Titlebook: Cellular Lipid Binding Proteins; Jan F. C. Glatz Book 2002 Springer Science+Business Media Dordrecht 2002 DNA.Lipid.biochemistry.gene expr

出租車

書目名稱Cellular Lipid Binding Proteins影響因子(影響力)




書目名稱Cellular Lipid Binding Proteins影響因子(影響力)學(xué)科排名




書目名稱Cellular Lipid Binding Proteins網(wǎng)絡(luò)公開度




書目名稱Cellular Lipid Binding Proteins網(wǎng)絡(luò)公開度學(xué)科排名




書目名稱Cellular Lipid Binding Proteins被引頻次




書目名稱Cellular Lipid Binding Proteins被引頻次學(xué)科排名




書目名稱Cellular Lipid Binding Proteins年度引用




書目名稱Cellular Lipid Binding Proteins年度引用學(xué)科排名




書目名稱Cellular Lipid Binding Proteins讀者反饋




書目名稱Cellular Lipid Binding Proteins讀者反饋學(xué)科排名

懶惰民族

Critical steps in cellular fatty acid uptake and utilization,an organs are still incompletely understood. In non-fenestratred organs such as heart and skeletal muscle, membrane barriers for blood-borne FA are the luminal and abluminal membranes of endothelial cells, the sarcolemma and the mitochondrial membranes. Transport of FA through the phospholipid bilay

Femine

Glossy

錯(cuò)事

Crater

Insights into binding of fatty acids by fatty acid binding proteins,eal distinct binding preferences with regard to ligand structure and conformation, when binding is assessed by the Lipidex method (removal of unbound ligand by hydrophobic polymer) or by isothermal titration calorimetry, a true equilibrium method. Subfamily proteins bind retinoids, subfamily II prot

Crater

,The effect of charge reversal mutations in the α-helical region of liver fatty acid binding proteins. LFABP is able to bind long chain fatty acids with a 2:1 stoichiometry and the crystal structure has identified two fatty acid binding sites in the binding cavity. The presumed primary site (site 1 ) involves the fatty acid binding with the carboxylate group buried in the cavity whereas the fatty

acetylcholine

MANIA

Evolution of the family of intracellular lipid binding proteins in vertebrates,g-chain fatty acids and retinoids. iLBPs are low molecular mass proteins (14–16 kDa) sharing a common structural fold. The iLBP family likely arose through duplication and diversification of an ancestral iLBP gene. Phylogenetic analysis undertaken in the present study indicates that the ancestral iL

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