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Volumn 15, Issue 9, 2008, Pages 980-984

Structural basis for group A trichothiodystrophy

Author keywords

[No Author keywords available]

Indexed keywords

TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR B2; TRANSCRIPTION FACTOR B5; TRANSCRIPTION FACTOR IIH; UNCLASSIFIED DRUG;

EID: 51349101549     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1478     Document Type: Article
Times cited : (47)

References (23)
  • 1
    • 0027760994 scopus 로고
    • Dual roles of a multiprotein complex from S. cerevisiae in transcription and DNA repair
    • Feaver, W.J. et al. Dual roles of a multiprotein complex from S. cerevisiae in transcription and DNA repair. Cell 75, 1379-1387 (1993).
    • (1993) Cell , vol.75 , pp. 1379-1387
    • Feaver, W.J.1
  • 2
    • 0027905008 scopus 로고
    • DNA repair helicase: A component of BTF2 (TFIIH) basic transcription factor
    • Schaeffer, L. et al. DNA repair helicase: a component of BTF2 (TFIIH) basic transcription factor. Science 260, 58-63 (1993).
    • (1993) Science , vol.260 , pp. 58-63
    • Schaeffer, L.1
  • 3
    • 0037115936 scopus 로고    scopus 로고
    • Subpathways of nucleotide excision repair and their regulation
    • Hanawalt, P.C. Subpathways of nucleotide excision repair and their regulation. Oncogene 21, 8949-8956 (2002).
    • (2002) Oncogene , vol.21 , pp. 8949-8956
    • Hanawalt, P.C.1
  • 4
    • 0030749609 scopus 로고    scopus 로고
    • Genes for Tfb2, Tfb3, and Tfb4 subunits of yeast transcription/repair factor IIH. Homology to human cyclin-dependent kinase activating kinase and IIH subunits
    • Feaver, W.J. et al. Genes for Tfb2, Tfb3, and Tfb4 subunits of yeast transcription/repair factor IIH. Homology to human cyclin-dependent kinase activating kinase and IIH subunits. J. Biol. Chem. 272, 19319-19327 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 19319-19327
    • Feaver, W.J.1
  • 5
    • 3042703022 scopus 로고    scopus 로고
    • Identification of TFB5, a new component of general transcription and DNA repair factor IIH
    • Ranish, J.A. et al. Identification of TFB5, a new component of general transcription and DNA repair factor IIH. Nat. Genet. 36, 707-713 (2004).
    • (2004) Nat. Genet , vol.36 , pp. 707-713
    • Ranish, J.A.1
  • 6
    • 34247482968 scopus 로고    scopus 로고
    • DNA repair and transcriptional deficiencies caused by mutations in the Drosophila p52 subunit of TFIIH generate developmental defects and chromosome fragility
    • Fregoso, M. et al. DNA repair and transcriptional deficiencies caused by mutations in the Drosophila p52 subunit of TFIIH generate developmental defects and chromosome fragility. Mol. Cell. Biol. 27, 3640-3650 (2007).
    • (2007) Mol. Cell. Biol , vol.27 , pp. 3640-3650
    • Fregoso, M.1
  • 7
    • 34247169028 scopus 로고    scopus 로고
    • Xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome: A complex genotype-phenotype relationship
    • Kraemer, K.H. et al. Xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome: a complex genotype-phenotype relationship. Neuroscience 145, 1388-1396 (2007).
    • (2007) Neuroscience , vol.145 , pp. 1388-1396
    • Kraemer, K.H.1
  • 8
    • 0038094503 scopus 로고    scopus 로고
    • Basal transcription defect discriminates between xeroderma pigmentosum and trichothiodystrophy in XPD patients
    • Dubaele, S. et al. Basal transcription defect discriminates between xeroderma pigmentosum and trichothiodystrophy in XPD patients. Mol. Cell 11, 1635-1646 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 1635-1646
    • Dubaele, S.1
  • 9
    • 30744438055 scopus 로고    scopus 로고
    • p8/TTD-A as a repair-specific TFIIH subunit
    • Coin, F. et al. p8/TTD-A as a repair-specific TFIIH subunit. Mol. Cell 21, 215-226 (2006).
    • (2006) Mol. Cell , vol.21 , pp. 215-226
    • Coin, F.1
  • 10
    • 33847415445 scopus 로고    scopus 로고
    • Tfb5 interacts with Tfb2 and facilitates nucleotide excision repair in yeast
    • Zhou, Y., Kou, H. & Wang, Z. Tfb5 interacts with Tfb2 and facilitates nucleotide excision repair in yeast. Nucleic Acids Res. 35, 861-871 (2007).
