The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA
Abstract
The solution structure of the central domain of the human nucleotide excision repair protein XPA, which binds to damaged DNA and replication protein A (RPA), was determined by nuclear magnetic resonance (NMR) spectroscopy. The central domain consists of a zinc-containing subdomain and a C-terminal subdomain. The zinc-containing subdomain has a compact globular structure and is distinct from the zinc-fingers found in transcription factors. The C-terminal subdomain folds into a novel alpha/beta structure with a positively charged superficial cleft. From the NMR spectra of the complexes, DNA and RPA binding surfaces are suggested.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Hilton et al. recently demonstrated that in binding to ds-ssDNA junctions XPA employs a larger DNA-binding domain 102 than was previously described for repair substrates 103, 104.”
From Xeroderma Pigmentosa Group A (XPA), Nucleotide Excision Repair and Regulation by ATR in Response to Ultraviolet Irradiation (2017) · cites this paper as [104]
Citations
Cites
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
MOLMOL: A program for display and analysis of macromolecular structures
Koradi, R., Billeter, M., & Wüthrich, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00009-4 · Cited by 7,156
AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502
Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,230
Raster3D Version 2.0. A program for photorealistic molecular graphics
Merritt, E. A., & Murphy, M. E. P. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994006396 · Cited by 2,493
Mammalian DNA nucleotide excision repair reconstituted with purified protein components
Aboussekhra, A., Biggerstaff, M., Shivji, M. K. K., Vilpo, J. A., Moncollin, V., Podust, V. N., Protić, M., Hübscher, U., Egly, J.-M., & Wood, R. D. (1995) · Cell · doi:10.1016/0092-8674(95)90289-9 · Cited by 837
Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
Bochkarev, A. V., Pfuetzner, R. A., Edwards, A. M., & Frappier, L. (1997) · Nature · doi:10.1038/385176a0 · Cited by 559
Proposed structure for the zinc-binding domains from transcription factor IIIA and related proteins.
Berg, J. M. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.1.99 · Cited by 412
RPA involvement in the damage-recognition and incision steps of nucleotide excision repair
He, Z., Henricksen, L. A., Wold, M. S., & Ingles, C. J. (1995) · Nature · doi:10.1038/374566a0 · Cited by 389
Tanaka, K., Miura, N., Satokata, I., Miyamoto, I., Yoshida, M. C., Satoh, Y., Kondo, S., Yasui, A., Okayama, H., & Okada, Y. (1990) · Nature · doi:10.1038/348073a0 · Cited by 388
Self-citation
Research works printed but not linked: 1
- Blake P.R., 1994, Adv. Biophys. Chem., 4, 1
Cited by
Sorted by citations
Structure, Recognition, and Processing of Cisplatin−DNA Adducts
Jamieson, E. R., & Lippard, S. J. (1999) · Chemical Reviews · doi:10.1021/cr980421n · Cited by 2,953
Molecular mechanism of nucleotide excision repair
de Laat, W. L., Jaspers, N. G. J., & Hoeijmakers, J. H. J. (1999) · Genes & Development · doi:10.1101/gad.13.7.768 · Cited by 1,122
Flexible nets: The roles of intrinsic disorder in protein interaction networks
Dunker, A. K., Cortese, M. S., Romero, P., Iakoucheva, L. M., & Uversky, V. N. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04948.x · Cited by 1,122
Bertin, G., & Averbeck, D. (2006) · Biochimie · doi:10.1016/j.biochi.2006.10.001 · Cited by 934
The many faces of the helix-turn-helix domain: Transcription regulation and beyond
Aravind, L., Anantharaman, V., BALAJI, S., Babu, M. M., & IYER, L. (2005) · FEMS Microbiology Reviews · doi:10.1016/j.femsre.2004.12.008 · Cited by 734
Molecular Mechanisms of Mammalian Global Genome Nucleotide Excision Repair
Gillet, L. C. J., & Schärer, O. D. (2006) · Chemical Reviews · doi:10.1021/cr040483f · Cited by 642
Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 449
Recognition of DNA damage by the Rad4 nucleotide excision repair protein
Min, J., & Pavletich, N. P. (2007) · Nature · doi:10.1038/nature06155 · Cited by 431
Chemistry and Biology of DNA Repair
Schärer, O. D. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200200523 · Cited by 395
Reardon, J. T., & Sancar, A. (2005) · Progress in Nucleic Acid Research and Molecular Biology · doi:10.1016/s0079-6603(04)79004-2 · Cited by 350
Prokaryotic Nucleotide Excision Repair: The UvrABC System
Truglio, J. J., Croteau, D. L., Van Houten, B., & Kisker, C. (2006) · Chemical Reviews · doi:10.1021/cr040471u · Cited by 340
TFIIH: when transcription met DNA repair
Compe, E., & Egly, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3350 · Cited by 357
Damage recognition in nucleotide excision repair of DNA
Batty, D. P., & Wood, R. D. (2000) · Gene · doi:10.1016/s0378-1119(99)00489-8 · Cited by 298
Eukaryotic nucleotide excision repair: from understanding mechanisms to influencing biology
Shuck, S. C., Short, E. A., & Turchi, J. J. (2008) · Cell Research · doi:10.1038/cr.2008.2 · Cited by 289
