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Volumn 40, Issue 7, 1999, Pages 1343-1350

Pax-6 interactions with TATA-box-binding protein and retinoblastoma protein

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTALLIN; RETINOBLASTOMA PROTEIN; TATA BINDING PROTEIN;

EID: 0033014232     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (56)

References (63)
  • 2
    • 0030219742 scopus 로고    scopus 로고
    • Lens development and crystallin gene expression: Many roles for Pax-6
    • Cvekl A, Piatigorsky J. Lens development and crystallin gene expression: many roles for Pax-6. Bioessays. 1996;18:621-630.
    • (1996) Bioessays , vol.18 , pp. 621-630
    • Cvekl, A.1    Piatigorsky, J.2
  • 5
    • 0028308664 scopus 로고
    • Mutations at the PAX6 locus are found in heterogeneous anterior segment malformations including Peter's anomaly
    • Hanson IM, Fletcher JM, Jordan T, et al. Mutations at the PAX6 locus are found in heterogeneous anterior segment malformations including Peter's anomaly. Nat Genet. 1994;6:168-173.
    • (1994) Nat Genet. , vol.6 , pp. 168-173
    • Hanson, I.M.1    Fletcher, J.M.2    Jordan, T.3
  • 6
  • 8
    • 0026345992 scopus 로고
    • Mouse small eye results from mutations in a paired-like homeobox-containing gene
    • Hill RE, Favor J, Hogan BLM, et al. Mouse small eye results from mutations in a paired-like homeobox-containing gene. Nature. 1991;354:522-525.
    • (1991) Nature , vol.354 , pp. 522-525
    • Hill, R.E.1    Favor, J.2    Hogan, B.L.M.3
  • 9
    • 0028074973 scopus 로고
    • PAX6 gene dosage effects in a family with congenital cataracts, aniridia, anophthalmia and central nervous system defects
    • Glaser T, Jepeal L, Edwards JG, Young SR, Favor J, Maas RL. PAX6 gene dosage effects in a family with congenital cataracts, aniridia, anophthalmia and central nervous system defects. Nat Genet. 1994;7:463-471.
    • (1994) Nat Genet. , vol.7 , pp. 463-471
    • Glaser, T.1    Jepeal, L.2    Edwards, J.G.3    Young, S.R.4    Favor, J.5    Maas, R.L.6
  • 10
    • 0030581164 scopus 로고    scopus 로고
    • Influence of PAX6 gene dosage on development: Overexpression causes severe eye abnormalities
    • Schedl A, Ross A, Lee M, et al. Influence of PAX6 gene dosage on development: overexpression causes severe eye abnormalities. Cell. 1996;86:71-82.
    • (1996) Cell , vol.86 , pp. 71-82
    • Schedl, A.1    Ross, A.2    Lee, M.3
  • 11
    • 0030923056 scopus 로고    scopus 로고
    • Direct regulation of rhodopsin 1 by Pax-6/eyeless in Drosophila: Evidence for a conserved function in photoreceptors
    • Sheng G, Thouvenot E, Schmucker D, Wilson DS, Desplan C. Direct regulation of rhodopsin 1 by Pax-6/eyeless in Drosophila: evidence for a conserved function in photoreceptors. Genes Dev. 1997;11:1122-1131.
    • (1997) Genes Dev. , vol.11 , pp. 1122-1131
    • Sheng, G.1    Thouvenot, E.2    Schmucker, D.3    Wilson, D.S.4    Desplan, C.5
  • 12
    • 23444441161 scopus 로고
    • Pax-6 is first expressed in a region of ectoderm anterior to the early neural plate: Implications for stepwise determination of the lens
    • Li, HS, Yang JM, Jacobson RD, Pasko D, Sundin O. Pax-6 is first expressed in a region of ectoderm anterior to the early neural plate: implications for stepwise determination of the lens. Dev Biol. 1994;162:181-194.
