Nucleotide Excision Repair (Homo sapiens)

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Bibliography

1. Wang QE, Zhu Q, Wani G, Chen J, Wani AA.; ''UV radiation-induced XPC translocation within chromatin is mediated by damaged-DNA binding protein, DDB2.''; PubMed Europe PMC Scholia
2. Robu M, Shah RG, Petitclerc N, Brind'Amour J, Kandan-Kulangara F, Shah GM.; ''Role of poly(ADP-ribose) polymerase-1 in the removal of UV-induced DNA lesions by nucleotide excision repair.''; PubMed Europe PMC Scholia
3. Fousteri M, Vermeulen W, van Zeeland AA, Mullenders LH.; ''Cockayne syndrome A and B proteins differentially regulate recruitment of chromatin remodeling and repair factors to stalled RNA polymerase II in vivo.''; PubMed Europe PMC Scholia
4. Lee KB, Wang D, Lippard SJ, Sharp PA.; ''Transcription-coupled and DNA damage-dependent ubiquitination of RNA polymerase II in vitro.''; PubMed Europe PMC Scholia
5. Shiyanov P, Nag A, Raychaudhuri P.; ''Cullin 4A associates with the UV-damaged DNA-binding protein DDB.''; PubMed Europe PMC Scholia
6. Masutani C, Sugasawa K, Yanagisawa J, Sonoyama T, Ui M, Enomoto T, Takio K, Tanaka K, van der Spek PJ, Bootsma D.; ''Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23.''; PubMed Europe PMC Scholia
7. Winkler GS, Sugasawa K, Eker AP, de Laat WL, Hoeijmakers JH.; ''Novel functional interactions between nucleotide excision DNA repair proteins influencing the enzymatic activities of TFIIH, XPG, and ERCC1-XPF.''; PubMed Europe PMC Scholia
8. Wang H, Zhai L, Xu J, Joo HY, Jackson S, Erdjument-Bromage H, Tempst P, Xiong Y, Zhang Y.; ''Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage.''; PubMed Europe PMC Scholia
9. Ito S, Kuraoka I, Chymkowitch P, Compe E, Takedachi A, Ishigami C, Coin F, Egly JM, Tanaka K.; ''XPG stabilizes TFIIH, allowing transactivation of nuclear receptors: implications for Cockayne syndrome in XP-G/CS patients.''; PubMed Europe PMC Scholia
10. Birger Y, West KL, Postnikov YV, Lim JH, Furusawa T, Wagner JP, Laufer CS, Kraemer KH, Bustin M.; ''Chromosomal protein HMGN1 enhances the rate of DNA repair in chromatin.''; PubMed Europe PMC Scholia
11. Coin F, Oksenych V, Mocquet V, Groh S, Blattner C, Egly JM.; ''Nucleotide excision repair driven by the dissociation of CAK from TFIIH.''; PubMed Europe PMC Scholia
12. Brueckner F, Hennecke U, Carell T, Cramer P.; ''CPD damage recognition by transcribing RNA polymerase II.''; PubMed Europe PMC Scholia
13. Ziani S, Nagy Z, Alekseev S, Soutoglou E, Egly JM, Coin F.; ''Sequential and ordered assembly of a large DNA repair complex on undamaged chromatin.''; PubMed Europe PMC Scholia
14. Schultz P, Fribourg S, Poterszman A, Mallouh V, Moras D, Egly JM.; ''Molecular structure of human TFIIH.''; PubMed Europe PMC Scholia
15. Bregman DB, Halaban R, van Gool AJ, Henning KA, Friedberg EC, Warren SL.; ''UV-induced ubiquitination of RNA polymerase II: a novel modification deficient in Cockayne syndrome cells.''; PubMed Europe PMC Scholia
16. Furuta T, Ueda T, Aune G, Sarasin A, Kraemer KH, Pommier Y.; ''Transcription-coupled nucleotide excision repair as a determinant of cisplatin sensitivity of human cells.''; PubMed Europe PMC Scholia
17. Friedberg EC.; ''How nucleotide excision repair protects against cancer.''; PubMed Europe PMC Scholia
18. Orelli B, McClendon TB, Tsodikov OV, Ellenberger T, Niedernhofer LJ, Schärer OD.; ''The XPA-binding domain of ERCC1 is required for nucleotide excision repair but not other DNA repair pathways.''; PubMed Europe PMC Scholia
19. Selby CP, Sancar A.; ''Cockayne syndrome group B protein enhances elongation by RNA polymerase II.''; PubMed Europe PMC Scholia
20. Kuper J, Wolski SC, Michels G, Kisker C.; ''Functional and structural studies of the nucleotide excision repair helicase XPD suggest a polarity for DNA translocation.''; PubMed Europe PMC Scholia
21. Yokoi M, Masutani C, Maekawa T, Sugasawa K, Ohkuma Y, Hanaoka F.; ''The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA.''; PubMed Europe PMC Scholia
22. Fujiwara Y, Masutani C, Mizukoshi T, Kondo J, Hanaoka F, Iwai S.; ''Characterization of DNA recognition by the human UV-damaged DNA-binding protein.''; PubMed Europe PMC Scholia
23. Ng JM, Vermeulen W, van der Horst GT, Bergink S, Sugasawa K, Vrieling H, Hoeijmakers JH.; ''A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein.''; PubMed Europe PMC Scholia
