메뉴 건너뛰기




Volumn 159, Issue 6, 2018, Pages 2397-2406

Profiling of 3696 nuclear receptor-coregulator interactions: A resource for biological and clinical discovery

Author keywords

[No Author keywords available]

Indexed keywords

ANDROGEN RECEPTOR; CELL NUCLEUS RECEPTOR; CONSTITUTIVE ANDROSTANE RECEPTOR; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; FARNESOID X RECEPTOR; GLUCOCORTICOID RECEPTOR; LIVER X RECEPTOR; MINERALOCORTICOID RECEPTOR; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR DELTA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PROGESTERONE RECEPTOR; RETINOIC ACID RECEPTOR; RETINOID X RECEPTOR ALPHA; RETINOID X RECEPTOR BETA; THYROID HORMONE RECEPTOR; VITAMIN D RECEPTOR; CELL RECEPTOR; COREPRESSOR PROTEIN; PROTEIN BINDING; TRANSCRIPTION FACTOR;

EID: 85054423283     PISSN: 00137227     EISSN: 19457170     Source Type: Journal    
DOI: 10.1210/en.2018-00149     Document Type: Article
Times cited : (30)

References (81)
  • 1
    • 84897147399 scopus 로고    scopus 로고
    • Nuclear receptors, RXR, and the big bang
    • Evans RM, Mangelsdorf DJ. Nuclear receptors, RXR, and the big bang. Cell. 2014;157(1):255-266.
    • (2014) Cell , vol.157 , Issue.1 , pp. 255-266
    • Evans, R.M.1    Mangelsdorf, D.J.2
  • 4
    • 84875363845 scopus 로고    scopus 로고
    • Multidomain integration in the structure of the HNF-4a nuclear receptor complex
    • Chandra V, Huang P, Potluri N, Wu D, Kim Y, Rastinejad F. Multidomain integration in the structure of the HNF-4a nuclear receptor complex. Nature. 2013;495(7441):394-398.
    • (2013) Nature , vol.495 , Issue.7441 , pp. 394-398
    • Chandra, V.1    Huang, P.2    Potluri, N.3    Wu, D.4    Kim, Y.5    Rastinejad, F.6
  • 6
    • 85031120007 scopus 로고    scopus 로고
    • The quaternary architecture of RARb-RXRa heterodimer facilitates domain-domain signal transmission
    • Chandra V, Wu D, Li S, Potluri N, Kim Y, Rastinejad F. The quaternary architecture of RARb-RXRa heterodimer facilitates domain-domain signal transmission. Nat Commun.2017;8(1):868.
    • (2017) Nat Commun , vol.8 , Issue.1 , pp. 868
    • Chandra, V.1    Wu, D.2    Li, S.3    Potluri, N.4    Kim, Y.5    Rastinejad, F.6
  • 7
    • 84887357178 scopus 로고    scopus 로고
    • Understanding nuclear receptor form and function using structural biology
    • Rastinejad F, Huang P, Chandra V, Khorasanizadeh S. Understanding nuclear receptor form and function using structural biology. J Mol Endocrinol. 2013;51(3):T1-T21.
    • (2013) J Mol Endocrinol , vol.51 , Issue.3 , pp. T1-T21
    • Rastinejad, F.1    Huang, P.2    Chandra, V.3    Khorasanizadeh, S.4
  • 8
    • 3242784885 scopus 로고    scopus 로고
    • Mechanism of the nuclear receptor molecular switch
    • Nagy L, Schwabe JWR. Mechanism of the nuclear receptor molecular switch. Trends Biochem Sci. 2004;29(6):317-324.
    • (2004) Trends Biochem Sci , vol.29 , Issue.6 , pp. 317-324
    • Nagy, L.1    Schwabe, J.W.R.2
  • 9
    • 0030925531 scopus 로고    scopus 로고
    • Analysis of the functional role of steroid receptor coactivator-1 in ligand-induced transactivation by thyroid hormone receptor
    • Jeyakumar M, Tanen MR, Bagchi MK. Analysis of the functional role of steroid receptor coactivator-1 in ligand-induced transactivation by thyroid hormone receptor. Mol Endocrinol. 1997; 11(6):755-767.
