(Q34049353)

English

Binding-folding induced regulation of AF1 transactivation domain of the glucocorticoid receptor by a cofactor that binds to its DNA binding domain

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Binding-folding induced regulation of AF1 transactivation domain of the glucocorticoid receptor by a cofactor that binds to its DNA binding domain (English)

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

author name string

Anna S Garza

1

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Shagufta H Khan

2

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Carmen M Moure

3

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Dean P Edwards

4

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Raj Kumar

5

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

language of work or name

0 references

publication date

7 October 2011

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

6

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

10

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

e25875

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

copyright license

Creative Commons Attribution 4.0 International

7 October 2011

1 reference

April 2022 Public Data File from Crossref

copyright status

0 references

TBP binding-induced folding of the glucocorticoid receptor AF1 domain facilitates its interaction with steroid receptor coactivator-1

1 reference

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The glucocorticoid receptor and the coregulator Brm selectively modulate each other's occupancy and activity in a gene-specific manner

1 reference

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Naturally occurring osmolyte, trehalose induces functional conformation in an intrinsically disordered activation domain of glucocorticoid receptor

1 reference

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5 July 2018

Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor

1 reference

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5 July 2018

A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain

1 reference

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5 July 2018

DNA Binding Site Sequence Directs Glucocorticoid Receptor Structure and Activity

1 reference

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Multi-modulation of nuclear receptor coactivators through posttranslational modifications

1 reference

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5 July 2018

Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins

1 reference

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5 July 2018

Structure of the progesterone receptor-deoxyribonucleic acid complex: novel interactions required for binding to half-site response elements

1 reference

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Intrinsic disorder in transcription factors

1 reference

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Activation function 1 of glucocorticoid receptor binds TATA-binding protein in vitro and in vivo.

1 reference

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Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism

1 reference

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Gene regulation by the glucocorticoid receptor: structure:function relationship

1 reference

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Intrinsically unstructured proteins and their functions

1 reference

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Natively unfolded proteins

1 reference

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TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain.

1 reference

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5 July 2018

Overview of the structural basis for transcription regulation by nuclear hormone receptors

1 reference

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Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

1 reference

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5 July 2018

Target-specific utilization of transcriptional regulatory surfaces by the glucocorticoid receptor

1 reference

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DNA binding of nuclear hormone receptors influences their structure and function

1 reference

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Partial oncogenic transformation of chicken embryo fibroblasts by Jun dimerization protein 2, a negative regulator of TRE- and CRE-dependent transcription

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5 July 2018

Transactivation functions of the N-terminal domains of nuclear hormone receptors: protein folding and coactivator interactions

1 reference

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Intrinsic disorder in cell-signaling and cancer-associated proteins

1 reference

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Intrinsically unstructured proteins

1 reference

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Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition

1 reference

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Jun dimerization protein 2 functions as a progesterone receptor N-terminal domain coactivator

1 reference

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JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells

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Natively unfolded proteins: a point where biology waits for physics

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Identification of mouse Jun dimerization protein 2 as a novel repressor of ATF-2

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The structure of the nuclear hormone receptors

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Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor tau 1-core activation domain and target factors

1 reference

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Protein-protein interactions are implied in glucocorticoid receptor mutant 465*-mediated cell death

1 reference

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Role of the Ada adaptor complex in gene activation by the glucocorticoid receptor

1 reference

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RARs and RXRs: evidence for two autonomous transactivation functions (AF-1 and AF-2) and heterodimerization in vivo

1 reference

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Steroid receptor regulated transcription of specific genes and gene networks

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Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors

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Colocalization of DNA-binding and transcriptional activation functions in the human glucocorticoid receptor

1 reference

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1 reference

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1 reference

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Glucocorticoid receptor mutants that define a small region sufficient for enhancer activation

1 reference

https://pubmed.ncbi.nlm.nih.gov/22003412

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Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement

1 reference

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Identifiers

10.1371/JOURNAL.PONE.0025875

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

2011PLoSO...625875G

0 references

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

ResearchGate publication ID

0 references

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