    • (1994) Dev Biol. , vol.162 , pp. 181-194
    • Li, H.S.1    Yang, J.M.2    Jacobson, R.D.3    Pasko, D.4    Sundin, O.5
  • 13
    • 0026340588 scopus 로고
    • Pax-6, a murine paired box gene, is expressed in the developing CNS
    • Walther C, Gruss P. Pax-6, a murine paired box gene, is expressed in the developing CNS. Development. 1991;113:1435-1449.
    • (1991) Development , vol.113 , pp. 1435-1449
    • Walther, C.1    Gruss, P.2
  • 14
    • 0029944653 scopus 로고    scopus 로고
    • A role for the Msx-1 homeodomain in transcriptional regulation: Residues in the N-terminal arm mediate TATA binding protein interaction and transcriptional repression
    • Zhang H, Catron KM, Abate-Shen C. A role for the Msx-1 homeodomain in transcriptional regulation: residues in the N-terminal arm mediate TATA binding protein interaction and transcriptional repression. Proc Natl Acad Sci USA. 1996;93:1764-1769.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1764-1769
    • Zhang, H.1    Catron, K.M.2    Abate-Shen, C.3
  • 15
    • 0029098480 scopus 로고
    • The transcriptional repressor even-skipped interacts directly with TATA-binding protein
    • Um M, Li C, Manley JL. The transcriptional repressor Even-skipped interacts directly with TATA-binding protein. Mol Cell Biol. 1995; 15:5007-5016.
    • (1995) Mol Cell Biol. , vol.15 , pp. 5007-5016
    • Um, M.1    Li, C.2    Manley, J.L.3
  • 16
    • 0030013203 scopus 로고    scopus 로고
    • Biochemistry and structural biology of transcription factor HD (TFIID)
    • Burley SK, Roeder RG. Biochemistry and structural biology of transcription factor HD (TFIID). Annu Rev Biochem. 1996;65: 769-799.
    • (1996) Annu Rev Biochem. , vol.65 , pp. 769-799
    • Burley, S.K.1    Roeder, R.G.2
  • 17
    • 0029042392 scopus 로고
    • Common themes in assembly and function of eukaryotic transcription complexes
    • Zawel L, Reinberg D. Common themes in assembly and function of eukaryotic transcription complexes. Annu Rev Biochem. 1995;64: 533-561.
    • (1995) Annu Rev Biochem. , vol.64 , pp. 533-561
    • Zawel, L.1    Reinberg, D.2
  • 19
    • 0032518906 scopus 로고    scopus 로고
    • Interaction of the pRB-family proteins with factors containing paired-like homeodomains
    • Wiggan O, Taniguchi-Sidle A, Hamel PA. Interaction of the pRB-family proteins with factors containing paired-like homeodomains. Oncogene. 1998;16:227-236.
    • (1998) Oncogene , vol.16 , pp. 227-236
    • Wiggan, O.1    Taniguchi-Sidle, A.2    Hamel, P.A.3
  • 20
    • 0027999510 scopus 로고
    • A complex array of positive and negative elements regulates the chicken αA-crystallin gene: Involvement of Pax-6, USF, CREB and/or CREM, and AP-1 proteins
    • Cvekl A, Sax CM, Bresnick EH, Piatigorsky J. A complex array of positive and negative elements regulates the chicken αA-crystallin gene: involvement of Pax-6, USF, CREB and/or CREM, and AP-1 proteins. Mol Cell Biol. 1994;14:7363-7376.
    • (1994) Mol Cell Biol. , vol.14 , pp. 7363-7376
    • Cvekl, A.1    Sax, C.M.2    Bresnick, E.H.3    Piatigorsky, J.4
  • 21
    • 0028869811 scopus 로고
    • Transcriptional regulation of the mouse αA-crystallin gene: Activation dependent on a cyclic AMP-responsive element (DE1/CRE) and a Pax-6-binding site
    • Cvekl A, Kashanchi F, Sax CM, Brady JN, Piatigorsky J. Transcriptional regulation of the mouse αA-crystallin gene: activation dependent on a cyclic AMP-responsive element (DE1/CRE) and a Pax-6-binding site. Mol Cell Biol. 1995;15:653-660.
