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	<title>TOP MEDICAL JOURNALS &#187; biochemical UPDATE</title>
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		<title>Bioinformatic analysis of xenobiotic reactive metabolite target proteins and their interacting partners</title>
		<link>http://topmedicaljournals.com/index.php/biochemical-update/bioinformatic-analysis-of-xenobiotic-reactive-metabolite-target-proteins-and-their-interacting-partners/</link>
		<comments>http://topmedicaljournals.com/index.php/biochemical-update/bioinformatic-analysis-of-xenobiotic-reactive-metabolite-target-proteins-and-their-interacting-partners/#comments</comments>
		<pubDate>Wed, 29 Jul 2009 19:18:42 +0000</pubDate>
		<dc:creator>admin</dc:creator>
				<category><![CDATA[biochemical UPDATE]]></category>

		<guid isPermaLink="false">http://topmedicaljournals.com/index.php/biochemical-update/bioinformatic-analysis-of-xenobiotic-reactive-metabolite-target-proteins-and-their-interacting-partners/</guid>
		<description><![CDATA[


 Background:
Protein covalent binding by reactive metabolites of drugs, chemicals and natural products can lead to acute cytotoxicity. Recent rapid progress in reactive metabolite target protein identification has shown that adduction is surprisingly selective and inspired the hope that analysis of target proteins might reveal protein factors that differentiate target- vs. non-target proteins and illuminate [...]]]></description>
		<wfw:commentRss>http://topmedicaljournals.com/index.php/biochemical-update/bioinformatic-analysis-of-xenobiotic-reactive-metabolite-target-proteins-and-their-interacting-partners/feed/</wfw:commentRss>
		<slash:comments>0</slash:comments>
		</item>
		<item>
		<title>DNA binding kinetics of two response regulators, PlnC and PlnD, from the bacteriocin regulon of Lactobacillus plantarum C11</title>
		<link>http://topmedicaljournals.com/index.php/biochemical-update/dna-binding-kinetics-of-two-response-regulators-plnc-and-plnd-from-the-bacteriocin-regulon-of-lactobacillus-plantarum-c11/</link>
		<comments>http://topmedicaljournals.com/index.php/biochemical-update/dna-binding-kinetics-of-two-response-regulators-plnc-and-plnd-from-the-bacteriocin-regulon-of-lactobacillus-plantarum-c11/#comments</comments>
		<pubDate>Wed, 29 Jul 2009 19:18:16 +0000</pubDate>
		<dc:creator>admin</dc:creator>
				<category><![CDATA[biochemical UPDATE]]></category>

		<guid isPermaLink="false">http://topmedicaljournals.com/index.php/biochemical-update/dna-binding-kinetics-of-two-response-regulators-plnc-and-plnd-from-the-bacteriocin-regulon-of-lactobacillus-plantarum-c11/</guid>
		<description><![CDATA[Background:
Bacteriocin production in the lactic acid bacterium Lactobacillus plantarum C11 is regulated through a quorum sensing based pathway involving two highly homologous response regulators (59% identity and 76% similarity), PlnC as a transcriptional activator and PlnD as a repressor. Previous in vitro studies have shown that both regulators bind, as homodimers, to the same DNA [...]]]></description>
		<wfw:commentRss>http://topmedicaljournals.com/index.php/biochemical-update/dna-binding-kinetics-of-two-response-regulators-plnc-and-plnd-from-the-bacteriocin-regulon-of-lactobacillus-plantarum-c11/feed/</wfw:commentRss>
		<slash:comments>0</slash:comments>
		</item>
		<item>
		<title>Analysis of DNA relaxation and cleavage activities of recombinant Mycobacterium tuberculosis DNA topoisomerase I from a new expression and purification protocol</title>
		<link>http://topmedicaljournals.com/index.php/biochemical-update/analysis-of-dna-relaxation-and-cleavage-activities-of-recombinant-mycobacterium-tuberculosis-dna-topoisomerase-i-from-a-new-expression-and-purification-protocol/</link>
		<comments>http://topmedicaljournals.com/index.php/biochemical-update/analysis-of-dna-relaxation-and-cleavage-activities-of-recombinant-mycobacterium-tuberculosis-dna-topoisomerase-i-from-a-new-expression-and-purification-protocol/#comments</comments>
		<pubDate>Wed, 29 Jul 2009 19:18:16 +0000</pubDate>
		<dc:creator>admin</dc:creator>
				<category><![CDATA[biochemical UPDATE]]></category>

