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		<title>Pharmaceuticals: Monoclonal Antibody</title>
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	<title>Pharmaceuticals, Vol. 4, Pages 950-963: Monoclonal Antibodies against Small Molecule Natural Products and Their Applications, Eastern Blotting and Knockout Extract</title>
	<link>http://www.mdpi.com/1424-8247/4/7/950/</link>
	<description>To determine the hapten number in hapten-carrier protein conjugate matrix-assisted laser desorption/ionization (MALDI) tof mass spectrometry was applied. Highly specific anti-ginsenoside Rb1 and Rg1 monoclonal antibodies (MAbs) were prepared. Ginsenosides were developed on thin layer chromatography (TLC) plates which were covered by a polyvinylidene difluoride (PVDF) membrane resulting in blotting. The membrane was treated with NaIO4 solution to release the aldehyde group on the sugar moiety of the ginsenosides. By treatment of the membrane with a protein solution the ginsenoside-protein conjugation as a Schiff-base occurred, which can function to fix it to the PVDF membrane. A part of the ginsenoside aglycone was reacted with anti-ginsenoside Rb1 MAb, secondary MAb conjugated with enzyme and finally a substrate was added, resulting in a specific and highly sensitive staining that we named Eastern blotting. Furthermore, it makes one-step isolation of ginsenoside Rb1 possible using an immuno-affinity column conjugated with anti-ginsenoside Rb1 MAb. Furthermore, immunoaffinity concentration was carried out allowing high sensitivity analysis of lower concentrations of ginsenoside Rb1 so that several unknown bands could be structurally determined.</description>
	
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	<pubDate>Tue, 28 Jun 2011 00:00:00 CEST</pubDate>
	
	<prism:publicationName>Pharmaceuticals</prism:publicationName>
	<prism:publicationDate>2011-06-28</prism:publicationDate>
	<prism:volume>4</prism:volume>
	<prism:number>7</prism:number>
	<prism:section>Article</prism:section>
	<prism:startingPage>950</prism:startingPage>
		<prism:endingPage>963</prism:endingPage>
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	<dc:title>Monoclonal Antibodies against Small Molecule Natural Products and Their Applications, Eastern Blotting and Knockout Extract</dc:title>
	<dc:date>2011-06-28</dc:date>
	<dc:identifier>doi: 10.3390/ph4070950</dc:identifier>
		<dc:creator>Yukihiro Shoyama</dc:creator>
	
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	<title>Pharmaceuticals, Vol. 3, Pages 3258-3274: The Role of Monoclonal Antibodies in the Management of Leukemia</title>
	<link>http://www.mdpi.com/1424-8247/3/10/3258/</link>
	<description>This article will review the monoclonal antibodies more commonly used in leukemias. In the last three decades, scientists have made considerable progress understanding the structure and the functions of various surface antigens, such as CD20, CD33. The introduction of rituximab, an anti CD20 monoclonal antibody, had a great impact in the treatment of lymphoproliferative disorders. Gemtuzumab, an anti CD 33 conjugated monoclonal antibody has activity in acute mylegenous leukemia (AML). As this field is undergoing a rapid growth, the years will see an increasing use of monoclonal antibodies in hematological malignancies.</description>
	
	<guid>http://www.mdpi.com/1424-8247/3/10/3258/</guid>
	<pubDate>Mon, 18 Oct 2010 00:00:00 CEST</pubDate>
	
	<prism:publicationName>Pharmaceuticals</prism:publicationName>
	<prism:publicationDate>2010-10-18</prism:publicationDate>
	<prism:volume>3</prism:volume>
	<prism:number>10</prism:number>
	<prism:section>Review</prism:section>
	<prism:startingPage>3258</prism:startingPage>
		<prism:endingPage>3274</prism:endingPage>
		<prism:issn>1424-8247</prism:issn>
	
	<dc:title>The Role of Monoclonal Antibodies in the Management of Leukemia</dc:title>
	<dc:date>2010-10-18</dc:date>
	<dc:identifier>doi: 10.3390/ph3103258</dc:identifier>
		<dc:creator>Ali Al-Ameri</dc:creator>
		<dc:creator>Mohamad Cherry</dc:creator>
		<dc:creator>Aref Al-Kali</dc:creator>
		<dc:creator>Alessandra Ferrajoli</dc:creator>
	
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	<item rdf:about="http://www.mdpi.com/1424-8247/3/6/1887/">
	<title>Pharmaceuticals, Vol. 3, Pages 1887-1891: In Response to: ‘Impact of Glycosylation on Effector Functions of Therapeutic IgG’ (Pharmaceuticals 2010, 3, 146–157)</title>
	<link>http://www.mdpi.com/1424-8247/3/6/1887/</link>
	<description>To complete the review article by Abes and colleagues (Pharmaceuticals 2010, 3, 146–157) which provides a good overview on recently developed approaches for generation of glyco-modified antibodies and the impact of glyco-modification of antibodies on their effector functions, important information should be added, namely that — besides the Glycart and the Biowa approach to generate de-fucosylated antibodies — innovative, moss derived methods have been shown to generate glyco-modified antibodies with improved effector function profile.</description>
	
	<guid>http://www.mdpi.com/1424-8247/3/6/1887/</guid>
	<pubDate>Thu, 10 Jun 2010 00:00:00 CEST</pubDate>
	