    • (1995) Mol Cell Biol. , vol.15 , pp. 653-660
    • Cvekl, A.1    Kashanchi, F.2    Sax, C.M.3    Brady, J.N.4    Piatigorsky, J.5
  • 23
    • 0029013329 scopus 로고
    • Pax-6 is essential for lens-specific expression of ζ-crystallin
    • Richardson J, Cvekl A, Wistow G. Pax-6 is essential for lens-specific expression of ζ-crystallin. Proc Natl Acad Sci USA. 1995;92:4676-4680.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4676-4680
    • Richardson, J.1    Cvekl, A.2    Wistow, G.3
  • 24
    • 0031900978 scopus 로고    scopus 로고
    • Lens-specific recruitment of ζ-crystallin through Pax6, Nrl-Maf, and brain suppressor sites
    • Sharon-Friling R, Richardson J, Sperbeck S, et al. Lens-specific recruitment of ζ-crystallin through Pax6, Nrl-Maf, and brain suppressor sites. Mol Cell Biol. 1998;18:2067-2076.
    • (1998) Mol Cell Biol. , vol.18 , pp. 2067-2076
    • Sharon-Friling, R.1    Richardson, J.2    Sperbeck, S.3
  • 25
    • 0029661444 scopus 로고    scopus 로고
    • Pax-6 and αB-crystallin/small heat shock protein gene regulation in the murine lens: Interaction with the lens-specific regions, LSR1 and LSR2
    • Gopal-Srivastava R, Cvekl A, Piatigorsky J. Pax-6 and αB-crystallin/small heat shock protein gene regulation in the murine lens: interaction with the lens-specific regions, LSR1 and LSR2. J Biol Chem. 1996;271:23029-23036.
    • (1996) J Biol Chem. , vol.271 , pp. 23029-23036
    • Gopal-Srivastava, R.1    Cvekl, A.2    Piatigorsky, J.3
  • 26
    • 0031840442 scopus 로고    scopus 로고
    • Dual roles for Pax-6: A transcriptional repressor of lens fiber-cell specific β-crystallin genes
    • Duncan M, Haynes JI, Cvekl A, Piatigorsky J. Dual roles for Pax-6: a transcriptional repressor of lens fiber-cell specific β-crystallin genes. Mol Cell Biol. 1998;18:5579-5586.
    • (1998) Mol Cell Biol. , vol.18 , pp. 5579-5586
    • Duncan, M.1    Haynes, J.I.2    Cvekl, A.3    Piatigorsky, J.4
  • 27
    • 0027934570 scopus 로고
    • p53-dependent apoptosis produced by RB-deficiency in the developing mouse lens
    • Morgenbesser SD, Williams BO, Jacks T, DePinho RA. p53-dependent apoptosis produced by RB-deficiency in the developing mouse lens. Nature. 1994;371:72-74.
    • (1994) Nature. , vol.371 , pp. 72-74
    • Morgenbesser, S.D.1    Williams, B.O.2    Jacks, T.3    DePinho, R.A.4
  • 28
    • 0028101051 scopus 로고
    • Developmental rescue of an embryonic-lethal mutation in the retinoblastoma gene in chimeric mice
    • Maandag ECR, van der Valk M, Vlaar M, et al. Developmental rescue of an embryonic-lethal mutation in the retinoblastoma gene in chimeric mice. EMBOJ. 1994;13:4260-4268.
    • (1994) EMBOJ. , vol.13 , pp. 4260-4268
    • Maandag, E.C.R.1    Van Der Valk, M.2    Vlaar, M.3
  • 29
    • 0027968207 scopus 로고
    • Extensive contribution of Rb-deficient cells to adult chimeric mice with limited histopathological consequences
    • Williams, BO, Schmitt EM, Remington L, et al. Extensive contribution of Rb-deficient cells to adult chimeric mice with limited histopathological consequences. EMBOJ. 1994;13:4251-4259.
    • (1994) EMBOJ. , vol.13 , pp. 4251-4259
    • Williams, B.O.1    Schmitt, E.M.2    Remington, L.3
  • 30
    • 0028071541 scopus 로고
    • The retinoblastoma protein-binding region of simian virus 40 large T antigen alters cell cycle regulation in lens of transgenic mice
    • Fromm L, Shawlot W, Gunning K, Butel JS, Overbeek PA. The retinoblastoma protein-binding region of simian virus 40 large T antigen alters cell cycle regulation in lens of transgenic mice. Mol Cell Biol. 1994;14:6743-6754.
