Glucocorticoid receptor: Wikis

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Nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor)

Crystallographic structures of the glucocorticoid receptor DNA binding domain (DBD, left, PDB 1R4O bound to DNA) and ligand binding domain [LBD, right, 1M2Z bound to dexamethasone (white sticks) and the TIF2 coactivator protein (red)]. Dashed yellow lines represent hydrogen bonding interactions between the receptor and ligand. The 2D structure of dexamethasone is also depicted in the lower right hand side of the picture for reference.
Available structures
1gdc, 1glu, 1m2z, 1nhz, 1p93, 1r4o, 1r4r, 1rgd, 2gda
Identifiers
Symbols NR3C1; GCCR; GCR; GR; GRL
External IDs OMIM138040 MGI95824 HomoloGene30960 GeneCards: NR3C1 Gene
RNA expression pattern
PBB GE NR3C1 216321 s at tn.png
PBB GE NR3C1 201865 x at tn.png
PBB GE NR3C1 201866 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 2908 14815
Ensembl ENSG00000113580 ENSMUSG00000024431
UniProt P04150 Q05DD1
RefSeq (mRNA) NM_000176 NM_008173
RefSeq (protein) NP_000167 NP_032199
Location (UCSC) Chr 5:
142.64 - 142.8 Mb
Chr 18:
39.54 - 39.62 Mb
PubMed search [1] [2]

The glucocorticoid receptor (GR, or GCR) also known as NR3C1 (nuclear receptor subfamily 3, group C, member 1) is the receptor that cortisol and other glucocorticoids bind to.

The GR is expressed in almost every cell in the body and regulates genes controlling the development, metabolism, and immune response. Because the receptor gene is expressed in several forms, it has many different (pleiotropic) effects in different parts of the body.

When the GR binds to glucorticoids, its primary mechanism of action is the regulation of gene transcription.[1][2] The unbound receptor resides in the cytosol of the cell (the part of the cell outside of the nucleus). After the receptor is bound to glucocorticoid, the receptor-glucorticoid complex can take either of two paths. The activated GR complex up-regulates the expression of anti-inflammatory proteins in the nucleus or represses the expression of pro-inflammatory proteins in the cytosol (by preventing the translocation of other transcription factors from the cytosol into the nucleus).

The GR protein is encoded by gene NR3C1 on chromosome 5 (5q31).

Contents

Structure

Like the other steroid receptors,[3] the glucocorticoid receptor is modular in structure[4] and contains the following domains (labeled A - F):

Ligand binding and response

In the absence of hormone, the glucocorticoid receptor (GR) resides in the cytosol complexed with a variety of proteins including heat shock protein 90 (hsp90), the heat shock protein 70 (hsp70) and the protein FKBP52 (FK506-binding protein 52).[5] The endogenous glucocorticoid hormone cortisol diffuses through the cell membrane into the cytoplasm and binds to the glucocorticoid receptor (GR) resulting in release of the heat shock proteins. The resulting activated form GR has two principal mechanisms of action, transactivation and transrepression,[6][7] described below.

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Transactivation

A direct mechanism of action involves homodimerization of the receptor, translocation via active transport into the nucleus, and binding to specific DNA responsive elements activating gene transcription. This mechanism of action is referred to as transactivation. The biologic response depends on the cell type.

Transrepression

In the absence of activated GR, other transcription factors such as NF-κB or AP-1 themselves are able to transactivate target genes. However activated GR can complex with these other transcription factors and prevent them from binding their target genes and hence repress the expression of genes that are normally upregulated by NF-κB or AP-1. This indirect mechanism of action is referred to as transrepression.

Clinical significance

The GR is abnormal in familial glucocorticoid resistance.[8]

Agonists and antagonists

Dexamethasone is an agonist, and RU486 and cyproterone are antagonists of the GR. Also, progesterone and DHEA have antagonist effects on the GR.