    • (1997) Mol Endocrinol , vol.11 , Issue.6 , pp. 755-767
    • Jeyakumar, M.1    Tanen, M.R.2    Bagchi, M.K.3
  • 10
    • 0033118328 scopus 로고    scopus 로고
    • Mice deficient in the steroid receptor co-activator 1 (SRC-1) are resistant to thyroid hormone
    • Weiss RE, Xu J, Ning G, Pohlenz J, O'Malley BW, Refetoff S. Mice deficient in the steroid receptor co-activator 1 (SRC-1) are resistant to thyroid hormone. EMBO J. 1999;18(7):1900-1904.
    • (1999) EMBO J , vol.18 , Issue.7 , pp. 1900-1904
    • Weiss, R.E.1    Xu, J.2    Ning, G.3    Pohlenz, J.4    O'Malley, B.W.5    Refetoff, S.6
  • 11
    • 0030974043 scopus 로고    scopus 로고
    • Nuclear receptor corepressors activate rather than suppress basal transcription of genes that are negatively regulated by thyroid hormone
    • Tagami T, Madison LD, Nagaya T, Jameson JL. Nuclear receptor corepressors activate rather than suppress basal transcription of genes that are negatively regulated by thyroid hormone. Mol Cell Biol. 1997;17(5):2642-2648.
    • (1997) Mol Cell Biol , vol.17 , Issue.5 , pp. 2642-2648
    • Tagami, T.1    Madison, L.D.2    Nagaya, T.3    Jameson, J.L.4
  • 12
    • 0037147224 scopus 로고    scopus 로고
    • Corepressor SMRT functions as a coactivator for thyroid hormone receptor T3Ralpha from a negative hormone response element
    • Berghagen H, Ragnhildstveit E, Krogsrud K, Thuestad G, Apriletti J, Saatcioglu F. Corepressor SMRT functions as a coactivator for thyroid hormone receptor T3Ralpha from a negative hormone response element. J Biol Chem. 2002;277(51):49517-49522.
    • (2002) J Biol Chem , vol.277 , Issue.51 , pp. 49517-49522
    • Berghagen, H.1    Ragnhildstveit, E.2    Krogsrud, K.3    Thuestad, G.4    Apriletti, J.5    Saatcioglu, F.6
  • 13
    • 0033523917 scopus 로고    scopus 로고
    • The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors
    • Hu X, Lazar MA. The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors. Nature. 1999; 402(6757):93-96.
    • (1999) Nature , vol.402 , Issue.6757 , pp. 93-96
    • Hu, X.1    Lazar, M.A.2
  • 14
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery DM, Kalkhoven E, Hoare S, Parker MG. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature. 1997;387(6634):733-736.
    • (1997) Nature , vol.387 , Issue.6634 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 17
    • 84887338695 scopus 로고    scopus 로고
    • An evolving understanding of nuclear receptor coregulator proteins
    • Millard CJ, Watson PJ, Fairall L, Schwabe JWR. An evolving understanding of nuclear receptor coregulator proteins. J Mol Endocrinol. 2013;51(3):T23-T36.
    • (2013) J Mol Endocrinol , vol.51 , Issue.3 , pp. T23-T36
    • Millard, C.J.1    Watson, P.J.2    Fairall, L.3    Schwabe, J.W.R.4
  • 19
    • 13844262924 scopus 로고    scopus 로고
    • Core-pressors selectively control the transcriptional activity of PPARgamma in adipocytes
    • Guan H-P, Ishizuka T, Chui PC, Lehrke M, Lazar MA. Core-pressors selectively control the transcriptional activity of PPARgamma in adipocytes. Genes Dev. 2005;19(4):453-461.