	<prism:publicationName>Pharmaceuticals</prism:publicationName>
	<prism:publicationDate>2010-06-10</prism:publicationDate>
	<prism:volume>3</prism:volume>
	<prism:number>6</prism:number>
	<prism:section>Commentary</prism:section>
	<prism:startingPage>1887</prism:startingPage>
		<prism:endingPage>1891</prism:endingPage>
		<prism:issn>1424-8247</prism:issn>
	
	<dc:title>In Response to: ‘Impact of Glycosylation on Effector Functions of Therapeutic IgG’ (Pharmaceuticals 2010, 3, 146–157)</dc:title>
	<dc:date>2010-06-10</dc:date>
	<dc:identifier>doi: 10.3390/ph3061887</dc:identifier>
		<dc:creator> Nechansky</dc:creator>
		<dc:creator> Koller</dc:creator>
		<dc:creator> Kircheis</dc:creator>
	
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	<item rdf:about="http://www.mdpi.com/1424-8247/3/1/300/">
	<title>Pharmaceuticals, Vol. 3, Pages 300-322: Monoclonal Antibodies for Systemic Lupus Erythematosus (SLE)</title>
	<link>http://www.mdpi.com/1424-8247/3/1/300/</link>
	<description>A number of monoclonal antibodies (mAb) are now under investigation in clinical trials to assess their potential role in Systemic Lupus Erythematosus (SLE). The most frequently used mAb is rituximab, which is directed against CD20, a membrane protein expressed on B lymphocytes. Uncontrolled trials reported an improvement of SLE activity in non-renal patients and other studies even reported an improvement of severe lupus nephritis unresponsive to conventional treatments. However two randomized trials failed to show the superiority of rituximab over conventional treatment in non renal SLE and in lupus nephritis. Preliminary trials reported promising results with epratuzumab, a humanized mAb directed against CD22, and with belimumab, a human mAb that specifically recognizes and inhibits the biological activity of BLyS a cytokine of the tumornecrosis-factor (TNF) ligand superfamily. Other clinical trials with mAb directed against TNF-alpha, interleukin-10 (Il-10), Il-6, CD154, CD40 ligand, IL-18 or complement component C5 are under way. At present, however, in spite of good results reported by some studies, no firm conclusion on the risk-benefit profile of these mAbs in patients with SLE can be drawn from the available studies.</description>
	
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	<pubDate>Wed, 20 Jan 2010 00:00:00 CET</pubDate>
	
	<prism:publicationName>Pharmaceuticals</prism:publicationName>
	<prism:publicationDate>2010-01-20</prism:publicationDate>
	<prism:volume>3</prism:volume>
	<prism:number>1</prism:number>
	<prism:section>Review</prism:section>
	<prism:startingPage>300</prism:startingPage>
		<prism:endingPage>322</prism:endingPage>
		<prism:issn>1424-8247</prism:issn>
	
	<dc:title>Monoclonal Antibodies for Systemic Lupus Erythematosus (SLE)</dc:title>
	<dc:date>2010-01-20</dc:date>
	<dc:identifier>doi: 10.3390/ph3010300</dc:identifier>
		<dc:creator>Claudio Ponticelli</dc:creator>
		<dc:creator>Gabriella Moroni</dc:creator>
	
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	<item rdf:about="http://www.mdpi.com/1424-8247/3/1/146/">
	<title>Pharmaceuticals, Vol. 3, Pages 146-157: Impact of Glycosylation on Effector Functions of Therapeutic IgG</title>
	<link>http://www.mdpi.com/1424-8247/3/1/146/</link>
	<description>Human IgG has only one conserved glycosylation site located in the Cγ2 domain of the Fc region that accounts for the presence of two sugar moieties per IgG. These IgG sugar cores play a critical role in a number of IgG effector functions. In the present review, we describe the main characteristics of IgG Fc glycosylation and some abnormalities of serum IgG glycosylation. We also discuss how glycosylation impacts on monoclonal antibodies (mAbs) and IVIg effector functions and how these molecules can be engineered. Several therapeutic antibodies have now been engineered to be no- or low-fucose antibodies and are currently tested in clinical trials. They exhibit an increased binding to activating FcγRIIIA and trigger a strong antibody-dependent cell cytotoxicity (ADCC) as compared to their highly-fucosylated counterparts. They represent a new generation of therapeutic antibodies that are likely to show a better clinical efficacy in patients, notably in cancer patients where cytotoxic antibodies are needed.</description>
	
	<guid>http://www.mdpi.com/1424-8247/3/1/146/</guid>
	<pubDate>Tue, 12 Jan 2010 00:00:00 CET</pubDate>
	
	<prism:publicationName>Pharmaceuticals</prism:publicationName>
	<prism:publicationDate>2010-01-12</prism:publicationDate>
	<prism:volume>3</prism:volume>
	<prism:number>1</prism:number>
	<prism:section>Review</prism:section>
	<prism:startingPage>146</prism:startingPage>
		<prism:endingPage>157</prism:endingPage>
		<prism:issn>1424-8247</prism:issn>
	
	<dc:title>Impact of Glycosylation on Effector Functions of Therapeutic IgG</dc:title>
	<dc:date>2010-01-12</dc:date>
	<dc:identifier>doi: 10.3390/ph3010146</dc:identifier>
		<dc:creator>Riad Abès</dc:creator>
		<dc:creator>Jean-Luc Teillaud</dc:creator>
	
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