메뉴 건너뛰기




Volumn 76, Issue SUPPL. 32/33, 1999, Pages 32-40

Dual functions for transcriptional regulators: Myth or reality?

Author keywords

Coactivators; Transcriptional control

Indexed keywords

DNA BINDING PROTEIN; GENE PRODUCT; HOMEODOMAIN PROTEIN; TRANSCRIPTION FACTOR; BETA CATENIN; CARRIER PROTEIN; CHAPERONE; COPS5 PROTEIN, HUMAN; CTNNB1 PROTEIN, HUMAN; CYTOSKELETON PROTEIN; FUNGAL PROTEIN; HYDROLYASE; NASCENT POLYPEPTIDE ASSOCIATED COMPLEX; NASCENT-POLYPEPTIDE-ASSOCIATED COMPLEX; PEPTIDE HYDROLASE; PTERIN 4A CARBINOLAMINE DEHYDRATASE; PTERIN-4A-CARBINOLAMINE DEHYDRATASE; REPRESSOR PROTEIN; RPT6 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SIGNAL PEPTIDE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SUG1 PROTEIN, MAMMALIAN; THYROID HORMONE RECEPTOR INTERACTING PROTEIN; THYROID-HORMONE-RECEPTOR INTERACTING PROTEIN; TRANSACTIVATOR PROTEIN;

EID: 0033403274     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-4644(1999)75:32+<32::aid-jcb5>3.3.co;2-o     Document Type: Article
Times cited : (10)

