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		<dc:publisher>The Royal Society of Chemistry</dc:publisher>
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	<item rdf:about="http://xlink.rsc.org/?DOI=b914428e&amp;RSS=1"><title>Investigation of microsphere-mediated cellular delivery by chemical, microscopic and gene expression analysis</title>
		<link>http://xlink.rsc.org/?DOI=b914428e&amp;RSS=1</link>
		<description>The detailed uptake mechanism of microspheres into a range of cell lines was studied. Gene expression profiles of "beadfected" and untreated cells were used to establish the effect of microsphere uptake at the transcriptional level.</description><content:encoded>&lt;p&gt;&lt;img align="center" src="http://www.rsc.org/ejga/MB/2010/b914428e-ga.gif"/&gt;
	&lt;/p&gt;Lois M. Alexander, Salvatore Pernagallo, Alessandra Livigni, Rosario M. Sanchez-Martin, Joshua M. Brickman, Mark Bradley &lt;br/&gt;
(Paper from Mol. BioSyst.)&lt;br/&gt;
Lois M. Alexander, Mol. BioSyst., 2010, DOI: 10.1039/b914428e&lt;br/&gt;
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&lt;br/&gt;The content of this RSS Feed (c) The Royal Society of Chemistry</content:encoded>
		<dc:title>Investigation of microsphere-mediated cellular delivery by chemical, microscopic and gene expression analysis</dc:title>
		<dc:creator>Lois M. Alexander</dc:creator>
		<dc:creator>Salvatore Pernagallo </dc:creator><dc:creator>Alessandra Livigni </dc:creator><dc:creator>Rosario M. Sanchez-Martin </dc:creator><dc:creator>Joshua M. Brickman </dc:creator><dc:creator>Mark Bradley </dc:creator><dc:identifier>10.1039/b914428e</dc:identifier>
		<dc:source>Mol. BioSyst., 2010, DOI: 10.1039/b914428e</dc:source>
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		<dc:date>2009-11-26</dc:date>
		<dc:publisher>The Royal Society of Chemistry</dc:publisher>
		<dc:rights>Copyright (c) 2010 The Royal Society of Chemistry</dc:rights>
		<dc:identifier>DOI 10.1039/b914428e</dc:identifier>
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		<link>http://xlink.rsc.org/?DOI=b903019k&amp;RSS=1</link>
		<description>Side-chain interactions in protein structure networks show random behavior and deviations from this random model have significant biological implications.</description><content:encoded>&lt;p&gt;&lt;img align="center" src="http://www.rsc.org/ejga/MB/2010/b903019k-ga.gif"/&gt;
	&lt;/p&gt;K. V. Brinda, Saraswathi Vishveshwara, Smitha Vishveshwara &lt;br/&gt;
(Paper from Mol. BioSyst.)&lt;br/&gt;
K. V. Brinda, Mol. BioSyst., 2010, DOI: 10.1039/b903019k&lt;br/&gt;
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&lt;br/&gt;The content of this RSS Feed (c) The Royal Society of Chemistry</content:encoded>
		<dc:title>Random network behaviour of protein structures</dc:title>
		<dc:creator>K. V. Brinda</dc:creator>
		<dc:creator>Saraswathi Vishveshwara </dc:creator><dc:creator>Smitha Vishveshwara </dc:creator><dc:identifier>10.1039/b903019k</dc:identifier>
		<dc:source>Mol. BioSyst., 2010, DOI: 10.1039/b903019k</dc:source>
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		<dc:date>2009-11-16</dc:date>
		<dc:publisher>The Royal Society of Chemistry</dc:publisher>
		<dc:rights>Copyright (c) 2010 The Royal Society of Chemistry</dc:rights>
		<dc:identifier>DOI 10.1039/b903019k</dc:identifier>
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		<description>PUPylation is a prokaryotic post-translation modification that, similar to ubiquitin, has been previously implicated in proteasomal degradation. By performing a global proteomic pull-down from Mycobacterium smegmatis 155 protein targets for PUPylation were identifed.</description><content:encoded>&lt;p&gt;&lt;img align="center" src="http://www.rsc.org/ejga/MB/2010/b916104j-ga.gif"/&gt;
	&lt;/p&gt;Jeramie Watrous, Kristin Burns, Wei-Ting Liu, Anand Patel, Vivian Hook, Vineet Bafna, Clifton E. Barry 3rd, Steve Bark, Pieter C. Dorrestein &lt;br/&gt;
(Paper from Mol. BioSyst.)&lt;br/&gt;
Jeramie Watrous, Mol. BioSyst., 2010, DOI: 10.1039/b916104j&lt;br/&gt;
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&lt;br/&gt;The content of this RSS Feed (c) The Royal Society of Chemistry</content:encoded>