24. Camenisch U, Dip R, Schumacher SB, Schuler B, Naegeli H.; ''Recognition of helical kinks by xeroderma pigmentosum group A protein triggers DNA excision repair.''; PubMed Europe PMC Scholia
25. Pines A, Vrouwe MG, Marteijn JA, Typas D, Luijsterburg MS, Cansoy M, Hensbergen P, Deelder A, de Groot A, Matsumoto S, Sugasawa K, Thoma N, Vermeulen W, Vrieling H, Mullenders L.; ''PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1.''; PubMed Europe PMC Scholia
26. Anindya R, Mari PO, Kristensen U, Kool H, Giglia-Mari G, Giglia-Mari G, Mullenders LH, Fousteri M, Vermeulen W, Egly JM, Svejstrup JQ.; ''A ubiquitin-binding domain in Cockayne syndrome B required for transcription-coupled nucleotide excision repair.''; PubMed Europe PMC Scholia
27. Overmeer RM, Moser J, Volker M, Kool H, Tomkinson AE, van Zeeland AA, Mullenders LH, Fousteri M.; ''Replication protein A safeguards genome integrity by controlling NER incision events.''; PubMed Europe PMC Scholia
28. Dunand-Sauthier I, Hohl M, Thorel F, Jaquier-Gubler P, Clarkson SG, Schärer OD.; ''The spacer region of XPG mediates recruitment to nucleotide excision repair complexes and determines substrate specificity.''; PubMed Europe PMC Scholia
29. King BS, Cooper KL, Liu KJ, Hudson LG.; ''Poly(ADP-ribose) contributes to an association between poly(ADP-ribose) polymerase-1 and xeroderma pigmentosum complementation group A in nucleotide excision repair.''; PubMed Europe PMC Scholia
30. Park CH, Bessho T, Matsunaga T, Sancar A.; ''Purification and characterization of the XPF-ERCC1 complex of human DNA repair excision nuclease.''; PubMed Europe PMC Scholia
31. Nakatsu Y, Asahina H, Citterio E, Rademakers S, Vermeulen W, Kamiuchi S, Yeo JP, Khaw MC, Saijo M, Kodo N, Matsuda T, Hoeijmakers JH, Tanaka K.; ''XAB2, a novel tetratricopeptide repeat protein involved in transcription-coupled DNA repair and transcription.''; PubMed Europe PMC Scholia
32. Dinant C, Ampatziadis-Michailidis G, Lans H, Tresini M, Lagarou A, Grosbart M, Theil AF, van Cappellen WA, Kimura H, Bartek J, Fousteri M, Houtsmuller AB, Vermeulen W, Marteijn JA.; ''Enhanced chromatin dynamics by FACT promotes transcriptional restart after UV-induced DNA damage.''; PubMed Europe PMC Scholia
33. Conaway RC, Conaway JW.; ''The INO80 chromatin remodeling complex in transcription, replication and repair.''; PubMed Europe PMC Scholia
34. Mackinnon-Roy C, Stubbert LJ, McKay BC.; ''RNA interference against transcription elongation factor SII does not support its role in transcription-coupled nucleotide excision repair.''; PubMed Europe PMC Scholia
35. Riedl T, Hanaoka F, Egly JM.; ''The comings and goings of nucleotide excision repair factors on damaged DNA.''; PubMed Europe PMC Scholia
36. Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M.; ''Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA.''; PubMed Europe PMC Scholia
37. Christmann M, Tomicic MT, Roos WP, Kaina B.; ''Mechanisms of human DNA repair: an update.''; PubMed Europe PMC Scholia
38. Min JH, Pavletich NP.; ''Recognition of DNA damage by the Rad4 nucleotide excision repair protein.''; PubMed Europe PMC Scholia
39. Schwertman P, Lagarou A, Dekkers DH, Raams A, van der Hoek AC, Laffeber C, Hoeijmakers JH, Demmers JA, Fousteri M, Vermeulen W, Marteijn JA.; ''UV-sensitive syndrome protein UVSSA recruits USP7 to regulate transcription-coupled repair.''; PubMed Europe PMC Scholia
40. Marteijn JA, Lans H, Vermeulen W, Hoeijmakers JH.; ''Understanding nucleotide excision repair and its roles in cancer and ageing.''; PubMed Europe PMC Scholia
41. Araki M, Masutani C, Takemura M, Uchida A, Sugasawa K, Kondoh J, Ohkuma Y, Hanaoka F.; ''Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair.''; PubMed Europe PMC Scholia
42. Sollier J, Stork CT, García-Rubio ML, Paulsen RD, Aguilera A, Cimprich KA.; ''Transcription-coupled nucleotide excision repair factors promote R-loop-induced genome instability.''; PubMed Europe PMC Scholia
43. Mourgues S, Gautier V, Lagarou A, Bordier C, Mourcet A, Slingerland J, Kaddoum L, Coin F, Vermeulen W, Gonzales de Peredo A, Monsarrat B, Mari PO, Giglia-Mari G.; ''ELL, a novel TFIIH partner, is involved in transcription restart after DNA repair.''; PubMed Europe PMC Scholia
44. Wang QE, Zhu Q, Wani G, El-Mahdy MA, Li J, Wani AA.; ''DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation.''; PubMed Europe PMC Scholia
45. Balajee AS, May A, Dianova I, Bohr VA.; ''Efficient PCNA complex formation is dependent upon both transcription coupled repair and genome overall repair.''; PubMed Europe PMC Scholia
