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<title>Nature Methods</title>
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<title>Summer reading: science in fiction</title>
<link>http://dx.doi.org/10.1038/nmeth0709-471</link>
<description>Though somewhat rare, there are a few good fiction books to be found with refreshingly realistic biologists as central characters in laboratory settings.</description>
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<p>
<b>Summer reading: science in fiction</b>
</p>
<p>Nature Methods 6, 471 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-471">doi:10.1038/nmeth0709-471</a>
</p>
<p>Though somewhat rare, there are a few good fiction books to be found with refreshingly realistic biologists as central characters in laboratory settings.</p>
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<dc:title>Summer reading: science in fiction</dc:title>
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<p>
<b>MoDIL: detecting small indels from clone-end sequencing with mixtures of distributions</b>
</p>
<p>Nature Methods 6, 473 (2009). <a href="http://dx.doi.org/10.1038/nmeth.f.256">doi:10.1038/nmeth.f.256</a>
</p>
<p>Authors: Seunghak Lee, Fereydoun Hormozdiari, Can Alkan &amp; Michael Brudno</p>
]]></content:encoded>
<dc:title>MoDIL: detecting small indels from clone-end sequencing with mixtures of distributions</dc:title>
<dc:creator>Seunghak Lee</dc:creator>
<dc:creator>Fereydoun Hormozdiari</dc:creator>
<dc:creator>Can Alkan</dc:creator>
<dc:creator>Michael Brudno</dc:creator>
<dc:identifier>doi:10.1038/nmeth.f.256</dc:identifier>
<dc:source>Nature Methods 6, 473 (2009)</dc:source>
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<title>Limitations and possibilities of small RNA digital gene expression profiling</title>
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<p>
<b>Limitations and possibilities of small RNA digital gene expression profiling</b>
</p>
<p>Nature Methods 6, 474 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-474">doi:10.1038/nmeth0709-474</a>
</p>
<p>Authors: Sam E V Linsen, Elzo de Wit, Georges Janssens, Sheila Heater, Laura Chapman, Rachael K Parkin, Brian Fritz, Stacia K Wyman, Ewart de Bruijn, Emile E Voest, Scott Kuersten, Muneesh Tewari &amp; Edwin Cuppen</p>
]]></content:encoded>
<dc:title>Limitations and possibilities of small RNA digital gene expression profiling</dc:title>
<dc:creator>Sam E V Linsen</dc:creator>
<dc:creator>Elzo de Wit</dc:creator>
<dc:creator>Georges Janssens</dc:creator>
<dc:creator>Sheila Heater</dc:creator>
<dc:creator>Laura Chapman</dc:creator>
<dc:creator>Rachael K Parkin</dc:creator>
<dc:creator>Brian Fritz</dc:creator>
<dc:creator>Stacia K Wyman</dc:creator>
<dc:creator>Ewart de Bruijn</dc:creator>
<dc:creator>Emile E Voest</dc:creator>
<dc:creator>Scott Kuersten</dc:creator>
<dc:creator>Muneesh Tewari</dc:creator>
<dc:creator>Edwin Cuppen</dc:creator>
<dc:identifier>doi:10.1038/nmeth0709-474</dc:identifier>
<dc:source>Nature Methods 6, 474 (2009)</dc:source>
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<title>RNAiCut: automated detection of significant genes from functional genomic screens</title>
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<description/>
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<p>
<b>RNAiCut: automated detection of significant genes from functional genomic screens</b>
</p>
<p>Nature Methods 6, 476 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-476">doi:10.1038/nmeth0709-476</a>
</p>
<p>Authors: Irene M Kaplow, Rohit Singh, Adam Friedman, Chris Bakal, Norbert Perrimon &amp; Bonnie Berger</p>
]]></content:encoded>
<dc:title>RNAiCut: automated detection of significant genes from functional genomic screens</dc:title>
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<dc:creator>Rohit Singh</dc:creator>
<dc:creator>Adam Friedman</dc:creator>
<dc:creator>Chris Bakal</dc:creator>
<dc:creator>Norbert Perrimon</dc:creator>
<dc:creator>Bonnie Berger</dc:creator>
<dc:identifier>doi:10.1038/nmeth0709-476</dc:identifier>
<dc:source>Nature Methods 6, 476 (2009)</dc:source>
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<title>Enabling IMAC purification of low abundance recombinant proteins from E. coli lysates</title>
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<description/>
<content:encoded><![CDATA[

