>295</prism:startingPage>
<prism:section>Articles</prism:section>
</item>

<item rdf:about="http://jcb.rupress.org/cgi/content/short/187/1/101?rss=1">
<title><![CDATA[Molecular mechanisms that enhance synapse stability despite persistent disruption of the spectrin/ankyrin/microtubule cytoskeleton]]></title>
<link>http://jcb.rupress.org/cgi/content/short/187/1/101?rss=1</link>
<description><![CDATA[
<p>Neuromuscular junctions crippled by a disrupted microtubule cytoskeleton are rescued by stress-induced activation of MAPK-JNK-Fos signaling.</p>
]]></description>
<dc:creator><![CDATA[Massaro, C. M., Pielage, J., Davis, G. W.]]></dc:creator>
<dc:date>Mon, 05 Oct 2009 12:07:45 PDT</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200903166</dc:identifier>
<dc:title><![CDATA[Molecular mechanisms that enhance synapse stability despite persistent disruption of the spectrin/ankyrin/microtubule cytoskeleton]]></dc:title>
<dc:publisher>The Rockefeller University Press</dc:publisher>
<prism:object>hw_mjid:jcb;187/1/101</prism:object>
<prism:number>1</prism:number>
<prism:volume>187</prism:volume>
<prism:endingPage>117</prism:endingPage>
<prism:publicationDate>2009-10-05</prism:publicationDate>
<prism:startingPage>101</prism:startingPage>
<prism:section>Articles</prism:section>
</item>

<item rdf:about="http://jcb.rupress.org/cgi/content/short/187/1/119?rss=1">
<title><![CDATA[Cdc42 antagonizes Rho1 activity at adherens junctions to limit epithelial cell apical tension]]></title>
<link>http://jcb.rupress.org/cgi/content/short/187/1/119?rss=1</link>
<description><![CDATA[
<p>Rho promotes actomyosin contractility during epithelial cell remodeling, but Cdc42 keeps the epithelium in shape by limiting RhoA activity.</p>
]]></description>
<dc:creator><![CDATA[Warner, S. J., Longmore, G. D.]]></dc:creator>
<dc:date>Mon, 05 Oct 2009 12:07:45 PDT</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200906047</dc:identifier>
<dc:title><![CDATA[Cdc42 antagonizes Rho1 activity at adherens junctions to limit epithelial cell apical tension]]></dc:title>
<dc:publisher>The Rockefeller University Press</dc:publisher>
<prism:object>hw_mjid:jcb;187/1/119</prism:object>
<prism:number>1</prism:number>
<prism:volume>187</prism:volume>
<prism:endingPage>133</prism:endingPage>
<prism:publicationDate>2009-10-05</prism:publicationDate>
<prism:startingPage>119</prism:startingPage>
<prism:section>Articles</prism:section>
</item>

<item rdf:about="http://jcb.rupress.org/cgi/content/short/187/1/135?rss=1">
<title><![CDATA[Electron-tomographic analysis of intraflagellar transport particle trains in situ]]></title>
<link>http://jcb.rupress.org/cgi/content/short/187/1/135?rss=1</link>
<description><![CDATA[
<p>Ultrastructural study of <I>Chlamydomonas</I> cilia shows that anterograde IFT particles form trains that are long and narrow, while retrograde IFT form short, compact particle trains.</p>
]]></description>
<dc:creator><![CDATA[Pigino, G., Geimer, S., Lanzavecchia, S., Paccagnini, E., Cantele, F., Diener, D. R., Rosenbaum, J. L., Lupetti, P.]]></dc:creator>
<dc:date>Mon, 05 Oct 2009 12:07:45 PDT</dc:date>
<dc:identifier>info:doi/10.1083/jcb.200905103</dc:identifier>
<dc:title><![CDATA[Electron-tomographic analysis of intraflagellar transport particle trains in situ]]></dc:title>
<dc:publisher>The Rockefeller University Press</dc:publisher>
<prism:object>hw_mjid:jcb;187/1/135</prism:object>
<prism:number>1</prism:number>
<prism:volume>187</prism:volume>
<prism:endingPage>148</prism:endingPage>
<prism:publicationDate>2009-10-05</prism:publicationDate>
<prism:startingPage>135</prism:startingPage>
<prism:section>Articles</prism:section>
</item>

</rdf:RDF>