46. Scrima A, Konícková R, Czyzewski BK, Kawasaki Y, Jeffrey PD, Groisman R, Groisman R, Nakatani Y, Iwai S, Pavletich NP, Thomä NH.; ''Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex.''; PubMed Europe PMC Scholia
47. Hanawalt PC, Spivak G.; ''Transcription-coupled DNA repair: two decades of progress and surprises.''; PubMed Europe PMC Scholia
48. Jiang Y, Wang X, Bao S, Guo R, Johnson DG, Shen X, Li L.; ''INO80 chromatin remodeling complex promotes the removal of UV lesions by the nucleotide excision repair pathway.''; PubMed Europe PMC Scholia
49. Wakasugi M, Shimizu M, Morioka H, Linn S, Nikaido O, Matsunaga T.; ''Damaged DNA-binding protein DDB stimulates the excision of cyclobutane pyrimidine dimers in vitro in concert with XPA and replication protein A.''; PubMed Europe PMC Scholia
50. Fei J, Chen J.; ''KIAA1530 protein is recruited by Cockayne syndrome complementation group protein A (CSA) to participate in transcription-coupled repair (TCR).''; PubMed Europe PMC Scholia
51. Sugasawa K, Akagi J, Nishi R, Iwai S, Hanaoka F.; ''Two-step recognition of DNA damage for mammalian nucleotide excision repair: Directional binding of the XPC complex and DNA strand scanning.''; PubMed Europe PMC Scholia
52. Tsodikov OV, Ivanov D, Orelli B, Staresincic L, Shoshani I, Oberman R, Schärer OD, Wagner G, Ellenberger T.; ''Structural basis for the recruitment of ERCC1-XPF to nucleotide excision repair complexes by XPA.''; PubMed Europe PMC Scholia
53. Sarker AH, Tsutakawa SE, Kostek S, Ng C, Shin DS, Peris M, Campeau E, Tainer JA, Nogales E, Cooper PK.; ''Recognition of RNA polymerase II and transcription bubbles by XPG, CSB, and TFIIH: insights for transcription-coupled repair and Cockayne Syndrome.''; PubMed Europe PMC Scholia
54. Rossignol M, Kolb-Cheynel I, Egly JM.; ''Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH.''; PubMed Europe PMC Scholia
55. Mathieu N, Kaczmarek N, Naegeli H.; ''Strand- and site-specific DNA lesion demarcation by the xeroderma pigmentosum group D helicase.''; PubMed Europe PMC Scholia
56. Zhang X, Horibata K, Saijo M, Ishigami C, Ukai A, Kanno S, Tahara H, Neilan EG, Honma M, Nohmi T, Yasui A, Tanaka K.; ''Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6 in transcription-coupled DNA repair.''; PubMed Europe PMC Scholia
57. Poulsen SL, Hansen RK, Wagner SA, van Cuijk L, van Belle GJ, Streicher W, Wikström M, Choudhary C, Houtsmuller AB, Marteijn JA, Bekker-Jensen S, Mailand N.; ''RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response.''; PubMed Europe PMC Scholia
58. Fang L, Wang X, Yamoah K, Chen PL, Pan ZQ, Huang L.; ''Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry.''; PubMed Europe PMC Scholia
59. Jawhari A, Lainé JP, Dubaele S, Lamour V, Poterszman A, Coin F, Moras D, Egly JM.; ''p52 Mediates XPB function within the transcription/repair factor TFIIH.''; PubMed Europe PMC Scholia
60. Epshtein V, Kamarthapu V, McGary K, Svetlov V, Ueberheide B, Proshkin S, Mironov A, Nudler E.; ''UvrD facilitates DNA repair by pulling RNA polymerase backwards.''; PubMed Europe PMC Scholia
61. Moser J, Kool H, Giakzidis I, Caldecott K, Mullenders LH, Fousteri MI.; ''Sealing of chromosomal DNA nicks during nucleotide excision repair requires XRCC1 and DNA ligase III alpha in a cell-cycle-specific manner.''; PubMed Europe PMC Scholia
62. Akita M, Tak YS, Shimura T, Matsumoto S, Okuda-Shimizu Y, Shimizu Y, Nishi R, Saitoh H, Iwai S, Mori T, Ikura T, Sakai W, Hanaoka F, Sugasawa K.; ''SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair.''; PubMed Europe PMC Scholia
63. Oksenych V, Bernardes de Jesus B, Zhovmer A, Egly JM, Coin F.; ''Molecular insights into the recruitment of TFIIH to sites of DNA damage.''; PubMed Europe PMC Scholia
64. Ahel D, Horejsí Z, Wiechens N, Polo SE, Garcia-Wilson E, Ahel I, Flynn H, Skehel M, West SC, Jackson SP, Owen-Hughes T, Boulton SJ.; ''Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1.''; PubMed Europe PMC Scholia
65. Coin F, Marinoni JC, Rodolfo C, Fribourg S, Pedrini AM, Egly JM.; ''Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH.''; PubMed Europe PMC Scholia
66. Reardon JT, Ge H, Gibbs E, Sancar A, Hurwitz J, Pan ZQ.; ''Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH.''; PubMed Europe PMC Scholia
67. Groisman R, Groisman R, Kuraoka I, Chevallier O, Gaye N, Magnaldo T, Tanaka K, Kisselev AF, Harel-Bellan A, Nakatani Y.; ''CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome.''; PubMed Europe PMC Scholia