<p>
<b>Enabling IMAC purification of low abundance recombinant proteins from E. coli lysates</b>
</p>
<p>Nature Methods 6, 477 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-477">doi:10.1038/nmeth0709-477</a>
</p>
<p>Authors: Audur Magnusdottir, Ida Johansson, Lars-G&#246;ran Dahlgren, P&#228;r Nordlund &amp; Helena Berglund</p>
]]></content:encoded>
<dc:title>Enabling IMAC purification of low abundance recombinant proteins from E. coli lysates</dc:title>
<dc:creator>Audur Magnusdottir</dc:creator>
<dc:creator>Ida Johansson</dc:creator>
<dc:creator>Lars-G&#246;ran Dahlgren</dc:creator>
<dc:creator>P&#228;r Nordlund</dc:creator>
<dc:creator>Helena Berglund</dc:creator>
<dc:identifier>doi:10.1038/nmeth0709-477</dc:identifier>
<dc:source>Nature Methods 6, 477 (2009)</dc:source>
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<title>A question of culture</title>
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<description>Two groups report culture conditions for long-term in vitro growth of intestinal tissue from the mouse.</description>
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<p>
<b>A question of culture</b>
</p>
<p>Nature Methods 6, 481 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-481">doi:10.1038/nmeth0709-481</a>
</p>
<p>Author: Natalie de Souza</p>
<p>Two groups report culture conditions for long-term in vitro growth of intestinal tissue from the mouse.</p>
]]></content:encoded>
<dc:title>A question of culture</dc:title>
<dc:creator>Natalie de Souza</dc:creator>
<dc:identifier>doi:10.1038/nmeth0709-481</dc:identifier>
<dc:source>Nature Methods 6, 481 (2009)</dc:source>
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<prism:number>7</prism:number>
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<title>Fluorescent proteins: into the infrared</title>
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<description>An engineered infrared fluorescent protein is the first member of a new class of genetically encodable probes, with special advantages over visible-wavelength fluorescent proteins for in vivo imaging.</description>
<content:encoded><![CDATA[

<p>
<b>Fluorescent proteins: into the infrared</b>
</p>
<p>Nature Methods 6, 482 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-482a">doi:10.1038/nmeth0709-482a</a>
</p>
<p>Author: Allison Doerr</p>
<p>An engineered infrared fluorescent protein is the first member of a new class of genetically encodable probes, with special advantages over visible-wavelength fluorescent proteins for in vivo imaging.</p>
]]></content:encoded>
<dc:title>Fluorescent proteins: into the infrared</dc:title>
<dc:creator>Allison Doerr</dc:creator>
<dc:identifier>doi:10.1038/nmeth0709-482a</dc:identifier>
<dc:source>Nature Methods 6, 482 (2009)</dc:source>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:volume>6</prism:volume>
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<prism:section>Research Highlights</prism:section>
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<prism:endingPage>483</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nmeth0709-482b">
<title>Going with the skewed flow</title>
<link>http://dx.doi.org/10.1038/nmeth0709-482b</link>
<description>Computational and experimental biologists teamed up to develop a new software tool to analyze the rich data generated by new and powerful flow cytometers.</description>
<content:encoded><![CDATA[

<p>
<b>Going with the skewed flow</b>
</p>
<p>Nature Methods 6, 482 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-482b">doi:10.1038/nmeth0709-482b</a>
</p>
<p>Author: Wayne Peng</p>
<p>Computational and experimental biologists teamed up to develop a new software tool to analyze the rich data generated by new and powerful flow cytometers.</p>
]]></content:encoded>
<dc:title>Going with the skewed flow</dc:title>
<dc:creator>Wayne Peng</dc:creator>
<dc:identifier>doi:10.1038/nmeth0709-482b</dc:identifier>
<dc:source>Nature Methods 6, 482 (2009)</dc:source>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Research Highlights</prism:section>
<prism:startingPage>482</prism:startingPage>
<prism:endingPage>483</prism:endingPage>
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<title>News in brief</title>
<link>http://dx.doi.org/10.1038/nmeth0709-483</link>
<description/>
<content:encoded><![CDATA[

<p>
<b>News in brief</b>
</p>
<p>Nature Methods 6, 483 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-483">doi:10.1038/nmeth0709-483</a>
</p>
]]></content:encoded>
<dc:title>News in brief</dc:title>
<dc:identifier>doi:10.1038/nmeth0709-483</dc:identifier>
<dc:source>Nature Methods 6, 483 (2009)</dc:source>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Research Highlights</prism:section>
<prism:startingPage>483</prism:startingPage>
<prism:endingPage>483</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nmeth0709-484">
<title>Grafting as a potent molecular tool</title>
<link>http://dx.doi.org/10.1038/nmeth0709-484</link>
<description>Grafting two transgenic plants triggers lateral gene transfer at the graft site but does not elicit long-distance transport of DNA into the scion or root of the graft.</description>
<content:encoded><![CDATA[

<p>
<b>Grafting as a potent molecular tool</b>
</p>
<p>Nature Methods 6, 484 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-484">doi:10.1038/nmeth0709-484</a>
</p>
<p>Author: Nicole Rusk</p>
<p>Grafting two transgenic plants triggers lateral gene transfer at the graft site but does not elicit long-distance transport of DNA into the scion or root of the graft.</p>
]]></content:encoded>
<dc:title>Grafting as a potent molecular tool</dc:title>
<dc:creator>Nicole Rusk</dc:creator>
<dc:identifier>doi:10.1038/nmeth0709-484</dc:identifier>
<dc:source>Nature Methods 6, 484 (2009)</dc:source>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Research Highlights</prism:section>
<prism:startingPage>484</prism:startingPage>
<prism:endingPage>484</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth0709-486">
<title>Fluorescent false neurotransmitters</title>
<link>http://dx.doi.org/10.1038/nmeth0709-486</link>
<description>A fluorescent probe designed to incorporate a fluorophore into the structure of a neurotransmitter finds activity-dependent heterogeneity in dopamine release at individual synapses.</description>
<content:encoded><![CDATA[

