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Volumn 24, Issue 11, 2004, Pages 4994-5004

The nuclear hormone receptor coactivator NRC is a pleiotropic modulator affecting growth, development, apoptosis, reproduction, and wound repair

Author keywords

[No Author keywords available]

Indexed keywords

DNA; NUCLEAR HORMONE RECEPTOR; NUCLEAR HORMONE RECEPTOR COACTIVATOR; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 2542496225     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.11.4994-5004.2004     Document Type: Article
Times cited : (52)

References (73)
  • 1
    • 0035971572 scopus 로고    scopus 로고
    • Function and regulation of AP-1 subunits in skin physiology and pathology
    • Angel, P., A. Szabowski, and M. Schorpp-Kistner. 2001. Function and regulation of AP-1 subunits in skin physiology and pathology. Oncogene 20: 413-423.
    • (2001) Oncogene , vol.20 , pp. 413-423
    • Angel, P.1    Szabowski, A.2    Schorpp-Kistner, M.3
  • 4
    • 0034957480 scopus 로고    scopus 로고
    • Nuclear hormone receptors and gene expression
    • Aranda, A., and A. Pascual. 2001. Nuclear hormone receptors and gene expression. Physiol. Rev. 81:1269-1304.
    • (2001) Physiol. Rev. , vol.81 , pp. 1269-1304
    • Aranda, A.1    Pascual, A.2
  • 6
    • 0033587187 scopus 로고    scopus 로고
    • Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein
    • Boyer, T. G., M. E. Martin, E. Lees, R. P. Ricciardi, and A. J. Berk. 1999. Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein. Nature 399:276-279.
    • (1999) Nature , vol.399 , pp. 276-279
    • Boyer, T.G.1    Martin, M.E.2    Lees, E.3    Ricciardi, R.P.4    Berk, A.J.5
  • 7
    • 0034007998 scopus 로고    scopus 로고
    • Cloning and characterization of RAP250, a novel nuclear receptor coactivator
    • Caira, F., P. Antonson, M. Pelto-Huikko, E. Treuter, and J. A. Gustafsson. 2000. Cloning and characterization of RAP250, a novel nuclear receptor coactivator. J. Biol. Chem. 275:5308-5317.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5308-5317
    • Caira, F.1    Antonson, P.2    Pelto-Huikko, M.3    Treuter, E.4    Gustafsson, J.A.5
  • 10
    • 0034916613 scopus 로고    scopus 로고
    • p300/CBP proteins: HATs for transcriptional bridges and scaffolds
    • Chan, H. M., and N. B. La Thangue. 2001. p300/CBP proteins: HATs for transcriptional bridges and scaffolds. J. Cell Sci. 114:2363-2373.
    • (2001) J. Cell Sci. , vol.114 , pp. 2363-2373
    • Chan, H.M.1    La Thangue, N.B.2
  • 11
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen, H., R. J. Lin, R. L. Schiltz, D. Chakravarti, A. Nash, L. Nagy, M. L. Privalsky, Y. Nakatani, and R. M. Evans. 1997. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90:569-580.
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 13
    • 0036771764 scopus 로고    scopus 로고
    • Antiapoptotic role of PPARb in keratinocytes via transcriptional control of the Akt1 signaling pathway
    • Di-Poi, N., N. S. Tan, L. Michalik, W. Wahli, and B. Desvergne. 2002. Antiapoptotic role of PPARb in keratinocytes via transcriptional control of the Akt1 signaling pathway. Mol. Cell 10:721-733.