Interactions

Glucocorticoid receptor has been shown to interact with Thioredoxin,[9] MED14,[10] CREB binding protein,[11] Nuclear receptor coactivator 2,[12][13] HNRPU,[14] POU2F1,[15][16][17] STAT5B,[18] RELA,[19][20][21] Nuclear receptor co-repressor 1,[22][23] TRIM28,[24] Nuclear receptor coactivator 3,[25][12] NRIP1,[26][12][27] CEBPB,[28] Mothers against decapentaplegic homolog 3,[29][30] Mineralocorticoid receptor,[31] Death associated protein 6,[32] STAT3,[33][34] DAP3,[35] Heat shock protein 90kDa alpha (cytosolic), member A1,[36][35][37][38][39][40][41] RANBP9,[42] MED1,[12][10] Nuclear receptor coactivator 1,[12][43] BAG1,[44][45] SMARCD1,[25] SMARCA4[25][46] and YWHAH.[47]

References

  1. ^ Lu NZ, Wardell SE, Burnstein KL, Defranco D, Fuller PJ, Giguere V, Hochberg RB, McKay L, Renoir JM, Weigel NL, Wilson EM, McDonnell DP, Cidlowski JA (2006). "International Union of Pharmacology. LXV. The pharmacology and classification of the nuclear receptor superfamily: glucocorticoid, mineralocorticoid, progesterone, and androgen receptors". Pharmacol Revl 58 (4): 782–97. doi:10.1124/pr.58.4.9. PMID 17132855.   [Free full text]
  2. ^ Rhen T, Cidlowski JA (October 2005). "Antiinflammatory action of glucocorticoids--new mechanisms for old drugs". N. Engl. J. Med. 353 (16): 1711–23. doi:10.1056/NEJMra050541. PMID 16236742.  
  3. ^ Kumar R, Thompson EB (1999). "The structure of the nuclear hormone receptors". Steroids 64 (5): 310–9. doi:10.1016/S0039-128X(99)00014-8. PMID 10406480.  
  4. ^ Kumar R, Thompson EB (2005). "Gene regulation by the glucocorticoid receptor: structure:function relationship". J. Steroid Biochem. Mol. Biol. 94 (5): 383–94. doi:10.1016/j.jsbmb.2004.12.046. PMID 15876404.  
  5. ^ Pratt WB, Morishima Y, Murphy M, Harrell M (2006). "Chaperoning of glucocorticoid receptors". Handb Exp Pharmacol 172: 111–38. doi:10.1007/3-540-29717-0_5. PMID 16610357.  
  6. ^ Buckingham JC (2006). "Glucocorticoids: exemplars of multi-tasking". Br J Pharmacol 147 (Supplement 1): S258–68. doi:10.1038/sj.bjp.0706456. PMID 16402112.  
  7. ^ Hayashi R, Wada H, Ito K, Adcock IM (2004). "Effects of glucocorticoids on gene transcription". Eur J Pharmacol 500 (1-3): 51–62. doi:10.1016/j.ejphar.2004.07.011. PMID 15464020.  
  8. ^ Mendonca B, Leite M, de Castro M, Kino T, Elias L, Bachega T, Arnhold I, Chrousos G, Latronico A (2002). "Female pseudohermaphroditism caused by a novel homozygous missense mutation of the GR gene". J Clin Endocrinol Metab 87 (4): 1805–9. doi:10.1210/jc.87.4.1805. PMID 11932321.  
  9. ^ Makino, Y; Yoshikawa N, Okamoto K, Hirota K, Yodoi J, Makino I, Tanaka H (Jan. 1999). "Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function". J. Biol. Chem. (UNITED STATES) 274 (5): 3182–8. ISSN 0021-9258. PMID 9915858.  
  10. ^ a b Hittelman, A B; Burakov D, Iñiguez-Lluhí J A, Freedman L P, Garabedian M J (Oct. 1999). "Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins". EMBO J. (ENGLAND) 18 (19): 5380–8. doi:10.1093/emboj/18.19.5380. ISSN 0261-4189. PMID 10508170.  
  11. ^ Almlöf, T; Wallberg A E, Gustafsson J A, Wright A P (Jun. 1998). "Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor tau 1-core activation domain and target factors". Biochemistry (UNITED STATES) 37 (26): 9586–94. doi:10.1021/bi973029x. ISSN 0006-2960. PMID 9649342.  
  12. ^ a b c d e Zilliacus, J; Holter E, Wakui H, Tazawa H, Treuter E, Gustafsson J A (Apr. 2001). "Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140". Mol. Endocrinol. (United States) 15 (4): 501–11. ISSN 0888-8809. PMID 11266503.  