    • (1994) Mol Cell Biol. , vol.14 , pp. 6743-6754
    • Fromm, L.1    Shawlot, W.2    Gunning, K.3    Butel, J.S.4    Overbeek, P.A.5
  • 31
    • 0028334011 scopus 로고
    • Altered cell cycle regulation in the lens of HPV-16 E6 or E7 transgenic mice: Implications for tumor suppressor gene function in development
    • Pan H, Griep AE. Altered cell cycle regulation in the lens of HPV-16 E6 or E7 transgenic mice: implications for tumor suppressor gene function in development. Genes Dev. 1994;8:1285-1299.
    • (1994) Genes Dev. , vol.8 , pp. 1285-1299
    • Pan, H.1    Griep, A.E.2
  • 32
    • 0027426925 scopus 로고
    • DNA sequence recognition structure of the paired domain and its binding site
    • Czemy T, Schaffner G, Busslinger M. DNA sequence recognition structure of the paired domain and its binding site. Genes Dev. 1993;7:2048-2061.
    • (1993) Genes Dev. , vol.7 , pp. 2048-2061
    • Czemy, T.1    Schaffner, G.2    Busslinger, M.3
  • 33
    • 0025186708 scopus 로고
    • Differential transcriptional activation by Oct-1 and Oct-2: Interdependent activation domains induce Oct-2 phosphorylation
    • Tanaka M, Herr W. Differential transcriptional activation by Oct-1 and Oct-2: interdependent activation domains induce Oct-2 phosphorylation. Cell. 1990;60:375-386.
    • (1990) Cell , vol.60 , pp. 375-386
    • Tanaka, M.1    Herr, W.2
  • 34
    • 0029762617 scopus 로고    scopus 로고
    • Domains: A and B in the Rb pocket interact to form a transcriptional repressor motif
    • Chow KNB, Dean DC. Domains: A and B in the Rb pocket interact to form a transcriptional repressor motif. Mol Cell Biol. 1996; 16: 4862-4868.
    • (1996) Mol Cell Biol. , vol.16 , pp. 4862-4868
    • Chow, K.N.B.1    Dean, D.C.2
  • 35
    • 0029769523 scopus 로고    scopus 로고
    • The retinoblastoma gene product (Rb) induces binding of a conformationally inactive nuclear factor-κB
    • Tamami M, Lindholm PF, Brady JN. The retinoblastoma gene product (Rb) induces binding of a conformationally inactive nuclear factor-κB. J Biol Chem. 1996;271:24551-24556.
    • (1996) J Biol Chem. , vol.271 , pp. 24551-24556
    • Tamami, M.1    Lindholm, P.F.2    Brady, J.N.3
  • 36
    • 0029951161 scopus 로고    scopus 로고
    • Conservation and diversification in homeodomain-DNA interactions: A comparative genetic analysis
    • Wilson DS, Sheng G, Jun S, Desplan C. Conservation and diversification in homeodomain-DNA interactions: a comparative genetic analysis. Proc Natl Acad Sci USA. 1996;93:6886-6891.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6886-6891
    • Wilson, D.S.1    Sheng, G.2    Jun, S.3    Desplan, C.4
  • 37
    • 0026410043 scopus 로고
    • A quick procedure for purification of functional recombinant proteins over-expressed in E. coli
    • Pognonec P, Kato H, Sumimoto H, Kretzschmar M, Roeder RG. A quick procedure for purification of functional recombinant proteins over-expressed in E. coli. Nucleic Acids Res. 1991;19: 6650.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6650
    • Pognonec, P.1    Kato, H.2    Sumimoto, H.3    Kretzschmar, M.4    Roeder, R.G.5
  • 38
    • 0027367938 scopus 로고
    • Characterization of quail Pax-6 (Pax-QNR) proteins expressed in the neuroretina
    • Carriere C, Plaza S, Martin P, et al. Characterization of quail Pax-6 (Pax-QNR) proteins expressed in the neuroretina. Mol Cell Biol. 1993;13:7257-7266.
