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Shaoqian Zhao, Wen Liu, Jiqiu Wang, Juan Shi, Yingkai Sun, Weiqing Wang, Guang Ning, Ruixin Liu and Jie Hong

for 15 min at 1000  g , 4°C, and plasma was isolated and stored at −80°C for subsequent biochemical testing, and plasma LBP (Abnova, KA4302) and leptin (Millipore, EZML-82K) levels were measured using a commercial ELISA kit. Inguinal fat, epididymal

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V Vivat, D Gofflo, T Garcia, J-M Wurtz, W Bourguet, D Philibert and H Gronemeyer


The natural ligands of the progesterone (PR) and androgen (AR) receptors, progesterone and testosterone, differ only by their 17β-substitution. To identify within the AR and PR ligand-binding domains (LBDs) the sequences responsible for the differential recognition of these ligands, chimeric LBDs assembled from five homologous AR/PR 'cassettes' linked to the GAL4-DNA binding domain were constructed, and their ligand binding and transactivation characteristics were determined. Replacing the central cassette 3 of PR by that of AR generated a progesterone- and testosterone-responsive PR LBD with the AR residues 788-RHLS-791 being specifically involved in testosterone recognition, while the introduction of the C-terminal PR cassette 5 into AR conferred progestin responsiveness onto the AR LBD. These results suggest that residues within AR 788-RHLS-791 interact with the testosterone 17β-OH, while PR cassette 5 apparently contains the amino acid(s) specifically involved in the recognition of the progesterone 17β-acetyl group. However, ligand binding and transactivation by these chimeras were significantly decreased compared with those of the parental LBDs, indicating that residues located outside of these cassettes contribute to the proper positioning of the steroids in the AR and PR ligand-binding pockets (LBPs). Indeed, certain AR/PR chimeras acquired efficient ligand binding, but were unable to transactivate, indicating that the ligand was improperly bound in the chimeric LBP and could not induce the conformational changes leading to a transcriptionally competent activation function (AF-2) within the LBD. The properties of the various LBD chimeras are discussed in view of the recently solved three-dimensional structures of the retinoid X receptor α apo- and retinoic acid receptor γ holo-LBDs.

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Ana Luísa Neves, João Coelho, Luciana Couto, Adelino Leite-Moreira and Roberto Roncon-Albuquerque Jr

(TIR domain) ( Chow et al . 1999 ). The LPS-sensing machinery is constituted primarily by a LPS-binding protein (LBP), a glycosylphosphatidylinositol-anchored monocyte differentiation antigen (cluster of differentiation 14 (CD14)), an accessory protein

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Shannon E Mullican, Joanna R DiSpirito and Mitchell A Lazar

reported to bind and enhance the repressive function of SHP ( Miao et al . 2011 , Ehrlund & Treuter 2012 ). Indeed, a crystal structure study of DAX1 demonstrated a ligand-binding pocket (LBP) filled with amino acid side chains, suggesting typical ligand

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H Watanabe, A Suzuki, M Goto, S Ohsako, C Tohyama, H Handa and T Iguchi

1.0 1.9 2.5 LBP gene; LPS-binding protein M31885 1.0 0.9 2.5 helix-loop-helix DNA binding

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D J Flint, M Boutinaud, C B A Whitelaw, G J Allan and A F Kolb

of the mouse mammary gland is associated with an immune cascade and an acute-phase response, involving LBP, CD14 and STAT3. Breast Cancer Research 6 R75 –R91. Thomasset N , Lochter A, Sympson CJ, Lund LR, Williams DR

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Alexander Kot, Zhendong A Zhong, Hongliang Zhang, Yu-An Evan Lay, Nancy E Lane and Wei Yao

, Blnk, Btk, Ccl4, Cd14, Cxcl2, Cxcl12, Icam1, Il1b, Il1r1, Lbp, Lyn, Nfkbia, Plcg2, Prkcb, Prkcq, Syk, Ticam2, Tnf, Tnfaip3, Tnfrsf11a, Tnfsf11, Tnfsf13b, Tnfsf14, Traf1, Vcam1 1.04E-01 5.13E-18 TNF signaling Csf1, Rps6ka4 Bcl3, Birc3, Ccl2

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Amelia J Brennan, Julie A Sharp, Christophe M Lefèvre and Kevin R Nicholas

Duffy MA Heath VJ Bell AK Ferrier RK Sandilands GP Gusterson BA 2004 Involution of the mouse mammary gland is associated with an immune cascade and an acute-phase response, involving LBP, CD14 and STAT3 . Breast Cancer Research 6 R75