<p>
<b>Fluorescent false neurotransmitters</b>
</p>
<p>Nature Methods 6, 486 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-486">doi:10.1038/nmeth0709-486</a>
</p>
<p>Author: Daniel Evanko</p>
<p>A fluorescent probe designed to incorporate a fluorophore into the structure of a neurotransmitter finds activity-dependent heterogeneity in dopamine release at individual synapses.</p>
]]></content:encoded>
<dc:title>Fluorescent false neurotransmitters</dc:title>
<dc:creator>Daniel Evanko</dc:creator>
<dc:identifier>doi:10.1038/nmeth0709-486</dc:identifier>
<dc:source>Nature Methods 6, 486 (2009)</dc:source>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Research Highlights</prism:section>
<prism:startingPage>486</prism:startingPage>
<prism:endingPage>486</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nmeth0709-487">
<title>Will planets reveal the light of their life?</title>
<link>http://dx.doi.org/10.1038/nmeth0709-487</link>
<description>Optical signatures from organic chemicals may help scientists detect traces of life on other planets.</description>
<content:encoded><![CDATA[

<p>
<b>Will planets reveal the light of their life?</b>
</p>
<p>Nature Methods 6, 487 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-487">doi:10.1038/nmeth0709-487</a>
</p>
<p>Author: Michael Eisenstein</p>
<p>Optical signatures from organic chemicals may help scientists detect traces of life on other planets.</p>
]]></content:encoded>
<dc:title>Will planets reveal the light of their life?</dc:title>
<dc:creator>Michael Eisenstein</dc:creator>
<dc:identifier>doi:10.1038/nmeth0709-487</dc:identifier>
<dc:source>Nature Methods 6, 487 (2009)</dc:source>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Research Highlights</prism:section>
<prism:startingPage>487</prism:startingPage>
<prism:endingPage>487</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nmeth0709-489">
<title>Finding multiple needles in one immune haystack</title>
<link>http://dx.doi.org/10.1038/nmeth0709-489</link>
<description>An approach using multiple fluorochrome combinations allows the simultaneous detection of many T-cell populations within a single blood sample.</description>
<content:encoded><![CDATA[

<p>
<b>Finding multiple needles in one immune haystack</b>
</p>
<p>Nature Methods 6, 489 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-489">doi:10.1038/nmeth0709-489</a>
</p>
<p>Authors: Katherine Kedzierska, John Stambas &amp; Peter C Doherty</p>
<p>An approach using multiple fluorochrome combinations allows the simultaneous detection of many T-cell populations within a single blood sample.</p>
]]></content:encoded>
<dc:title>Finding multiple needles in one immune haystack</dc:title>
<dc:creator>Katherine Kedzierska</dc:creator>
<dc:creator>John Stambas</dc:creator>
<dc:creator>Peter C Doherty</dc:creator>
<dc:identifier>doi:10.1038/nmeth0709-489</dc:identifier>
<dc:source>Nature Methods 6, 489 (2009)</dc:source>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>News and Views</prism:section>
<prism:startingPage>489</prism:startingPage>
<prism:endingPage>490</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nmeth0709-490">
<title>Downhill protein folding under pressure</title>
<link>http://dx.doi.org/10.1038/nmeth0709-490</link>
<description>Sub-microsecond, downhill-reaction protein folding can be investigated by a method to generate large and fast pressure drops. The approach is complementary to nanosecond temperature-jump methods and could provide new insights into the biophysics of protein folding.</description>
<content:encoded><![CDATA[

<p>
<b>Downhill protein folding under pressure</b>
</p>
<p>Nature Methods 6, 490 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-490">doi:10.1038/nmeth0709-490</a>
</p>
<p>Author: Victor Mu&#241;oz</p>
<p>Sub-microsecond, downhill-reaction protein folding can be investigated by a method to generate large and fast pressure drops. The approach is complementary to nanosecond temperature-jump methods and could provide new insights into the biophysics of protein folding.</p>
]]></content:encoded>
<dc:title>Downhill protein folding under pressure</dc:title>
<dc:creator>Victor Mu&#241;oz</dc:creator>
<dc:identifier>doi:10.1038/nmeth0709-490</dc:identifier>
<dc:source>Nature Methods 6, 490 (2009)</dc:source>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>News and Views</prism:section>
<prism:startingPage>490</prism:startingPage>
<prism:endingPage>491</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nmeth.1342">
<title>Agouti C57BL/6N embryonic stem cells for mouse genetic resources</title>
<link>http://dx.doi.org/10.1038/nmeth.1342</link>
<description>Mouse embryonic stem cell lines from the C57BL/6 strain are reported. The lines are highly germline competent, suitable for high-throughput genetic manipulation and will enable the generation of large knockout mouse resources.</description>
<content:encoded><![CDATA[