    • (2002) Mol. Cell , vol.10 , pp. 721-733
    • Di-Poi, N.1    Tan, N.S.2    Michalik, L.3    Wahli, W.4    Desvergne, B.5
  • 15
    • 0029758906 scopus 로고    scopus 로고
    • Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex
    • Fondell, J. D., H. Ge, and R. G. Roeder. 1996. Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex. Proc. Natl. Acad. Sci. USA 93:8329-8333.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8329-8333
    • Fondell, J.D.1    Ge, H.2    Roeder, R.G.3
  • 16
    • 0042913170 scopus 로고    scopus 로고
    • Evidence that Myc activation depletes the epidermal stem cell compartment by modulating adhesive interactions with the local microenvironment
    • Frye, M., C. Gardner, E. R. Li, I. Arnold, and F. M. Watt. 2003. Evidence that Myc activation depletes the epidermal stem cell compartment by modulating adhesive interactions with the local microenvironment. Development 130:2793-2808.
    • (2003) Development , vol.130 , pp. 2793-2808
    • Frye, M.1    Gardner, C.2    Li, E.R.3    Arnold, I.4    Watt, F.M.5
  • 17
    • 0037198679 scopus 로고    scopus 로고
    • Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis
    • Ge, K., M. Guermah, C. X. Yuan, M. Ito, A. E. Wallberg, B. M. Spiegelman, and R. G. Roeder. 2002. Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis. Nature 417:563-567.
    • (2002) Nature , vol.417 , pp. 563-567
    • Ge, K.1    Guermah, M.2    Yuan, C.X.3    Ito, M.4    Wallberg, A.E.5    Spiegelman, B.M.6    Roeder, R.G.7
  • 18
    • 0036311892 scopus 로고    scopus 로고
    • The function of TIF2/GRIP1 in mouse reproduction is distinct from those of SRC-1 and p/CIP
    • Gehin, M., M. Mark, C. Dennefeld, A. Dierich, H. Gronemeyer, and P. Chambon. 2002. The function of TIF2/GRIP1 in mouse reproduction is distinct from those of SRC-1 and p/CIP. Mol. Cell. Biol. 22:5923-5937.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5923-5937
    • Gehin, M.1    Mark, M.2    Dennefeld, C.3    Dierich, A.4    Gronemeyer, H.5    Chambon, P.6
  • 20
    • 0034234237 scopus 로고    scopus 로고
    • CBP/p300 in cell growth, transformation, and development
    • Goodman, R. H., and S. Smolik. 2000. CBP/p300 in cell growth, transformation, and development. Genes Dev. 14:1553-1577.
    • (2000) Genes Dev , vol.14 , pp. 1553-1577
    • Goodman, R.H.1    Smolik, S.2
  • 22
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery, D. M., E. Kalkhoven, S. Hoare, and M. G. Parker. 1997. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387:733-736.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 23
    • 0029978605 scopus 로고    scopus 로고
    • GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors
    • Hong, H., K. Kohli, A. Trivedi, D. L. Johnson, and M. R. Stallcup. 1996. GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors. Proc. Natl. Acad. Sci. USA 93:4948-4952.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4948-4952
    • Hong, H.1    Kohli, K.2    Trivedi, A.3    Johnson, D.L.4    Stallcup, M.R.5
  • 24
    • 0032547734 scopus 로고    scopus 로고
    • Functional differences between keratins of stratified and simple epithelia
    • Hutton, E., R. D. Paladini, Q. C. Yu, M. Yen, P. A. Coulombe, and E. Fuchs. 1998. Functional differences between keratins of stratified and simple epithelia. J. Cell Biol. 142:487-499.
    • (1998) J. Cell Biol. , vol.142 , pp. 487-499
    • Hutton, E.1    Paladini, R.D.2    Yu, Q.C.3    Yen, M.4    Coulombe, P.A.5    Fuchs, E.6
  • 25
    • 0035318741 scopus 로고    scopus 로고
    • The TRAP/SMCC/Mediator complex and thyroid hormone receptor function
    • Ito, M., and R. G. Roeder. 2001. The TRAP/SMCC/Mediator complex and thyroid hormone receptor function. Trends Endocrinol. Metab. 12:127-134.