    • (2005) Genes Dev , vol.19 , Issue.4 , pp. 453-461
    • Guan, H.-P.1    Ishizuka, T.2    Chui, P.C.3    Lehrke, M.4    Lazar, M.A.5
  • 20
    • 0037192501 scopus 로고    scopus 로고
    • Molecular determinants for the tissue specificity of SERMs
    • Shang Y, Brown M. Molecular determinants for the tissue specificity of SERMs. Science. 2002;295(5564):2465-2468.
    • (2002) Science , vol.295 , Issue.5564 , pp. 2465-2468
    • Shang, Y.1    Brown, M.2
  • 22
    • 34547731515 scopus 로고    scopus 로고
    • Nuclear receptor coregulators and human disease
    • Lonard DM, Lanz RB, O'Malley BW. Nuclear receptor coregulators and human disease. Endocr Rev. 2007;28(5):575-587.
    • (2007) Endocr Rev , vol.28 , Issue.5 , pp. 575-587
    • Lonard, D.M.1    Lanz, R.B.2    O'Malley, B.W.3
  • 23
    • 0032472408 scopus 로고    scopus 로고
    • Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor
    • Kalkhoven E, Valentine JE, Heery DM, Parker MG. Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor. EMBO J. 1998;17(1): 232-243.
    • (1998) EMBO J , vol.17 , Issue.1 , pp. 232-243
    • Kalkhoven, E.1    Valentine, J.E.2    Heery, D.M.3    Parker, M.G.4
  • 24
    • 33846209597 scopus 로고    scopus 로고
    • Analysis of ligand-dependent recruitment of coactivator peptides to RXRbeta in a time-resolved fluorescence resonance energy transfer assay
    • Stafslien DK, Vedvik KL, De Rosier T, Ozers MS. Analysis of ligand-dependent recruitment of coactivator peptides to RXRbeta in a time-resolved fluorescence resonance energy transfer assay. Mol Cell Endocrinol. 2007;264(1-2):82-89.
    • (2007) Mol Cell Endocrinol , vol.264 , Issue.1-2 , pp. 82-89
    • Stafslien, D.K.1    Vedvik, K.L.2    De Rosier, T.3    Ozers, M.S.4
  • 25
    • 33748468022 scopus 로고    scopus 로고
    • Development of a coactivator displacement assay for the orphan receptor estrogen-related receptor-g using time-resolved fluorescence resonance energy transfer
    • Gowda K, Marks BD, Zielinski TK, Ozers MS. Development of a coactivator displacement assay for the orphan receptor estrogen-related receptor-g using time-resolved fluorescence resonance energy transfer. Anal Biochem. 2006;357(1):105-115.
    • (2006) Anal Biochem , vol.357 , Issue.1 , pp. 105-115
    • Gowda, K.1    Marks, B.D.2    Zielinski, T.K.3    Ozers, M.S.4
  • 26
    • 0034802615 scopus 로고    scopus 로고
    • Use of homogeneous time-resolved fluorescence energy transfer in the measurement of nuclear receptor activation
    • Zhou G, Cummings R, Hermes J, Moller DE. Use of homogeneous time-resolved fluorescence energy transfer in the measurement of nuclear receptor activation. Methods. 2001;25(1):54-61.
    • (2001) Methods , vol.25 , Issue.1 , pp. 54-61
    • Zhou, G.1    Cummings, R.2    Hermes, J.3    Moller, D.E.4
  • 27
    • 33845966382 scopus 로고    scopus 로고
    • The use of in vitro peptide binding profiles and in silico ligand-receptor interaction profiles to describe ligand-induced conformations of the retinoid X receptor a ligand-binding domain
    • Folkertsma S, van Noort PI, de Heer A, Carati P, Brandt R, Visser A, Vriend G, de Vlieg J. The use of in vitro peptide binding profiles and in silico ligand-receptor interaction profiles to describe ligand-induced conformations of the retinoid X receptor a ligand-binding domain. Mol Endocrinol. 2007;21(1):30-48.