<p>
<b>Agouti C57BL/6N embryonic stem cells for mouse genetic resources</b>
</p>
<p>Nature Methods 6, 493 (2009). <a href="http://dx.doi.org/10.1038/nmeth.1342">doi:10.1038/nmeth.1342</a>
</p>
<p>Authors: Stephen J Pettitt, Qi Liang, Xin Y Rairdan, Jennifer L Moran, Haydn M Prosser, David R Beier, Kent C Lloyd, Allan Bradley &amp; William C Skarnes</p>
<p>We report the characterization of a highly germline competent C57BL/6N mouse embryonic stem cell line, JM8. To simplify breeding schemes, the dominant agouti coat color gene was restored in JM8 cells by targeted repair of the C57BL/6 nonagouti mutation. These cells provide a robust foundation for large-scale mouse knockout programs that aim to provide a public resource of targeted mutations in the C57BL/6 genetic background.</p>
]]></content:encoded>
<dc:title>Agouti C57BL/6N embryonic stem cells for mouse genetic resources</dc:title>
<dc:creator>Stephen J Pettitt</dc:creator>
<dc:creator>Qi Liang</dc:creator>
<dc:creator>Xin Y Rairdan</dc:creator>
<dc:creator>Jennifer L Moran</dc:creator>
<dc:creator>Haydn M Prosser</dc:creator>
<dc:creator>David R Beier</dc:creator>
<dc:creator>Kent C Lloyd</dc:creator>
<dc:creator>Allan Bradley</dc:creator>
<dc:creator>William C Skarnes</dc:creator>
<dc:identifier>doi:10.1038/nmeth.1342</dc:identifier>
<dc:source>Nature Methods 6, 493 (2009)</dc:source>
<dc:date>2009-06-14</dc:date>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:publicationDate>2009-06-14</prism:publicationDate>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Brief Communication</prism:section>
<prism:startingPage>493</prism:startingPage>
<prism:endingPage>495</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth.1344">
<title>Simultaneous detection of many T-cell specificities using combinatorial tetramer staining</title>
<link>http://dx.doi.org/10.1038/nmeth.1344</link>
<description>Combinations of fluorescently labeled peptide&#8211;major histocompatability (pMHC) tetramers are used to simultaneously detect T cells with multiple antigen specificities from human blood samples. Also in this issue, Hadrup et al. present a very similar combinatorial encoding approach.</description>
<content:encoded><![CDATA[

<p>
<b>Simultaneous detection of many T-cell specificities using combinatorial tetramer staining</b>
</p>
<p>Nature Methods 6, 497 (2009). <a href="http://dx.doi.org/10.1038/nmeth.1344">doi:10.1038/nmeth.1344</a>
</p>
<p>Authors: Evan W Newell, Lawrence O Klein, Wong Yu &amp; Mark M Davis</p>
<p>The direct detection of antigen-specific T cells using tetramers of soluble peptide&#8211;major histocompatibilty complex (pMHC) molecules is widely used in both basic and clinical immunology. However, the number of specificities that can be assessed simultaneously has been a major limitation. Here we describe and validate a method using combinations of fluorescent pMHC tetramers to simultaneously detect and enrich for many (&#8805;15) T-cell specificities in a single human blood sample.</p>
]]></content:encoded>
<dc:title>Simultaneous detection of many T-cell specificities using combinatorial tetramer staining</dc:title>
<dc:creator>Evan W Newell</dc:creator>
<dc:creator>Lawrence O Klein</dc:creator>
<dc:creator>Wong Yu</dc:creator>
<dc:creator>Mark M Davis</dc:creator>
<dc:identifier>doi:10.1038/nmeth.1344</dc:identifier>
<dc:source>Nature Methods 6, 497 (2009)</dc:source>
<dc:date>2009-06-21</dc:date>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:publicationDate>2009-06-21</prism:publicationDate>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Brief Communication</prism:section>
<prism:startingPage>497</prism:startingPage>
<prism:endingPage>499</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth.1337">
<title>Protein interaction platforms: visualization of interacting proteins in yeast</title>
<link>http://dx.doi.org/10.1038/nmeth.1337</link>
<description>The protein interaction platform or PIP assay uses a viral scaffolding protein fused to a bait and a fluorescent reporter protein fused to putative prey as the basis for a simple visual screen for protein-protein interactions in yeast.</description>
<content:encoded><![CDATA[

<p>
<b>Protein interaction platforms: visualization of interacting proteins in yeast</b>
</p>
<p>Nature Methods 6, 500 (2009). <a href="http://dx.doi.org/10.1038/nmeth.1337">doi:10.1038/nmeth.1337</a>
</p>
<p>Authors: Alexa M Schmitz, Monica F Morrison, Akochi O Agunwamba, Max L Nibert &amp; Cammie F Lesser</p>
<p>Here we describe the protein interaction platform assay, a method for identifying interacting proteins in Saccharomyces cerevisiae. This assay relies on the reovirus scaffolding protein &#956;NS, which forms large focal inclusions in living cells. When a query protein is fused to &#956;NS and potential interaction partners are fused to a fluorescent reporter, interactors can be identified by screening for yeast that display fluorescent foci.</p>
]]></content:encoded>
<dc:title>Protein interaction platforms: visualization of interacting proteins in yeast</dc:title>
<dc:creator>Alexa M Schmitz</dc:creator>
<dc:creator>Monica F Morrison</dc:creator>
<dc:creator>Akochi O Agunwamba</dc:creator>
<dc:creator>Max L Nibert</dc:creator>
<dc:creator>Cammie F Lesser</dc:creator>
<dc:identifier>doi:10.1038/nmeth.1337</dc:identifier>
<dc:source>Nature Methods 6, 500 (2009)</dc:source>
<dc:date>2009-05-31</dc:date>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:publicationDate>2009-05-31</prism:publicationDate>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Brief Communication</prism:section>
<prism:startingPage>500</prism:startingPage>
<prism:endingPage>502</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth.1338">
<title>Quantitative analysis of gene expression in a single cell by qPCR</title>
<link>http://dx.doi.org/10.1038/nmeth.1338</link>
<description>There have been many attempts to measure gene expression in single cells but counting several different mRNAs in the same cell has been a challenge. A reusable single-cell cDNA library immobilized on beads allows quantitative measurement of multiple mRNAs in a single cell with a large dynamic range and small experimental error.</description>
<content:encoded><![CDATA[