    • (1993) Mol Cell Biol. , vol.13 , pp. 7257-7266
    • Carriere, C.1    Plaza, S.2    Martin, P.3
  • 39
    • 0029738393 scopus 로고    scopus 로고
    • Role of Olf-1 and Pax-6 transcription factors in neurodevelopment
    • Davis JA, Reed RR. Role of Olf-1 and Pax-6 transcription factors in neurodevelopment. J Neurosci. 1996;16:5082-5094.
    • (1996) J Neurosci. , vol.16 , pp. 5082-5094
    • Davis, J.A.1    Reed, R.R.2
  • 40
    • 0023732884 scopus 로고    scopus 로고
    • Factors involved in specific transcription by mammalian RNA polymerase: Purification, genetic specificity and TATA-box promoter interactions of TFIID
    • Nakajima N, Horikoshi M, Roeder RG. Factors involved in specific transcription by mammalian RNA polymerase: purification, genetic specificity and TATA-box promoter interactions of TFIID. Mol Cell Biol. 1998;8:4028-4040.
    • (1998) Mol Cell Biol. , vol.8 , pp. 4028-4040
    • Nakajima, N.1    Horikoshi, M.2    Roeder, R.G.3
  • 41
    • 0028181310 scopus 로고
    • Direct interaction of human TFIID with the HIV-1 transactivator Tat
    • Kashanchi F, Piras G, Radonovich MF, et al. Direct interaction of human TFIID with the HIV-1 transactivator Tat. Nature. 1994;367: 295-299.
    • (1994) Nature , vol.367 , pp. 295-299
    • Kashanchi, F.1    Piras, G.2    Radonovich, M.F.3
  • 42
    • 0026651978 scopus 로고
    • Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations
    • Lai JS, Herr W. Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations. Proc Natl Acad Sci USA. 1992;89:6958-6962.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6958-6962
    • Lai, J.S.1    Herr, W.2
  • 43
    • 0028908796 scopus 로고
    • Two domains of p53 interact with the TATA-binding protein, and the Adenovirus 13S E1A protein disrupts the association, relieving p53-mediated transcriptional repression
    • Horikoshi N, Usheva A, Chen J, Levine AJ, Weinmann R, Shenk T. Two domains of p53 interact with the TATA-binding protein, and the Adenovirus 13S E1A protein disrupts the association, relieving p53-mediated transcriptional repression. Mol Cell Biol. 1995;15: 227-234.
    • (1995) Mol Cell Biol. , vol.15 , pp. 227-234
    • Horikoshi, N.1    Usheva, A.2    Chen, J.3    Levine, A.J.4    Weinmann, R.5    Shenk, T.6
  • 44
    • 0027511495 scopus 로고
    • The activation domain of transcription factor PU. 1 binds the retinoblastoma (RB) protein and the transcription factor TFIID in vitro: RB shows sequence similarity to TFIID and TFIIB
    • Hagemeier C, Bannister AJ, Cook A, Kouzarides T. The activation domain of transcription factor PU. 1 binds the retinoblastoma (RB) protein and the transcription factor TFIID in vitro: RB shows sequence similarity to TFIID and TFIIB. Proc Natl Acad Sci USA. 1993;90:1580-1584.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1580-1584
    • Hagemeier, C.1    Bannister, A.J.2    Cook, A.3    Kouzarides, T.4
  • 45
    • 0026526437 scopus 로고
    • E2F: A link between the Rb tumor suppressor protein and viral oncoproteins
    • Nevins JR. E2F: a link between the Rb tumor suppressor protein and viral oncoproteins. Science. 1992;258:424-429.
    • (1992) Science , vol.258 , pp. 424-429
    • Nevins, J.R.1
  • 46
    • 0031016121 scopus 로고    scopus 로고
    • RB kinases and RB-binding proteins: New points of view
    • Taya Y. RB kinases and RB-binding proteins: new points of view. Trends Biochem Sci. 1997;22:14-17.