    • (2007) Mol Endocrinol , vol.21 , Issue.1 , pp. 30-48
    • Folkertsma, S.1    Van Noort, P.I.2    De Heer, A.3    Carati, P.4    Brandt, R.5    Visser, A.6    Vriend, G.7    De Vlieg, J.8
  • 29
    • 0034465495 scopus 로고    scopus 로고
    • Selection of estrogen receptor b- and thyroid hormone receptor b-specific coactivator-mimetic peptides using recombinant peptide libraries
    • Northrop JP, Nguyen D, Piplani S, Olivan SE, Kwan ST, Go NF, Hart CP, Schatz PJ. Selection of estrogen receptor b- and thyroid hormone receptor b-specific coactivator-mimetic peptides using recombinant peptide libraries. Mol Endocrinol. 2000;14(5):605-622.
    • (2000) Mol Endocrinol , vol.14 , Issue.5 , pp. 605-622
    • Northrop, J.P.1    Nguyen, D.2    Piplani, S.3    Olivan, S.E.4    Kwan, S.T.5    Go, N.F.6    Hart, C.P.7    Schatz, P.J.8
  • 31
    • 34948830554 scopus 로고    scopus 로고
    • The nuclear receptor-coactivator interaction surface as a target for peptide antagonists of the peroxisome proliferator-activated receptors
    • Mettu NB, Stanley TB, Dwyer MA, Jansen MS, Allen JE, Hall JM, McDonnell DP. The nuclear receptor-coactivator interaction surface as a target for peptide antagonists of the peroxisome proliferator-activated receptors. Mol Endocrinol. 2007;21(10): 2361-2377.
    • (2007) Mol Endocrinol , vol.21 , Issue.10 , pp. 2361-2377
    • Mettu, N.B.1    Stanley, T.B.2    Dwyer, M.A.3    Jansen, M.S.4    Allen, J.E.5    Hall, J.M.6    McDonnell, D.P.7
  • 33
    • 34249654613 scopus 로고    scopus 로고
    • An improved high throughput protein-protein interaction assay for nuclear hormone receptors
    • Goodson ML, Farboud B, Privalsky ML. An improved high throughput protein-protein interaction assay for nuclear hormone receptors. Nucl Recept Signal. 2007;5:e002.
    • (2007) Nucl Recept Signal , vol.5
    • Goodson, M.L.1    Farboud, B.2    Privalsky, M.L.3
  • 35
    • 15944408802 scopus 로고    scopus 로고
    • A pro-teomic microarray approach for exploring ligand-initiated nuclear hormone receptor pharmacology, receptor selectivity, and heterodimer functionality
    • Kim SH, Tamrazi A, Carlson KE, Katzenellenbogen JA. A pro-teomic microarray approach for exploring ligand-initiated nuclear hormone receptor pharmacology, receptor selectivity, and heterodimer functionality. Mol Cell Proteomics. 2005;4(3):267-277.
    • (2005) Mol Cell Proteomics , vol.4 , Issue.3 , pp. 267-277
    • Kim, S.H.1    Tamrazi, A.2    Carlson, K.E.3    Katzenellenbogen, J.A.4
  • 37
    • 71049127324 scopus 로고    scopus 로고
    • Nuclear receptor-coregulator interaction profiling identifies TRIP3 as a novel peroxisome proliferator-activated receptor g cofactor
    • Koppen A, Houtman R, Pijnenburg D, Jeninga EH, Ruijtenbeek R, Kalkhoven E. Nuclear receptor-coregulator interaction profiling identifies TRIP3 as a novel peroxisome proliferator-activated receptor g cofactor. Mol Cell Proteomics. 2009;8(10):2212-2226.