<p>
<b>Quantitative analysis of gene expression in a single cell by qPCR</b>
</p>
<p>Nature Methods 6, 503 (2009). <a href="http://dx.doi.org/10.1038/nmeth.1338">doi:10.1038/nmeth.1338</a>
</p>
<p>Authors: Kiyomi Taniguchi, Tomoharu Kajiyama &amp; Hideki Kambara</p>
<p>We developed a quantitative PCR method featuring a reusable single-cell cDNA library immobilized on beads for measuring the expression of multiple genes in a single cell. We used this method to analyze multiple cDNA targets (from several copies to several hundred thousand copies) with an experimental error of 15.9% or less. This method is sufficiently accurate to investigate the heterogeneity of single cells.</p>
]]></content:encoded>
<dc:title>Quantitative analysis of gene expression in a single cell by qPCR</dc:title>
<dc:creator>Kiyomi Taniguchi</dc:creator>
<dc:creator>Tomoharu Kajiyama</dc:creator>
<dc:creator>Hideki Kambara</dc:creator>
<dc:identifier>doi:10.1038/nmeth.1338</dc:identifier>
<dc:source>Nature Methods 6, 503 (2009)</dc:source>
<dc:date>2009-06-14</dc:date>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:publicationDate>2009-06-14</prism:publicationDate>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Brief Communication</prism:section>
<prism:startingPage>503</prism:startingPage>
<prism:endingPage>506</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth.1343">
<title>Filter-based hybridization capture of subgenomes enables resequencing and copy-number detection</title>
<link>http://dx.doi.org/10.1038/nmeth.1343</link>
<description>Concatenated PCR products serve as subgenomic traps in this targeted genome capture technique; subsequent high-throughput sequencing allows the detection of nucleotide and structural variations in the captured genomic regions.</description>
<content:encoded><![CDATA[

<p>
<b>Filter-based hybridization capture of subgenomes enables resequencing and copy-number detection</b>
</p>
<p>Nature Methods 6, 507 (2009). <a href="http://dx.doi.org/10.1038/nmeth.1343">doi:10.1038/nmeth.1343</a>
</p>
<p>Authors: Daniel S Herman, G Kees Hovingh, Oleg Iartchouk, Heidi L Rehm, Raju Kucherlapati, J G Seidman &amp; Christine E Seidman</p>
<p>To exploit contemporary sequencing technologies for targeted genetic analyses, we developed a hybridization enrichment strategy for DNA capture that uses PCR products as subgenomic traps. We applied this strategy to 115 kilobases of the human genome encompassing 47 genes implicated in cardiovascular disease. Massively parallel sequencing of captured subgenomic libraries interrogated 99.8% of targeted nucleotides &#8805;20 times (&#8764;40,000-fold enrichment), enabling sensitive and specific detection of sequence variation and copy-number variation.</p>
]]></content:encoded>
<dc:title>Filter-based hybridization capture of subgenomes enables resequencing and copy-number detection</dc:title>
<dc:creator>Daniel S Herman</dc:creator>
<dc:creator>G Kees Hovingh</dc:creator>
<dc:creator>Oleg Iartchouk</dc:creator>
<dc:creator>Heidi L Rehm</dc:creator>
<dc:creator>Raju Kucherlapati</dc:creator>
<dc:creator>J G Seidman</dc:creator>
<dc:creator>Christine E Seidman</dc:creator>
<dc:identifier>doi:10.1038/nmeth.1343</dc:identifier>
<dc:source>Nature Methods 6, 507 (2009)</dc:source>
<dc:date>2009-06-21</dc:date>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:publicationDate>2009-06-21</prism:publicationDate>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Brief Communication</prism:section>
<prism:startingPage>507</prism:startingPage>
<prism:endingPage>510</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth.1339">
<title>In vivo fluorescence imaging with high-resolution microlenses</title>
<link>http://dx.doi.org/10.1038/nmeth.1339</link>
<description>A combination of gradient refractive index lenses with plano-convex lenses produces high-resolution microlenses with image quality similar to a conventional high quality microscope objective. The microlenses are capable of imaging dendritic spines on hippocampal neurons in live mice.</description>
<content:encoded><![CDATA[

