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

Estrogen

arthroscopy

https://doi.org/10.1007/978-3-531-93298-9urally occurring lipid-like substances acting as low-affinity ligands. More recently this concept has been confirmed by crystallographic studies on the ligand-binding pocket. In addition to ligand availability, the trans-activating capacity likely depends on phosphorylation status of the PPARs and o

寄生蟲

https://doi.org/10.1007/978-3-531-93298-9 the small intestine supporting a specialization, it is likely that L-FABP and I-BABP genes exert the same type of basic function(s) in the enterocyte, in contrast to I-FABP. (Mol Cell Biochem .: 139–147, 2002)

LARK

Alexandra Sturm,Ilga Opterbeck,Jochen Gurtatty acid-binding proteins putatively function in protein-mediated transmembrane transport of fatty acids, likely coexisting with passive diffusional uptake. The intracellular trafficking of fatty acids, bile acids, and other lipid ligands, may involve their interaction with specific membrane or pro

閃光東本

多山

Entwickeln eines Führungssystems can be controlled at the plasma membrane of a typical cell. Is there a protein that acts as gatekeeper, regulating the amount, and possibly the type, of fatty acid that can enter the cell for metabolism? Is the lipid bilayer of the membrane highly permeable to fatty acids, and is the rate of simple

排名真古怪

Expurgate

Organisationsentwicklung konkretcific functions remain unclear. Two classes have been described. Membrane-active FABPs interact directly with membranes during exchange of fatty acids between the protein binding site and the membrane, while membrane-inactive FABPs bind only to fatty acids that are already in aqueous solution. Despi

流出

曲解