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Cited by 231

The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.

Diverse roles of androgen receptor (AR) domains in AR-mediated signaling

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Claessens, Frank, Denayer, Sarah, Van Tilborgh, Nora, Kerkhofs, Stefanie, Helsen, Christine, Haelens, Annemie·2008·Nuclear Receptor Signaling
DOI 10.1621/nrs.06008
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Abstract

Androgens control male sexual development and maintenance of the adult male phenotype. They have very divergent effects on their target organs like the reproductive organs, muscle, bone, brain and skin. This is explained in part by the fact that different cell types respond differently to androgen stimulus, even when all these responses are mediated by the same intracellular androgen receptor. To understand these tissue- and cell-specific readouts of androgens, we have to learn the many different steps in the transcription activation mechanisms of the androgen receptor (NR3C4). Like all nuclear receptors, the steroid receptors have a central DNA-binding domain connected to a ligand-binding domain by a hinge region. In addition, all steroid receptors have a relatively large amino-terminal domain. Despite the overall structural homology with other nuclear receptors, the androgen receptor has several specific characteristics which will be discussed here. This receptor can bind two types of androgen response elements (AREs): one type being similar to the classical GRE/PRE-type elements, the other type being the more divergent and more selective AREs. The hormone-binding domain has low intrinsic transactivation properties, a feature that correlates with the low affinity of this domain for the canonical LxxLL-bearing coactivators. For the androgen receptor, transcriptional activation involves the alternative recruitment of coactivators to different regions in the amino-terminal domain, as well as the hinge region. Finally, a very strong ligand-induced interaction between the amino-terminal domain and the ligand-binding domain of the androgen receptor seems to be involved in many aspects of its function as a transcription factor. This review describes the current knowledge on the structure-function relationships within the domains of the androgen receptor and tries to integrate the involvement of different domains, subdomains and motifs in the functioning of this receptor as a transcription factor with tissue- and cell-specific readouts.

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Research works printed but not linked: 110

