The carboxy-terminal domain of the XPC protein plays a crucial role in nucleotide excision repair through interactions with transcription factor IIH.
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Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein.A DNA repair complex functions as an Oct4/Sox2 coactivator in embryonic stem cellsGlobal-genome Nucleotide Excision Repair Controlled by Ubiquitin/Sumo ModifiersXeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulationDNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5aStructural and functional evidence that Rad4 competes with Rad2 for binding to the Tfb1 subunit of TFIIH in NERThe Rad4 homologue YDR314C is essential for strand-specific repair of RNA polymerase I-transcribed rDNA in Saccharomyces cerevisiae.Xeroderma pigmentosum group C protein possesses a high affinity binding site to human centrin 2 and calmodulinTwo-stage dynamic DNA quality check by xeroderma pigmentosum group C protein.Biochemical analysis of the damage recognition process in nucleotide excision repair.The protein shuffle. Sequential interactions among components of the human nucleotide excision repair pathway.The involvement of ataxia-telangiectasia mutated protein activation in nucleotide excision repair-facilitated cell survival with cisplatin treatment.Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein.An aromatic sensor with aversion to damaged strands confers versatility to DNA repairIn vivo destabilization and functional defects of the xeroderma pigmentosum C protein caused by a pathogenic missense mutationRegulation of nucleotide excision repair by UV-DDB: prioritization of damage recognition to internucleosomal DNASequential and ordered assembly of a large DNA repair complex on undamaged chromatin.Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways.XPA: A key scaffold for human nucleotide excision repair.Functional and mechanistic studies of XPC DNA-repair complex as transcriptional coactivator in embryonic stem cells.Recognition of DNA damage by XPC coincides with disruption of the XPC-RAD23 complexUbiquitylation-independent degradation of Xeroderma pigmentosum group C protein is required for efficient nucleotide excision repairDiagnosis of Xeroderma Pigmentosum Groups A and C by Detection of Two Prevalent Mutations in West Algerian Population: A Rapid Genotyping Tool for the Frequent XPC Mutation c.1643_1644delTGArchitecture of the human XPC DNA repair and stem cell coactivator complex.Nucleotide excision repair factor XPC enhances DNA damage-induced apoptosis by downregulating the antiapoptotic short isoform of caspase-2.Dissection of the molecular defects caused by pathogenic mutations in the DNA repair factor XPC.Eukaryotic nucleotide excision repair: from understanding mechanisms to influencing biology.Cells from long-lived mutant mice exhibit enhanced repair of ultraviolet lesions.The sequence dependence of human nucleotide excision repair efficiencies of benzo[a]pyrene-derived DNA lesions: insights into the structural factors that favor dual incisionsThe involvement of XPC protein in the cisplatin DNA damaging treatment-mediated cellular response.Analysis of DNA binding by human factor xeroderma pigmentosum complementation group A (XPA) provides insight into its interactions with nucleotide excision repair substrates.Structure of the XPC binding domain of hHR23A reveals hydrophobic patches for protein interaction.The C-terminal region of Xpc is dispensable for the transcriptional activity of Oct3/4 in mouse embryonic stem cells.RAD4 and RAD23/HMR Contribute to Arabidopsis UV Tolerance.Enhanced spontaneous DNA twisting/bending fluctuations unveiled by fluorescence lifetime distributions promote mismatch recognition by the Rad4 nucleotide excision repair complex.Chromatin remodeler CHD1 promotes XPC-to-TFIIH handover of nucleosomal UV lesions in nucleotide excision repair.
P2860
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P2860
The carboxy-terminal domain of the XPC protein plays a crucial role in nucleotide excision repair through interactions with transcription factor IIH.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
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2002年學術文章
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name
The carboxy-terminal domain of ...... with transcription factor IIH.
@en
type
label
The carboxy-terminal domain of ...... with transcription factor IIH.
@en
prefLabel
The carboxy-terminal domain of ...... with transcription factor IIH.
@en
P2093
P1433
P1476
The carboxy-terminal domain of ...... with transcription factor IIH
@en
P2093
Akio Uchida
Chikahide Masutani
Fumio Hanaoka
Kaoru Sugasawa
Naoshi Dohmae
Yoshiaki Ohkuma
P304
P356
10.1016/S1568-7864(02)00031-9
P577
2002-06-01T00:00:00Z