WRI116-Research_Review
... Integrins are a group of heterodimer cell surface receptors that are considered as the central extracellular matrix receptors. They convey cell-matrix and cell-to-cell interactions that involve adhesion, invasion, proliferation, and migration. In particular, alpha-v-beta-6 (avb6) and alpha-v-beta-3( ...
... Integrins are a group of heterodimer cell surface receptors that are considered as the central extracellular matrix receptors. They convey cell-matrix and cell-to-cell interactions that involve adhesion, invasion, proliferation, and migration. In particular, alpha-v-beta-6 (avb6) and alpha-v-beta-3( ...
expression and function of receptors for leptin and ghrelin in sh
... inducing appetite, like ghrelin, mainly produced by the stomach, or satiety, like the adipocytesecreted peptide, leptin. These agents appear to specifically regulate hypothalamic neurons producing the potent orexigenic peptide neuropeptide Y (NPY). In the rat, leptin, acting via OBRb, the long lepti ...
... inducing appetite, like ghrelin, mainly produced by the stomach, or satiety, like the adipocytesecreted peptide, leptin. These agents appear to specifically regulate hypothalamic neurons producing the potent orexigenic peptide neuropeptide Y (NPY). In the rat, leptin, acting via OBRb, the long lepti ...
Gene Section MSF (MLL septin-like fusion) Atlas of Genetics and Cytogenetics
... multiple MSF isoforms with distinct amino-and carboxy-termini. MSF-B and MSF-C proteins are identical and are sub-sequences within the other larger isoforms. All isoforms contain a GTPase domain, a xylose isomerase domain of unknown mammalian function but previously identified for sugar interconvers ...
... multiple MSF isoforms with distinct amino-and carboxy-termini. MSF-B and MSF-C proteins are identical and are sub-sequences within the other larger isoforms. All isoforms contain a GTPase domain, a xylose isomerase domain of unknown mammalian function but previously identified for sugar interconvers ...
Synthetic cell surface receptors for delivery of therapeutics and probes
... Cholesterol has been termed the central lipid of mammalian cells [43]. Among its many biological roles, this sterol is critically important for stabilization of animal cell membranes. To estimate the number of cholesterol molecules in cellular membranes, the plasma membrane of a typical mammalian ce ...
... Cholesterol has been termed the central lipid of mammalian cells [43]. Among its many biological roles, this sterol is critically important for stabilization of animal cell membranes. To estimate the number of cholesterol molecules in cellular membranes, the plasma membrane of a typical mammalian ce ...
Identification of a novel human ... through its interaction with the ...
... a mitogen-activated protein kinase substrate implicated in regulation of Golgi vesicle trafficking. In this study, a novel human Tankyrase, designated Tankyrase 2, was isolated in a yeast two hybrid screen as a binding partner for the Src homology 2 domain-containing adaptor protein Grb14 . Tankyras ...
... a mitogen-activated protein kinase substrate implicated in regulation of Golgi vesicle trafficking. In this study, a novel human Tankyrase, designated Tankyrase 2, was isolated in a yeast two hybrid screen as a binding partner for the Src homology 2 domain-containing adaptor protein Grb14 . Tankyras ...
Cloning of the Human Interferon-Related Developmental Regulator
... and the whole interferon-g protein, suggesting the existence of a functional domain within the PC4 protein. Furthermore, the mouse PC4 homolog (TIS7) was identified as a tetradecanoyl phorbol acetate-induced gene in mouse NIH3T3 cells (Varnum et al., 1989). Although PC4 function remains unknown, its ...
... and the whole interferon-g protein, suggesting the existence of a functional domain within the PC4 protein. Furthermore, the mouse PC4 homolog (TIS7) was identified as a tetradecanoyl phorbol acetate-induced gene in mouse NIH3T3 cells (Varnum et al., 1989). Although PC4 function remains unknown, its ...
VLDL receptor
The very-low-density-lipoprotein receptor (VLDLR) is a transmembrane lipoprotein receptor of the low-density-lipoprotein (LDL) receptor family. VLDLR shows considerable homology with the members of this lineage. Discovered in 1992 by T. Yamamoto, VLDLR is widely distributed throughout the tissues of the body, including the heart, skeletal muscle, adipose tissue, and the brain, but is absent from the liver. This receptor has an important role in cholesterol uptake, metabolism of apoprotein-E-containing triacylglycerol-rich lipoproteins, and neuronal migration in the developing brain. In humans, VLDLR is encoded by the VLDLR gene. Mutations of this gene may lead to a variety of symptoms and diseases, which include type I lissencephaly, cerebellar hypoplasia, and atherosclerosis.