Type II estrogen binding site agonist:

Chirality ◽  
2003 ◽  
Vol 15 (8) ◽  
pp. 674-679 ◽  
Author(s):  
Lester Pretlow ◽  
Roy Williams ◽  
Mark Elliott
Keyword(s):  
Binding Site ◽  
Type Ii ◽  
Estrogen Binding

Chromatographic resolution of the type II estrogen binding site and a tyrosinase-like enzymatic activity from rat uterine nuclei

Steroids ◽  
1994 ◽  
Vol 59 (4) ◽  
pp. 282-287 ◽  
Author(s):  
Charles L. Densmore ◽  
Thomas H. Schauweker ◽  
Rebecca R. Gregory ◽  
Brett Webb ◽  
Elvia Garcia ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Binding Site ◽  
Type Ii ◽  
Chromatographic Resolution ◽  
Estrogen Binding

Cytosolic Type II Estrogen Binding Site in Rat Uterus: Specific Photolabeling with Estrone

1992 ◽  
Vol 12 (2) ◽  
pp. 217-231 ◽  
Author(s):  
Marc Poirot ◽  
Catherine Chailleux ◽  
Francis Bayard ◽  
Jean-Charles Faye
Keyword(s):  
Binding Site ◽  
Type Ii ◽  
Rat Uterus ◽  
Estrogen Binding

scholarly journals A potent and selective photoaffinity probe for the anti-estrogen binding site of rat liver.

1990 ◽  
Vol 265 (28) ◽  
pp. 17039-17043
Author(s):  
M Poirot ◽  
C Chailleux ◽  
A Fargin ◽  
F Bayard ◽  
J C Faye
Keyword(s):  
Binding Site ◽  
Rat Liver ◽  
Estrogen Binding

scholarly journals Eosinophils as the source of uterine nuclear type II estrogen binding sites.

1984 ◽  
Vol 259 (5) ◽  
pp. 2697-2700
Author(s):  
C R Lyttle ◽  
K L Medlock ◽  
D M Sheehan
Keyword(s):  
Binding Sites ◽  
Type Ii ◽  
Estrogen Binding

scholarly journals In Vivo and In Vitro Analysis of Factor Binding Sites in Jaagsiekte Sheep Retrovirus Long Terminal Repeat Enhancer Sequences: Roles of HNF-3, NF-I, and C/EBP for Activity in Lung Epithelial Cells

2006 ◽  
Vol 80 (1) ◽  
pp. 332-341 ◽  
Author(s):  
Kathleen McGee-Estrada ◽  
Hung Fan
Keyword(s):  
Epithelial Cells ◽  
Long Terminal Repeat ◽  
Binding Site ◽  
Terminal Repeat ◽  
Lung Epithelial Cells ◽  
Type Ii ◽  
Jaagsiekte Sheep Retrovirus ◽  
Efficient System ◽  
Lung Epithelial

ABSTRACT Jaagsiekte sheep retrovirus (JSRV) is the causative agent of ovine pulmonary adenocarcinoma, a contagious lung cancer of sheep that arises from type II pneumocytes and Clara cells of the lung epithelium. Studies of the tropism of this virus have been hindered by the lack of an efficient system for viral replication in tissue culture. To map regulatory regions important for transcriptional activation, an in vivo footprinting method that couples dimethyl sulfate treatment and ligation-mediated PCR was performed in murine type II pneumocyte-derived MLE-15 cells infected with a chimeric Moloney murine leukemia virus driven by the JSRV enhancers (ΔMo+JS Mo-MuLV). In vivo footprints were found in the JSRV enhancers in two regions previously shown to be important for JSRV long terminal repeat (LTR) activity: a binding site for the lung-specific transcription factor HNF-3β and an E-box element in the distal enhancer adjacent to an NF-κB-like binding site. In addition, in vivo footprints were detected in two downstream motifs likely to bind C/EBP and NF-I. Mutational analysis of a JSRV LTR reporter construct (pJS21luc) revealed that the C/EBP binding site is critical for LTR activity, while the putative NF-I binding element is less important; elimination of these sites resulted in 70% and 40% drops in LTR activity, respectively. Electrophoretic mobility shift assays using nuclear extracts from MLE-15 murine Clara cell-derived mtCC1-2 cells with probes corresponding to the NF-I or C/EBP sites revealed several complexes. Antiserum directed against NF-IA, C/EBPα, or C/EBPβ supershifted the corresponding protein-DNA complexes, indicating that these isoforms, which are also important for the expression of several cellular lung-specific genes, may be important for JSRV expression in lung epithelial cells.