		<dc:title>Expansion of the mycobacterial "PUPylome"</dc:title>
		<dc:creator>Jeramie Watrous</dc:creator>
		<dc:creator>Kristin Burns </dc:creator><dc:creator>Wei-Ting Liu </dc:creator><dc:creator>Anand Patel </dc:creator><dc:creator>Vivian Hook </dc:creator><dc:creator>Vineet Bafna </dc:creator><dc:creator>Clifton E. Barry 3rd </dc:creator><dc:creator>Steve Bark </dc:creator><dc:creator>Pieter C. Dorrestein </dc:creator><dc:identifier>10.1039/b916104j</dc:identifier>
		<dc:source>Mol. BioSyst., 2010, DOI: 10.1039/b916104j</dc:source>
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		<dc:date>2009-11-16</dc:date>
		<dc:publisher>The Royal Society of Chemistry</dc:publisher>
		<dc:rights>Copyright (c) 2010 The Royal Society of Chemistry</dc:rights>
		<dc:identifier>DOI 10.1039/b916104j</dc:identifier>
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	<item rdf:about="http://xlink.rsc.org/?DOI=b910552m&amp;RSS=1"><title>Therapeutic applications of hyaluronan</title>
		<link>http://xlink.rsc.org/?DOI=b910552m&amp;RSS=1</link>
		<description>Hyaluronan is an extracellular component whose expression is perturbed in disease. Manipulation of hyaluronan by nanotechnology may be of therapeutic benefit.</description><content:encoded>&lt;p&gt;&lt;img align="center" src="http://www.rsc.org/ejga/MB/2010/b910552m-ga.gif"/&gt;
	&lt;/p&gt;John Gaffney, Sabine Matou-Nasri, Marta Grau-Olivares, Mark Slevin &lt;br/&gt;
(Review from Mol. BioSyst.)&lt;br/&gt;
John Gaffney, Mol. BioSyst., 2010, DOI: 10.1039/b910552m&lt;br/&gt;
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&lt;br/&gt;&lt;a href='http://obofoundry.org/' target="'_BLANK'"&gt;Ontology Terms:&lt;/a&gt;
	cytoskeleton; gold nanoparticle; nanoparticle; activation; sperm; fibroblast; epithelial cell; endothelial cell; glial cell; astrocyte; microglial cell; chondrocyte; beta-glucuronidase activity; macrophage; neuron; endothelial cell proliferation; RNA-directed DNA polymerase activity; hyalurononglucosaminidase activity; epidermal growth factor receptor binding; MAP kinase 1 activity; cell motility; dicarba-closo-dodecaborane(12); amino-acid residue; hydrazide; disaccharide; tyramines; polysaccharide; chondroitin sulfate; hydroxy group; indicator; Schiff base; sugar; glycoprotein; gene expression; silver nanoparticle; glycosylation; optical micrograph; inorganic nanoparticle; angiogenesis; stress fiber; peroxidase activity; death receptor activity; receptor binding; extracellular region; chromosome; mitochondrion; lysosome; plasma membrane; endocytosis; apoptosis; inflammatory response; immune response; leukocyte adhesion; signal transduction; metabolic process; cell death; cell proliferation; biosynthetic process; post-embryonic development; cell surface; death; kinase activity; phosphorylation; hyaluronate lyase activity; extracellular matrix; immunoglobulin complex, circulating; neuron projection; cell soma; hyaluronan synthase activity; water binding; cell division; exon; pseudogene; siRNA; gene; tandem_repeat; post-translational protein modification; glucuronic acids; drug; amino acid; messenger RNA; glycosaminoglycan; proteoglycan; glucose; hyaluronic acid; protein; macromolecule; carboxy group; poly(ethylene glycol); alternate_sequence_site; tetrasaccharide; confocal microscopy
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		<dc:title>Therapeutic applications of hyaluronan</dc:title>
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		<dc:creator>Sabine Matou-Nasri </dc:creator><dc:creator>Marta Grau-Olivares </dc:creator><dc:creator>Mark Slevin </dc:creator><dc:identifier>10.1039/b910552m</dc:identifier>
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		<dc:date>2009-11-12</dc:date>
		<dc:publisher>The Royal Society of Chemistry</dc:publisher>
		<dc:rights>Copyright (c) 2010 The Royal Society of Chemistry</dc:rights>
		<dc:identifier>DOI 10.1039/b910552m</dc:identifier>
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	<item rdf:about="http://xlink.rsc.org/?DOI=b916175a&amp;RSS=1"><title>Combining nanotechnology with current biomedical knowledge for the vascular imaging and treatment of atherosclerosis</title>
		<link>http://xlink.rsc.org/?DOI=b916175a&amp;RSS=1</link>
