Structural determinants for substrate binding and catalysis by the structure-specific endonuclease XPG (Q24298019)

endodeoxyribonuclease activity

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

Marcel Hohl

1

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Fabrizio Thorel

2

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Stuart G Clarkson

3

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Orlando D Schärer

Journal of Biological Chemistry

4

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language of work or name

English

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publication date

23 May 2003

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published in

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volume

278

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issue

21

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page(s)

19500-8

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cites work

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Requirement of yeast RAD2, a homolog of human XPG gene, for efficient RNA polymerase II transcription. implications for Cockayne syndrome

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Cockayne syndrome: defective repair of transcription?

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Retracted: A common mutational pattern in Cockayne syndrome patients from xeroderma pigmentosum group G: implications for a second XPG function

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DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair

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Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome

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XPG protein has a structure-specific endonuclease activity

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Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein

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Essential amino acids for substrate binding and catalysis of human flap endonuclease 1

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Conserved residues of human XPG protein important for nuclease activity and function in nucleotide excision repair

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DNA recognition by structure-selective nucleases

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Base excision repair of oxidative DNA damage activated by XPG protein

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In eukaryotic flap endonuclease 1, the C terminus is essential for substrate binding

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Transcription-induced cleavage of immunoglobulin switch regions by nucleotide excision repair nucleases in vitro

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1074/JBC.M213155200

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Fatcat ID

release_wq6wxx3ldrb7jhw7o4gspwerrm

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/wq6wxx3ldrb7jhw7o4gspwerrm