Crossref
journal-article
Elsevier BV
The Journal of Steroid Biochemistry and Molecular Biology (78)
References
51
Referenced
34
10.1023/A:1010062929140
/ Rev. Endocr. Metab. Disord. / Molecular nature of the Vitamin D receptor and its role in regulation of gene expression by Jurutka (2001)10.1210/me.2002-0363
/ Mol. Endocrinol. / Vitamin D: more than a “bone-a-fide” hormone by Sutton (2003)10.1016/S0021-9258(19)37087-5
/ J. Biol. Chem. / Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II) by Ing (1992)10.1101/gad.7.7b.1400
/ Genes Dev. / Unliganded thyroid hormone receptor inhibits formation of a functional preinitiation complex: implications for active repression by Fondell (1993)10.1073/pnas.90.19.8832
/ Proc. Natl. Acad. Sci. U.S.A. / Interaction of human thyroid hormone receptor b with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone by Baniahmad (1993)10.1074/jbc.270.9.4748
/ J. Biol. Chem. / The Vitamin D receptor interacts with general transcription factor IIB by MacDonald (1995)10.1073/pnas.92.5.1535
/ Proc. Natl. Acad. Sci. U.S.A. / Transcription factor TFIIB and the Vitamin D receptor cooperatively activate ligand-dependent transcription by Blanco (1995)10.1210/me.11.2.218
/ Mol. Endocrinol. / The N-terminal domain of transcription factor IIB is required for direct interaction with the Vitamin D receptor and participates in Vitamin D-mediated transcription by Masuyama (1997)10.1210/me.14.3.401
/ Mol. Endocrinol. / The polymorphic N terminus in human Vitamin D receptor isoforms influences transcriptional activity by modulating interaction with transcription factor IIB by Jurutka (2000)10.1016/S0092-8674(02)00641-4
/ Cell / Combinatorial control of gene expression by nuclear receptors and coregulators by McKenna (2002)10.1023/A:1020016208071
/ Rev. Endocr. Metab. Disord. / Molecular mechanisms and cellular biology of the steroid receptor coactivator (SRC) family in steroid receptor function by Xu (2002)10.1038/38304
/ Nature / Steroid receptor coactivator-1 is a histone acetyltransferase by Spencer (1997)10.1016/S0092-8674(00)80516-4
/ Cell / Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300 by Chen (1997)10.1210/er.20.3.321
/ Endocr. Rev. / Nuclear receptor coregulators: cellular and molecular biology by McKenna (1999)10.1126/science.270.5240.1354
/ Science / Sequence and characterization of a coactivator for the steroid hormone receptor superfamily by Onate (1995)10.1073/pnas.93.10.4948
/ Proc. Natl. Acad. Sci. U.S.A. / GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors by Hong (1996)10.1002/j.1460-2075.1996.tb00736.x
/ EMBO J. / TIF2, a 160kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors by J Voegel (1996)10.1038/42750
/ Nature (USA) / A signature motif in transcriptional co-activators mediates binding to nuclear receptors (see comments) by Heery (1997)-
H. Masuyama, C.M. Brownfield, R. St.-Arnaud, P.N. MacDonald, Evidence for ligand-dependent intramolecular folding of the AF-2 domain in Vitamin D receptor-activated transcription and coactivator interaction, Mol. Endocrinol., 1997, in press.