  13. ^ Bledsoe, Randy K; Montana Valerie G, Stanley Thomas B, Delves Chris J, Apolito Christopher J, McKee David D, Consler Thomas G, Parks Derek J, Stewart Eugene L, Willson Timothy M, Lambert Millard H, Moore John T, Pearce Kenneth H, Xu H Eric (Jul. 2002). "Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition". Cell (United States) 110 (1): 93–105. ISSN 0092-8674. PMID 12151000.  
  14. ^ Eggert, M; Michel J, Schneider S, Bornfleth H, Baniahmad A, Fackelmayer F O, Schmidt S, Renkawitz R (Nov. 1997). "The glucocorticoid receptor is associated with the RNA-binding nuclear matrix protein hnRNP U". J. Biol. Chem. (UNITED STATES) 272 (45): 28471–8. ISSN 0021-9258. PMID 9353307.  
  15. ^ Préfontaine, G G; Walther R, Giffin W, Lemieux M E, Pope L, Haché R J (Sep. 1999). "Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter". J. Biol. Chem. (UNITED STATES) 274 (38): 26713–9. ISSN 0021-9258. PMID 10480874.  
  16. ^ Wang, J M; Préfontaine G G, Lemieux M E, Pope L, Akimenko M A, Haché R J (Oct. 1999). "Developmental effects of ectopic expression of the glucocorticoid receptor DNA binding domain are alleviated by an amino acid substitution that interferes with homeodomain binding". Mol. Cell. Biol. (UNITED STATES) 19 (10): 7106–22. ISSN 0270-7306. PMID 10490647.  
  17. ^ Préfontaine, G G; Lemieux M E, Giffin W, Schild-Poulter C, Pope L, LaCasse E, Walker P, Haché R J (Jun. 1998). "Recruitment of octamer transcription factors to DNA by glucocorticoid receptor". Mol. Cell. Biol. (UNITED STATES) 18 (6): 3416–30. ISSN 0270-7306. PMID 9584182.  
  18. ^ Stöcklin, E; Wissler M, Gouilleux F, Groner B (Oct. 1996). "Functional interactions between Stat5 and the glucocorticoid receptor". Nature (ENGLAND) 383 (6602): 726–8. doi:10.1038/383726a0. ISSN 0028-0836. PMID 8878484.  
  19. ^ Ray, A; Prefontaine K E (Jan. 1994). "Physical association and functional antagonism between the p65 subunit of transcription factor NF-kappa B and the glucocorticoid receptor". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 91 (2): 752–6. ISSN 0027-8424. PMID 8290595.  
  20. ^ Nissen, R M; Yamamoto K R (Sep. 2000). "The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain". Genes Dev. (UNITED STATES) 14 (18): 2314–29. ISSN 0890-9369. PMID 10995388.  
  21. ^ Caldenhoven, E; Liden J, Wissink S, Van de Stolpe A, Raaijmakers J, Koenderman L, Okret S, Gustafsson J A, Van der Saag P T (Apr. 1995). "Negative cross-talk between RelA and the glucocorticoid receptor: a possible mechanism for the antiinflammatory action of glucocorticoids". Mol. Endocrinol. (UNITED STATES) 9 (4): 401–12. ISSN 0888-8809. PMID 7659084.  
  22. ^ Stevens, Adam; Garside Helen, Berry Andrew, Waters Charlotte, White Anne, Ray David (May. 2003). "Dissociation of steroid receptor coactivator 1 and nuclear receptor corepressor recruitment to the human glucocorticoid receptor by modification of the ligand-receptor interface: the role of tyrosine 735". Mol. Endocrinol. (United States) 17 (5): 845–59. doi:10.1210/me.2002-0320. ISSN 0888-8809. PMID 12569182.  
  23. ^ Schulz, Martin; Eggert Martin, Baniahmad Aria, Dostert Anja, Heinzel Thorsten, Renkawitz Rainer (Jul. 2002). "RU486-induced glucocorticoid receptor agonism is controlled by the receptor N terminus and by corepressor binding". J. Biol. Chem. (United States) 277 (29): 26238–43. doi:10.1074/jbc.M203268200. ISSN 0021-9258. PMID 12011091.  
