Amino acids 3-13 and amino acids in and flanking the 23FxxLF27 motif modulate the interaction between the N-terminal and ligand-binding domain of the androgen receptor (Q38360677)

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English	Amino acids 3-13 and amino acids in and flanking the 23FxxLF27 motif modulate the interaction between the N-terminal and ligand-binding domain of the androgen receptor	scientific article

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Europe PubMed Central

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2 September 2017

Amino acids 3-13 and amino acids in and flanking the 23FxxLF27 motif modulate the interaction between the N-terminal and ligand-binding domain of the androgen receptor (English)

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Europe PubMed Central

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2 September 2017

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Karine Steketee

1

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Europe PubMed Central

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2 September 2017

Cor A Berrevoets

2

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Europe PubMed Central

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2 September 2017

Hendrikus J Dubbink

3

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Europe PubMed Central

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2 September 2017

Paul Doesburg

4

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Europe PubMed Central

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2 September 2017

Remko Hersmus

5

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Europe PubMed Central

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2 September 2017

Albert O Brinkmann

6

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2 September 2017

Jan Trapman

7

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2 September 2017

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publication date

1 December 2002

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2 September 2017

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2 September 2017

269

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2 September 2017

23

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Europe PubMed Central

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2 September 2017

5780-5791

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Europe PubMed Central

PubMed publication ID

2 September 2017

The nuclear receptor superfamily: the second decade

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The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors.

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Estrogen receptor activation function 1 works by binding p160 coactivator proteins

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Synergy between estrogen receptor alpha activation functions AF1 and AF2 mediated by transcription intermediary factor TIF2.

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The androgen receptor amino-terminal domain plays a key role in p160 coactivator-stimulated gene transcription

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The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1

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Domains of the Human Androgen Receptor Involved in Steroid Binding, Transcriptional Activation, and Subcellular Localization

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FXXLF and WXXLF sequences mediate the NH2-terminal interaction with the ligand binding domain of the androgen receptor

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The human androgen receptor: domain structure, genomic organization and regulation of expression.

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Identification of two transcription activation units in the N-terminal domain of the human androgen receptor

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Synergism between androgens and protein kinase-C on androgen-regulated gene expression

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Ligand-induced conformational alterations of the androgen receptor analyzed by limited trypsinization. Studies on the mechanism of antiandrogen action

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Amphipathic helix motif: classes and properties

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Mechanism of corepressor binding and release from nuclear hormone receptors.

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The alpha-helical FXXPhiPhi motif in p53: TAF interaction and discrimination by MDM2

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Evolution of the androgen receptor: structure-function implications

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A signature motif in transcriptional co-activators mediates binding to nuclear receptors

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Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation

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Hormone-dependent coactivator binding to a hydrophobic cleft on nuclear receptors

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1 reference

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NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors

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The orphan nuclear receptor SHP utilizes conserved LXXLL-related motifs for interactions with ligand-activated estrogen receptors

1 reference

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Characterization of the interaction between androgen receptor and a new transcriptional inhibitor, SHP.

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The FXXLF motif mediates androgen receptor-specific interactions with coregulators

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Domain interactions between coregulator ARA(70) and the androgen receptor (AR).

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Activation Function 2 in the Human Androgen Receptor Ligand Binding Domain Mediates Interdomain Communication with the NH2-terminal Domain

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Intermolecular NH2-/carboxyl-terminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity

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10.1046/J.1432-1033.2002.03276.X

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

ResearchGate publication ID

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