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NTIS 바로가기Cell, v.94 no.5, 1998년, pp.573 - 583
Liu, Dingjiang (Department of Medical Biophysics, Division of Molecular and Structural Biology, Ontario Cancer Institute, University of Toronto, Toronto, Ontario M5G 2M9, Canada) , Ishima, Rieko (Department of Medical Biophysics, Division of Molecular and Structural Biology, Ontario Cancer Institute, University of Toronto, Toronto, Ontario M5G 2M9, Canada) , Tong, Kit I (Department of Medical Biophysics, Division of Molecular and Structural Biology, Ontario Cancer Institute, University of Toronto, Toronto, Ontario M5G 2M9, Canada) , Bagby, Stefan (Department of Medical Biophysics, Division of Molecular and Structural Biology, Ontario Cancer Institute, University of Toronto, Toronto, Ontario M5G 2M9, Canada) , Kokubo, Tetsuro (Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA) , Muhandiram, D.R (Protein Engineering Network Centres of Excellence, Departments of Molecular and Medical Genetics, Biochemistry, and Chemistry, University of Toronto, Toronto, Ontario M5S 1A8, Cana) , Kay, Lewis E , Nakatani, Yoshihiro , Ikura, Mitsuhiko
AbstractGeneral transcription factor TFIID consists of TATA box–binding protein (TBP) and TBP-associated factors (TAFIIs), which together play a central role in both positive and negative regulation of transcription. The N-terminal region of the 230 kDa Drosophila TAFII (dTAFII230) binds dire...
EMBO J. Arndt 14 1490 1995 10.1002/j.1460-2075.1995.tb07135.x TBP mutants defective in activated transcription in vivo
J. Biol. Chem. Aso 269 26575 1994 10.1016/S0021-9258(18)47233-X Role of core promoter structure in assembly of the RNA polymerase II preinitiation complex. A common pathway for formation of preinitiation intermediates at many TATA and TATA-less promoters
J. Biomol. NMR Bagby 10 279 1997 10.1023/A:1018359305544 The button test
Brunger 1993 X-PLOR Version 3.1
Annu. Rev. Biochem. Burley 65 769 1996 10.1146/annurev.bi.65.070196.004005 Biochemistry and structural biology of transcription factor IID (TFIID)
Proc. Natl. Acad. Sci. USA Chasman 90 8174 1993 10.1073/pnas.90.17.8174 Crystal structure of yeast TATA-binding protein and model for interaction with DNA
J. Biol. Chem. Coleman 270 13842 1995 10.1074/jbc.270.23.13842 Dimerization of the TATA binding protein
J. Biomol. NMR Delaglio 6 277 1995 10.1007/BF00197809 NMRPipe
Cell Dikstein 84 781 1996 10.1016/S0092-8674(00)81055-7 TAFII250 is a bipartite protein kinase that phosphorylates the basal transcription factor RAP74
Mol. Cell. Biol. Drysdale 18 1711 1998 10.1128/MCB.18.3.1711 The Gcn4p activation domain interacts specifically in vitro with RNA polymerase II holoenzyme, TFIID, and the Adap-Gcn5p coactivator complex
Cell Frankel 92 149 1998 10.1016/S0092-8674(00)80908-3 Induced folding in RNA-protein recognition
J. Magn. Reson. Garrett 95 214 1991 A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams
Science Geiger 272 830 1996 10.1126/science.272.5263.830 Crystal structure of the yeast TFIIA-TBP-DNA complex
Mol. Cell. Biol. Guermah 18 3234 1998 10.1128/MCB.18.6.3234 Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-κB and Sp1
Genes Dev. Hernandez 7 1291 1993 10.1101/gad.7.7b.1291 TBP, a universal eukaryotic transcription factor?
J. Mol. Biol. Holm 233 123 1993 10.1006/jmbi.1993.1489 Protein structure comparison by alignment of distance matrices
J. Biomol. NMR Johnson 4 603 1994 10.1007/BF00404272 NMRView
Trends Biochem. Sci. Kaiser 21 342 1996 10.1016/S0968-0004(96)10043-8 The human general co-factors
J. Magn. Reson. Kay 86 110 1990 New methods for the measurement of NH-CαH coupling constants in 15N-labeled proteins
Curr. Opin. Struct. Biol. Kay 7 722 1997 10.1016/S0959-440X(97)80084-X Solution NMR spectroscopy beyond 25 kDa
Nat. Struct. Biol. Kim 1 638 1994 10.1038/nsb0994-638 1.9 A resolution refined structure of TBP recognizing the minor groove of TATAAAAG
Nature Kim 365 512 1993 10.1038/365512a0 Crystal structure of a yeast TBP/TATA-box complex
Nature Kim 365 520 1993 10.1038/365520a0 Co-crystal structure of TBP recognizing the minor groove of a TATA element
Nature Kim 369 252 1994 10.1038/369252a0 Effects of activation-defective TBP mutations on transcription initiation in yeast
J. Biol. Chem. Kokubo 268 17554 1993 10.1016/S0021-9258(19)85368-1 Identification of TFIID components required for transcriptional activation by upstream stimulatory factor
Proc. Natl. Acad. Sci. USA Kokubo 91 3520 1994 10.1073/pnas.91.9.3520 Interaction between the N-terminal domain of the 230-kDa subunit and the TATA box-binding subunit of TFIID negatively regulates TATA-box binding
Mol. Cell. Biol. Kokubo 18 1003 1998 10.1128/MCB.18.2.1003 The yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding protein