  24. ^ Chang, C J; Chen Y L, Lee S C (Oct. 1998). "Coactivator TIF1beta interacts with transcription factor C/EBPbeta and glucocorticoid receptor to induce alpha1-acid glycoprotein gene expression". Mol. Cell. Biol. (UNITED STATES) 18 (10): 5880–7. ISSN 0270-7306. PMID 9742105.  
  25. ^ a b c Hsiao, Pei-Wen; Fryer Christy J, Trotter Kevin W, Wang Weidong, Archer Trevor K (Sep. 2003). "BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation". Mol. Cell. Biol. (United States) 23 (17): 6210–20. ISSN 0270-7306. PMID 12917342.  
  26. ^ Tazawa, Hiroshi; Osman Waffa, Shoji Yutaka, Treuter Eckardt, Gustafsson Jan-Ake, Zilliacus Johanna (Jun. 2003). "Regulation of subnuclear localization is associated with a mechanism for nuclear receptor corepression by RIP140". Mol. Cell. Biol. (United States) 23 (12): 4187–98. ISSN 0270-7306. PMID 12773562.  
  27. ^ Subramaniam, N; Treuter E, Okret S (Jun. 1999). "Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids". J. Biol. Chem. (UNITED STATES) 274 (25): 18121–7. ISSN 0021-9258. PMID 10364267.  
  28. ^ Boruk, M; Savory J G, Haché R J (Nov. 1998). "AF-2-dependent potentiation of CCAAT enhancer binding protein beta-mediated transcriptional activation by glucocorticoid receptor". Mol. Endocrinol. (UNITED STATES) 12 (11): 1749–63. ISSN 0888-8809. PMID 9817600.  
  29. ^ Li, Gangyong; Wang Shengfu, Gelehrter Thomas D (Oct. 2003). "Identification of glucocorticoid receptor domains involved in transrepression of transforming growth factor-beta action". J. Biol. Chem. (United States) 278 (43): 41779–88. doi:10.1074/jbc.M305350200. ISSN 0021-9258. PMID 12902338.  
  30. ^ Song, C Z; Tian X, Gelehrter T D (Oct. 1999). "Glucocorticoid receptor inhibits transforming growth factor-beta signaling by directly targeting the transcriptional activation function of Smad3". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (21): 11776–81. ISSN 0027-8424. PMID 10518526.  
  31. ^ Savory, J G; Préfontaine G G, Lamprecht C, Liao M, Walther R F, Lefebvre Y A, Haché R J (Feb. 2001). "Glucocorticoid receptor homodimers and glucocorticoid-mineralocorticoid receptor heterodimers form in the cytoplasm through alternative dimerization interfaces". Mol. Cell. Biol. (UNITED STATES) 21 (3): 781–93. doi:10.1128/MCB.21.3.781-793.2001. ISSN 0270-7306. PMID 11154266.  
  32. ^ Lin, Ding-Yen; Lai Ming-Zong, Ann David K, Shih Hsiu-Ming (May. 2003). "Promyelocytic leukemia protein (PML) functions as a glucocorticoid receptor co-activator by sequestering Daxx to the PML oncogenic domains (PODs) to enhance its transactivation potential". J. Biol. Chem. (United States) 278 (18): 15958–65. doi:10.1074/jbc.M300387200. ISSN 0021-9258. PMID 12595526.  
  33. ^ Lerner, Lorena; Henriksen Melissa A, Zhang Xiaokui, Darnell James E (Oct. 2003). "STAT3-dependent enhanceosome assembly and disassembly: synergy with GR for full transcriptional increase of the alpha 2-macroglobulin gene". Genes Dev. (United States) 17 (20): 2564–77. doi:10.1101/gad.1135003. ISSN 0890-9369. PMID 14522952.  
  34. ^ Zhang, Z; Jones S, Hagood J S, Fuentes N L, Fuller G M (Dec. 1997). "STAT3 acts as a co-activator of glucocorticoid receptor signaling". J. Biol. Chem. (UNITED STATES) 272 (49): 30607–10. ISSN 0021-9258. PMID 9388192.  
  35. ^ a b Hulkko, S M; Wakui H, Zilliacus J (Aug. 2000). "The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function". Biochem. J. (ENGLAND) 349 Pt 3: 885–93. ISSN 0264-6021. PMID 10903152.  