    • (2009) Mol Cell Proteomics , vol.8 , Issue.10 , pp. 2212-2226
    • Koppen, A.1    Houtman, R.2    Pijnenburg, D.3    Jeninga, E.H.4    Ruijtenbeek, R.5    Kalkhoven, E.6
  • 38
    • 84877636653 scopus 로고    scopus 로고
    • A 155-plex high-throughput in vitro coregulator binding assay for (anti-)estrogenicity testing evaluated with 23 reference compounds
    • Wang S, Houtman R, Melchers D, Aarts J, Peijnenburg A, van Beuningen R, Rietjens I, Bovee TF. A 155-plex high-throughput in vitro coregulator binding assay for (anti-)estrogenicity testing evaluated with 23 reference compounds. ALTEX. 2013;30(2): 145-157.
    • (2013) ALTEX , vol.30 , Issue.2 , pp. 145-157
    • Wang, S.1    Houtman, R.2    Melchers, D.3    Aarts, J.4    Peijnenburg, A.5    Van Beuningen, R.6    Rietjens, I.7    Bovee, T.F.8
  • 40
    • 84864489995 scopus 로고    scopus 로고
    • T-Rex: A web server for inferring, validating and visualizing phylogenetic trees and networks
    • Web Server
    • Boc A, Diallo AB, Makarenkov V. T-REX: a web server for inferring, validating and visualizing phylogenetic trees and networks. Nucleic Acids Res. 2012;40(Web Server issue, W1)W573-W579.
    • (2012) Nucleic Acids Res , vol.40 , Issue.W1 , pp. W573-W579
    • Boc, A.1    Diallo, A.B.2    Makarenkov, V.3
  • 43
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen JD, Evans RM. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature. 1995;377(6548):454-457.
    • (1995) Nature , vol.377 , Issue.6548 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 44
    • 0032493455 scopus 로고    scopus 로고
    • The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion
    • Yuan C-X, Ito M, Fondell JD, Fu Z-Y, Roeder RG. The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion. Proc Natl Acad Sci USA. 1998;95(14):7939-7944.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.14 , pp. 7939-7944
    • Yuan, C.-X.1    Ito, M.2    Fondell, J.D.3    Fu, Z.-Y.4    Roeder, R.G.5
  • 45
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Oñate SA, Tsai SY, Tsai M-J, O'Malley BW. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science. 1995;270(5240):1354-1357.
    • (1995) Science , vol.270 , Issue.5240 , pp. 1354-1357
    • Oñate, S.A.1    Tsai, S.Y.2    Tsai, M.-J.3    O'Malley, B.W.4
  • 46
    • 74549224652 scopus 로고    scopus 로고
    • The benzene-sulfoamide T0901317 (2,2,2-Trifluoroethyl)[4-[2,2,2-trifluoro-1-hydroxy-1-(trifluoromethyl)ethyl]phenyl]-benzenesulfonamide] is a novel retinoic acid receptor-related orphan receptor-a/g inverse A
    • Kumar N, Solt LA, Conkright JJ, Wang Y, Istrate MA, Busby SA, Garcia-Ordonez RD, Burris TP, Griffin PR. The benzene-sulfoamide T0901317 (2,2,2-Trifluoroethyl)[4-[2,2,2-trifluoro-1-hydroxy-1-(trifluoromethyl)ethyl]phenyl]-benzenesulfonamide] is a novel retinoic acid receptor-related orphan receptor-a/g inverse A. Mol Pharmacol. 2010;77(2):228-236.
    • (2010) Mol Pharmacol , vol.77 , Issue.2 , pp. 228-236
    • Kumar, N.1    Solt, L.A.2    Conkright, J.J.3    Wang, Y.4    Istrate, M.A.5    Busby, S.A.6    Garcia-Ordonez, R.D.7    Burris, T.P.8    Griffin, P.R.9
  • 47
    • 7444271980 scopus 로고    scopus 로고
    • Identification of a selective inverse agonist for the orphan nuclear receptor estrogen-related receptor a
    • Busch BB, Stevens WC Jr, Martin R, Ordentlich P, Zhou S, Sapp DW, Horlick RA, Mohan R. Identification of a selective inverse agonist for the orphan nuclear receptor estrogen-related receptor a. J Med Chem. 2004;47(23):5593-5596.