scholarly journals Biochemical and structural characterization of the novel sialic acid-binding site of Escherichia coli heat-labile enterotoxin LT-IIb

2016 ◽  
Vol 473 (21) ◽  
pp. 3923-3936 ◽  
Author(s):  
Dani Zalem ◽  
João P. Ribeiro ◽  
Annabelle Varrot ◽  
Michael Lebens ◽  
Anne Imberty ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Cholera Toxin ◽  
Carbohydrate Binding ◽  
Type I ◽  
Type Ii ◽  
E Coli ◽  
B Subunit ◽  
Heat Labile ◽  
B Subunits

The structurally related AB5-type heat-labile enterotoxins of Escherichia coli and Vibrio cholerae are classified into two major types. The type I group includes cholera toxin (CT) and E. coli LT-I, whereas the type II subfamily comprises LT-IIa, LT-IIb and LT-IIc. The carbohydrate-binding specificities of LT-IIa, LT-IIb and LT-IIc are distinctive from those of cholera toxin and E. coli LT-I. Whereas CT and LT-I bind primarily to the GM1 ganglioside, LT-IIa binds to gangliosides GD1a, GD1b and GM1, LT-IIb binds to the GD1a and GT1b gangliosides, and LT-IIc binds to GM1, GM2, GM3 and GD1a. These previous studies of the binding properties of type II B-subunits have been focused on ganglio core chain gangliosides. To further define the carbohydrate binding specificity of LT-IIb B-subunits, we have investigated its binding to a collection of gangliosides and non-acid glycosphingolipids with different core chains. A high-affinity binding of LT-IIb B-subunits to gangliosides with a neolacto core chain, such as Neu5Gcα3- and Neu5Acα3-neolactohexaosylceramide, and Neu5Gcα3- and Neu5Acα3-neolactooctaosylceramide was detected. An LT-IIb-binding ganglioside was isolated from human small intestine and characterized as Neu5Acα3-neolactohexaosylceramide. The crystal structure of the B-subunit of LT-IIb with the pentasaccharide moiety of Neu5Acα3-neolactotetraosylceramide (Neu5Ac-nLT: Neu5Acα3Galβ4GlcNAcβ3Galβ4Glc) was determined providing the first information for a sialic-binding site in this subfamily, with clear differences from that of CT and LT-I.

Evaluation of an enzyme immunoassay kit for estrogen receptor measurement--report II.

1988 ◽  
Vol 34 (10) ◽  
pp. 2053-2057 ◽  
Author(s):  
S Raam ◽  
D M Vrabel
Keyword(s):  
Enzyme Immunoassay ◽  
Binding Sites ◽  
Solid Phase ◽  
Functional Characterization ◽  
Quantitative Agreement ◽  
Type I ◽  
Type Ii ◽  
Immunoreactive Protein ◽  
Estrogen Binding

Abstract We present evidence to show that monoclonal antibodies to estrogen receptors (ER) in solid phase recognize the secondary estrogen binding sites with moderate to low affinity for estradiol (E2). An excellent quantitative agreement was found in five cytosols between the ER values obtained by the enzyme immunoassay (ER-EIA) and the amount of secondary estrogen binding sites measured by the assay involving dextran-coated charcoal (Clin Chem 1986;32:1496). The immunoreactive protein recognized by the antibody-coated beads, when allowed to react with ER(+) cytosols, is shown to bind [3H]estradiol only when the ligand concentration exceeds 8 nmol/L. Further biochemical and functional characterization of the immunoreactive protein is required to establish similarities/dissimilarities between this protein, high-affinity Type I ER sites, and the secondary sites such as Type II sites.

Exploring the binding properties of agonists interacting with human TGR5 using structural modeling, molecular docking and dynamics simulations

RSC Advances ◽  
2015 ◽  
Vol 5 (19) ◽  
pp. 14202-14213 ◽  
Author(s):  
Thangaraj Sindhu ◽  
Pappu Srinivasan
Keyword(s):  
Molecular Docking ◽  
Binding Site ◽  
Type Ii Diabetes ◽  
Computational Study ◽  
Structural Modeling ◽  
Type Ii ◽  
Binding Properties ◽  
Pharmacological Target ◽  
Dynamics Simulations ◽  
Molecular Docking And Dynamics

TGR5, act as a potential pharmacological target in the treatment of type II diabetes. In the computational study, structural modeling and binding site prediction of TGR5 receptor was performed. Two well-known agonists of TGR5 used to investigate the mode and mechanism of binding.

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