  36. ^ Jibard, N; Meng X, Leclerc P, Rajkowski K, Fortin D, Schweizer-Groyer G, Catelli M G, Baulieu E E, Cadepond F (Mar. 1999). "Delimitation of two regions in the 90-kDa heat shock protein (Hsp90) able to interact with the glucocorticosteroid receptor (GR)". Exp. Cell Res. (UNITED STATES) 247 (2): 461–74. doi:10.1006/excr.1998.4375. ISSN 0014-4827. PMID 10066374.  
  37. ^ Kanelakis, Kimon C; Shewach Donna S, Pratt William B (Sep. 2002). "Nucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assembly". J. Biol. Chem. (United States) 277 (37): 33698–703. doi:10.1074/jbc.M204164200. ISSN 0021-9258. PMID 12093808.  
  38. ^ Hecht, K; Carlstedt-Duke J, Stierna P, Gustafsson J, Brönnegârd M, Wikström A C (Oct. 1997). "Evidence that the beta-isoform of the human glucocorticoid receptor does not act as a physiologically significant repressor". J. Biol. Chem. (UNITED STATES) 272 (42): 26659–64. ISSN 0021-9258. PMID 9334248.  
  39. ^ de Castro, M; Elliot S, Kino T, Bamberger C, Karl M, Webster E, Chrousos G P (Sep. 1996). "The non-ligand binding beta-isoform of the human glucocorticoid receptor (hGR beta): tissue levels, mechanism of action, and potential physiologic role". Mol. Med. (UNITED STATES) 2 (5): 597–607. ISSN 1076-1551. PMID 8898375.  
  40. ^ van den Berg, J D; Smets L A, van Rooij H (Feb. 1996). "Agonist-free transformation of the glucocorticoid receptor in human B-lymphoma cells". J. Steroid Biochem. Mol. Biol. (ENGLAND) 57 (3-4): 239–49. ISSN 0960-0760. PMID 8645634.  
  41. ^ Stancato, L F; Silverstein A M, Gitler C, Groner B, Pratt W B (Apr. 1996). "Use of the thiol-specific derivatizing agent N-iodoacetyl-3-[125I]iodotyrosine to demonstrate conformational differences between the unbound and hsp90-bound glucocorticoid receptor hormone binding domain". J. Biol. Chem. (UNITED STATES) 271 (15): 8831–6. ISSN 0021-9258. PMID 8621522.  
  42. ^ Rao, Mira A; Cheng Helen, Quayle Alandra N, Nishitani Hideo, Nelson Colleen C, Rennie Paul S (Dec. 2002). "RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor". J. Biol. Chem. (United States) 277 (50): 48020–7. doi:10.1074/jbc.M209741200. ISSN 0021-9258. PMID 12361945.  
  43. ^ Kucera, Tomas; Waltner-Law Mary, Scott Donald K, Prasad Ratna, Granner Daryl K (Jul. 2002). "A point mutation of the AF2 transactivation domain of the glucocorticoid receptor disrupts its interaction with steroid receptor coactivator 1". J. Biol. Chem. (United States) 277 (29): 26098–102. doi:10.1074/jbc.M204013200. ISSN 0021-9258. PMID 12118039.  
  44. ^ Kullmann, M; Schneikert J, Moll J, Heck S, Zeiner M, Gehring U, Cato A C (Jun. 1998). "RAP46 is a negative regulator of glucocorticoid receptor action and hormone-induced apoptosis". J. Biol. Chem. (UNITED STATES) 273 (23): 14620–5. ISSN 0021-9258. PMID 9603979.  
  45. ^ Schneikert, J; Hübner S, Langer G, Petri T, Jäättelä M, Reed J, Cato A C (Dec. 2000). "Hsp70-RAP46 interaction in downregulation of DNA binding by glucocorticoid receptor". EMBO J. (ENGLAND) 19 (23): 6508–16. doi:10.1093/emboj/19.23.6508. ISSN 0261-4189. PMID 11101523.  
  46. ^ Wallberg, A E; Neely K E, Hassan A H, Gustafsson J A, Workman J L, Wright A P (Mar. 2000). "Recruitment of the SWI-SNF chromatin remodeling complex as a mechanism of gene activation by the glucocorticoid receptor tau1 activation domain". Mol. Cell. Biol. (UNITED STATES) 20 (6): 2004–13. ISSN 0270-7306. PMID 10688647.  
  47. ^ Wakui, H; Wright A P, Gustafsson J, Zilliacus J (Mar. 1997). "Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein". J. Biol. Chem. (UNITED STATES) 272 (13): 8153–6. ISSN 0021-9258. PMID 9079630.  