    • (2004) J Med Chem , vol.47 , Issue.23 , pp. 5593-5596
    • Busch, B.B.1    Stevens, W.C.2    Martin, R.3    Ordentlich, P.4    Zhou, S.5    Sapp, D.W.6    Horlick, R.A.7    Mohan, R.8
  • 48
    • 0035902557 scopus 로고    scopus 로고
    • 4-Hydroxytamoxifen binds to and deactivates the estrogen-related receptor g
    • Coward P, Lee D, Hull MV, Lehmann JM. 4-Hydroxytamoxifen binds to and deactivates the estrogen-related receptor g. Proc Natl Acad Sci U S A. 2001;98(15):8880-8884.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.15 , pp. 8880-8884
    • Coward, P.1    Lee, D.2    Hull, M.V.3    Lehmann, J.M.4
  • 49
    • 0034812571 scopus 로고    scopus 로고
    • 4-Hydroxytamoxifen is an isoform-specific inhibitor of orphan estrogen-receptor-related (ERR) nuclear receptors b and g
    • Tremblay GB, Bergeron D, Giguere V. 4-Hydroxytamoxifen is an isoform-specific inhibitor of orphan estrogen-receptor-related (ERR) nuclear receptors b and g. Endocrinology. 2001;142(10): 4572-4575.
    • (2001) Endocrinology , vol.142 , Issue.10 , pp. 4572-4575
    • Tremblay, G.B.1    Bergeron, D.2    Giguere, V.3
  • 51
    • 0033855471 scopus 로고    scopus 로고
    • Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix
    • Gampe RT Jr, Montana VG, Lambert MH, Wisely GB, Milburn MV, Xu HE. Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix. Genes Dev. 2000;14(17):2229-2241.
    • (2000) Genes Dev , vol.14 , Issue.17 , pp. 2229-2241
    • Gampe, R.T.1    Montana, V.G.2    Lambert, M.H.3    Wisely, G.B.4    Milburn, M.V.5    Xu, H.E.6
  • 52
    • 0028887017 scopus 로고
    • Role of ligand in retinoid signaling: 9-cis-retinoic acid modulates the oligomeric state of the retinoid X receptor
    • Kersten S, Pan L, Chambon P, Gronemeyer H, Noy N. Role of ligand in retinoid signaling: 9-cis-retinoic acid modulates the oligomeric state of the retinoid X receptor. Biochemistry. 1995; 34(42):13717-13721.
    • (1995) Biochemistry , vol.34 , Issue.42 , pp. 13717-13721
    • Kersten, S.1    Pan, L.2    Chambon, P.3    Gronemeyer, H.4    Noy, N.5
  • 53
    • 0033513582 scopus 로고    scopus 로고
    • Dissection of the LXXLL nuclear receptor-coactivator interaction motif using combinatorial peptide libraries: Discovery of peptide antagonists of estrogen receptors a and b
    • Chang C, Norris JD, Grøn H, Paige LA, Hamilton PT, Kenan DJ, Fowlkes D, McDonnell DP. Dissection of the LXXLL nuclear receptor-coactivator interaction motif using combinatorial peptide libraries: discovery of peptide antagonists of estrogen receptors a and b. Mol Cell Biol. 1999;19(12):8226-8239.
    • (1999) Mol Cell Biol , vol.19 , Issue.12 , pp. 8226-8239
    • Chang, C.1    Norris, J.D.2    Grøn, H.3    Paige, L.A.4    Hamilton, P.T.5    Kenan, D.J.6    Fowlkes, D.7    McDonnell, D.P.8
  • 56
    • 0035861571 scopus 로고    scopus 로고
    • Tip60 is a co-activator specific for class I nuclear hormone receptors
    • Gaughan L, Brady ME, Cook S, Neal DE, Robson CN. Tip60 is a co-activator specific for class I nuclear hormone receptors. J Biol Chem. 2001;276(50):46841-46848.