68. Vermeulen W, Fousteri M.; ''Mammalian transcription-coupled excision repair.''; PubMed Europe PMC Scholia
69. Ogi T, Limsirichaikul S, Overmeer RM, Volker M, Takenaka K, Cloney R, Nakazawa Y, Niimi A, Miki Y, Jaspers NG, Mullenders LH, Yamashita S, Fousteri MI, Lehmann AR.; ''Three DNA polymerases, recruited by different mechanisms, carry out NER repair synthesis in human cells.''; PubMed Europe PMC Scholia
70. Donahue BA, Yin S, Taylor JS, Reines D, Hanawalt PC.; ''Transcript cleavage by RNA polymerase II arrested by a cyclobutane pyrimidine dimer in the DNA template.''; PubMed Europe PMC Scholia
71. Groisman R, Groisman R, Polanowska J, Kuraoka I, Sawada J, Saijo M, Drapkin R, Kisselev AF, Tanaka K, Nakatani Y.; ''The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage.''; PubMed Europe PMC Scholia
72. Moser J, Volker M, Kool H, Alekseev S, Vrieling H, Yasui A, van Zeeland AA, Mullenders LH.; ''The UV-damaged DNA binding protein mediates efficient targeting of the nucleotide excision repair complex to UV-induced photo lesions.''; PubMed Europe PMC Scholia
73. Zotter A, Luijsterburg MS, Warmerdam DO, Ibrahim S, Nigg A, van Cappellen WA, Hoeijmakers JH, van Driel R, Vermeulen W, Houtsmuller AB.; ''Recruitment of the nucleotide excision repair endonuclease XPG to sites of UV-induced dna damage depends on functional TFIIH.''; PubMed Europe PMC Scholia
74. Nishi R, Okuda Y, Watanabe E, Mori T, Iwai S, Masutani C, Sugasawa K, Hanaoka F.; ''Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein.''; PubMed Europe PMC Scholia
75. Perez-Oliva AB, Lachaud C, Szyniarowski P, Muñoz I, Macartney T, Hickson I, Rouse J, Alessi DR.; ''USP45 deubiquitylase controls ERCC1-XPF endonuclease-mediated DNA damage responses.''; PubMed Europe PMC Scholia
76. Kamitani T, Kito K, Nguyen HP, Fukuda-Kamitani T, Yeh ET.; ''Characterization of a second member of the sentrin family of ubiquitin-like proteins.''; PubMed Europe PMC Scholia
77. Nakazawa Y, Sasaki K, Mitsutake N, Matsuse M, Shimada M, Nardo T, Takahashi Y, Ohyama K, Ito K, Mishima H, Nomura M, Kinoshita A, Ono S, Takenaka K, Masuyama R, Kudo T, Slor H, Utani A, Tateishi S, Yamashita S, Stefanini M, Lehmann AR, Yoshiura K, Ogi T.; ''Mutations in UVSSA cause UV-sensitive syndrome and impair RNA polymerase IIo processing in transcription-coupled nucleotide-excision repair.''; PubMed Europe PMC Scholia
78. Wittschieben BØ, Iwai S, Wood RD.; ''DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA.''; PubMed Europe PMC Scholia
79. Wakasugi M, Kasashima H, Fukase Y, Imura M, Imai R, Yamada S, Cleaver JE, Matsunaga T.; ''Physical and functional interaction between DDB and XPA in nucleotide excision repair.''; PubMed Europe PMC Scholia
80. He Z, Henricksen LA, Wold MS, Ingles CJ.; ''RPA involvement in the damage-recognition and incision steps of nucleotide excision repair.''; PubMed Europe PMC Scholia
81. Volker M, Moné MJ, Karmakar P, van Hoffen A, Schul W, Vermeulen W, Hoeijmakers JH, van Driel R, van Zeeland AA, Mullenders LH.; ''Sequential assembly of the nucleotide excision repair factors in vivo.''; PubMed Europe PMC Scholia
82. Kapetanaki MG, Guerrero-Santoro J, Bisi DC, Hsieh CL, Rapić-Otrin V, Levine AS.; ''The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites.''; PubMed Europe PMC Scholia
83. Hofmann RM, Pickart CM.; ''Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair.''; PubMed Europe PMC Scholia
84. Sarkar S, Kiely R, McHugh PJ.; ''The Ino80 chromatin-remodeling complex restores chromatin structure during UV DNA damage repair.''; PubMed Europe PMC Scholia
85. Mocquet V, Lainé JP, Riedl T, Yajin Z, Lee MY, Egly JM.; ''Sequential recruitment of the repair factors during NER: the role of XPG in initiating the resynthesis step.''; PubMed Europe PMC Scholia
86. Mathieu N, Kaczmarek N, Rüthemann P, Luch A, Naegeli H.; ''DNA quality control by a lesion sensor pocket of the xeroderma pigmentosum group D helicase subunit of TFIIH.''; PubMed Europe PMC Scholia
87. Giglia-Mari G, Giglia-Mari G, Coin F, Ranish JA, Hoogstraten D, Theil A, Wijgers N, Jaspers NG, Raams A, Argentini M, van der Spek PJ, Botta E, Stefanini M, Egly JM, Aebersold R, Hoeijmakers JH, Vermeulen W.; ''A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A.''; PubMed Europe PMC Scholia