<p>
<b>In vivo fluorescence imaging with high-resolution microlenses</b>
</p>
<p>Nature Methods 6, 511 (2009). <a href="http://dx.doi.org/10.1038/nmeth.1339">doi:10.1038/nmeth.1339</a>
</p>
<p>Authors: Robert P J Barretto, Bernhard Messerschmidt &amp; Mark J Schnitzer</p>
<p>Micro-optics are increasingly used for minimally invasive in vivo imaging, in miniaturized microscopes and in lab-on-a-chip devices. Owing to optical aberrations and lower numerical apertures, a main class of microlens, gradient refractive index lenses, has not achieved resolution comparable to conventional microscopy. Here we describe high-resolution microlenses, and illustrate two-photon imaging of dendritic spines on hippocampal neurons and dual-color nonlinear optical imaging of neuromuscular junctions in live mice.</p>
]]></content:encoded>
<dc:title>In vivo fluorescence imaging with high-resolution microlenses</dc:title>
<dc:creator>Robert P J Barretto</dc:creator>
<dc:creator>Bernhard Messerschmidt</dc:creator>
<dc:creator>Mark J Schnitzer</dc:creator>
<dc:identifier>doi:10.1038/nmeth.1339</dc:identifier>
<dc:source>Nature Methods 6, 511 (2009)</dc:source>
<dc:date>2009-06-14</dc:date>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:publicationDate>2009-06-14</prism:publicationDate>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Brief Communication</prism:section>
<prism:startingPage>511</prism:startingPage>
<prism:endingPage>512</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth.1335">
<title>'Injecting' yeast</title>
<link>http://dx.doi.org/10.1038/nmeth.1335</link>
<description>Using a topographically patterned substrate for immobilization of single yeast cells and a piezo-impact micromanipulator to transiently disrupt the cell wall, molecules can be physically introduced into yeast.</description>
<content:encoded><![CDATA[

<p>
<b>'Injecting' yeast</b>
</p>
<p>Nature Methods 6, 513 (2009). <a href="http://dx.doi.org/10.1038/nmeth.1335">doi:10.1038/nmeth.1335</a>
</p>
<p>Authors: Daniel Riveline &amp; Paul Nurse</p>
<p>Yeast is a powerful genetic model system, but its rigid cell wall has prohibited microinjection. Using microfabricated channels to constrain the fission yeast Schizosaccharomyces pombe, we sheared local regions of individual cells with a piezoelectric unit. The cells remained viable, we detected actin patches in the cell after introduction of fluorescent phalloidin into the medium, and the cytokinetic ring was disrupted after injection of the myosin II inhibitor blebbistatin.</p>
]]></content:encoded>
<dc:title>'Injecting' yeast</dc:title>
<dc:creator>Daniel Riveline</dc:creator>
<dc:creator>Paul Nurse</dc:creator>
<dc:identifier>doi:10.1038/nmeth.1335</dc:identifier>
<dc:source>Nature Methods 6, 513 (2009)</dc:source>
<dc:date>2009-06-07</dc:date>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:publicationDate>2009-06-07</prism:publicationDate>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Brief Communication</prism:section>
<prism:startingPage>513</prism:startingPage>
<prism:endingPage>514</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth.1336">
<title>Reaching the protein folding speed limit with large, sub-microsecond pressure jumps</title>
<link>http://dx.doi.org/10.1038/nmeth.1336</link>
<description>Although fast temperature jump methods to study protein folding dynamics have long been applied, pressure has been a neglected thermodynamic parameter. A method to generate rapid and large drops in pressure is complementary to fast temperature jump methods and could be useful for direct comparisons to molecular dynamics simulations.</description>
<content:encoded><![CDATA[

<p>
<b>Reaching the protein folding speed limit with large, sub-microsecond pressure jumps</b>
</p>
<p>Nature Methods 6, 515 (2009). <a href="http://dx.doi.org/10.1038/nmeth.1336">doi:10.1038/nmeth.1336</a>
</p>
<p>Authors: Charles Dumont, Tryggvi Emilsson &amp; Martin Gruebele</p>
]]></content:encoded>
<dc:title>Reaching the protein folding speed limit with large, sub-microsecond pressure jumps</dc:title>
<dc:creator>Charles Dumont</dc:creator>
<dc:creator>Tryggvi Emilsson</dc:creator>
<dc:creator>Martin Gruebele</dc:creator>
<dc:identifier>doi:10.1038/nmeth.1336</dc:identifier>
<dc:source>Nature Methods 6, 515 (2009)</dc:source>
<dc:date>2009-05-31</dc:date>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:publicationDate>2009-05-31</prism:publicationDate>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>515</prism:startingPage>
<prism:endingPage>519</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth.1345">
<title>Parallel detection of antigen-specific T-cell responses by multidimensional encoding of MHC multimers</title>
<link>http://dx.doi.org/10.1038/nmeth.1345</link>
<description>Using combinations of fluorescently labeled peptide&#8211;major histocompatability complex (pMHC) tetramers, T-cell populations with multiple antigen specificities can be monitored in parallel from small samples of human blood. Also in this issue, Newell et al. present a very similar combinatorial encoding method for this purpose.</description>
<content:encoded><![CDATA[

