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Xeroderma pigmentosum, group G

Known as: XERODERMA PIGMENTOSUM VII, XP, GROUP G, XPGC 
National Institutes of Health

Related topics

Related topics

11 relations
Autosomal recessive inheritanceBasal cell carcinomaCutaneous MelanomaERCC5 gene

Broader (1)

Xeroderma Pigmentosum

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2013
Review
2013
Oxidative DNA damage and nucleotide excision repair.
SIGNIFICANCE Oxidative DNA damage is repaired by multiple, overlapping DNA repair pathways. Accumulating evidence supports the… 
Highly Cited
2007
Highly Cited
2007
XPG stabilizes TFIIH, allowing transactivation of nuclear receptors: implications for Cockayne syndrome in XP-G/CS patients.
Highly Cited
2006
Highly Cited
2006
Recruitment of the Nucleotide Excision Repair Endonuclease XPG to Sites of UV-Induced DNA Damage Depends on Functional TFIIH
ABSTRACT The structure-specific endonuclease XPG is an indispensable core protein of the nucleotide excision repair (NER… 
Highly Cited
2005
Highly Cited
2005
Recognition of RNA polymerase II and transcription bubbles by XPG, CSB, and TFIIH: insights for transcription-coupled repair and Cockayne Syndrome.
Highly Cited
2004
Highly Cited
2004
Definition of a Short Region of XPG Necessary for TFIIH Interaction and Stable Recruitment to Sites of UV Damage
ABSTRACT XPG is the human endonuclease that cuts 3′ to DNA lesions during nucleotide excision repair. Missense mutations in XPG… 
Review
2001
Review
2001
Xeroderma pigmentosum/cockayne syndrome complex: first neuropathological study and review of eight other cases.
This is the first detailed description of the neuropathology of a patient with xeroderma pigmentosum/Cockayne syndrome complex… 
Highly Cited
1999
Highly Cited
1999
Nucleotide excision repair 3' endonuclease XPG stimulates the activity of base excision repairenzyme thymine glycol DNA glycosylase.
An ionizing radiation-induced DNA lesion, thymine glycol, is removed from DNA by a thymine glycol DNA glycosylase with an… 
Highly Cited
1997
Highly Cited
1997
Characterization of Reaction Intermediates of Human Excision Repair Nuclease*
Nucleotide excision repair in humans is a complex reaction involving 14 polypeptides in six repair factors for dual incisions on… 
Highly Cited
1997
Highly Cited
1997
The Non-catalytic Function of XPG Protein during Dual Incision in Human Nucleotide Excision Repair*
XPG is a member of the FEN-1 structure-specific endonuclease family. It has 3′-junction cutting activity on bubble substrates and… 
Highly Cited
1996
Highly Cited
1996
Reaction Mechanism of Human DNA Repair Excision Nuclease (*)
Nucleotide excision repair consists of removal of the damaged nucleotide(s) from DNA by dual incision of the damaged strand on… 
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