		<guid isPermaLink="false">http://topmedicaljournals.com/index.php/biochemical-update/analysis-of-dna-relaxation-and-cleavage-activities-of-recombinant-mycobacterium-tuberculosis-dna-topoisomerase-i-from-a-new-expression-and-purification-protocol/</guid>
		<description><![CDATA[Background:
Mycobacterium tuberculosis DNA topoisomerase I is an attractive target for discovery of novel TB drugs that act by enhancing the accumulation of the topoisomerase-DNA cleavage product. It shares a common transesterification domain with other type IA DNA topoisomerases. There is, however, no homology between the C-terminal DNA binding domains of Escherichia coli and M. tuberculosis [...]]]></description>
		<wfw:commentRss>http://topmedicaljournals.com/index.php/biochemical-update/analysis-of-dna-relaxation-and-cleavage-activities-of-recombinant-mycobacterium-tuberculosis-dna-topoisomerase-i-from-a-new-expression-and-purification-protocol/feed/</wfw:commentRss>
		<slash:comments>0</slash:comments>
		</item>
		<item>
		<title>Insights into the role of Val45 and Gln182 of Escherichia coli MutY in DNA substrate binding and specificity</title>
		<link>http://topmedicaljournals.com/index.php/biochemical-update/insights-into-the-role-of-val45-and-gln182-of-escherichia-coli-muty-in-dna-substrate-binding-and-specificity/</link>
		<comments>http://topmedicaljournals.com/index.php/biochemical-update/insights-into-the-role-of-val45-and-gln182-of-escherichia-coli-muty-in-dna-substrate-binding-and-specificity/#comments</comments>
		<pubDate>Wed, 29 Jul 2009 19:18:16 +0000</pubDate>
		<dc:creator>admin</dc:creator>
				<category><![CDATA[biochemical UPDATE]]></category>

		<guid isPermaLink="false">http://topmedicaljournals.com/index.php/biochemical-update/insights-into-the-role-of-val45-and-gln182-of-escherichia-coli-muty-in-dna-substrate-binding-and-specificity/</guid>
		<description><![CDATA[Background:
Escherichia coli MutY (EcMutY) reduces mutagenesis by removing adenines paired with guanines or 7,8-dihydro-8-oxo-guanines (8-oxoG). V45 and Q182 of EcMutY are considered to be the key determinants of adenine specificity. Both residues are spatially close to each other in the active site and are conserved in MutY family proteins but not in Methanobacterium thermoautotrophicum Mig.MthI [...]]]></description>
		<wfw:commentRss>http://topmedicaljournals.com/index.php/biochemical-update/insights-into-the-role-of-val45-and-gln182-of-escherichia-coli-muty-in-dna-substrate-binding-and-specificity/feed/</wfw:commentRss>
		<slash:comments>0</slash:comments>
		</item>
		<item>
		<title>Biochemical characterization of malate synthase G of P. aeruginosa</title>
		<link>http://topmedicaljournals.com/index.php/biochemical-update/biochemical-characterization-of-malate-synthase-g-of-p-aeruginosa/</link>
		<comments>http://topmedicaljournals.com/index.php/biochemical-update/biochemical-characterization-of-malate-synthase-g-of-p-aeruginosa/#comments</comments>
		<pubDate>Wed, 29 Jul 2009 19:18:16 +0000</pubDate>
		<dc:creator>admin</dc:creator>
				<category><![CDATA[biochemical UPDATE]]></category>