		<description>This review will describe the importance of angiogenesis in mediation of atherosclerotic plaque growth and superparamagnetic/perfluorocarbon-derived nanoparticles for imaging of the vasculature in this disease.</description><content:encoded>&lt;p&gt;&lt;img align="center" src="http://www.rsc.org/ejga/MB/2010/b916175a-ga.gif"/&gt;
	&lt;/p&gt;M. Slevin, L. Badimon, M. Grau-Olivares, M. Ramis, J. Sendra, M. Morrison, J. Krupinski &lt;br/&gt;
(Review from Mol. BioSyst.)&lt;br/&gt;
M. Slevin, Mol. BioSyst., 2010, DOI: 10.1039/b916175a&lt;br/&gt;
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&lt;br/&gt;The content of this RSS Feed (c) The Royal Society of Chemistry</content:encoded>
		<dc:title>Combining nanotechnology with current biomedical knowledge for the vascular imaging and treatment of atherosclerosis</dc:title>
		<dc:creator>M. Slevin</dc:creator>
		<dc:creator>L. Badimon </dc:creator><dc:creator>M. Grau-Olivares </dc:creator><dc:creator>M. Ramis </dc:creator><dc:creator>J. Sendra </dc:creator><dc:creator>M. Morrison </dc:creator><dc:creator>J. Krupinski </dc:creator><dc:identifier>10.1039/b916175a</dc:identifier>
		<dc:source>Mol. BioSyst., 2010, DOI: 10.1039/b916175a</dc:source>
		<dc:format>html/pdf</dc:format>
		<dc:date>2009-11-12</dc:date>
		<dc:publisher>The Royal Society of Chemistry</dc:publisher>
		<dc:rights>Copyright (c) 2010 The Royal Society of Chemistry</dc:rights>
		<dc:identifier>DOI 10.1039/b916175a</dc:identifier>
	</item>
	<item rdf:about="http://xlink.rsc.org/?DOI=b921381n&amp;RSS=1"><title>Computational and Systems Biology</title>
		<link>http://xlink.rsc.org/?DOI=b921381n&amp;RSS=1</link>
		<description>M. Madan Babu and Hirotada Mori introduce this themed issue of Molecular BioSystems focusing on Computational and systems biology</description><content:encoded>&lt;p&gt;&lt;img align="center" src="http://www.rsc.org/ejga/MB/2009/b921381n-ga.gif"/&gt;
	&lt;/p&gt;
(Editorial from Mol. BioSyst.)&lt;br/&gt;
Mol. BioSyst., 2009, 5, 1391 &lt;br/&gt;DOI: 10.1039/b921381n
&lt;br/&gt;The content of this RSS Feed (c) The Royal Society of Chemistry</content:encoded>
		<dc:title>Computational and Systems Biology</dc:title>
		<dc:creator>RSC</dc:creator>
		<dc:identifier>10.1039/b921381n</dc:identifier>
		<dc:source>Mol. BioSyst., 2009, 5, 1391 DOI: 10.1039/b921381n</dc:source>
		<dc:format>html/pdf</dc:format>
		<dc:date>2009-11-06</dc:date>
		<dc:publisher>The Royal Society of Chemistry</dc:publisher>
		<dc:rights>Copyright (c) 2010 The Royal Society of Chemistry</dc:rights>
		<dc:identifier>DOI 10.1039/b921381n</dc:identifier>
		<prism:volume>5</prism:volume><prism:number>12</prism:number><prism:startingPage>1391</prism:startingPage></item>
	<item rdf:about="http://xlink.rsc.org/?DOI=b916030m&amp;RSS=1"><title>Protein intrinsic disorder and oligomericity in cell signaling</title>
		<link>http://xlink.rsc.org/?DOI=b916030m&amp;RSS=1</link>
		<description>Receptor oligomerization induced upon ligand binding outside the cell is suggested to be translated across the membrane into protein oligomerization inside the cell, providing a general platform for receptor-mediated signaling.</description><content:encoded>&lt;p&gt;&lt;img align="center" src="http://www.rsc.org/ejga/MB/2010/b916030m-ga.gif"/&gt;
	&lt;/p&gt;Alexander B. Sigalov &lt;br/&gt;
(Review from Mol. BioSyst.)&lt;br/&gt;
Alexander B. Sigalov, Mol. BioSyst., 2010, DOI: 10.1039/b916030m&lt;br/&gt;
To cite this article before page numbers are assigned, use the DOI form of citation above.

&lt;br/&gt;The content of this RSS Feed (c) The Royal Society of Chemistry</content:encoded>
		<dc:title>Protein intrinsic disorder and oligomericity in cell signaling</dc:title>
		<dc:creator>Alexander B. Sigalov</dc:creator>
		<dc:identifier>10.1039/b916030m</dc:identifier>
		<dc:source>Mol. BioSyst., 2010, DOI: 10.1039/b916030m</dc:source>
		<dc:format>html/pdf</dc:format>
		<dc:date>2009-11-03</dc:date>
		<dc:publisher>The Royal Society of Chemistry</dc:publisher>
		<dc:rights>Copyright (c) 2010 The Royal Society of Chemistry</dc:rights>
		<dc:identifier>DOI 10.1039/b916030m</dc:identifier>
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