    • (2001) Trends Endocrinol. Metab. , vol.12 , pp. 127-134
    • Ito, M.1    Roeder, R.G.2
  • 26
    • 0033635048 scopus 로고    scopus 로고
    • Involvement of the TRAP220 component of the TRAP/SMCC coactivator complex in embryonic development and thyroid hormone action
    • Ito, M., C. X. Yuan, H. J. Okano, R. B. Darnell, and B. G. Roeder. 2000. Involvement of the TRAP220 component of the TRAP/SMCC coactivator complex in embryonic development and thyroid hormone action. Mol. Cell 5:683-693.
    • (2000) Mol. Cell , vol.5 , pp. 683-693
    • Ito, M.1    Yuan, C.X.2    Okano, H.J.3    Darnell, R.B.4    Roeder, B.G.5
  • 27
    • 0035823583 scopus 로고    scopus 로고
    • Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM)
    • Iwasaki, T., W. W. Chin, and L. Ko. 2001. Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM). J. Biol. Chem. 276:33375-33383.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33375-33383
    • Iwasaki, T.1    Chin, W.W.2    Ko, L.3
  • 28
    • 0037059798 scopus 로고    scopus 로고
    • Molecular cloning and characterization of CAPER, a novel coactivator of activating protein-1 and estrogen receptors
    • Jung, D. J., S. Y. Na, D. S. Na, and J. W. Lee. 2002. Molecular cloning and characterization of CAPER, a novel coactivator of activating protein-1 and estrogen receptors. J. Biol. Chem. 277:1229-1234.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1229-1234
    • Jung, D.J.1    Na, S.Y.2    Na, D.S.3    Lee, J.W.4
  • 29
    • 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., J. E. Valentine, D. M. Heery, and M. G. Parker. 1998. Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor. EMBO J. 17:232-243.
    • (1998) EMBO J. , vol.17 , pp. 232-243
    • Kalkhoven, E.1    Valentine, J.E.2    Heery, D.M.3    Parker, M.G.4
  • 31
    • 0034705203 scopus 로고    scopus 로고
    • Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator
    • Ko, L., G. R. Cardona, and W. W. Chin. 2000. Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator. Proc. Natl. Acad. Sci. USA 97:6212-6217.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6212-6217
    • Ko, L.1    Cardona, G.R.2    Chin, W.W.3
  • 32
    • 0037160140 scopus 로고    scopus 로고
    • Deletion of the cancer-amplified coactivator AIB3 results in defective placentation and embryonic lethality
    • Kuang, S. Q., L. Liao, H. Zhang, F. A. Pereira, Y. Yuan, F. J. DeMayo, L. Ko, and J. Xu. 2002. Deletion of the cancer-amplified coactivator AIB3 results in defective placentation and embryonic lethality. J. Biol. Chem. 277:45356-45360.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45356-45360
    • Kuang, S.Q.1    Liao, L.2    Zhang, H.3    Pereira, F.A.4    Yuan, Y.5    DeMayo, F.J.6    Ko, L.7    Xu, J.8
  • 33
    • 0347480263 scopus 로고    scopus 로고
    • The thyroid hormone receptor-associated protein TRAP220 is required at distinct embryonic stages in placental, cardiac, and hepatic development
    • Landles, C., S. Chalk, J. H. Steel, I. Rosewell, B. Spencer-Dene, N. Lalani el, and M. G. Parker. 2003. The thyroid hormone receptor-associated protein TRAP220 is required at distinct embryonic stages in placental, cardiac, and hepatic development. Mol. Endocrinol. 17:2418-2435.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 2418-2435
    • Landles, C.1    Chalk, S.2    Steel, J.H.3    Rosewell, I.4    Spencer-Dene, B.5    Lalani El, N.6    Parker, M.G.7
  • 35
    • 0035150432 scopus 로고    scopus 로고
    • Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2
    • Lee, S. K., S. Y. Jung, Y. S. Kim, S. Y. Na, Y. C. Lee, and J. W. Lee. 2001. Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2. Mol. Endocrinol. 15:241-254.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 241-254
