Search Results

You are looking at 1 - 10 of 955 items for :

  • "structure" x
  • Refine by Access: All content x
Clear All
Free access

Ulrich Schweizer and Clemens Steegborn

potential drugs for the treatment of some forms of hyperthyroidism, hypothyroidism, and cancer ( Manna et al . 2013 , Ciavardelli et al . 2014 ). We will review the reaction mechanism, regulation and molecular structure of deiodinases based on the

Free access

Fraydoon Rastinejad

Introduction The retinoic acid receptors (RARs) and retinoid X receptors (RXRs) are the earliest and most intensely studied nuclear receptors (NRs) for their three-dimensional (3D) structures. Both receptor groups bind to retinoic acids (RAs

Open access

Ricardo Núñez Miguel, Paul Sanders, Lloyd Allen, Michele Evans, Matthew Holly, William Johnson, Andrew Sullivan, Jane Sanders, Jadwiga Furmaniak, and Bernard Rees Smith

receptor’s leucine-rich-repeat domain (LRD, amino acids 22–279). The crystal structures of the human TSHR LRD (amino acids, 22–260; TSHR260) bound to the thyroid-stimulating human monoclonal autoantibody (MAB) M22™ ( Sanders et al. 2003 ) and the blocking

Open access

Stuart Baker, Ricardo Núñez Miguel, Daniel Thomas, Michael Powell, Jadwiga Furmaniak, and Bernard Rees Smith

consisting of an N-terminal domain, peroxidase domain (POD), complement control protein (CCP)-like domain, epidermal growth factor (EGF)-like domain and the transmembrane domain with a cytoplasmic tail ( Ruf & Carayon 2006 ). To date, the structure of TPO

Free access

Jennifer Miller-Gallacher, Paul Sanders, Stuart Young, Andrew Sullivan, Stuart Baker, Samuel C Reddington, Matthew Clue, Katarzyna Kabelis, Jill Clark, Jane Wilmot, Daniel Thomas, Monika Chlebowska, Francesca Cole, Emily Pearson, Emma Roberts, Matthew Holly, Michele Evans, Ricardo Núñez Miguel, Michael Powell, Jane Sanders, Jadwiga Furmaniak, and Bernard Rees Smith

, Evans et al. 2010 ). The crystal structures of residues 22–260 of wild-type (WT) TSHR (TSHR260; comprising most of the LRD) in complex with the antigen-binding fragments (Fab) of both a stimulating human monoclonal autoantibody (mAb), M22 TM

Free access

Paul Sanders, Stuart Young, Jane Sanders, Katarzyna Kabelis, Stuart Baker, Andrew Sullivan, Michele Evans, Jill Clark, Jane Wilmot, Xiaoling Hu, Emma Roberts, Michael Powell, Ricardo Núñez Miguel, Jadwiga Furmaniak, and Bernard Rees Smith

TSHR–autoantibody interaction, and in the case of thyroid-stimulating autoantibodies, the crystal structure of a human monoclonal autoantibody (M22) in complex with the TSHR (amino acids 22–260; TSHR260) has been determined at 2.55 Å resolution

Free access

Kjersti M Aagaard-Tillery, Kevin Grove, Jacalyn Bishop, Xingrao Ke, Qi Fu, Robert McKnight, and Robert H Lane

reprograming of gene expression via alterations in the chromatin structure (epigenetic regulation). We and other researchers have previously demonstrated that uteroplacental insufficiency and IUGR in the rat results in covalent modifications of chromatin

Free access

Bjarne Faurholm, Shaun Cochrane, Robert R Millar, and Arieh A Katz

chimpanzee (GenBank accession number NW_102275.1) only the genes encoding the type II GnRH-R have been sequenced and their coding regions predicted. The type II GnRH-R genes comprise of three exons and have the same gene structure as the type I GnRH-Rs. The

Free access

Andrew P Trotta, Eleanor F Need, Lisa M Butler, Luke A Selth, Melissa A O'Loughlin, Gerhard A Coetzee, Wayne D Tilley, and Grant Buchanan

for 10 s. Secondary structure prediction, residue composition, and logo creation The nnpredict online server (∼nomi/nnpredict.html ; Katzman et al . 2008 ) was used to define potential alpha helical and beta sheet structural

Free access

Jyotsna B Pippal and Peter J Fuller

and functional aspects of the MR. Mineralocorticoid receptor structure The human MR gene has been mapped to chromosome 4 in the q31.1–q31.2 region ( Fan et al . 1989 , Morrison et al . 1990 ). The MR gene spans over ∼450 kilobases and is