88. Fischer ES, Scrima A, Böhm K, Matsumoto S, Lingaraju GM, Faty M, Yasuda T, Cavadini S, Wakasugi M, Hanaoka F, Iwai S, Gut H, Sugasawa K, Thomä NH.; ''The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation.''; PubMed Europe PMC Scholia
89. Staresincic L, Fagbemi AF, Enzlin JH, Gourdin AM, Wijgers N, Dunand-Sauthier I, Giglia-Mari G, Giglia-Mari G, Clarkson SG, Vermeulen W, Schärer OD.; ''Coordination of dual incision and repair synthesis in human nucleotide excision repair.''; PubMed Europe PMC Scholia
90. Camenisch U, Träutlein D, Clement FC, Fei J, Leitenstorfer A, Ferrando-May E, Naegeli H.; ''Two-stage dynamic DNA quality check by xeroderma pigmentosum group C protein.''; PubMed Europe PMC Scholia
91. de Laat WL, Appeldoorn E, Sugasawa K, Weterings E, Jaspers NG, Hoeijmakers JH.; ''DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair.''; PubMed Europe PMC Scholia
92. Takedachi A, Saijo M, Tanaka K.; ''DDB2 complex-mediated ubiquitylation around DNA damage is oppositely regulated by XPC and Ku and contributes to the recruitment of XPA.''; PubMed Europe PMC Scholia
93. Fitch ME, Nakajima S, Yasui A, Ford JM.; ''In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by the DDB2 gene product.''; PubMed Europe PMC Scholia
94. Sugasawa K, Okuda Y, Saijo M, Nishi R, Matsuda N, Chu G, Mori T, Iwai S, Tanaka K, Tanaka K, Hanaoka F.; ''UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex.''; PubMed Europe PMC Scholia
95. Coin F, Oksenych V, Egly JM.; ''Distinct roles for the XPB/p52 and XPD/p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair.''; PubMed Europe PMC Scholia
96. Oh KS, Imoto K, Emmert S, Tamura D, DiGiovanna JJ, Kraemer KH.; ''Nucleotide excision repair proteins rapidly accumulate but fail to persist in human XP-E (DDB2 mutant) cells.''; PubMed Europe PMC Scholia
97. Kuraoka I, Ito S, Wada T, Hayashida M, Lee L, Saijo M, Nakatsu Y, Matsumoto M, Matsunaga T, Handa H, Qin J, Nakatani Y, Tanaka K.; ''Isolation of XAB2 complex involved in pre-mRNA splicing, transcription, and transcription-coupled repair.''; PubMed Europe PMC Scholia
98. van Cuijk L, van Belle GJ, van Belle GJ, Turkyilmaz Y, Poulsen SL, Janssens RC, Theil AF, Sabatella M, Lans H, Mailand N, Houtsmuller AB, Vermeulen W, Marteijn JA.; ''SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair.''; PubMed Europe PMC Scholia
99. Su HL, Li SS.; ''Molecular features of human ubiquitin-like SUMO genes and their encoded proteins.''; PubMed Europe PMC Scholia
100. Morris DP, Michelotti GA, Schwinn DA.; ''Evidence that phosphorylation of the RNA polymerase II carboxyl-terminal repeats is similar in yeast and humans.''; PubMed Europe PMC Scholia
101. Lindahl T, Wood RD.; ''Quality control by DNA repair.''; PubMed Europe PMC Scholia
102. Araújo SJ, Wood RD.; ''Protein complexes in nucleotide excision repair.''; PubMed Europe PMC Scholia

History

External references

DataNodes

Name	Type	Database reference	Comment
Active Pol II complex with repaired DNA template:mRNA hybrid	Complex	R-HSA-110296 (Reactome)
Active Pol II transcription complex with damaged DNA hybrid	Complex	R-HSA-110292 (Reactome)
CCNH	Protein	P51946 (Uniprot-TrEMBL)
CDK7	Protein	P50613 (Uniprot-TrEMBL)
DDB1	Protein	Q16531 (Uniprot-TrEMBL)
DDB1	Protein	Q16531 (Uniprot-TrEMBL)
DDB2	Protein	Q92466 (Uniprot-TrEMBL)
DDB2	Protein	Q92466 (Uniprot-TrEMBL)
DNA containing single strand nick (5' phosphate 3' hydroxyl) with mRNA hybrid		R-NUL-5688511 (Reactome)
ERCC1	Protein	P07992 (Uniprot-TrEMBL)
ERCC1:XPF complex	Complex	R-HSA-109943 (Reactome)
ERCC1	Protein	P07992 (Uniprot-TrEMBL)
ERCC2	Protein	P18074 (Uniprot-TrEMBL)
ERCC3	Protein	P19447 (Uniprot-TrEMBL)
ERCC4	Protein	Q92889 (Uniprot-TrEMBL)
ERCC4	Protein	Q92889 (Uniprot-TrEMBL)
ERCC5	Protein	P28715 (Uniprot-TrEMBL)
ERCC5	Protein	P28715 (Uniprot-TrEMBL)
ERCC6	Protein	Q03468 (Uniprot-TrEMBL)
ERCC6	Protein	Q03468 (Uniprot-TrEMBL)
ERCC8	Protein	Q13216 (Uniprot-TrEMBL)
ERCC8	Protein	Q13216 (Uniprot-TrEMBL)
GTF2H1	Protein	P32780 (Uniprot-TrEMBL)
GTF2H2	Protein	Q13888 (Uniprot-TrEMBL)
GTF2H3	Protein	Q13889 (Uniprot-TrEMBL)
GTF2H4	Protein	Q92759 (Uniprot-TrEMBL)
GTF2H5	Protein	Q6ZYL4 (Uniprot-TrEMBL)
Incision complex with 3'-incised damaged DNA	Complex	R-HSA-109947 (Reactome)
LIG1	Protein	P18858 (Uniprot-TrEMBL)
MNAT1	Protein	P51948 (Uniprot-TrEMBL)
PCNA	Protein	P12004 (Uniprot-TrEMBL)
PCNA:POLD,POLE:RPA:RFC	Complex	R-HSA-5651799 (Reactome)
POLR2B	Protein	P30876 (Uniprot-TrEMBL)
POLR2C	Protein	P19387 (Uniprot-TrEMBL)
POLR2D	Protein	O15514 (Uniprot-TrEMBL)