    • Lee, S.K.1    Jung, S.Y.2    Kim, Y.S.3    Na, S.Y.4    Lee, Y.C.5    Lee, J.W.6
  • 36
    • 0032849086 scopus 로고    scopus 로고
    • NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors
    • Li, D., V. Desai-Yajnik, E. Lo, M. Schapira, R. Abagyan, and H. H. Samuels. 1999. NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors. Mol. Cell. Biol. 19:7191-7202.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7191-7202
    • Li, D.1    Desai-Yajnik, V.2    Lo, E.3    Schapira, M.4    Abagyan, R.5    Samuels, H.H.6
  • 37
    • 0035192927 scopus 로고    scopus 로고
    • Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation
    • Li, D., F. Wang, and H. H. Samuels. 2001. Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation. Mol. Cell. Biol. 21:8371-8384.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8371-8384
    • Li, D.1    Wang, F.2    Samuels, H.H.3
  • 39
    • 0030872716 scopus 로고    scopus 로고
    • RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2
    • Li, H., P. J. Gomes, and J. D. Chen. 1997. RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc. Natl. Acad. Sci. USA 94:8479-8484.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8479-8484
    • Li, H.1    Gomes, P.J.2    Chen, J.D.3
  • 40
    • 0036784615 scopus 로고    scopus 로고
    • NRC-interacting factor 1 is a novel cotransducer that interacts with and regulates the activity of the nuclear hormone receptor coactivator NRC
    • Mahajan, M. A., A. Murray, and H. H. Samuels. 2002. NRC-interacting factor 1 is a novel cotransducer that interacts with and regulates the activity of the nuclear hormone receptor coactivator NRC. Mol. Cell. Biol. 22:6883-6894.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6883-6894
    • Mahajan, M.A.1    Murray, A.2    Samuels, H.H.3
  • 41
    • 0033920259 scopus 로고    scopus 로고
    • A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein
    • Mahajan, M. A., and H. H. Samuels. 2000. A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein. Mol. Cell. Biol. 20:5048-5063.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5048-5063
    • Mahajan, M.A.1    Samuels, H.H.2
  • 42
    • 0042284848 scopus 로고    scopus 로고
    • PSF-TFE3 oncoprotein in papillary renal cell carcinoma inactivates TFE3 and p53 through cytoplasmic sequestration
    • Mathur, M., S. Das, and H. H. Samuels. 2003. PSF-TFE3 oncoprotein in papillary renal cell carcinoma inactivates TFE3 and p53 through cytoplasmic sequestration. Oncogene 22:5031-5044.
    • (2003) Oncogene , vol.22 , pp. 5031-5044
    • Mathur, M.1    Das, S.2    Samuels, H.H.3
  • 43
    • 0036096533 scopus 로고    scopus 로고
    • An ex vivo assay to assess the potential of skin keratinocytes for wound epithelialization
    • Mazzalupo, S., M. J. Wawersik, and P. A. Coulombe. 2002. An ex vivo assay to assess the potential of skin keratinocytes for wound epithelialization. J. Investig. Dermatol. 118:866-870.
    • (2002) J. Investig. Dermatol. , vol.118 , pp. 866-870
    • Mazzalupo, S.1    Wawersik, M.J.2    Coulombe, P.A.3
  • 45
    • 0033305547 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Cellular and molecular biology
    • McKenna, N. J., R. B. Lanz, and B. W. O'Malley. 1999. Nuclear receptor coregulators: cellular and molecular biology. Endocr. Rev. 20:321-344.
    • (1999) Endocr. Rev. , vol.20 , pp. 321-344
    • McKenna, N.J.1    Lanz, R.B.2    O'Malley, B.W.3
  • 46
    • 0036284103 scopus 로고    scopus 로고
    • Minireview: Nuclear receptor coactivators-an update
    • McKenna, N. J., and B. W. O'Malley. 2002. Minireview: nuclear receptor coactivators-an update. Endocrinology 143:2461-2465.
