Novel FXXFF and FXXMF motifs in androgen receptor cofactors mediate high affinity and specific interactions with the ligand-binding domain (Q83323002)

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21 January 2020

title

Novel FXXFF and FXXMF motifs in androgen receptor cofactors mediate high affinity and specific interactions with the ligand-binding domain (English)

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21 January 2020

2

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21 January 2020

Ashley Pike

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21 January 2020

author name string

Dennis J van de Wijngaart

1

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21 January 2020

Remko Hersmus

3

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21 January 2020

Adriaan B Houtsmuller

5

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21 January 2020

Guido Jenster

6

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Jan Trapman

7

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Hendrikus J Dubbink

8

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language of work or name

English

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publication date

11 May 2006

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Journal of Biological Chemistry

21 January 2020

published in

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21 January 2020

volume

281

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issue

28

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page(s)

19407-19416

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Endocrine mechanisms of disease: Expression and degradation of androgen receptor: mechanism and clinical implication

21 January 2020

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Differential interaction of steroid hormone receptors with LXXLL motifs in SRC-1a depends on residues flanking the motif

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Distinct recognition modes of FXXLF and LXXLL motifs by the androgen receptor

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The Use of Phage Display Technique for the Isolation of Androgen Receptor Interacting Peptides with (F/W)XXL(F/W) and FXXLY New Signature Motifs

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Evaluation of ligand-dependent changes in AR structure using peptide probes

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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

21 January 2018

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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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Androgen-induced NH2- and COOH-terminal Interaction Inhibits p160 coactivator recruitment by activation function 2.

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Dependence of selective gene activation on the androgen receptor NH2- and COOH-terminal interaction

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Dual function of an amino-terminal amphipatic helix in androgen receptor-mediated transactivation through specific and nonspecific response elements

21 January 2018

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The FXXLF motif mediates androgen receptor-specific interactions with coregulators

21 January 2018

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Functional domain and motif analyses of androgen receptor coregulator ARA70 and its differential expression in prostate cancer

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Human checkpoint protein hRad9 functions as a negative coregulator to repress androgen receptor transactivation in prostate cancer cells

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The androgen receptor gene mutations database (ARDB): 2004 update

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Identifiers

DOI

10.1074/JBC.M602567200

1 reference

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21 January 2020

1 reference