Titlebook: Regulation of Plasma Low Density Lipoprotein Levels Biopharmacological Regulation of Protein Phospho; W. R. Bartle,V. Braun,N. E. Winslade

NO610

書目名稱Regulation of Plasma Low Density Lipoprotein Levels Biopharmacological Regulation of Protein Phospho影響因子(影響力)




書目名稱Regulation of Plasma Low Density Lipoprotein Levels Biopharmacological Regulation of Protein Phospho影響因子(影響力)學科排名




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書目名稱Regulation of Plasma Low Density Lipoprotein Levels Biopharmacological Regulation of Protein Phospho年度引用




書目名稱Regulation of Plasma Low Density Lipoprotein Levels Biopharmacological Regulation of Protein Phospho年度引用學科排名




書目名稱Regulation of Plasma Low Density Lipoprotein Levels Biopharmacological Regulation of Protein Phospho讀者反饋




書目名稱Regulation of Plasma Low Density Lipoprotein Levels Biopharmacological Regulation of Protein Phospho讀者反饋學科排名

鞠躬

paragon

978-3-642-72904-1Springer-Verlag Berlin Heidelberg 1988

考古學

Regulation of Plasma Low Density Lipoprotein Levels Biopharmacological Regulation of Protein Phospho978-3-642-72902-7Series ISSN 0177-8757

背信

COLON

Regulation of Plasma Low Density Lipoprotein Levels: New Strategies for Drug Design,s reason, a concerted effort is now underway to develop effective strategies to decrease the concentration of this lipoprotein in the plasma. Over the last few years, new advances have been made in our understanding of the factors that control the plasma LDL-cholesterol concentration. It is now poss

抱狗不敢前

Biopharmacological Regulation of Protein Phosphorylation,In such cases, techniques involving molecular pharmacological approaches using selective inhibitors or activators come to the rescue like two way traffic. This article indicates pharmacological approaches to the roles which multiple protein kinases play in regulating various cell functions, using se

FLIT

Calcium-Activated Neutral Protease (CANP) and its Biological and Medical Implications,reveals a novel domain structure comprising domains highly homologous to papain-like cysteine proteinases and calmodulin-like Ca. binding proteins, and a glycine-rich hydrophobic domain that interacts with the cell membrane and phospholipid. This finding provides new insight into the protease action

peptic-ulcer

Microbial Iron Transport Structure and Function of Siderophores,ating electron transport chains and of the intermediary metabolism. The article emphasizes the intricate mechanisms by which microbes, bacteria as well as fungi, overcome iron deficiency imposed by the human host. In humans extracelluar iron is almost exclusively bound to transferrin and lactoferrin

Discrete