    • (2002) Endocrinology , vol.143 , pp. 2461-2465
    • McKenna, N.J.1    O'Malley, B.W.2
  • 48
    • 0040368298 scopus 로고    scopus 로고
    • Composite co-activator ARC mediates chromatin-directed transcriptional activation
    • Naar, A. M., P. A. Beaurang, S. Zhou, S. Abraham, W. Solomon, and R. Tjian. 1999. Composite co-activator ARC mediates chromatin-directed transcriptional activation. Nature 398:828-832.
    • (1999) Nature , vol.398 , pp. 828-832
    • Naar, A.M.1    Beaurang, P.A.2    Zhou, S.3    Abraham, S.4    Solomon, W.5    Tjian, R.6
  • 50
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator of the steroid hormone receptor superfamily
    • Onate, S. A., S. Y. Tsai, M.-J. Tsai, and B. W. O'Malley. 1995. Sequence and characterization of a coactivator of the steroid hormone receptor superfamily. Science 270:1354-1357.
    • (1995) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.-J.3    O'Malley, B.W.4
  • 52
    • 0032549811 scopus 로고    scopus 로고
    • A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis
    • Puigserver, P., Z. Wu, C. W. Park, R. Graves, M. Wright, and B. M. Spiegelman. 1998. A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 92:829-839.
    • (1998) Cell , vol.92 , pp. 829-839
    • Puigserver, P.1    Wu, Z.2    Park, C.W.3    Graves, R.4    Wright, M.5    Spiegelman, B.M.6
  • 53
    • 0038153901 scopus 로고    scopus 로고
    • Transcriptional coactivator PRIP, the peroxisome proliferator-activated receptor γ (PPAR-γ)-interacting protein, is required for PPAR-gamma-mediated adipogenesis
    • Qi, C., S. Surapureddi, Y. J. Zhu, S. Yu, P. Kashireddy, M. S. Rao, and J. K. Reddy. 2003. Transcriptional coactivator PRIP, the peroxisome proliferator-activated receptor γ (PPAR-γ)-interacting protein, is required for PPAR-gamma-mediated adipogenesis. J. Biol. Chem. 278:25281-25284.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25281-25284
    • Qi, C.1    Surapureddi, S.2    Zhu, Y.J.3    Yu, S.4    Kashireddy, P.5    Rao, M.S.6    Reddy, J.K.7
  • 55
    • 0030786270 scopus 로고    scopus 로고
    • TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1
    • Takeshita, A., G. R. Cardona, N. Koibuchi, C. S. Suen, and W. W. Chin. 1997. TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. J. Biol. Chem. 272:27629-27634.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27629-27634
    • Takeshita, A.1    Cardona, G.R.2    Koibuchi, N.3    Suen, C.S.4    Chin, W.W.5
  • 57
    • 0030923585 scopus 로고    scopus 로고
    • Abnormal skeletal patterning in embryos lacking a single Cbp allele: A partial similarity with Rubinstein-Taybi syndrome
    • Tanaka, Y., I. Naruse, T. Maekawa, H. Masuya, T. Shiroishi, and S. Ishii. 1997. Abnormal skeletal patterning in embryos lacking a single Cbp allele: a partial similarity with Rubinstein-Taybi syndrome. Proc. Natl. Acad. Sci. USA 94:10215-10220.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10215-10220
    • Tanaka, Y.1    Naruse, I.2    Maekawa, T.3    Masuya, H.4    Shiroishi, T.5    Ishii, S.6
  • 58
    • 84883840386 scopus 로고
    • Quantitative studies of the growth of mouse embryo cells in culture and their development into established lines
    • Todaro, G. J., and H. Green. 1963. Quantitative studies of the growth of mouse embryo cells in culture and their development into established lines. J. Cell Biol. 17:299-313.
    • (1963) J. Cell Biol. , vol.17 , pp. 299-313
    • Todaro, G.J.1    Green, H.2
  • 59
    • 0030912539 scopus 로고    scopus 로고
    • The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function
    • Torchia, J., D. W. Rose, J. Inostroza, Y. Kamei, S. Westin, C. K. Glass, and M. G. Rosenfeld. 1997. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387:677-684.