<p>
<b>Parallel detection of antigen-specific T-cell responses by multidimensional encoding of MHC multimers</b>
</p>
<p>Nature Methods 6, 520 (2009). <a href="http://dx.doi.org/10.1038/nmeth.1345">doi:10.1038/nmeth.1345</a>
</p>
<p>Authors: Sine Reker Hadrup, Arnold H Bakker, Chengyi J Shu, Rikke S Andersen, Jerre van Veluw, Pleun Hombrink, Emilie Castermans, Per thor Straten, Christian Blank, John B Haanen, Mirjam H Heemskerk &amp; Ton N Schumacher</p>
]]></content:encoded>
<dc:title>Parallel detection of antigen-specific T-cell responses by multidimensional encoding of MHC multimers</dc:title>
<dc:creator>Sine Reker Hadrup</dc:creator>
<dc:creator>Arnold H Bakker</dc:creator>
<dc:creator>Chengyi J Shu</dc:creator>
<dc:creator>Rikke S Andersen</dc:creator>
<dc:creator>Jerre van Veluw</dc:creator>
<dc:creator>Pleun Hombrink</dc:creator>
<dc:creator>Emilie Castermans</dc:creator>
<dc:creator>Per thor Straten</dc:creator>
<dc:creator>Christian Blank</dc:creator>
<dc:creator>John B Haanen</dc:creator>
<dc:creator>Mirjam H Heemskerk</dc:creator>
<dc:creator>Ton N Schumacher</dc:creator>
<dc:identifier>doi:10.1038/nmeth.1345</dc:identifier>
<dc:source>Nature Methods 6, 520 (2009)</dc:source>
<dc:date>2009-06-21</dc:date>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:publicationDate>2009-06-21</prism:publicationDate>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>520</prism:startingPage>
<prism:endingPage>526</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth.1340">
<title>Doxycycline-dependent photoactivated gene expression in eukaryotic systems</title>
<link>http://dx.doi.org/10.1038/nmeth.1340</link>
<description>Activation of caged doxycycline or cyanodoxycycline by biologically innocuous doses of UV light allows for precise temporal and spatial control of transgene expression in hippocampal slices, mouse embryos and Xenopus laevis tadpoles.</description>
<content:encoded><![CDATA[

<p>
<b>Doxycycline-dependent photoactivated gene expression in eukaryotic systems</b>
</p>
<p>Nature Methods 6, 527 (2009). <a href="http://dx.doi.org/10.1038/nmeth.1340">doi:10.1038/nmeth.1340</a>
</p>
<p>Authors: Sidney B Cambridge, Daniel Geissler, Federico Calegari, Konstantinos Anastassiadis, Mazahir T Hasan, A Francis Stewart, Wieland B Huttner, Volker Hagen &amp; Tobias Bonhoeffer</p>
]]></content:encoded>
<dc:title>Doxycycline-dependent photoactivated gene expression in eukaryotic systems</dc:title>
<dc:creator>Sidney B Cambridge</dc:creator>
<dc:creator>Daniel Geissler</dc:creator>
<dc:creator>Federico Calegari</dc:creator>
<dc:creator>Konstantinos Anastassiadis</dc:creator>
<dc:creator>Mazahir T Hasan</dc:creator>
<dc:creator>A Francis Stewart</dc:creator>
<dc:creator>Wieland B Huttner</dc:creator>
<dc:creator>Volker Hagen</dc:creator>
<dc:creator>Tobias Bonhoeffer</dc:creator>
<dc:identifier>doi:10.1038/nmeth.1340</dc:identifier>
<dc:source>Nature Methods 6, 527 (2009)</dc:source>
<dc:date>2009-06-07</dc:date>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:publicationDate>2009-06-07</prism:publicationDate>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>527</prism:startingPage>
<prism:endingPage>531</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth.1341">
<title>Mapping the structure and conformational movements of proteins with transition metal ion FRET</title>
<link>http://dx.doi.org/10.1038/nmeth.1341</link>
<description>Fluorescence resonance energy transfer (FRET) between a small-molecule fluorophore donor and a transition metal ion acceptor, a method called 'transition metal ion FRET,' works over shorter distances than the classical FRET approach and can thus be used to monitor very small conformational changes in proteins.</description>
<content:encoded><![CDATA[

<p>
<b>Mapping the structure and conformational movements of proteins with transition metal ion FRET</b>
</p>
<p>Nature Methods 6, 532 (2009). <a href="http://dx.doi.org/10.1038/nmeth.1341">doi:10.1038/nmeth.1341</a>
</p>
<p>Authors: Justin W Taraska, Michael C Puljung, Nelson B Olivier, Galen E Flynn &amp; William N Zagotta</p>
]]></content:encoded>
<dc:title>Mapping the structure and conformational movements of proteins with transition metal ion FRET</dc:title>
<dc:creator>Justin W Taraska</dc:creator>
<dc:creator>Michael C Puljung</dc:creator>
<dc:creator>Nelson B Olivier</dc:creator>
<dc:creator>Galen E Flynn</dc:creator>
<dc:creator>William N Zagotta</dc:creator>
<dc:identifier>doi:10.1038/nmeth.1341</dc:identifier>
<dc:source>Nature Methods 6, 532 (2009)</dc:source>
<dc:date>2009-06-14</dc:date>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:publicationDate>2009-06-14</prism:publicationDate>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>532</prism:startingPage>
<prism:endingPage>537</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth0709-539">
<title>Genomics: catch me if you can</title>
<link>http://dx.doi.org/10.1038/nmeth0709-539</link>
<description>Next-generation sequencing has made decoding entire genomes cheaper and faster. But what about those researchers who only want to sequence a small section of a genome or focus on a couple thousand specific exons? A wave of new technologies has recently emerged that should help these scientists target their sequencing efforts to sequences of interest.</description>
<content:encoded><![CDATA[