    • (2001) J Biol Chem , vol.276 , Issue.50 , pp. 46841-46848
    • Gaughan, L.1    Brady, M.E.2    Cook, S.3    Neal, D.E.4    Robson, C.N.5
  • 57
    • 0033583023 scopus 로고    scopus 로고
    • P300 interacts with the N- and C-terminal part of PPARgamma2 in a ligand-independent and -dependent manner, respectively
    • Gelman L, Zhou G, Fajas L, Raspé E, Fruchart J-C, Auwerx J. p300 interacts with the N- and C-terminal part of PPARgamma2 in a ligand-independent and -dependent manner, respectively. J Biol Chem. 1999;274(12):7681-7688.
    • (1999) J Biol Chem , vol.274 , Issue.12 , pp. 7681-7688
    • Gelman, L.1    Zhou, G.2    Fajas, L.3    Raspé, E.4    Fruchart, J.-C.5    Auwerx, J.6
  • 60
    • 22144449579 scopus 로고    scopus 로고
    • Roles of steroid receptor coactivator (SRC)-1 and transcriptional intermediary factor (TIF) 2 in androgen receptor activity in mice
    • Ye X, Han SJ, Tsai SY, DeMayo FJ, Xu J, Tsai MJ, O'Malley BW. Roles of steroid receptor coactivator (SRC)-1 and transcriptional intermediary factor (TIF) 2 in androgen receptor activity in mice. Proc Natl Acad Sci U S A. 2005;102(27):9487-9492.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.27 , pp. 9487-9492
    • Ye, X.1    Han, S.J.2    Tsai, S.Y.3    DeMayo, F.J.4    Xu, J.5    Tsai, M.J.6    O'Malley, B.W.7
  • 63
    • 84862749595 scopus 로고    scopus 로고
    • Serine-305 phos-phorylation modulates estrogen receptor alpha binding to a coregulator peptide array, with potential application in predicting responses to tamoxifen
    • Houtman R, de Leeuw R, Rondaij M, et al. Serine-305 phos-phorylation modulates estrogen receptor alpha binding to a coregulator peptide array, with potential application in predicting responses to tamoxifen. Mol Cancer Ther. 2012;11(4):805-816.
    • (2012) Mol Cancer Ther , vol.11 , Issue.4 , pp. 805-816
    • Houtman, R.1    De Leeuw, R.2    Rondaij, M.3
  • 64
    • 0034740164 scopus 로고    scopus 로고
    • Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: Requirement for the AF-1 a-helical core and for a direct interaction between the N- and C-terminal domains
    • Métivier R, Penot G, Flouriot G, Pakdel F. Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 a-helical core and for a direct interaction between the N- and C-terminal domains. Mol Endocrinol. 2001;15(11):1953-1970.
    • (2001) Mol Endocrinol , vol.15 , Issue.11 , pp. 1953-1970
    • Métivier, R.1    Penot, G.2    Flouriot, G.3    Pakdel, F.4
  • 65
    • 0032230283 scopus 로고    scopus 로고
    • Functional interactions of the AF-2 activation domain core region of the human androgen receptor with the amino-terminal domain and with the transcriptional coactivator TIF2 (transcriptional intermediary factor2)
    • Berrevoets CA, Doesburg P, Steketee K, Trapman J, Brinkmann AO. Functional interactions of the AF-2 activation domain core region of the human androgen receptor with the amino-terminal domain and with the transcriptional coactivator TIF2 (transcriptional intermediary factor2). Mol Endocrinol. 1998;12(8): 1172-1183.
