Advance online publication
The latest research papers, published online ahead of print. These online versions are definitive and may be cited using the digital object identifier (DOI).
About advance online publicationResearch
Brief Communications
High-resolution analysis of DNA regulatory elements by synthetic saturation mutagenesis
Rupali P Patwardhan, Choli Lee, Oren Litvin, David L Young, Dana Pe'er & Jay Shendure
Published online: 15 November 2009 | doi:10.1038/nbt.1589
Patwardhan et al. describe synthetic saturation mutagenesis—a high-throughput technology for analyzing at single-nucleotide resolution the DNA regulatory sequences that control gene expression. Characterizing these sequences in a massively parallel manner will be useful for deciphering the regulatory logic of the cell and for synthetic biology.
First Paragraph - | Full Text - High-resolution analysis of DNA regulatory elements by synthetic saturation mutagenesis | PDF (380 KB) - High-resolution analysis of DNA regulatory elements by synthetic saturation mutagenesis | Supplementary information
Letters
Direct photosynthetic recycling of carbon dioxide to isobutyraldehyde
Shota Atsumi, Wendy Higashide & James C Liao
Published online: 15 November 2009 | doi:10.1038/nbt.1586
The feasibility of recycling CO2 to biofuels in photosynthetic organisms will depend on advances in productivity and product-purification efficiency. Atsumi et al. improve the direct conversion of CO2 by engineering Synechococcus elongatus to produce isobutyraldehyde, which can be easily recovered from the production medium.
First Paragraph - | Full Text - Direct photosynthetic recycling of carbon dioxide to isobutyraldehyde | PDF (519 KB) - Direct photosynthetic recycling of carbon dioxide to isobutyraldehyde | Supplementary information
A recombinant polypeptide extends the in vivo half-life of peptides and proteins in a tunable manner
Volker Schellenberger, Chia-wei Wang, Nathan C Geething, Benjamin J Spink, Andrew Campbell, Wayne To, Michael D Scholle, Yong Yin, Yi Yao, Oren Bogin, Jeffrey L Cleland, Joshua Silverman & Willem P C Stemmer
Published online: 15 November 2009 | doi:10.1038/nbt.1588
Rapid clearance frequently complicates therapeutic use of proteins and peptides. Schellenberger et al. demonstrate that genetic fusion of an unstructured polypeptide offers a general strategy to extend peptide or protein half-life in vivo in a tunable manner.
First Paragraph - | Full Text - A recombinant polypeptide extends the in vivo half-life of peptides and proteins in a tunable manner | PDF (618 KB) - A recombinant polypeptide extends the in vivo half-life of peptides and proteins in a tunable manner | Supplementary information
Until print versions of AOP papers are published, they should be cited in the style "Author(s) Nature Biotechnology advance online publication, day month year (doi:10.1038/nbtXXXXX)". Once the print version (identical to the AOP) is published, it should be cited as follows: "Author(s) Nature Biotechnology volume, page (year); advance online publication, (doi:10.1038/nbtXXXXX)".
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