نتایج جستجو برای: carbohydrate sulfotransferase 6 gene chst6

تعداد نتایج: 2014793  

Journal: :Cancer research 1975
C C Irving

Male Spraque-Dawley rats were 6 or 7 times more susceptible than females to the acute toxic effects of a single i.p. injection of N-hydroxy-2-acetylaminofluorene. The N-hydroxy compound were equally toxic in male and female Fischer rats and about twice as toxic to male as to female Wistar rats. A negative correlation between the 50% lethal dose of N-hydroxy-2-acetylaminofluorene and hepatic N-h...

Journal: :Cancer research 2000
P Seth K L Lunetta D W Bell H Gray S M Nasser E Rhei C M Kaelin D J Iglehart J R Marks J E Garber D A Haber K Polyak

In recent years, significant effort has been made to identify genes that influence breast cancer risk. Because the high-penetrance breast cancer susceptibility genes BRCA1 and 2 play a role only in a small fraction of breast cancer cases, understanding the genetic risk of the majority of breast cancers will require the identification and analysis of several lower penetrance genes. The estrogen-...

Journal: :Glycobiology 2008
Maki Ishii Nobuaki Maeda

Chondroitin sulfate (CS) proteoglycans are major components of the cell surface and the extracellular matrix in the developing brain and bind to various proteins via CS chains in a CS structure-dependent manner. This study demonstrated the expression pattern of three CS sulfotransferase genes, dermatan 4-O-sulfotransferase (D4ST), uronyl 2-O-sulfotransferase (UST), and N-acetylgalactosamine 4-s...

Journal: :Methods in molecular biology 2012
Xuezheng Song Jamie Heimburg-Molinaro Nancy M Dahms David F Smith Richard D Cummings

Glycan microarrays prepared by immobilization of amino-functionalized glycans on NHS-activated glass slides have been successfully used to study protein-glycan interactions. Fluorescently tagged glycans with an amino functional group can be prepared from natural glycans released from glycoproteins. These tagged glycans can be enzymatically modified with various glycosyltransferases, phosphotran...

2006
MIN SOOK KWON SUN JUNG KIM SU - YOUNG LEE EUN SOOK LEE HAN - SUNG KANG

Sulfotransferase 1A1 (SULT1A1) is reported to be involved in the conjugation with sulfate, resulting in the inactivation of estrogens. Aberrant methylation of promoter CpG islands is known to be responsible for the alteration and silencing of the gene in cancers. This study was intended to evaluate the methylation status and transcriptional activity of SULT1A1 in breast cancer tissue (n=56), be...

Journal: :The Journal of biological chemistry 1971
D F Farrell G M McKhann

Cerebroside sulfotransferase, the enzyme which catalyzes the transfer of the sulfate group from d’-phosphoadenosine 5’-phosphosulfate to galactosylceramide to form sulfogalactosylceramide is located primarily in microsomes and possibly in myelin of 17-day-old rat brain. Subfractionation of the microsomes demonstrates the enzyme activity to be present in the lighter, smooth membrane fraction. Vi...

Journal: :Cancer research 1979
J B Adams T Pewnim D P Chandra L Archibald M S Foo

Estrogen sulfotransferase (EC 2.8.2.4) activity and estrogen receptor levels were measured in 32 human primary breast cancer cytosol preparations. Two types of tumors were identified: type 1, in which estrogen sulfotransferase levels were low (less than 40 pmol 17 beta-estradiol 3-sulfate formed per mg protein per 2 hr) and were independent of [35S]adenosine 3'-phosphate 5'-phosphosulfate produ...

Journal: :Endocrinology 1997
E Kaptein G A van Haasteren E Linkels W J de Greef T J Visser

Sulfation is an important pathway in the metabolism of thyroid hormone because it strongly facilitates the degradation of the hormone by the type I iodothyronine deiodinase. However, little is known about the properties and possible regulation of the sulfotransferase(s) involved in the sulfation of thyroid hormone. We have developed a convenient method for the analysis of iodothyronine sulfotra...

2011
Ilana Berger Chen Guttman Dotan Amar Raz Zarivach Amir Aharoni

Cytosolic sulfotransferases (SULTs) are mammalian enzymes that detoxify a wide variety of chemicals through the addition of a sulfate group. Despite extensive research, the molecular basis for the broad specificity of SULTs is still not understood. Here, structural, protein engineering and kinetic approaches were employed to obtain deep understanding of the molecular basis for the broad specifi...

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