Maria Fousteri

 ORCID
https://orcid.org/0000-0003-1729-5899
Affiliation
Biomedical Sciences Research Center 'Alexander Fleming'
Reviewed Pathways (10/10)
Date Identifier Pathway Reference
2015-08-03 R-HSA-5696398 Nucleotide Excision Repair BibTex
2015-08-03 R-HSA-5696399 Global Genome Nucleotide Excision Repair (GG-NER) BibTex
2015-08-03 R-HSA-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER BibTex
2015-08-03 R-HSA-5696400 Dual Incision in GG-NER BibTex
2015-08-03 R-HSA-5696395 Formation of Incision Complex in GG-NER BibTex
2015-08-03 R-HSA-5696394 DNA Damage Recognition in GG-NER BibTex
2015-08-03 R-HSA-6781827 Transcription-Coupled Nucleotide Excision Repair (TC-NER) BibTex
2015-08-03 R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER BibTex
2015-08-03 R-HSA-6782135 Dual incision in TC-NER BibTex
2015-08-03 R-HSA-6781823 Formation of TC-NER Pre-Incision Complex BibTex
Reviewed Reactions (15/36)
Date Identifier Reaction Reference
2015-08-03 R-HSA-5690997 Ligation of newly synthesized repair patch to incised DNA in GG-NER BibTex
2015-08-03 R-HSA-5691001 Repair DNA synthesis of ~27-30 bases long patch by POLD, POLE or POLK in GG-NER BibTex
2015-08-03 R-HSA-5690988 3'-incision of DNA by ERCC5 (XPG) in GG-NER BibTex
2015-08-03 R-HSA-5690213 DNA polymerases delta, epsilon or kappa bind the GG-NER site BibTex
2015-08-03 R-HSA-5690990 5'- incision of DNA by ERCC1:ERCC4 in GG-NER BibTex
2015-08-03 R-HSA-5690991 Binding of ERCC1:ERCC4 (ERCC1:XPF) to pre-incision complex in GG-NER BibTex
2015-08-03 R-HSA-5689317 Formation of the pre-incision complex in GG-NER BibTex
2015-08-03 R-HSA-6790487 RNF111 ubiquitinates SUMOylated XPC BibTex
2015-08-03 R-HSA-6790454 SUMOylation of XPC BibTex
2015-08-03 R-HSA-5690996 ERCC2 and ERCC3 DNA helicases form an open bubble structure in damaged DNA BibTex
2015-08-03 R-HSA-5696670 CHD1L is recruited to GG-NER site BibTex
2015-08-03 R-HSA-5689861 Recruitment of XPA and release of CAK BibTex
2015-08-03 R-HSA-5691000 TFIIH binds GG-NER site to form a verification complex BibTex
2015-08-03 R-HSA-5696655 PARP1 or PARP2 PARylates DDB2 and autoPARylates BibTex
2015-08-03 R-HSA-5696664 PARP1 or PARP2 binds DDB2 at GG-NER site BibTex