		<guid isPermaLink="false">http://topmedicaljournals.com/index.php/biochemical-update/biochemical-characterization-of-malate-synthase-g-of-p-aeruginosa/</guid>
		<description><![CDATA[Background:
Malate synthase catalyzes the second step of the glyoxylate bypass, the condensation of acetyl coenzyme A and glyoxylate to form malate and coenzyme A (CoA). In several microorganisms, the glyoxylate bypass is of general importance to microbial pathogenesis. The predicted malate synthase G of Pseudomonas aeruginosa has also been implicated in virulence of this opportunistic [...]]]></description>
		<wfw:commentRss>http://topmedicaljournals.com/index.php/biochemical-update/biochemical-characterization-of-malate-synthase-g-of-p-aeruginosa/feed/</wfw:commentRss>
		<slash:comments>0</slash:comments>
		</item>
		<item>
		<title>The endocannabinoid anandamide is a precursor for the signaling lipid N-arachidonyl glycine through two distinct pathways</title>
		<link>http://topmedicaljournals.com/index.php/biochemical-update/the-endocannabinoid-anandamide-is-a-precursor-for-the-signaling-lipid-n-arachidonyl-glycine-through-two-distinct-pathways/</link>
		<comments>http://topmedicaljournals.com/index.php/biochemical-update/the-endocannabinoid-anandamide-is-a-precursor-for-the-signaling-lipid-n-arachidonyl-glycine-through-two-distinct-pathways/#comments</comments>
		<pubDate>Wed, 29 Jul 2009 19:18:15 +0000</pubDate>
		<dc:creator>admin</dc:creator>
				<category><![CDATA[biochemical UPDATE]]></category>

		<guid isPermaLink="false">http://topmedicaljournals.com/index.php/biochemical-update/the-endocannabinoid-anandamide-is-a-precursor-for-the-signaling-lipid-n-arachidonyl-glycine-through-two-distinct-pathways/</guid>
		<description><![CDATA[Background:
N-arachidonoyl glycine (NAGly) is an endogenous signaling lipid with a wide variety of biological activity whose biosynthesis is poorly understood. Two primary biosynthetic pathways have been proposed. One suggests that NAGly is formed via an enzymatically regulated conjugation of arachidonic acid (AA) and glycine. The other suggests that NAGly is an oxidative metabolite of the [...]]]></description>
		<wfw:commentRss>http://topmedicaljournals.com/index.php/biochemical-update/the-endocannabinoid-anandamide-is-a-precursor-for-the-signaling-lipid-n-arachidonyl-glycine-through-two-distinct-pathways/feed/</wfw:commentRss>
		<slash:comments>0</slash:comments>
		</item>
		<item>
		<title>A novel human NatA N-alpha-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)</title>
		<link>http://topmedicaljournals.com/index.php/biochemical-update/a-novel-human-nata-n-alpha-terminal-acetyltransferase-complex-hnaa16p-hnaa10p-hnat2-hard1/</link>
		<comments>http://topmedicaljournals.com/index.php/biochemical-update/a-novel-human-nata-n-alpha-terminal-acetyltransferase-complex-hnaa16p-hnaa10p-hnat2-hard1/#comments</comments>
		<pubDate>Wed, 29 Jul 2009 19:18:15 +0000</pubDate>
		<dc:creator>admin</dc:creator>
				<category><![CDATA[biochemical UPDATE]]></category>

		<guid isPermaLink="false">http://topmedicaljournals.com/index.php/biochemical-update/a-novel-human-nata-n-alpha-terminal-acetyltransferase-complex-hnaa16p-hnaa10p-hnat2-hard1/</guid>
		<description><![CDATA[Background:
Protein acetylation is among the most common protein modifications. The two major types are post-translational N?-lysine acetylation catalyzed by KATs (Lysine acetyltransferases, previously named HATs (histone acetyltransferases) and co-translational N?-terminal acetylation catalyzed by NATs (N-terminal acetyltransferases). The major NAT complex in yeast, NatA, is composed of the catalytic subunit Naa10p (N alpha acetyltransferase 10 protein) [...]]]></description>
		<wfw:commentRss>http://topmedicaljournals.com/index.php/biochemical-update/a-novel-human-nata-n-alpha-terminal-acetyltransferase-complex-hnaa16p-hnaa10p-hnat2-hard1/feed/</wfw:commentRss>
		<slash:comments>0</slash:comments>
		</item>
		<item>
		<title>TIPT2 and geminin interact with basal transcription factors to synergize in transcriptional regulation</title>
		<link>http://topmedicaljournals.com/index.php/biochemical-update/tipt2-and-geminin-interact-with-basal-transcription-factors-to-synergize-in-transcriptional-regulation/</link>
		<comments>http://topmedicaljournals.com/index.php/biochemical-update/tipt2-and-geminin-interact-with-basal-transcription-factors-to-synergize-in-transcriptional-regulation/#comments</comments>
		<pubDate>Wed, 29 Jul 2009 19:18:15 +0000</pubDate>
		<dc:creator>admin</dc:creator>
				<category><![CDATA[biochemical UPDATE]]></category>

