Common TFIIH recruitment mechanism in global genome and transcription-coupled repair subpathways.

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The essential and multi-functional TFIIH complex.Overexpression of xeroderma pigmentosum group C decreases the chemotherapeutic sensitivity of colorectal carcinoma cells to cisplatin.

P2860

Q52319133-E5BB1E44-D55D-4F79-BBAC-E1FF5CF90089 Q52721819-CAD6198A-E959-44C0-B871-F767CC75D8E7

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Common TFIIH recruitment mechanism in global genome and transcription-coupled repair subpathways.

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http://www.wikidata.org/entity/Q47122825

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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Common TFIIH recruitment mecha ...... on-coupled repair subpathways.

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Common TFIIH recruitment mecha ...... on-coupled repair subpathways.

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label

Common TFIIH recruitment mecha ...... on-coupled repair subpathways.

@en

Common TFIIH recruitment mecha ...... on-coupled repair subpathways.

@nl

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Common TFIIH recruitment mecha ...... on-coupled repair subpathways.

@en

Common TFIIH recruitment mecha ...... on-coupled repair subpathways.

@nl

P1476

Common TFIIH recruitment mecha ...... ion-coupled repair subpathways

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Chaowan Guo

http://www.w3.org/2001/XMLSchema#string

Masahiko Okuda

http://www.w3.org/2001/XMLSchema#string

Yuka Nakazawa

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P2860

Tools for integrated sequence-structure analysis with UCSF Chimera.

The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA

Mutations in UVSSA cause UV-sensitive syndrome and impair RNA polymerase IIo processing in transcription-coupled nucleotide-excision repair

UV-sensitive syndrome protein UVSSA recruits USP7 to regulate transcription-coupled repair

Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6 in transcription-coupled DNA repair

Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair

Structural insight into the TFIIE-TFIIH interaction: TFIIE and p53 share the binding region on TFIIH

Structural and functional characterization of an atypical activation domain in erythroid Kruppel-like factor (EKLF)

p53 and TFIIEalpha share a common binding site on the Tfb1/p62 subunit of TFIIH

NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53

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13043-13055

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scholarly article

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10.1093/NAR/GKX970

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English

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http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

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Tomoo Ogi

Yoshifumi Nishimura

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2017-12-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

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29069470

http://www.w3.org/2001/XMLSchema#string

P932

5727438

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Common TFIIH recruitment mechanism in global genome and transcription-coupled repair subpathways.

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P2860

P2860

Common TFIIH recruitment mechanism in global genome and transcription-coupled repair subpathways.

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932