    • (1997) Trends Biochem Sci. , vol.22 , pp. 14-17
    • Taya, Y.1
  • 47
    • 0032556919 scopus 로고    scopus 로고
    • pRb and p107 regulate E2F activity during lens fiber cell differentiation
    • Rampalli AM, Chauthaiwale VM, Gao CY, Zelenka PS. pRb and p107 regulate E2F activity during lens fiber cell differentiation. Oncogene. 1998;16:399-408.
    • (1998) Oncogene , vol.16 , pp. 399-408
    • Rampalli, A.M.1    Chauthaiwale, V.M.2    Gao, C.Y.3    Zelenka, P.S.4
  • 48
    • 0025265810 scopus 로고
    • Synthesis of α-crystallin by a cell line derived from the lens of a transgenic animal
    • Yamada T, Nakamura T, Westphal H, Russell P. Synthesis of α-crystallin by a cell line derived from the lens of a transgenic animal. Curr Eye Res. 1989;9:31-37.
    • (1989) Curr Eye Res. , vol.9 , pp. 31-37
    • Yamada, T.1    Nakamura, T.2    Westphal, H.3    Russell, P.4
  • 49
    • 0026507091 scopus 로고
    • Transcription factor IID mutants defective for interactions with transcription factor IIA
    • Buratowski S, Zhou H. Transcription factor IID mutants defective for interactions with transcription factor IIA. Science. 1992;255: 1130-1132.
    • (1992) Science , vol.255 , pp. 1130-1132
    • Buratowski, S.1    Zhou, H.2
  • 50
    • 0026040678 scopus 로고
    • Adenovirus E1A activation domain binds the basic repeat in the TATA box transcription factor
    • Lee WS, Kao CC, Bryant GO, Liu X, Berk AJ. Adenovirus E1A activation domain binds the basic repeat in the TATA box transcription factor. Cell. 1991;67:365-376.
    • (1991) Cell , vol.67 , pp. 365-376
    • Lee, W.S.1    Kao, C.C.2    Bryant, G.O.3    Liu, X.4    Berk, A.J.5
  • 51
    • 0027454228 scopus 로고
    • Association between protooncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-κB
    • Kerr LD, Ransone LJ, Wamsley P, et al Association between protooncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-κB. Nature. 1993;365:412-419.
    • (1993) Nature , vol.365 , pp. 412-419
    • Kerr, L.D.1    Ransone, L.J.2    Wamsley, P.3
  • 52
    • 0028930848 scopus 로고
    • GAL4 interacts with TATA-binding protein and coactivators
    • Melcher K, Johnston SA. GAL4 interacts with TATA-binding protein and coactivators. Mol Cell Biol. 1995;15:2839-2848.
    • (1995) Mol Cell Biol. , vol.15 , pp. 2839-2848
    • Melcher, K.1    Johnston, S.A.2
  • 53
    • 0028209305 scopus 로고
    • Species-specific interaction of the glutamine-rich activation domains of Sp1 with the TATA box-binding protein
    • Emili A, Greenbelt J, Ingles CJ. Species-specific interaction of the glutamine-rich activation domains of Sp1 with the TATA box-binding protein. Mol Cell Biol. 1994;14:1582-1593.
    • (1994) Mol Cell Biol. , vol.14 , pp. 1582-1593
    • Emili, A.1    Greenbelt, J.2    Ingles, C.J.3
  • 54
    • 15644384251 scopus 로고    scopus 로고
    • Cooperative and competitive interactions at the hsp70 promoter
    • Mason PB, Lis JT Cooperative and competitive interactions at the hsp70 promoter. J Biol Chem. 1997;272:33227-33233.
    • (1997) J Biol Chem. , vol.272 , pp. 33227-33233
    • Mason, P.B.1    Lis, J.T.2
  • 55
    • 0032555505 scopus 로고    scopus 로고
    • Truncation mutations in the transactivation region of PAX6 result in dominant-negative mutants
    • Singh S, Tang HK, Lee JY, Saunders GF. Truncation mutations in the transactivation region of PAX6 result in dominant-negative mutants. J Biol Chem. 1998;273:21531-21541.