POLR2E	Protein	P19388 (Uniprot-TrEMBL)
POLR2F	Protein	P61218 (Uniprot-TrEMBL)
POLR2G	Protein	P62487 (Uniprot-TrEMBL)
POLR2H	Protein	P52434 (Uniprot-TrEMBL)
POLR2I	Protein	P36954 (Uniprot-TrEMBL)
POLR2J	Protein	P52435 (Uniprot-TrEMBL)
POLR2K	Protein	P53803 (Uniprot-TrEMBL)
POLR2L	Protein	P62875 (Uniprot-TrEMBL)
PPi	Metabolite	CHEBI:29888 (ChEBI)
RAD23B	Protein	P54727 (Uniprot-TrEMBL)
RAD23B	Protein	P54727 (Uniprot-TrEMBL)
RFC1	Protein	P35251 (Uniprot-TrEMBL)
RFC2	Protein	P35250 (Uniprot-TrEMBL)
RFC3	Protein	P40938 (Uniprot-TrEMBL)
RFC4	Protein	P35249 (Uniprot-TrEMBL)
RFC5	Protein	P40937 (Uniprot-TrEMBL)
RNA Polymerase II holoenzyme complex (hyperphosphorylated)	Complex	R-HSA-109909 (Reactome)
RPA heterotrimer	Complex	R-HSA-68462 (Reactome)
RPA1	Protein	P27694 (Uniprot-TrEMBL)
RPA2	Protein	P15927 (Uniprot-TrEMBL)
RPA3	Protein	P35244 (Uniprot-TrEMBL)
SSB-dsDNA		R-HSA-110340 (Reactome)
Stalled Pol II complex with damaged DNA hybrid	Complex	R-HSA-110293 (Reactome)
TCEA1	Protein	P23193 (Uniprot-TrEMBL)
TCEA1	Protein	P23193 (Uniprot-TrEMBL)
TFIIH	Complex	R-HSA-109634 (Reactome)
Transcription-coupled (TC) repair complex:Stalled Pol II complex with damaged DNA hybrid	Complex	R-HSA-5688512 (Reactome)
Transcription-coupled (TC) repair complex:damaged DNA substrate:nascent mRNA hybrid with 3' incision	Complex	R-HSA-5688517 (Reactome)
Transcription-coupled (TC) repair complex:damaged DNA substrate:nascent mRNA hybrid	Complex	R-HSA-5688515 (Reactome)
Transcription-coupled (TC) repair complex	Complex	R-HSA-110276 (Reactome)
XAB2	Protein	Q9HCS7 (Uniprot-TrEMBL)
XAB2	Protein	Q9HCS7 (Uniprot-TrEMBL)
XPA	Protein	P23025 (Uniprot-TrEMBL)
XPA	Protein	P23025 (Uniprot-TrEMBL)
XPC	Protein	Q01831 (Uniprot-TrEMBL)
XPC:HR23B:damaged DNA complex	Complex	R-HSA-109940 (Reactome)
XPC:RAD23B	Complex	R-HSA-109938 (Reactome)
XPC	Protein	Q01831 (Uniprot-TrEMBL)
dNTP	Metabolite	CHEBI:16516 (ChEBI)
damaged DNA substrate:nascent mRNA hybrid with dual incisions		R-NUL-110303 (Reactome)
damaged DNA substrate:nascent mRNA hybrid		R-NUL-110291 (Reactome)
damaged DNA substrate		R-NUL-109939 (Reactome)
dsDNA		R-HSA-5649637 (Reactome)
excised DNA fragment with lesion		R-NUL-109960 (Reactome)
incised DNA without lesion		R-NUL-109961 (Reactome)
incision complex for GG-NER	Complex	R-HSA-109946 (Reactome)
p-S2,S5-POLR2A	Protein	P24928 (Uniprot-TrEMBL)
pre-incision complex in GG-NER	Complex	R-HSA-109941 (Reactome)
pre-incision complex with open DNA bubble	Complex	R-HSA-109945 (Reactome)
repaired DNA template:nascent mRNA hybrid		R-NUL-110295 (Reactome)

Annotated Interactions

Source	Target	Type	Database reference	Comment
	Active Pol II complex with repaired DNA template:mRNA hybrid	Arrow	R-HSA-109980 (Reactome)
	Active Pol II transcription complex with damaged DNA hybrid	Arrow	R-HSA-110301 (Reactome)
Active Pol II transcription complex with damaged DNA hybrid			R-HSA-109972 (Reactome)
	DDB1	Arrow	R-HSA-73939 (Reactome)
DDB1			R-HSA-73936 (Reactome)
	DDB2	Arrow	R-HSA-73939 (Reactome)
DDB2			R-HSA-73936 (Reactome)
	DNA containing single strand nick (5' phosphate 3' hydroxyl) with mRNA hybrid	Arrow	R-HSA-110305 (Reactome)
DNA containing single strand nick (5' phosphate 3' hydroxyl) with mRNA hybrid			R-HSA-109978 (Reactome)
	ERCC1:XPF complex	Arrow	R-HSA-109955 (Reactome)
	ERCC1:XPF complex	Arrow	R-HSA-73939 (Reactome)
ERCC1:XPF complex			R-HSA-109953 (Reactome)
ERCC1:XPF complex			R-HSA-109973 (Reactome)
ERCC1			R-HSA-109955 (Reactome)
ERCC4			R-HSA-109955 (Reactome)
	ERCC5	Arrow	R-HSA-73939 (Reactome)
ERCC5			R-HSA-109973 (Reactome)
ERCC5			R-HSA-73936 (Reactome)
ERCC6			R-HSA-109973 (Reactome)
ERCC8			R-HSA-109973 (Reactome)
	Incision complex with 3'-incised damaged DNA	Arrow	R-HSA-73938 (Reactome)
Incision complex with 3'-incised damaged DNA			R-HSA-73939 (Reactome)
Incision complex with 3'-incised damaged DNA		mim-catalysis	R-HSA-73939 (Reactome)
LIG1		mim-catalysis	R-HSA-109978 (Reactome)
LIG1		mim-catalysis	R-HSA-74968 (Reactome)
PCNA:POLD,POLE:RPA:RFC		mim-catalysis	R-HSA-109968 (Reactome)
PCNA:POLD,POLE:RPA:RFC		mim-catalysis	R-HSA-110305 (Reactome)
	PPi	Arrow	R-HSA-109968 (Reactome)
	PPi	Arrow	R-HSA-110305 (Reactome)
			R-HSA-109948 (Reactome)	XPC is mutated in individuals with xeroderma pigmentosum from genetic Complementation Group C (XP-C). It forms a tight heterodimeric complex with human Rad 23B homolog, HR23B and is thought to bind to the damaged site with lesion first, triggering subsequent reactions.