    • (1997) Nature , vol.387 , pp. 677-684
    • Torchia, J.1    Rose, D.W.2    Inostroza, J.3    Kamei, Y.4    Westin, S.5    Glass, C.K.6    Rosenfeld, M.G.7
  • 60
    • 0032518944 scopus 로고    scopus 로고
    • The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways
    • Voegel, J. J., M. J. Heine, M. Tini, V. Vivat, P. Chambon, and H. Gronemeyer. 1998. The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways. EMBO J. 17:507-519.
    • (1998) EMBO J. , vol.17 , pp. 507-519
    • Voegel, J.J.1    Heine, M.J.2    Tini, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6
  • 61
    • 0029954339 scopus 로고    scopus 로고
    • TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors
    • Voegel, J. J., M. J. S. Heine, C. Zechel, P. Chambon, and H. Gronemeyer. 1996. TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15:3667-3675.
    • (1996) EMBO J. , vol.15 , pp. 3667-3675
    • Voegel, J.J.1    Heine, M.J.S.2    Zechel, C.3    Chambon, P.4    Gronemeyer, H.5
  • 62
    • 0034978920 scopus 로고    scopus 로고
    • Deregulated expression of c-Myc depletes epidermal stem cells
    • Waikel, R. L., Y. Kawachi, P. A. Waikel, X.-J. Wang, and D. R. Roop. 2001. Deregulated expression of c-Myc depletes epidermal stem cells. Nat. Genet. 28:165-168.
    • (2001) Nat. Genet. , vol.28 , pp. 165-168
    • Waikel, R.L.1    Kawachi, Y.2    Waikel, P.A.3    Wang, X.-J.4    Roop, D.R.5
  • 63
    • 0034612264 scopus 로고    scopus 로고
    • The steroid receptor coactivator SRC-3 (p/CIP/RAC3/AIB1/ACTR/TRAM-1) is required for normal growth, puberty, female reproductive function, and mammary gland development
    • Xu, J., L. Liao, G. Ning, H. Yoshida-Komiya, C. Deng, and B. W. O'Malley. 2000. The steroid receptor coactivator SRC-3 (p/CIP/RAC3/AIB1/ACTR/TRAM-1) is required for normal growth, puberty, female reproductive function, and mammary gland development. Proc. Natl. Acad. Sci. USA 97:6379-6384.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6379-6384
    • Xu, J.1    Liao, L.2    Ning, G.3    Yoshida-Komiya, H.4    Deng, C.5    O'Malley, B.W.6
  • 64
    • 0036744821 scopus 로고    scopus 로고
    • Molecular mechanisms and cellular biology of the steroid receptor coactivator (SRC) family in steroid receptor function
    • Xu, J., and B. W. O'Malley. 2002. Molecular mechanisms and cellular biology of the steroid receptor coactivator (SRC) family in steroid receptor function. Rev. Endocr. Metab. Disord. 3:185-192.
    • (2002) Rev. Endocr. Metab. Disord. , vol.3 , pp. 185-192
    • Xu, J.1    O'Malley, B.W.2
  • 65
    • 0032549744 scopus 로고    scopus 로고
    • Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1) gene
    • Xu, J., Y. Qiu, F. J. DeMayo, S. Y. Tsai, M. J. Tsai, and B. W. O'Malley. 1998. Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1) gene. Science 279:1922-1925.