    • (1998) J Biol Chem. , vol.273 , pp. 21531-21541
    • Singh, S.1    Tang, H.K.2    Lee, J.Y.3    Saunders, G.F.4
  • 56
    • 0028920396 scopus 로고
    • Lens-specific activity of the mouse αA-crystallin promoter in the absence of a TATA box: Functional and protein binding analysis of the mouse αA-crystallin PE1 region
    • Sax CM, Cvekl A, Kantorow M, et al. Lens-specific activity of the mouse αA-crystallin promoter in the absence of a TATA box: functional and protein binding analysis of the mouse αA-crystallin PE1 region. Nucleic Acids Res. 1995;23:442-451.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 442-451
    • Sax, C.M.1    Cvekl, A.2    Kantorow, M.3
  • 57
    • 0031577746 scopus 로고    scopus 로고
    • αB-crystallin TATA sequence mutations: Lens-preference for the proximal TATA box and the distal TATA-like sequence in transgenic mice
    • Haynes JI, Gopal-Srivastava R, Piatigorsky J. αB-crystallin TATA sequence mutations: lens-preference for the proximal TATA box and the distal TATA-like sequence in transgenic mice. Biochem Biophys Res Commun. 1997;241:407-413.
    • (1997) Biochem Biophys Res Commun. , vol.241 , pp. 407-413
    • Haynes, J.I.1    Gopal-Srivastava, R.2    Piatigorsky, J.3
  • 58
    • 0029874066 scopus 로고    scopus 로고
    • C-terminal activating and inhibitory domains determine the transactivation potential of BSAP (Pax-5), Pax-2 and Pax-8
    • Dorfler P, Busslinger M. C-terminal activating and inhibitory domains determine the transactivation potential of BSAP (Pax-5), Pax-2 and Pax-8. EMBO J. 1996;15:1971-1982.
    • (1996) EMBO J. , vol.15 , pp. 1971-1982
    • Dorfler, P.1    Busslinger, M.2
  • 59
    • 0029829889 scopus 로고    scopus 로고
    • Mapping of Pax-2 transcription activation domains
    • Lechner MS, Dressier GR. Mapping of Pax-2 transcription activation domains. J Biol Chem. 1996;271:21088-21093.
    • (1996) J Biol Chem. , vol.271 , pp. 21088-21093
    • Lechner, M.S.1    Dressier, G.R.2
  • 60
    • 0028269517 scopus 로고
    • A mechanism for TAFs in transcriptional activation: Activation domain enhancement of TFIID-TFIIA-promoter DNA complex formation
    • Lieberman PM, Berk AJ. A mechanism for TAFs in transcriptional activation: activation domain enhancement of TFIID-TFIIA-promoter DNA complex formation. Genes Dev. 1994;8:995-1006.
    • (1994) Genes Dev. , vol.8 , pp. 995-1006
    • Lieberman, P.M.1    Berk, A.J.2
  • 61
    • 0032483574 scopus 로고    scopus 로고
    • TATA box mimicry by TFIID: Autoinhibition of Pol II transcription
    • Burley SK, Roeder RG. TATA box mimicry by TFIID: autoinhibition of Pol II transcription. Cell. 1998;94:551-553.
    • (1998) Cell , vol.94 , pp. 551-553
    • Burley, S.K.1    Roeder, R.G.2
  • 62
    • 0032524742 scopus 로고    scopus 로고
    • The expanding role of cell cycle regulators
    • Jacks T, Weinberg RA. The expanding role of cell cycle regulators. Science. 1998;280:1035-1036.
    • (1998) Science , vol.280 , pp. 1035-1036
    • Jacks, T.1    Weinberg, R.A.2
  • 63
    • 0027252649 scopus 로고
    • The oncogenic potential of Pax genes
    • Maulbecker CC, Gruss P. The oncogenic potential of Pax genes. EMBO J. 1993;12:2361-2367.
    • (1993) EMBO J. , vol.12 , pp. 2361-2367
    • Maulbecker, C.C.1    Gruss, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.