(
10.1210/mend.11.10.9990
) 10.1074/jbc.272.23.14592
/ J. Biol. Chem. by Jurutka (1997)10.1038/378681a0
/ Nature / Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid by Renaud (1995)10.1016/S0092-8674(00)81717-1
/ Cell / The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen by Shiau (1998)10.1126/science.280.5370.1747
/ Science / Hormone-dependent coactivator binding to a hydrophobic cleft on nuclear receptors by Feng (1998)10.1101/gad.12.21.3343
/ Genes. Dev. / Structure and specificity of nuclear receptor–coactivator interactions by Darimont (1998)10.1038/25931
/ Nature / Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma by Nolte (1998)10.1101/gad.12.12.1787
/ Genes Dev. / A novel protein complex that interacts with the Vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free system by Rachez (1998)10.1073/pnas.93.16.8329
/ Proc. Natl. Acad. Sci. U.S.A. / Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex by Fondell (1996)10.1073/pnas.95.15.8538
/ Proc. Natl. Acad. Sci. U.S.A. / Mammalian mediator of transcriptional regulation and its possible role as an end-point of signal transduction pathways by Jiang (1998)10.1128/MCB.20.8.2718-2726.2000
/ Mol. Cell. Biol. / The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes by Rachez (2000)10.1038/19783
/ Nature / Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex by Rachez (1999)10.1074/jbc.275.15.10719
/ J. Biol. Chem. / Binding of liganded Vitamin D receptor to the Vitamin D receptor interacting protein coactivator complex induces interaction with RNA polymerase II holoenzyme by Chiba (2000)10.1074/jbc.C200099200
/ J. Biol. Chem. / Reciprocal recruitment of DRIP/mediator and p160 coactivator complexes in vivo by estrogen receptor by Burakov (2002)10.1128/JVI.39.3.920-934.1981
/ J. Virol. / Generation of transforming viruses in cultures of chicken fibroblasts infected with an avian leukosis virus by Stavnezer (1981)10.1016/S1097-2765(00)80201-4
/ Mol. Cell / Interaction of the Ski oncoprotein with Smad3 regulates TGF-beta signaling by Sun (1999)10.1073/pnas.090097797
/ Proc. Natl. Acad. Sci. U.S.A. / Ski acts as a co-repressor with Smad2 and Smad3 to regulate the response to type beta transforming growth factor by Xu (2000)10.1074/jbc.273.26.16434
/ J. Biol. Chem. / Isolation and characterization of a novel coactivator protein, NCoA-62, involved in Vitamin D-mediated transcription by Baudino (1998)10.1038/sj.onc.1201687
/ Oncogene / The Ski oncoprotein interacts with Skip, the human homolog of Drosophila Bx42 by Dahl (1998)10.1073/pnas.112213799
/ Proc. Natl. Acad. Sci. U.S.A. / SKIP is an indispensable factor for Caenorhabditis elegans development by Kostrouchova (2002)10.1093/oxfordjournals.jbchem.a003257
/ J. Biochem. (Tokyo) / Functional mapping of Saccharomyces cerevisiae Prp45 identifies the SNW domain as essential for viability by Martinkova (2002)10.1016/S0925-4773(02)00193-4
/ Mech. Dev. / Inducible RNA interference uncovers the Drosophila protein Bx42 as an essential nuclear cofactor involved in Notch signal transduction by Negeri (2002)10.1016/S0039-128X(00)00200-2
/ Steroids / Vitamin D receptor and nuclear receptor coactivators: crucial interactions in Vitamin D-mediated transcription by MacDonald (2001)10.1074/jbc.M106263200
/ J. Biol. Chem. / Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in Vitamin D receptor-mediated transcription by Zhang (2001)-
C. Zhang, D.R. Dowd, A. Staal, C. Gu, J.B. Lian, A.J. Van Wijnen, G.S. Stein, P.N. MacDonald, NCoA62/SKIP is a nuclear matrix-associated coactivator that may couple Vitamin D receptor-mediated transcription and RNA splicing, J. Biol. Chem., 2003.
(
10.1074/jbc.M305191200
) 10.1038/1700
/ Nat. Genet. / Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex by Neubauer (1998)10.1093/emboj/18.15.4308
/ EMBO J. / Purification and biochemical characterization of interchromatin granule clusters by Mintz (1999)10.1126/science.1077783
/ Science / Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome by Makarov (2002)10.1038/416499a
/ Nature / An extensive network of coupling among gene expression machines by Maniatis (2002)10.1016/S0092-8674(02)00617-7
/ Cell / Integrating mRNA processing with transcription by Proudfoot (2002)10.1016/S0092-8674(02)00655-4
/ Cell / A unified theory of gene expression by Orphanides (2002)10.1126/science.1073734
/ Science / Coordinate regulation of transcription and splicing by steroid receptor coregulators by Auboeuf (2002)10.1016/S1097-2765(00)00031-9
/ Mol. Cell / Direct coupling of transcription and mRNA processing through the thermogenic coactivator PGC-1 by Monsalve (2000)
Dates
Type | When |
---|---|
Created | 21 years, 1 month ago (June 29, 2004, 12:40 p.m.) |
Deposited | 4 years, 2 months ago (June 23, 2021, 5:05 p.m.) |
Indexed | 9 months ago (Nov. 19, 2024, 10:51 a.m.) |
Issued | 21 years, 3 months ago (May 1, 2004) |
Published | 21 years, 3 months ago (May 1, 2004) |
Published Print | 21 years, 3 months ago (May 1, 2004) |
@article{MacDonald_2004, title={Emerging insights into the coactivator role of NCoA62/SKIP in Vitamin D-mediated transcription}, volume={89–90}, ISSN={0960-0760}, url={http://dx.doi.org/10.1016/j.jsbmb.2004.03.097}, DOI={10.1016/j.jsbmb.2004.03.097}, journal={The Journal of Steroid Biochemistry and Molecular Biology}, publisher={Elsevier BV}, author={MacDonald, Paul N. and Dowd, Diane R. and Zhang, Chi and Gu, Chun}, year={2004}, month=may, pages={179–186} }