		<guid isPermaLink="false">http://topmedicaljournals.com/index.php/biochemical-update/tipt2-and-geminin-interact-with-basal-transcription-factors-to-synergize-in-transcriptional-regulation/</guid>
		<description><![CDATA[Background:
The re-replication inhibitor Geminin binds to several transcription factors including homeodomain proteins, and to members of the polycomb and the SWI/SNF complexes.
Results:
Here we describe the TATA-binding protein-like factor-interacting protein (TIPT) isoform 2, as a strong binding partner of Geminin. TIPT2 is widely expressed in mouse embryonic and adult tissues, residing both in cyto- and nucleoplasma, [...]]]></description>
		<wfw:commentRss>http://topmedicaljournals.com/index.php/biochemical-update/tipt2-and-geminin-interact-with-basal-transcription-factors-to-synergize-in-transcriptional-regulation/feed/</wfw:commentRss>
		<slash:comments>0</slash:comments>
		</item>
		<item>
		<title>Charting calcium-regulated apoptosis pathways using chemical biology: role of calmodulin kinase II</title>
		<link>http://topmedicaljournals.com/index.php/biochemical-update/charting-calcium-regulated-apoptosis-pathways-using-chemical-biology-role-of-calmodulin-kinase-ii/</link>
		<comments>http://topmedicaljournals.com/index.php/biochemical-update/charting-calcium-regulated-apoptosis-pathways-using-chemical-biology-role-of-calmodulin-kinase-ii/#comments</comments>
		<pubDate>Sat, 16 May 2009 19:22:19 +0000</pubDate>
		<dc:creator>admin</dc:creator>
				<category><![CDATA[biochemical UPDATE]]></category>

		<guid isPermaLink="false">http://topmedicaljournals.com/index.php/biochemical-update/charting-calcium-regulated-apoptosis-pathways-using-chemical-biology-role-of-calmodulin-kinase-ii/</guid>
		<description><![CDATA[Background:
Intracellular free calcium ([Ca2+]i) is a key element in apoptotic signaling and a number of calcium-dependent apoptosis pathways have been described. We here used a chemical biology strategy to elucidate the relative importance of such different pathways.
Results:
A set of 40 agents (&#34;bioprobes&#34;) that induce apoptosis was first identified by screening of a chemical library. Using [...]]]></description>
		<wfw:commentRss>http://topmedicaljournals.com/index.php/biochemical-update/charting-calcium-regulated-apoptosis-pathways-using-chemical-biology-role-of-calmodulin-kinase-ii/feed/</wfw:commentRss>
		<slash:comments>0</slash:comments>
		</item>
		<item>
		<title>Chemogenetic fingerprinting by analysis of cellular growth dynamics</title>
		<link>http://topmedicaljournals.com/index.php/biochemical-update/chemogenetic-fingerprinting-by-analysis-of-cellular-growth-dynamics/</link>
		<comments>http://topmedicaljournals.com/index.php/biochemical-update/chemogenetic-fingerprinting-by-analysis-of-cellular-growth-dynamics/#comments</comments>
		<pubDate>Sat, 16 May 2009 19:22:19 +0000</pubDate>
		<dc:creator>admin</dc:creator>
				<category><![CDATA[biochemical UPDATE]]></category>

		<guid isPermaLink="false">http://topmedicaljournals.com/index.php/biochemical-update/chemogenetic-fingerprinting-by-analysis-of-cellular-growth-dynamics/</guid>
		<description><![CDATA[Background:
A fundamental goal in chemical biology is the elucidation of on- and off-target effects of drugs and biocides. To this aim chemogenetic screens that quantify drug induced changes in cellular fitness, typically taken as changes in composite growth, is commonly applied.
Results:
Using the model organism Saccharomyces cerevisiae we here report that resolving cellular growth dynamics into [...]]]></description>
		<wfw:commentRss>http://topmedicaljournals.com/index.php/biochemical-update/chemogenetic-fingerprinting-by-analysis-of-cellular-growth-dynamics/feed/</wfw:commentRss>
		<slash:comments>0</slash:comments>
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