    • (1998) Science , vol.279 , pp. 1922-1925
    • Xu, J.1    Qiu, Y.2    DeMayo, F.J.3    Tsai, S.Y.4    Tsai, M.J.5    O'Malley, B.W.6
  • 66
    • 0033999611 scopus 로고    scopus 로고
    • E1A-mediated repression of progesterone receptor-dependent transactivation involves inhibition of the assembly of a multisubunit coactivation complex
    • Xu, Y., L. Klein-Hitpass, and M. K. Bagchi. 2000. E1A-mediated repression of progesterone receptor-dependent transactivation involves inhibition of the assembly of a multisubunit coactivation complex. Mol. Cell. Biol. 20: 2138-2146.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2138-2146
    • Xu, Y.1    Klein-Hitpass, L.2    Bagchi, M.K.3
  • 67
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang, X. J., V. V. Ogryzko, J. Nishikawa, B. H. Howard, and Y. Nakatani. 1996. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382:319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 68
    • 17644445419 scopus 로고    scopus 로고
    • Gene dosage-dependent embryonic development and proliferation defects in mice lacking the transcriptional integrator p300
    • Yao, T. P., S. P. Oh, M. Fuchs, N. D. Zhou, L. E. Ch'ng, D. Newsome, R. T. Bronson, E. Li, D. M. Livingston, and R. Eckner. 1998. Gene dosage-dependent embryonic development and proliferation defects in mice lacking the transcriptional integrator p300. Cell 93:361-372.
    • (1998) Cell , vol.93 , pp. 361-372
    • Yao, T.P.1    Oh, S.P.2    Fuchs, M.3    Zhou, N.D.4    Ch'ng, L.E.5    Newsome, D.6    Bronson, R.T.7    Li, E.8    Livingston, D.M.9    Eckner, R.10
  • 69
    • 0029951486 scopus 로고    scopus 로고
    • Cloning and characterization of a specific coactivator, ARA70, for the androgen receptor in human prostate cells
    • Yeh, S., and C. Chang. 1996. Cloning and characterization of a specific coactivator, ARA70, for the androgen receptor in human prostate cells. Proc. Natl. Acad. Sci. USA 93:5517-5521.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5517-5521
    • Yeh, S.1    Chang, C.2
  • 70
    • 0034607983 scopus 로고    scopus 로고
    • Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR
    • Zhu, Y., L. Kan, C. Qi, Y. S. Kanwar, A. V. Yeldandi, M. S. Rao, and J. K. Reddy. 2000. Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR. J. Biol. Chem. 275:13510-13516.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13510-13516
    • Zhu, Y.1    Kan, L.2    Qi, C.3    Kanwar, Y.S.4    Yeldandi, A.V.5    Rao, M.S.6    Reddy, J.K.7
  • 71
    • 0035964208 scopus 로고    scopus 로고
    • Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function
    • Zhu, Y., C. Qi, W. Q. Cao, A. V. Yeldandi, M. S. Rao, and J. K. Reddy. 2001. Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function. Proc. Natl. Acad. Sci. USA 98:10380-10385.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10380-10385
    • Zhu, Y.1    Qi, C.2    Cao, W.Q.3    Yeldandi, A.V.4    Rao, M.S.5    Reddy, J.K.6
  • 72
    • 0030771856 scopus 로고    scopus 로고
    • Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor
    • Zhu, Y., C. Qi, S. Jain, M. S. Rao, and J. K. Reddy. 1997. Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor. J. Biol. Chem. 272:25500-25506.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25500-25506
    • Zhu, Y.1    Qi, C.2    Jain, S.3    Rao, M.S.4    Reddy, J.K.5
  • 73
    • 0037449714 scopus 로고    scopus 로고
    • Coactivator PRIP, the peroxisome proliferator-activated receptor-interacting protein, is a modulator of placental, cardiac, hepatic, and embryonic development
    • Zhu, Y. J., S. E. Crawford, V. Stellmach, R. S. Dwivedi, M. S. Rao, F. J. Gonzalez, C. Qi, and J. K. Reddy. 2003. Coactivator PRIP, the peroxisome proliferator-activated receptor-interacting protein, is a modulator of placental, cardiac, hepatic, and embryonic development. J. Biol. Chem. 278:1986-1990.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1986-1990
    • Zhu, Y.J.1    Crawford, S.E.2    Stellmach, V.3    Dwivedi, R.S.4    Rao, M.S.5    Gonzalez, F.J.6    Qi, C.7    Reddy, J.K.8


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