    • (2007) Nucleic Acids Res , vol.35 , pp. 861-871
    • Zhou, Y.1    Kou, H.2    Wang, Z.3
  • 11
    • 0036850542 scopus 로고    scopus 로고
    • Reduced level of the repair/transcription factor TFIIH in trichothiodystrophy
    • Botta, E. et al. Reduced level of the repair/transcription factor TFIIH in trichothiodystrophy. Hum. Mol. Genet. 11, 2919-2928 (2002).
    • (2002) Hum. Mol. Genet , vol.11 , pp. 2919-2928
    • Botta, E.1
  • 12
    • 3042781670 scopus 로고    scopus 로고
    • A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A
    • Giglia-Mari, G. et al. A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A. Nat. Genet. 36, 714-719 (2004).
    • (2004) Nat. Genet , vol.36 , pp. 714-719
    • Giglia-Mari, G.1
  • 13
    • 0031048846 scopus 로고    scopus 로고
    • Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH
    • Marinoni, J.C. et al. Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH. EMBO J. 16, 1093-1102 (1997).
    • (1997) EMBO J , vol.16 , pp. 1093-1102
    • Marinoni, J.C.1
  • 14
    • 0037200120 scopus 로고    scopus 로고
    • p52 mediates XPB function within the transcription/repair factor TFIIH
    • Jawhari, A. et al. p52 mediates XPB function within the transcription/repair factor TFIIH. J. Biol. Chem. 277, 31761-31767 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 31761-31767
    • Jawhari, A.1
  • 15
    • 33947578325 scopus 로고    scopus 로고
    • Solution structure and self-association properties of the p8 TFIIH subunit responsible for trichothiodystrophy
    • Vitorino, M. et al. Solution structure and self-association properties of the p8 TFIIH subunit responsible for trichothiodystrophy. J. Mol. Biol. 368, 473-480 (2007).
    • (2007) J. Mol. Biol , vol.368 , pp. 473-480
    • Vitorino, M.1
  • 16
    • 33746300776 scopus 로고    scopus 로고
    • Protein-protein interaction through β-strand addition
    • Remaut, H. & Waksman, G. Protein-protein interaction through β-strand addition. Trends Biochem. Sci. 31, 436-444 (2006).
    • (2006) Trends Biochem. Sci , vol.31 , pp. 436-444
    • Remaut, H.1    Waksman, G.2
  • 17
    • 0742321956 scopus 로고    scopus 로고
    • Chapados, B.R. et al. A. Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair. Cell 116, 39-50 (2004).
    • Chapados, B.R. et al. A. Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair. Cell 116, 39-50 (2004).
  • 18
    • 39749127748 scopus 로고    scopus 로고
    • The HhH domain of the human DNA repair protein XPF forms stable homodimers
    • Das, D. et al. The HhH domain of the human DNA repair protein XPF forms stable homodimers. Proteins 70, 1551-1563 (2008).
    • (2008) Proteins , vol.70 , pp. 1551-1563
    • Das, D.1
  • 19
    • 34247513888 scopus 로고    scopus 로고
    • Distinct roles for the XPB/p52 and XPD/p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair
    • Coin, F., Oksenych, V. & Egly, J.-M. Distinct roles for the XPB/p52 and XPD/p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair. Mol. Cell 26, 245-256 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 245-256
    • Coin, F.1    Oksenych, V.2    Egly, J.-M.3
  • 20
    • 0033768176 scopus 로고    scopus 로고
    • Sublimiting concentration of TFIIH transcription/DNA repair factor causes TTD-A trichothiodystrophy disorder
    • Vermeulen, W. et al. Sublimiting concentration of TFIIH transcription/DNA repair factor causes TTD-A trichothiodystrophy disorder. Nat. Genet. 26, 307-313 (2000).
    • (2000) Nat. Genet , vol.26 , pp. 307-313
    • Vermeulen, W.1
  • 21
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch, W.E., Morimoto, R.I., Dillin, A. & Kelly, J.W. Adapting proteostasis for disease intervention. Science 319, 916-919 (2008).
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 22
    • 33745199653 scopus 로고    scopus 로고
    • Dynamic interaction of TTDA with TFIIH is stabilized by nucleotide excision repair in living cells
    • Giglia-Mari, G. et al. Dynamic interaction of TTDA with TFIIH is stabilized by nucleotide excision repair in living cells. PLoS Biol. 4, e156 (2006).
    • (2006) PLoS Biol , vol.4
    • Giglia-Mari, G.1
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.