Further reading

  • Adcock IM, Ito K (2000). "Molecular mechanisms of corticosteroid actions.". Monaldi archives for chest disease = Archivio Monaldi per le malattie del torace / Fondazione clinica del lavoro, IRCCS [and] Istituto di clinica tisiologica e malattie apparato respiratorio, Università di Napoli, Secondo ateneo 55 (3): 256–66. PMID 10948677.  
  • Chikanza IC (2002). "Mechanisms of corticosteroid resistance in rheumatoid arthritis: a putative role for the corticosteroid receptor beta isoform.". Ann. N. Y. Acad. Sci. 966: 39–48. PMID 12114257.  
  • Neeck G, Kluter A, Dotzlaw H, Eggert M (2002). "Involvement of the glucocorticoid receptor in the pathogenesis of rheumatoid arthritis.". Ann. N. Y. Acad. Sci. 966: 491–5. PMID 12114309.  
  • Yudt MR, Cidlowski JA (2003). "The glucocorticoid receptor: coding a diversity of proteins and responses through a single gene.". Mol. Endocrinol. 16 (8): 1719–26. doi:10.1210/me.2002-0106. PMID 12145329.  
  • Torrego A, Pujols L, Picado C (2003). "[Response to glucocorticoid treatment in asthma. The role of alpha and beta isoforms of the glucocorticoid receptor]". Arch. Bronconeumol. 38 (9): 436–40. PMID 12237016.  
  • Bray PJ, Cotton RG (2003). "Variations of the human glucocorticoid receptor gene (NR3C1): pathological and in vitro mutations and polymorphisms.". Hum. Mutat. 21 (6): 557–68. doi:10.1002/humu.10213. PMID 12754700.  
  • Kino T, Pavlakis GN (2004). "Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1.". DNA Cell Biol. 23 (4): 193–205. doi:10.1089/104454904773819789. PMID 15142377.  
  • Lu NZ, Cidlowski JA (2004). "The origin and functions of multiple human glucocorticoid receptor isoforms.". Ann. N. Y. Acad. Sci. 1024: 102–23. doi:10.1196/annals.1321.008. PMID 15265776.  
  • Kino T, Chrousos GP (2004). "Human immunodeficiency virus type-1 accessory protein Vpr: a causative agent of the AIDS-related insulin resistance/lipodystrophy syndrome?". Ann. N. Y. Acad. Sci. 1024: 153–67. doi:10.1196/annals.1321.013. PMID 15265780.  
  • Andersen JL, Planelles V (2005). "The role of Vpr in HIV-1 pathogenesis.". Curr. HIV Res. 3 (1): 43–51. doi:10.2174/1570162052772988. PMID 15638722.  
  • Le Rouzic E, Benichou S (2006). "The Vpr protein from HIV-1: distinct roles along the viral life cycle.". Retrovirology 2: 11. doi:10.1186/1742-4690-2-11. PMID 15725353.  
  • Muthumani K, Choo AY, Premkumar A, et al. (2006). "Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism.". Cell Death Differ. 12 Suppl 1: 962–70. doi:10.1038/sj.cdd.4401583. PMID 15832179.  
  • Zhou J, Cidlowski JA (2005). "The human glucocorticoid receptor: one gene, multiple proteins and diverse responses.". Steroids 70 (5-7): 407–17. doi:10.1016/j.steroids.2005.02.006. PMID 15862824.  
  • Chrousos GP, Kino T (2006). "Intracellular glucocorticoid signaling: a formerly simple system turns stochastic.". Sci. STKE 2005 (304): pe48. doi:10.1126/stke.3042005pe48. PMID 16204701.  
  • Plotkin LL, Labutin AL, Lebedev LV, et al. (1975). "[Balloon probe for the removal of emboli and thrombi]". Meditsinskaia tekhnika (3): 42–3. PMID 1152650.  
  • Subramaniam M, Colvard D, Keeting PE, et al. (1993). "Glucocorticoid regulation of alkaline phosphatase, osteocalcin, and proto-oncogenes in normal human osteoblast-like cells.". J. Cell. Biochem. 50 (4): 411–24. doi:10.1002/jcb.240500410. PMID 1469072.  
  • Scherrer LC, Pratt WB (1992). "Association of the transformed glucocorticoid receptor with a cytoskeletal protein complex.". J. Steroid Biochem. Mol. Biol. 41 (3-8): 719–21. doi:10.1016/0960-0760(92)90411-B. PMID 1562545.  
  • Cadepond F, Gasc JM, Delahaye F, et al. (1992). "Hormonal regulation of the nuclear localization signals of the human glucocorticosteroid receptor.". Exp. Cell Res. 201 (1): 99–108. doi:10.1016/0014-4827(92)90352-9. PMID 1612132.  
  • Hurley DM, Accili D, Stratakis CA, et al. (1991). "Point mutation causing a single amino acid substitution in the hormone binding domain of the glucocorticoid receptor in familial glucocorticoid resistance.". J. Clin. Invest. 87 (2): 680–6. doi:10.1172/JCI115046. PMID 1704018.  
  • Encío IJ, Detera-Wadleigh SD (1991). "The genomic structure of the human glucocorticoid receptor.". J. Biol. Chem. 266 (11): 7182–8. PMID 1707881.  

See also

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