			R-HSA-109949 (Reactome)	Disruption of normal Watson-Crick base pairing and altered chemistry in the damaged strand involving bases may act as signals of damage that are recognized by XPC:HR23B complex.
			R-HSA-109953 (Reactome)	ERCC1-XPF complex with 5' endonuclease activity binds to the pre-incision complex around the bubble structure to form an active incision complex.
			R-HSA-109955 (Reactome)	ERCC1 binds ERCC4 (XPF) to form a heterodimeric ERCC1:ERCC4 (ERCC1:XPF) complex with a DNA endonuclease activity, where ERCC4 is the catalytic subunit. Suitable substrates for the ERCC1:ERCC4 endonuclease are single strand DNA (ssDNA) and ssDNA region of a duplex DNA with an open bubble structure (Park et al. 1995).
			R-HSA-109968 (Reactome)	The DNA replication complex consisting of PCNA, RPA, RFC and polymerase delta (POLD) or epsilon (POLE) complexes performs DNA repair synthesis after the damaged DNA strand is incised 5' to the lesion by the endonuclease complex ERCC1:ERCC4 (ERCC1:XPF) and 3' to the lesion by the endonuclease XPG (ERCC5). Depending on additional DNA damage present and the consequent PCNA monoubiquitination, DNA polymerase kappa (POLK) may also be involved in gap-filling DNA synthesis during nucleotide excision repair (NER) (Staresincic et al. 2009, Ogi et al. 2010, Overmeer et al. 2011).
			R-HSA-109972 (Reactome)	At the site of damage, the Pol II complex is arrested resulting in reduced levels of transcription. Several models have been proposed to explain the mechanism of this transcriptional downregulation. These include a. hyperphosphorylation of Pol II resulting in aborted entry to new pre-initiation complexes b. sequestration of TATA-binding proteins (TBP) c. enhanced use of TFIIH complexes for repair purposes precluding their use in transcription.
			R-HSA-109973 (Reactome)	A proper assembly of repair complex may require displacement of Pol II from the damage site exposing a significant length of the corresponding template DNA with the lesions. Speculations on the mode of this displacement of Pol II are available from experimental evidences: a. CSB mediated dissociation of Pol II b. degradation of Pol II c. CSB mediated remodeling of damaged DNA-RNA PII interface etc. The TC-repair complex now consists of damaged DNA template: nascent mRNA hybrid. The damage site needs to be exposed to subsequent endonuclease activities.
			R-HSA-109974 (Reactome)	At the beginning of this reaction, 1 molecule of 'Transcription-coupled (TC) repair complex', and 1 molecule of 'Stalled Pol II complex with damaged DNA hybrid' are present. At the end of this reaction, 1 molecule of 'Transcription-coupled (TC) repair complex', 1 molecule of 'Stalled Pol II in TC-NER', and 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid' are present. This reaction takes place in the 'nucleus'.
			R-HSA-109975 (Reactome)	At the beginning of this reaction, 1 molecule of 'Transcription-coupled (TC) repair complex', and 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid' are present. At the end of this reaction, 1 molecule of 'Transcription-coupled (TC) repair complex', and 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid with 3' incision' are present. This reaction takes place in the 'nucleus' and is mediated by the 'endodeoxyribonuclease activity' of 'Transcription-coupled (TC) repair complex'.
			R-HSA-109976 (Reactome)	At the beginning of this reaction, 1 molecule of 'Transcription-coupled (TC) repair complex', and 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid with 3' incision' are present. At the end of this reaction, 1 molecule of 'Transcription-coupled (TC) repair complex', 1 molecule of 'excised DNA fragment with lesion', and 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid with dual incisions' are present. This reaction takes place in the 'nucleus' and is mediated by the 'endodeoxyribonuclease activity' of 'Transcription-coupled (TC) repair complex'.
			R-HSA-109978 (Reactome)	At the beginning of this reaction, 1 molecule of 'newly synthesized DNA fragment ', 1 molecule of 'DNA ligase I ', and 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid with dual incisions' are present. At the end of this reaction, 1 molecule of 'repaired DNA template:nascent mRNA hybrid', and 1 molecule of 'DNA ligase I ' are present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA ligase activity' of 'DNA ligase I '.
			R-HSA-109980 (Reactome)	At the beginning of this reaction, 1 molecule of 'Stalled Pol II in TC-NER', and 1 molecule of 'repaired DNA template:nascent mRNA hybrid' are present. At the end of this reaction, 1 molecule of 'Active Pol II complex with repaired DNA template:mRNA hybrid' is present. This reaction takes place in the 'nucleus'.
			R-HSA-110301 (Reactome)	An active Pol II complex consisting mainly of the Pol II holoenzyme transcribes the damaged DNA template.
			R-HSA-110305 (Reactome)	After the damaged DNA strand is incised 5' to the lesion by the endonuclease complex ERCC1:ERCC4 (ERCC1:XPF) and 3' to the lesion by the endonuclease XPG (ERCC5) the resulting gap is filled by DNA synthesis. The DNA replication complex consisting of PCNA, RPA, RFC and polymerase delta (POLD) or epsilon (POLE) complexes performs the gap filling. Depending on additional DNA damage present and the consequent PCNA monoubiquitination, DNA polymerase kappa (POLK) may also be involved (Staresincic et al. 2009, Ogi et al. 2010, Overmeer et al. 2011).