Proc. Natl. Acad. Sci. USA Kosa 94 6042 1997 10.1073/pnas.94.12.6042 The 2.1-A crystal structure of an archaeal preinitiation complex
Science Kussie 274 948 1996 10.1126/science.274.5289.948 Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
Mol. Cell. Biol. Lee 15 5461 1995 10.1128/MCB.15.10.5461 Mutations on the DNA-binding surface of TATA-binding protein can specifically impair the response to acidic activators in vivo
FEBS Lett. Lee 350 87 1994 10.1016/0014-5793(94)00740-3 A pulsed field gradient isotope-filtered 3D 13C HMQC-NOESY experiment for extracting intermolecular NOE contacts in molecular complexes
Methods Enzymol. Merritt 277 503 1997 Raster3D photorealistic molecular graphics
Cell Mizzen 87 1261 1996 10.1016/S0092-8674(00)81821-8 The TAFII250 subunit of TFIID has histone acetyltransferase activity
Cell Mol 82 701 1995 10.1016/0092-8674(95)90467-0 Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor
Nature Nakatani 348 86 1990 10.1038/348086a0 A downstream initiation element required for efficient TATA box binding and in vitro function of TFIID
Nicholls 1993 GRASP Manual
Nature Nikolov 360 40 1992 10.1038/360040a0 Crystal structure of TFIID TATA-box binding protein
Nature Nikolov 377 119 1995 10.1038/377119a0 Crystal structure of a TFIIB-TBP-TATA-element ternary complex
10.1007/978-1-4757-9794-7_37 Nilges, M., Kuszewski, J., and Brunger, A.T. (1991). Sampling properties of simulated annealing and distance geometry. In Computational Aspects of the Study of Biological Macromolecules by Nuclear Magnetic Resonance Spectroscopy, J.C. Hoch, F.M. Poulsen, and C. Redfield, eds. (New York: Plenum Press), pp. 451-455.
Proc. Natl. Acad. Sci. USA Nishikawa 94 85 1997 10.1073/pnas.94.1.85 Drosophila TAFII230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein
Science Nissen 270 1464 1995 10.1126/science.270.5241.1464 Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog
Mol. Cell O’Brien 1 905 1998 10.1016/S1097-2765(00)80089-1 Functional analysis of the human TAFII250 N-terminal kinase domain
Mol. Cell Oelgeschlager 1 925 1998 10.1016/S1097-2765(00)80092-1 Transcription activation via enhanced preinitiation complex assembly in a human cell-free system lacking TAFIIs
Cell Ogryzko 87 953 1996 10.1016/S0092-8674(00)82001-2 The transcriptional coactivators p300 and CBP are histone acetyltransferases
Proteins Orengo 14 139 1992 10.1002/prot.340140203 Fast structural alignment for protein databank searching
Genes Dev. Orphanides 10 2657 1996 10.1101/gad.10.21.2657 The general transcription factors of RNA polymerase II
J. Magn. Reson. B. Pascal 103 197 1994 10.1006/jmrb.1994.1031 Simultaneous acquisition of 15N- and 13C-edited NOE spectra of proteins dissolved in H2O
Biochemistry Perez-Howard 34 8005 1995 10.1021/bi00025a006 Yeast TATA binding protein interaction with DNA
Cell Radhakrishnan 91 741 1997 10.1016/S0092-8674(00)80463-8 Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB
Trends Biochem. Sci. Roeder 21 327 1996 10.1016/S0968-0004(96)10050-5 The role of general initiation factors in transcription by RNA polymerase II
Nature Russo 382 325 1996 10.1038/382325a0 Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
Nat. Struct. Biol. Savva 2 752 1995 10.1038/nsb0995-752 Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex
Science Spolar 263 777 1994 10.1126/science.8303294 Coupling of local folding to site-specific binding of proteins to DNA
Nature Tan 381 127 1996 10.1038/381127a0 Crystal structure of a yeast TFIIA/TBP/DNA complex
Science Uesugi 277 1310 1997 10.1126/science.277.5330.1310 Induced α helix in the VP16 activation domain upon binding to a human TAF
Cell Verrijzer 81 1115 1995 10.1016/S0092-8674(05)80016-9 Binding of TAFs to core elements directs promoter selectivity by RNA polymerase II
J. Am. Chem. Soc. Vuister 115 7772 1993 10.1021/ja00070a024 Quantitative J correlation
J. Biomol. NMR Wishart 4 171 1994 10.1007/BF00175245 The 13C chemical-shift index
J. Mol. Biol. Wuthrich 169 949 1983 10.1016/S0022-2836(83)80144-2 Pseudostructures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance
J. Am. Chem. Soc. Yamazaki 116 11655 1994 10.1021/ja00105a005 A suite of triple resonance NMR experiments for the backbone assignment of 15N, 13C, 2H labeled proteins with high sensitivity
Nature Yang 382 319 1996 10.1038/382319a0 A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
Cell Zhou 92 687 1998 10.1016/S0092-8674(00)81136-8 Solution structure of the core NFATC1/DNA complex
J. Am. Chem. Soc. Zwahlen 119 6711 1997 10.1021/ja970224q Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy
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