Author: Anders Michael Näär
Publisher:
ISBN:
Category :
Languages : en
Pages : 426
Book Description
Molecular Mechanisms of Thyroid Hormone and Retinoid Receptor Transcriptional Regulation
Author: Anders Michael Näär
Publisher:
ISBN:
Category :
Languages : en
Pages : 426
Book Description
Publisher:
ISBN:
Category :
Languages : en
Pages : 426
Book Description
Analysis of the Molecular Mechanisms of DNA Recognition and Transcriptional Regulation by Nuclear Hormone Receptors
Author: Benjamin C. Lin
Publisher:
ISBN:
Category :
Languages : en
Pages : 234
Book Description
Publisher:
ISBN:
Category :
Languages : en
Pages : 234
Book Description
The Role of Isoform-specific Transcriptional Regulation in the Molecular Mechanisms of Resistance to Thyroid Hormone Syndrome (RTH)
Author: Wei Wan
Publisher:
ISBN:
Category :
Languages : en
Pages : 370
Book Description
Publisher:
ISBN:
Category :
Languages : en
Pages : 370
Book Description
Analysis of the Molecular Mechanisms of Isoform-specific Transcriptional Regulation by Thyroid Hormone Receptors
Author: Zhihong Yang
Publisher:
ISBN:
Category :
Languages : en
Pages : 238
Book Description
Publisher:
ISBN:
Category :
Languages : en
Pages : 238
Book Description
Thyroid Hormone Regulation of Gene Expression
Author: G.R. Williams
Publisher: Springer
ISBN:
Category : Medical
Languages : en
Pages : 160
Book Description
This book covers the historical perspective and physiological background of the role of thyroid hormones. In both specific target tissues and during development, it provides clinical perspectives and physiological and developmental implications of the interactions between retinoid and vitamin D3 signalling pathways.
Publisher: Springer
ISBN:
Category : Medical
Languages : en
Pages : 160
Book Description
This book covers the historical perspective and physiological background of the role of thyroid hormones. In both specific target tissues and during development, it provides clinical perspectives and physiological and developmental implications of the interactions between retinoid and vitamin D3 signalling pathways.
Analysis of the Molecular Basis of Transcriptional Regulation by Thyroid Hormone and Estrogen Receptors
Author: Jeffrey Morse Holloway
Publisher:
ISBN:
Category :
Languages : en
Pages : 390
Book Description
Publisher:
ISBN:
Category :
Languages : en
Pages : 390
Book Description
Nuclear Hormone Receptors
Author: Malcolm G. Parker
Publisher:
ISBN:
Category : Science
Languages : en
Pages : 434
Book Description
An overview of the supergene family made up of those nuclear hormone receptors which recognize thyroid and steroid hormones, vitamen D and retinoic acid and which are characterized by their ability to bind both ligands and the genes which respond to them.
Publisher:
ISBN:
Category : Science
Languages : en
Pages : 434
Book Description
An overview of the supergene family made up of those nuclear hormone receptors which recognize thyroid and steroid hormones, vitamen D and retinoic acid and which are characterized by their ability to bind both ligands and the genes which respond to them.
Molecular Analysis of Thyroid Hormone Receptors and Retinoic Acid Receptors
Author: Theresa Qui Phan
Publisher:
ISBN: 9781109662948
Category :
Languages : en
Pages :
Book Description
Thyroid hormone receptors (TRs) and retinoic acid receptors (RARs) are members of the nuclear hormone receptor family. These ligand-regulated transcription factors bind to specific DNA sequences, called response elements, as homodimers or heterodimers with retinoid-X receptor (RXR) and regulate specific target genes. In the absence of hormone, TR and RAR repress transcription by recruiting corepressor complexes. In the presence of hormone, a coactivator complex is recruited and results in transcriptional activation. TRs and RARs are highly structurally conserved and possess very similar DNA binding domains. Despite these similarities, these receptors bind to different response elements in the genome, regulate different target genes, and control distinct physiological processes. The work presented in this dissertation identifies the DNA recognition properties of TR and RAR that account for these receptors' response element binding specificity and, subsequently, their distinct physiological responses. While response elements based on the consensus half-site are high affinity binding sites for TR and RAR, they show poor specificity. In contrast, the variations in half-site sequence, flanking sequences, and spacing found in natural TR and RAR target genes generate response elements that are bound in vitro and transcriptionally activated in vivo in a receptor-specific manner. Not all DNA sequences that bind TR or RAR efficiently in vitro are able to confer transcriptional regulation in vivo; we provide evidence that auxiliary proteins in cells may destabilize the binding of nuclear receptors to improperly spaced response elements to generate an additional layer of receptor-specific target gene recognition.
Publisher:
ISBN: 9781109662948
Category :
Languages : en
Pages :
Book Description
Thyroid hormone receptors (TRs) and retinoic acid receptors (RARs) are members of the nuclear hormone receptor family. These ligand-regulated transcription factors bind to specific DNA sequences, called response elements, as homodimers or heterodimers with retinoid-X receptor (RXR) and regulate specific target genes. In the absence of hormone, TR and RAR repress transcription by recruiting corepressor complexes. In the presence of hormone, a coactivator complex is recruited and results in transcriptional activation. TRs and RARs are highly structurally conserved and possess very similar DNA binding domains. Despite these similarities, these receptors bind to different response elements in the genome, regulate different target genes, and control distinct physiological processes. The work presented in this dissertation identifies the DNA recognition properties of TR and RAR that account for these receptors' response element binding specificity and, subsequently, their distinct physiological responses. While response elements based on the consensus half-site are high affinity binding sites for TR and RAR, they show poor specificity. In contrast, the variations in half-site sequence, flanking sequences, and spacing found in natural TR and RAR target genes generate response elements that are bound in vitro and transcriptionally activated in vivo in a receptor-specific manner. Not all DNA sequences that bind TR or RAR efficiently in vitro are able to confer transcriptional regulation in vivo; we provide evidence that auxiliary proteins in cells may destabilize the binding of nuclear receptors to improperly spaced response elements to generate an additional layer of receptor-specific target gene recognition.
Molecular Mechanisms of Thyroid Hormone Receptor Activation
Author: Xiaohua Leng
Publisher:
ISBN:
Category :
Languages : en
Pages : 440
Book Description
Publisher:
ISBN:
Category :
Languages : en
Pages : 440
Book Description
Analysis of the Molecular Mechanisms of Action of the V-erbA Oncogene and the Retinoid X Receptors (RXRs)
Author: Hong-Wu Chen
Publisher:
ISBN:
Category :
Languages : en
Pages : 322
Book Description
Publisher:
ISBN:
Category :
Languages : en
Pages : 322
Book Description