References (22)
  • 1
    • 0030000980 scopus 로고    scopus 로고
    • Cadherin-catenin complex: Protein interactions and their implications for cadherin function
    • Aberle H, Schwartz H, Kemler R. 1996. Cadherin-catenin complex: protein interactions and their implications for cadherin function. J Cell Biochem 61:514-523.
    • (1996) J Cell Biochem , vol.61 , pp. 514-523
    • Aberle, H.1    Schwartz, H.2    Kemler, R.3
  • 2
    • 0342327346 scopus 로고    scopus 로고
    • Cadherins, catenins and APC protein: Interplay between cytoskeletal complexes and signaling pathways
    • Earth AIM, Nathke IS, Nelson WJ. 1997. Cadherins, catenins and APC protein: interplay between cytoskeletal complexes and signaling pathways. Curr Opin Cell Biol 9:683-690.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 683-690
    • Earth, A.I.M.1    Nathke, I.S.2    Nelson, W.J.3
  • 3
    • 0029761277 scopus 로고    scopus 로고
    • A new group of conserved coactivators that increase the specificity of AP-1 transcription factors
    • Claret FX, Hibi M, Dhut S, Toda T, Karin M. 1996. A new group of conserved coactivators that increase the specificity of AP-1 transcription factors. Nature 383:453-457.
    • (1996) Nature , vol.383 , pp. 453-457
    • Claret, F.X.1    Hibi, M.2    Dhut, S.3    Toda, T.4    Karin, M.5
  • 4
    • 0032941717 scopus 로고    scopus 로고
    • Regulation of LEF-1/TCF transcription factors by Wnt and other signals
    • Eastman Q, Grosschedl R. 1999. Regulation of LEF-1/TCF transcription factors by Wnt and other signals. Curr Opin Cell Biol 11:233-240.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 233-240
    • Eastman, Q.1    Grosschedl, R.2
  • 5
    • 0029001623 scopus 로고
    • Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator
    • Endrizzi JA, Cronk JD, Wang W, Crabtree GR, Alber T. 1995. Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator. Science 268:556-559.
    • (1995) Science , vol.268 , pp. 556-559
    • Endrizzi, J.A.1    Cronk, J.D.2    Wang, W.3    Crabtree, G.R.4    Alber, T.5
  • 6
    • 0032478067 scopus 로고    scopus 로고
    • The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo
    • George R, Beddoe T, Landl K, Lithgow T. 1998. The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo. Proc Natl Acad Sci USA 95:2296-2301.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2296-2301
    • George, R.1    Beddoe, T.2    Landl, K.3    Lithgow, T.4
  • 7
    • 0031470506 scopus 로고    scopus 로고
    • Studies on the enzymatic and transcriptional activity of the dimerization cofactor for hepatocyte nuclear factor 1
    • Johnen G, Kaufman S. 1997. Studies on the enzymatic and transcriptional activity of the dimerization cofactor for hepatocyte nuclear factor 1. Proc Natl Acad Sci USA 94:13469-13474.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13469-13474
    • Johnen, G.1    Kaufman, S.2
  • 8
    • 0028890361 scopus 로고
    • Interaction of thyroid-hormone receptor with a conserved transcriptional mediator
    • Lee JW, Ryan F, Swaffield JC, Johnston SA, Moore DD. 1995. Interaction of thyroid-hormone receptor with a conserved transcriptional mediator. Nature 374:91-94.
    • (1995) Nature , vol.374 , pp. 91-94
    • Lee, J.W.1    Ryan, F.2    Swaffield, J.C.3    Johnston, S.A.4    Moore, D.D.5
  • 9
    • 0032539626 scopus 로고    scopus 로고
    • Identification of hepatic nuclear factor 1 binding sites in the 5′ flanking region of the human phenylalanine hydroxylase gene: Implication of a dual function of phenylalanine hydroxylase stimulator in the phenylalanine hydroxylation system
    • Lei X-D, Kaufman S. 1998. Identification of hepatic nuclear factor 1 binding sites in the 5′ flanking region of the human phenylalanine hydroxylase gene: implication of a dual function of phenylalanine hydroxylase stimulator in the phenylalanine hydroxylation system. Proc Natl Acad Sci USA 95:1500-1504.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1500-1504
    • Lei, X.-D.1    Kaufman, S.2
  • 10
    • 0032404015 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of the vitamin D receptor (VDR) and a putative role for SUG1 interaction with the AF-2 domain of VDR
    • Masuyama H, MacDonald PN. 1998. Proteasome-mediated degradation of the vitamin D receptor (VDR) and a putative role for SUG1 interaction with the AF-2 domain of VDR. J Cell Biochem 71:429-440.
    • (1998) J Cell Biochem , vol.71 , pp. 429-440
    • Masuyama, H.1    MacDonald, P.N.2
  • 12
    • 0031888276 scopus 로고    scopus 로고
    • Bone-specific expression of the alpha chain of the nascent polypeptide-associated complex, a coactivator potentiating c-Jun-mediated transcription
    • Moreau A, Yotov WV, Glorieux FH, St-Arnaud, R. 1998. Bone-specific expression of the alpha chain of the nascent polypeptide-associated complex, a coactivator potentiating c-Jun-mediated transcription. Mol Cell Biol 18:1312-1321.
    • (1998) Mol Cell Biol , vol.18 , pp. 1312-1321
    • Moreau, A.1    Yotov, W.V.2    Glorieux, F.H.3    St-Arnaud, R.4
  • 13
    • 0031908790 scopus 로고    scopus 로고
    • Binding of signal recognition particle gives ribosome/nascent chain complexes a competitive advantage in endoplasmic reticulum membrane interaction
    • Neuhof A, Rolls MM, Jungnickel B, Kalies K-U, Rapoport TA. 1998. Binding of signal recognition particle gives ribosome/nascent chain complexes a competitive advantage in endoplasmic reticulum membrane interaction. Mol Biol Cell 9:103-115.
    • (1998) Mol Biol Cell , vol.9 , pp. 103-115
    • Neuhof, A.1    Rolls, M.M.2    Jungnickel, B.3    Kalies, K.-U.4    Rapoport, T.A.5
  • 16
    • 0025788098 scopus 로고
    • Oncogenic and transcriptional cooperation with Ha-ras requires phosphorylation of c-Jun on serines 63 and 73
    • Smeal T, Binetruy B, Mercola DA, Birrer M, Karin M. 1991. Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73. Nature 354:494-496.
    • (1991) Nature , vol.354 , pp. 494-496
    • Smeal, T.1    Binetruy, B.2    Mercola, D.A.3    Birrer, M.4    Karin, M.5
  • 17
    • 0030761857 scopus 로고    scopus 로고
    • The bifunctional DCOH protein binds to HNF1 independently of its 4α-carbinolamine dehydratase activity
    • Sourdive DJD, Transy C, Garbay S, Yaniv M. 1997. The bifunctional DCOH protein binds to HNF1 independently of its 4α-carbinolamine dehydratase activity. Nucleic Acids Res 25:1476-1484.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1476-1484
    • Sourdive, D.J.D.1    Transy, C.2    Garbay, S.3    Yaniv, M.4
  • 18
    • 0029860455 scopus 로고    scopus 로고
    • Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11), suppress G-protein-and mitogen-activated protein kinase-mediated signal transduction in yeast and mammalian cells
    • Spain BH, Bowdish KS, Pacal AR, Staub SF, Koo D, Chang CY, Xie W, Colicelli J. 1996. Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11), suppress G-protein-and mitogen-activated protein kinase-mediated signal transduction in yeast and mammalian cells. Mol Cell Biol 16:6698-6706.
    • (1996) Mol Cell Biol , vol.16 , pp. 6698-6706
    • Spain, B.H.1    Bowdish, K.S.2    Pacal, A.R.3    Staub, S.F.4    Koo, D.5    Chang, C.Y.6    Xie, W.7    Colicelli, J.8
  • 19
    • 0030600140 scopus 로고    scopus 로고
    • Structure and function of PCD/ DCoH, an enzyme with regulatory properties
    • Suck D, Ficner R. 1996. Structure and function of PCD/ DCoH, an enzyme with regulatory properties. FEBS Lett 389:35-39.
    • (1996) FEBS Lett , vol.389 , pp. 35-39
    • Suck, D.1    Ficner, R.2
  • 20
    • 0026681291 scopus 로고
    • Alterations in a yeast protein resembling HIV Tat-binding protein relieve requirement for an acidic activation domain in GAL4
    • Swaffield JC, Bromberg JF, Johnston SA. 1992. Alterations in a yeast protein resembling HIV Tat-binding protein relieve requirement for an acidic activation domain in GAL4. Nature 357:698-700.
    • (1992) Nature , vol.357 , pp. 698-700
    • Swaffield, J.C.1    Bromberg, J.F.2    Johnston, S.A.3
  • 21
    • 0028890360 scopus 로고
    • A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein
    • Swaffield JC, Melcher K, Johnston SA. 1995. A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein. Nature 374:88-91.
    • (1995) Nature , vol.374 , pp. 88-91
    • Swaffield, J.C.1    Melcher, K.2    Johnston, S.A.3
  • 22
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D, Zwickl P, Baumeister W. 1999. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 68:1015-1068.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.