<p>
<b>Genomics: catch me if you can</b>
</p>
<p>Nature Methods 6, 539 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-539">doi:10.1038/nmeth0709-539</a>
</p>
<p>Author: Nathan Blow</p>
<p>Next-generation sequencing has made decoding entire genomes cheaper and faster. But what about those researchers who only want to sequence a small section of a genome or focus on a couple thousand specific exons? A wave of new technologies has recently emerged that should help these scientists target their sequencing efforts to sequences of interest.</p>
]]></content:encoded>
<dc:title>Genomics: catch me if you can</dc:title>
<dc:creator>Nathan Blow</dc:creator>
<dc:identifier>doi:10.1038/nmeth0709-539</dc:identifier>
<dc:source>Nature Methods 6, 539 (2009)</dc:source>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Technology Feature</prism:section>
<prism:startingPage>539</prism:startingPage>
<prism:endingPage>544</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth0709-546a">
<title>Corrigendum: A HUPO test sample study reveals common problems in mass spectrometry&#8211;based proteomics</title>
<link>http://dx.doi.org/10.1038/nmeth0709-546a</link>
<description/>
<content:encoded><![CDATA[

<p>
<b>Corrigendum: A HUPO test sample study reveals common problems in mass spectrometry&#8211;based proteomics</b>
</p>
<p>Nature Methods 6, 546 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-546a">doi:10.1038/nmeth0709-546a</a>
</p>
]]></content:encoded>
<dc:title>Corrigendum: A HUPO test sample study reveals common problems in mass spectrometry&#8211;based proteomics</dc:title>
<dc:identifier>doi:10.1038/nmeth0709-546a</dc:identifier>
<dc:source>Nature Methods 6, 546 (2009)</dc:source>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Corrigendum</prism:section>
<prism:startingPage>546</prism:startingPage>
<prism:endingPage>546</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nmeth0709-546b">
<title>Erratum: Transposon-mediated genome manipulation in vertebrates</title>
<link>http://dx.doi.org/10.1038/nmeth0709-546b</link>
<description/>
<content:encoded><![CDATA[

<p>
<b>Erratum: Transposon-mediated genome manipulation in vertebrates</b>
</p>
<p>Nature Methods 6, 546 (2009). <a href="http://dx.doi.org/10.1038/nmeth0709-546b">doi:10.1038/nmeth0709-546b</a>
</p>
]]></content:encoded>
<dc:title>Erratum: Transposon-mediated genome manipulation in vertebrates</dc:title>
<dc:identifier>doi:10.1038/nmeth0709-546b</dc:identifier>
<dc:source>Nature Methods 6, 546 (2009)</dc:source>
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<title>Analysis of 5&#8242; transcript heterogeneity by high-throughput sequencing of cDNA</title>
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<p>
<b>Analysis of 5&#8242; transcript heterogeneity by high-throughput sequencing of cDNA</b>
</p>
<p>Nature Methods 6, (2009). <a href="http://dx.doi.org/10.1038/nmeth.f.257">doi:10.1038/nmeth.f.257</a>
</p>
<p>Authors: Pietro D Spanu &amp; Ken Doyle</p>
]]></content:encoded>
<dc:title>Analysis of 5&#8242; transcript heterogeneity by high-throughput sequencing of cDNA</dc:title>
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<dc:identifier>doi:10.1038/nmeth.f.257</dc:identifier>
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<prism:section>Application Note</prism:section>
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<item rdf:about="http://dx.doi.org/10.1038/nmeth.f.258">
<title>CYP2C9 and VKORC1 genotyping reagents from Idaho Technology: rapid turn-around, accurate results</title>
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<p>
<b>CYP2C9 and VKORC1 genotyping reagents from Idaho Technology: rapid turn-around, accurate results</b>
</p>
<p>Nature Methods 6, (2009). <a href="http://dx.doi.org/10.1038/nmeth.f.258">doi:10.1038/nmeth.f.258</a>
</p>
<p>Authors: Jason McKinney, Ranae Lems &amp; Cameron Gundry</p>
]]></content:encoded>
<dc:title>CYP2C9 and VKORC1 genotyping reagents from Idaho Technology: rapid turn-around, accurate results</dc:title>
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<dc:creator>Ranae Lems</dc:creator>
<dc:creator>Cameron Gundry</dc:creator>
<dc:identifier>doi:10.1038/nmeth.f.258</dc:identifier>
<dc:source>Nature Methods 6, (2009)</dc:source>
<prism:publicationName>Nature Methods</prism:publicationName>
<prism:volume>6</prism:volume>
<prism:number>7</prism:number>
<prism:section>Application Note</prism:section>
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<item rdf:about="http://dx.doi.org/10.1038/nmeth.f.259">
<title>Fluidigm Dynamic Arrays provide a platform for single-cell gene expression analysis</title>
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<p>
<b>Fluidigm Dynamic Arrays provide a platform for single-cell gene expression analysis</b>
</p>
<p>Nature Methods 6, (2009). <a href="http://dx.doi.org/10.1038/nmeth.f.259">doi:10.1038/nmeth.f.259</a>
</p>
<p>Authors: Martin Pieprzyk &amp; Howard High</p>
]]></content:encoded>
<dc:title>Fluidigm Dynamic Arrays provide a platform for single-cell gene expression analysis</dc:title>
<dc:creator>Martin Pieprzyk</dc:creator>
<dc:creator>Howard High</dc:creator>
<dc:identifier>doi:10.1038/nmeth.f.259</dc:identifier>
<dc:source>Nature Methods 6, (2009)</dc:source>
<prism:publicationName>Nature Methods</prism:publicationName>
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<prism:number>7</prism:number>
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