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	1. Isolation and Characterization of Total N-linked Glycans from Glycoproteins by Ultrafiltration Units and Mass Spectrometry
	YANG Ganglong,MA Tianran,LI Zheng
	Biology 16 January 2013
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	Abstract:Glycosylation is one of the most common post-translational modifications in proteins. Current methods for glycan analysis are generally based on multiple preparation processes to separate glycans. However, glycans are continuously lost and the difficulty for accurate quantitative analysis is increased in the procedure. Here, a filter aided sample preparation-based total N-linked glycans from the glycoproteins isolation method (N-glycan-FASP-T) was developed using ultrafiltration units according to the molecular weight difference among the glycans, the impurities and proteins. Results: The isolated glycans were characterized and confirmed by the MALDI-TOF/TOF-MS. A total of 23 distinctive N-linked glycans were characterized from human sera.
	TO cite this article:YANG Ganglong,MA Tianran,LI Zheng. Isolation and Characterization of Total N-linked Glycans from Glycoproteins by Ultrafiltration Units and Mass Spectrometry[OL].[16 January 2013] http://en.paper.edu.cn/en_releasepaper/content/4514464


	2. Revealing a marine natural product as a novel agonist for retinoic acid receptors with a unique binding mode and inhibitory effects on cancer cells
	Wang Shanshan,Wang Zhao,Lin Shengchen,Zheng Weili,Wang Rui,Chen Jinan,Jin Lihua,Li Yong
	Biology 31 May 2012
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	Abstract:Retinoids display antitumor activity on various cancer cells and thereby have been used as important therapeutic agents. However, adverse side effects and retinoic acid (RA) resistance limit further development and clinical application of retinoid-based therapeutic agents. We report here the identification of a natural marine product that activates retinoic acid receptors (RARs) with a chemical structure distinct from retinoids by high-throughput compound library screening. Luffariellolide, was uncovered as a novel RAR agonist by inducing coactivator binding to these receptors in vitro, further inhibiting cell growth and regulating RAR target genes in various cancer cells. Structural and molecular studies unraveled a unique binding mode of this natural ligand to RARs with an unexpected covalent modification on the RAR receptor. Functional characterization further revealed that luffariellolide displays chemotherapeutic potentials for overcoming RA resistance in colon cancer cells, suggesting that luffariellolide may represent a unique template for designing novel non-retinoid compounds with advantages over current retinoic acid drugs.
	TO cite this article:Wang Shanshan,Wang Zhao,Lin Shengchen, et al. Revealing a marine natural product as a novel agonist for retinoic acid receptors with a unique binding mode and inhibitory effects on cancer cells[J].


	3. Design，Preparation and in vitro Bioactivity of Monopegylated Recombinant Hirudin
	Hou Beibei ,Li Shirong ,Li Xiaohui ,Xiu Zhilong
	Biology 28 November 2006
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	Abstract:Hirudin is the most potent inhibitor of thrombin found in nature. As a promising anticoagulant, a significant drawback which significantly inhibits its clinical application, is the short serum half-life. In order to prolong circulation half-life in vivo, PEGylation is an effective and commonly used method. In this study Succinimidyl carbonyl mPEG (SC-mPEG) 20kDa was attached to recombinant hirudin (r-Hir) at mildly acidic pH to favor the formation of mono- PEGylated r-Hir, since histidine residues represent the preferred PEGylation sites under mildly acidic conditions, and there is only one histidine residue, His51, in r-Hir. Because of the high ratio of monopegylated product, the reaction mixture was easily separated by a one-step ion-exchange chromatographic(IEC) separation procedure. The proportion of urethane bonds involving carboxyalkylated histidines was assayed using its sensitivity to neutral hydroxylamine, and about 79.71% of the mono-substituted PEGylated r-Hir was PEGylated
	TO cite this article:Hou Beibei ,Li Shirong ,Li Xiaohui , et al. Design，Preparation and in vitro Bioactivity of Monopegylated Recombinant Hirudin[OL].[28 November 2006] http://en.paper.edu.cn/en_releasepaper/content/9973

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