    • (1998) Mol Endocrinol , vol.12 , Issue.8 , pp. 1172-1183
    • Berrevoets, C.A.1    Doesburg, P.2    Steketee, K.3    Trapman, J.4    Brinkmann, A.O.5
  • 66
    • 81755187015 scopus 로고    scopus 로고
    • Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1a/ERRg complex
    • Devarakonda S, Gupta K, Chalmers MJ, Hunt JF, Griffin PR, Van Duyne GD, Spiegelman BM. Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1a/ERRg complex. Proc Natl Acad Sci USA. 2011;108(46): 18678-18683.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.46 , pp. 18678-18683
    • Devarakonda, S.1    Gupta, K.2    Chalmers, M.J.3    Hunt, J.F.4    Griffin, P.R.5    Van Duyne, G.D.6    Spiegelman, B.M.7
  • 68
    • 85038856615 scopus 로고    scopus 로고
    • Unique interactome network signatures for PPARgamma modulation by functional selective ligands
    • Lam V, Zheng J, Griffin PR. Unique interactome network signatures for PPARgamma modulation by functional selective ligands. Mol Cell Proteomics. 2017;16(12):2098-2110.
    • (2017) Mol Cell Proteomics , vol.16 , Issue.12 , pp. 2098-2110
    • Lam, V.1    Zheng, J.2    Griffin, P.R.3
  • 71
    • 85011684848 scopus 로고    scopus 로고
    • Posttranslational modifications of lipid-activated nuclear receptors: Focus on metabolism
    • Becares N, Gage MC, Pineda-Torra I. Posttranslational modifications of lipid-activated nuclear receptors: focus on metabolism. Endocrinology. 2017;158(2):213-225.
    • (2017) Endocrinology , vol.158 , Issue.2 , pp. 213-225
    • Becares, N.1    Gage, M.C.2    Pineda-Torra, I.3
  • 73
    • 34548252291 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Judges, juries, and executioners of cellular regulation
    • Lonard DM, O'malley BW. Nuclear receptor coregulators: judges, juries, and executioners of cellular regulation. Mol Cell. 2007; 27(5):691-700.
    • (2007) Mol Cell , vol.27 , Issue.5 , pp. 691-700
    • Lonard, D.M.1    O'Malley, B.W.2
  • 74
    • 2442494302 scopus 로고    scopus 로고
    • Recruitment of distinct chromatin-modifying complexes by tamoxifen-complexed estrogen receptor at natural target gene promoters in vivo
    • Liu XF, Bagchi MK. Recruitment of distinct chromatin-modifying complexes by tamoxifen-complexed estrogen receptor at natural target gene promoters in vivo. J Biol Chem. 2004;279(15): 15050-15058.
    • (2004) J Biol Chem , vol.279 , Issue.15 , pp. 15050-15058
    • Liu, X.F.1    Bagchi, M.K.2
  • 75
    • 85029678258 scopus 로고    scopus 로고
    • Dynamic assembly and activation of estrogen receptor a enhancers through coregulator switching
    • Murakami S, Nagari A, Kraus WL. Dynamic assembly and activation of estrogen receptor a enhancers through coregulator switching. Genes Dev. 2017;31(15):1535-1548.
    • (2017) Genes Dev , vol.31 , Issue.15 , pp. 1535-1548
    • Murakami, S.1    Nagari, A.2    Kraus, W.L.3
  • 77
    • 84884534873 scopus 로고    scopus 로고
    • Complex genomic interactions in the dynamic regulation of transcription by the glucocorticoid receptor
    • Miranda TB, Morris SA, Hager GL. Complex genomic interactions in the dynamic regulation of transcription by the glucocorticoid receptor. Mol Cell Endocrinol. 2013;380(1-2):16-24.
    • (2013) Mol Cell Endocrinol , vol.380 , Issue.1-2 , pp. 16-24
    • Miranda, T.B.1    Morris, S.A.2    Hager, G.L.3
  • 81
    • 84865484646 scopus 로고    scopus 로고
    • Anti-inflammatory and metabolic actions of FXR: Insights into molecular mechanisms
    • Hollman DAA, Milona A, van Erpecum KJ, van Mil SWC. Anti-inflammatory and metabolic actions of FXR: insights into molecular mechanisms. Biochim Biophys Acta. 2012;1821(11): 1443-1452.
    • (2012) Biochim Biophys Acta , vol.1821 , Issue.11 , pp. 1443-1452
    • Hollman, D.A.A.1    Milona, A.2    Van Erpecum, K.J.3    Van Mil, S.W.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.