  1. 10.1210/mend-5-11-1587 · DOI
  2. 10.1128/MCB.13.10.6326 · DOI
  3. 10.1074/jbc.M703268200 · DOI · Paper page
  4. 10.1621/nrs.06001 · DOI · Paper page
  5. 10.1210/mend.12.8.0153 · doi:10.1210/mend.12.8.0153 · Paper page
  6. 10.1677/jme.0.0310427 · DOI
  7. 10.1016/j.tem.2005.09.006 · DOI
  8. 10.1128/MCB.19.12.8383 · DOI · Paper page
  9. 10.1128/MCB.01170-07 · DOI
  10. 10.1101/gad.1564207 · DOI · Paper page
  11. 10.1158/0008-5472.CAN-07-1646 · DOI
  12. 10.1093/hmg/ddh181 · DOI · Paper page
  13. 10.1210/me.2004-0266 · DOI
  14. 10.1210/me.2003-0313 · DOI
  15. 10.1074/jbc.M210744200 · DOI
  16. 10.1016/S0006-291X(03)00902-1 · DOI
  17. 10.1016/S0090-4295(01)01401-7 · DOI
  18. 10.1074/jbc.271.43.26772 · DOI
  19. 10.1093/nar/22.15.3181 · DOI · Paper page
  20. 10.1128/MCB.19.12.8226 · DOI · Paper page
  21. 10.1074/jbc.M209322200 · DOI
  22. 10.1016/S0960-0760(00)00154-0 · DOI · Paper page
  23. 10.1016/0303-7207(90)90225-W · DOI
  24. 10.1242/jcs.022103 · DOI · Paper page
  25. 10.1002/j.1460-2075.1992.tb05141.x · DOI · Paper page
  26. 10.1210/me.2007-0223 · DOI · Paper page
  27. 10.1002/pros.20128 · DOI
  28. 10.1073/pnas.0708036104 · DOI · Paper page
  29. 10.1126/science.3283939 · DOI · Paper page
  30. 10.1016/j.biopha.2006.07.082 · DOI · Paper page
  31. 10.1016/S0303-7207(02)00104-1 · DOI
  32. 10.1128/MCB.23.23.8563-8575.2003 · DOI · Paper page
  33. 10.1074/jbc.M000660200 · DOI · Paper page
  34. 10.1016/j.drudis.2007.01.003 · DOI · Paper page
  35. 10.1074/jbc.M602561200 · DOI
  36. 10.1074/jbc.M203423200 · DOI · Paper page
  37. 10.1210/me.2005-0351 · DOI · Paper page
  38. 10.1042/bj20020912 · DOI
  39. 10.1093/nar/16.12.5263 · DOI · Paper page
  40. 10.1074/jbc.M008207200 · DOI
  41. 10.1073/pnas.0408925102 · DOI · Paper page
  42. 10.1074/jbc.274.52.37219 · DOI · Paper page
  43. 10.1074/jbc.M403117200 · DOI
  44. 10.1210/me.2005-0479 · DOI
  45. 10.1074/jbc.M002807200 · DOI · Paper page
  46. 10.1016/j.molcel.2004.09.036 · DOI · Paper page
  47. 10.1074/jbc.M111975200 · DOI · Paper page
  48. 10.1371/journal.pbio.0020274 · DOI · Paper page
  49. 10.1074/jbc.272.47.29821 · DOI · Paper page
  50. 10.1128/MCB.20.16.6040-6050.2000 · DOI · Paper page
  51. 10.1093/hmg/9.2.267 · DOI · Paper page
  52. 10.1074/jbc.270.13.7341 · DOI · Paper page
  53. 10.1074/jbc.M209074200 · DOI · Paper page
  54. Kasper S., 1994, J Biol Chem, 269, 31763, 10.1016/S0021-9258(18)31761-7 · DOI
  55. 10.1128/MCB.01297-06 · DOI
  56. 10.1073/pnas.92.26.12314 · DOI · Paper page
  57. 10.1038/352077a0 · DOI · Paper page
  58. 10.1016/j.bcp.2006.05.024 · DOI
  59. 10.1210/me.2005-0298 · DOI
  60. 10.1074/jbc.M206374200 · DOI · Paper page
  61. 10.1128/MCB.25.6.2200-2215.2005 · DOI
  62. Link K. A., Cancer Res
  63. 10.1074/jbc.M204751200 · DOI
  64. 10.1016/j.cell.2008.01.018 · DOI · Paper page
  65. 10.1128/MCB.19.9.6164 · DOI · Paper page
  66. 10.1074/jbc.M004571200 · DOI · Paper page
  67. 10.1073/pnas.94.16.8485 · DOI · Paper page
  68. 10.1621/nrs.05001 · DOI
  69. 10.1016/S0092-8674(03)00934-6 · DOI · Paper page
  70. Metivier R., 2001, Mol Endocrinol, 15, 1953
  71. 10.1093/emboj/cdg023 · DOI
  72. 10.1042/BJ20071352 · DOI
  73. 10.1007/s00439-002-0776-5 · DOI
  74. 10.1016/S0955-0674(98)80015-X · DOI · Paper page
  75. 10.1210/mend.13.12.0396 · doi:10.1210/mend.13.12.0396 · Paper page
  76. 10.1016/j.cell.2008.01.051 · DOI
  77. 10.1074/jbc.271.39.24151 · DOI · Paper page
  78. 10.1073/pnas.97.26.14145 · DOI · Paper page
  79. Rennie P. S., 1993, Mol Endocrinol, 7, 23
  80. 10.1210/me.2005-0511 · DOI
  81. 10.1073/pnas.081565498 · DOI · Paper page
  82. 10.1073/pnas.0610814104 · DOI
  83. 10.1074/jbc.275.16.12290 · DOI
  84. 10.1042/bj3410515 · DOI · Paper page
  85. 10.1038/348458a0 · DOI · Paper page
  86. 10.1093/emboj/21.9.2242 · DOI
  87. 10.1515/BC.2005.009 · DOI
  88. 10.1038/sj.pcan.4500967 · DOI
  89. 10.1046/j.1432-1033.2002.03276.x · DOI
  90. 10.1196/annals.1329.068 · DOI
  91. 10.1002/jcb.10653 · DOI · Paper page
  92. 10.1210/mend.13.6.0300 · doi:10.1210/mend.13.6.0300 · Paper page
  93. 10.1074/jbc.M311761200 · DOI
  94. Tilley W. D., 1996, Clin Cancer Res, 2, 277
  95. 10.1210/me.2006-0228 · doi:10.1210/me.2006-0228
  96. 10.1074/jbc.M602567200 · DOI
  97. 10.1083/jcb.200609178 · DOI · Paper page
  98. 10.1210/mend.13.9.0347 · DOI
  99. 10.1074/jbc.275.16.12298 · DOI
  100. 10.1016/S1096-7192(03)00003-9 · DOI · Paper page
  101. 10.1042/BST0341089 · DOI
  102. 10.1016/j.molcel.2007.05.041 · DOI · Paper page
  103. 10.1210/mend.12.10.0185 · doi:10.1210/mend.12.10.0185 · Paper page
  104. 10.1210/jc.2006-0372 · DOI
  105. 10.1074/jbc.M609360200 · DOI · Paper page
  106. 10.1172/JCI28773. · DOI · Paper page
  107. Zhou Z. X., 1994, J Biol Chem, 269, 13115, 10.1016/S0021-9258(17)36806-0 · DOI · Paper page
  108. 10.1016/j.cell.2005.12.032 · DOI · Paper page
  109. Zilliacus J., 1995, Mol Endocrinol, 9, 389
  110. 10.1111/j.1365-2265.2007.03069.x · DOI

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Metadata

Authors
Claessens, F., Denayer, S., Van Tilborgh, N., Kerkhofs, S., Helsen, C., & Haelens, A.
Venue
Nuclear Receptor Signaling
Publisher
SAGE Publications
Published
2008-01
Volume
6
Issue
1
Pages
e008-e008
ISSN
1550-7629 (ISSN-L)
DOI
10.1621/nrs.06008
OpenAlex
W2069741812
Cited by
231
References
13
FWCI
14.75
Type
journal article
Language
en
Open access
hybrid
Licence
journals.sagepub.com/page/policies/text-and-data-mining-license (tdm)

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