			R-HSA-73934 (Reactome)	Two DNA helicases XPG and XPD, which are part of TFIIH, unwind DNA duplex around this lesion to form an open bubble structure that exposes the damaged site.
			R-HSA-73936 (Reactome)	Transcription factor II H (TFIIH) and XPG are added to the damaged site on the DNA to form a pre-incision complex along with lesioned DNA template.
			R-HSA-73938 (Reactome)	The cleavage of the damaged strand of DNA 3' to the site of damage occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound. The incision is carried out by XPG.
			R-HSA-73939 (Reactome)	The cleavage of the damaged strand of DNA 5' to the site of damage occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound. The incision is carried out by ERCC1-XPF complex.
			R-HSA-74968 (Reactome)	DNA Ligase 1 ligates the newly synthesized fragment to the gap in the template DNA.
RAD23B			R-HSA-109948 (Reactome)
	RNA Polymerase II holoenzyme complex (hyperphosphorylated)	Arrow	R-HSA-109974 (Reactome)
RNA Polymerase II holoenzyme complex (hyperphosphorylated)			R-HSA-109980 (Reactome)
RNA Polymerase II holoenzyme complex (hyperphosphorylated)			R-HSA-110301 (Reactome)
	RPA heterotrimer	Arrow	R-HSA-73939 (Reactome)
RPA heterotrimer			R-HSA-73936 (Reactome)
	SSB-dsDNA	Arrow	R-HSA-109968 (Reactome)
SSB-dsDNA			R-HSA-74968 (Reactome)
	Stalled Pol II complex with damaged DNA hybrid	Arrow	R-HSA-109972 (Reactome)
Stalled Pol II complex with damaged DNA hybrid			R-HSA-109973 (Reactome)
TCEA1			R-HSA-109973 (Reactome)
	TFIIH	Arrow	R-HSA-73939 (Reactome)
TFIIH			R-HSA-109973 (Reactome)
TFIIH			R-HSA-73936 (Reactome)
	Transcription-coupled (TC) repair complex:Stalled Pol II complex with damaged DNA hybrid	Arrow	R-HSA-109973 (Reactome)
Transcription-coupled (TC) repair complex:Stalled Pol II complex with damaged DNA hybrid			R-HSA-109974 (Reactome)
	Transcription-coupled (TC) repair complex:damaged DNA substrate:nascent mRNA hybrid with 3' incision	Arrow	R-HSA-109975 (Reactome)
Transcription-coupled (TC) repair complex:damaged DNA substrate:nascent mRNA hybrid with 3' incision			R-HSA-109976 (Reactome)
Transcription-coupled (TC) repair complex:damaged DNA substrate:nascent mRNA hybrid with 3' incision		mim-catalysis	R-HSA-109976 (Reactome)
	Transcription-coupled (TC) repair complex:damaged DNA substrate:nascent mRNA hybrid	Arrow	R-HSA-109974 (Reactome)
Transcription-coupled (TC) repair complex:damaged DNA substrate:nascent mRNA hybrid			R-HSA-109975 (Reactome)
Transcription-coupled (TC) repair complex:damaged DNA substrate:nascent mRNA hybrid		mim-catalysis	R-HSA-109975 (Reactome)
	Transcription-coupled (TC) repair complex	Arrow	R-HSA-109976 (Reactome)
XAB2			R-HSA-109973 (Reactome)
	XPA	Arrow	R-HSA-73939 (Reactome)
XPA			R-HSA-73936 (Reactome)
	XPC:HR23B:damaged DNA complex	Arrow	R-HSA-109949 (Reactome)
XPC:HR23B:damaged DNA complex			R-HSA-73936 (Reactome)
	XPC:RAD23B	Arrow	R-HSA-109948 (Reactome)
	XPC:RAD23B	Arrow	R-HSA-73939 (Reactome)
XPC:RAD23B			R-HSA-109949 (Reactome)
XPC			R-HSA-109948 (Reactome)
dNTP			R-HSA-109968 (Reactome)
dNTP			R-HSA-110305 (Reactome)
	damaged DNA substrate:nascent mRNA hybrid with dual incisions	Arrow	R-HSA-109976 (Reactome)
damaged DNA substrate:nascent mRNA hybrid with dual incisions			R-HSA-110305 (Reactome)
damaged DNA substrate:nascent mRNA hybrid			R-HSA-110301 (Reactome)
damaged DNA substrate			R-HSA-109949 (Reactome)
	dsDNA	Arrow	R-HSA-74968 (Reactome)
	excised DNA fragment with lesion	Arrow	R-HSA-109976 (Reactome)
	excised DNA fragment with lesion	Arrow	R-HSA-73939 (Reactome)
	incised DNA without lesion	Arrow	R-HSA-73939 (Reactome)
incised DNA without lesion			R-HSA-109968 (Reactome)
	incision complex for GG-NER	Arrow	R-HSA-109953 (Reactome)
incision complex for GG-NER			R-HSA-73938 (Reactome)
incision complex for GG-NER		mim-catalysis	R-HSA-73938 (Reactome)
	pre-incision complex in GG-NER	Arrow	R-HSA-73936 (Reactome)
pre-incision complex in GG-NER			R-HSA-73934 (Reactome)
pre-incision complex in GG-NER		mim-catalysis	R-HSA-73934 (Reactome)
	pre-incision complex with open DNA bubble	Arrow	R-HSA-73934 (Reactome)
pre-incision complex with open DNA bubble			R-HSA-109953 (Reactome)
	repaired DNA template:nascent mRNA hybrid	Arrow	R-HSA-109978 (Reactome)
repaired DNA template:nascent mRNA hybrid			R-HSA-109980 (Reactome)