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Metallothionein functions and structural characteristics
Metallothionein functions and structural characteristics

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... they bind to the receptor sites of an NT but do NOT produce the same effect thus preventing the NT from having its effect. The drug BENADRYL (an antihistamine) blocks H1 and H2 receptor sites for histamine. The drug PROCARDIA, a “calcium channel blocker,” inhibits smooth muscle contraction resulting ...
Human Vascular Smooth Muscle Cells Contain Functional Estrogen
Human Vascular Smooth Muscle Cells Contain Functional Estrogen

... To demonstrate the presence of E2-receptor message in VSMCs, an RNase protection assay was performed with total RNA prepared from HSVSMCs and a riboprobe from the hormone-binding domain of the E2 receptor. RNase protection assays were used rather than Northern blots because of the anticipated low ab ...
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... soluble T1R NTD proteins in sufficient quantities for biochemical studies. We took advantage of two bacterial expression strategies to accomplish this goal. In the first, T1R3NTD was expressed as an N-terminal fusion with a mini-intein and chitin-binding domain (CBD) using the IMPACT vector pTXB1 (N ...
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... 2507 + 6T ! C or IVS20þ6T!C , changes the sequence of the splice donor element of intron 20 from the consensus GTAAGT to a non-consensus GTAAGC, resulting in the generation of a transcript lacking exon 20. This mutation appears to be somewhat leaky as both the mutant and wild-type transcripts are de ...
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Identification of the first invertebrate interleukin

... The evidence presented here indicates that domeless encodes a receptor of the Drosophila JAK/STAT pathway and shows that the pathway is conserved in invertebrates. The previous failure to detect the receptor was due to sequence similarity being restricted to a few critical amino acids in otherwise q ...
< 1 ... 18 19 20 21 22 23 24 25 26 ... 34 >

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.
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