DNA damage recognition during nucleotide excision repair in mammalian cells
Wood, R. D. (1999) · Biochimie · doi:10.1016/s0300-9084(99)80036-4 · Cited by 264
Mer, G., Bochkarev, A. V., Gupta, R., Bochkareva, E. S., Frappier, L., Ingles, C. J., Edwards, A. M., & Chazin, W. (2000) · Cell · doi:10.1016/s0092-8674(00)00136-7 · Cited by 254
Nickel impact on human health: An intrinsic disorder perspective
Zambelli, B., Uversky, V. N., & Ciurli, S. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.09.008 · Cited by 261
DNA Damage and Repair: From Molecular Mechanisms to Health Implications
Fabio Altieri, F., Grillo, C., Maceroni, M., & Chichiarelli, S. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1830 · Cited by 222
Missura, M., Buterin, T., Hindges, R., Hübscher, U., Kašpárková, J., Brabec, V., & Naegeli, H. (2001) · The EMBO Journal · doi:10.1093/emboj/20.13.3554 · Cited by 195
The roles of intrinsic disorder in protein interaction networks
Uversky, V. N. (2013) · The biomedical & life sciences collection. · doi:10.69645/bdro2797 · Cited by 175
Structural basis for the recruitment of ERCC1‐XPF to nucleotide excision repair complexes by XPA
Tsodikov, O. V., Ivanov, D., Orelli, B., Staresincic, L., Shoshani, I., Oberman, R., Schärer, O. D., Wagner, G., & Ellenberger, T. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601894 · Cited by 166
Structural basis of TFIIH activation for nucleotide excision repair
Kokic, G., Chernev, A., Tegunov, D., Dienemann, C., Urlaub, H., & Cramer, P. (2019) · Nature Communications · doi:10.1038/s41467-019-10745-5 · Cited by 163
Bochkareva, E. S., Belegu, V., Korolev, S., & Bochkarev, A. V. (2001) · The EMBO Journal · doi:10.1093/emboj/20.3.612 · Cited by 159
Aberrant mobility phenomena of the DNA repair protein XPA
Iakoucheva, L. M., Kimzey, A. L., Masselon, C., Smith, R. D., Dunker, A. K., & Ackerman, E. J. (2001) · Protein Science · doi:10.1110/ps.ps.40101 · Cited by 132
Treble clef finger--a functionally diverse zinc-binding structural motif
Grishin, N. V. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.8.1703 · Cited by 131
Functional Analysis of the Four DNA Binding Domains of Replication Protein A
Bastin-Shanower, S. A., & Brill, S. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104386200 · Cited by 126
XPA: A key scaffold for human nucleotide excision repair
Sugitani, N., Sivley, R. M., Perry, K. E., Capra, J. A., & Chazin, W. J. (2016) · DNA Repair · doi:10.1016/j.dnarep.2016.05.018 · Cited by 116
Mechanisms of DNA damage recognition and strand discrimination in human nucleotide excision repair
Dip, R., Camenisch, U., & Naegeli, H. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.05.005 · Cited by 118
The xeroderma pigmentosum pathway: Decision tree analysis of DNA quality
Naegeli, H., & Sugasawa, K. (2011) · DNA repair · doi:10.1016/j.dnarep.2011.04.019 · Cited by 109
Ring‐shaped architecture of RecR: implications for its role in homologous recombinational DNA repair
Lee, B. I., Kim, K. H., Park, S.-J., Eom, S. H., Song, H. K., & Suh, S. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600222 · Cited by 108
Identification of intrinsic order and disorder in the DNA repair protein XPA
Iakoucheva, L. M., Kimzey, A. L., Masselon, C., Bruce, J. E., Garner, E. C., Brown, C. J., Dunker, A. K., Smith, R. D., & Ackerman, E. J. (2001) · Protein Science · doi:10.1110/ps.29401 · Cited by 108
Recognition of helical kinks by xeroderma pigmentosum group A protein triggers DNA excision repair
Camenisch, U., Dip, R., Schumacher, S. B., Schuler, B., & Naegeli, H. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1061 · Cited by 109
Interaction of selenium compounds with zinc finger proteins involved in DNA repair
Blessing, H., Kraus, S., Heindl, P., Bal, W., & Hartwig, A. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04251.x · Cited by 94
Regulation of Bin1 SH3 domain binding by phosphoinositides
Kojima, C., Hashimoto, A., Yabuta, I., Hirose, M., Hashimoto, S., Kanaho, Y., Sumimoto, H., Ikegami, T., & Sabe, H. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600442 · Cited by 92
Self-citationMolecular Mechanism of Global Genome Nucleotide Excision Repair
Petruseva, I. O., Evdokimov, A. N., & Lavrik, O. I. (2014) · Acta Naturae · doi:10.32607/20758251-2014-6-1-23-34 · Cited by 92
PCAF/GCN5-Mediated Acetylation of RPA1 Promotes Nucleotide Excision Repair
Zhao, M., Geng, R., Guo, X. Y., Yuan, R., Zhou, X. A., Zhong, Y., Huo, Y., Zhou, M., Shen, Q., Li, Y., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.015 · Cited by 87
Xeroderma pigmentosum genes: Functions inside and outside DNA repair
Sugasawa, K. (2007) · Carcinogenesis · doi:10.1093/carcin/bgm282 · Cited by 83
Buchko, G. W., Daughdrill, G. W., de Lorimier, R., Sudha Rao B. K., Isern, N. G., Lingbeck, J. M., Taylor, J.-S., Wold, M. S., Gochin, M., Spicer, L. D., et al. (1999) · Biochemistry · doi:10.1021/bi991755p · Cited by 83
Lesion recognition by XPC, TFIIH and XPA in DNA excision repair
Kim, J., Li, C., Chen, X., Cui, Y., Gołębiowski, F., Wang, H., Hanaoka, F., Sugasawa, K., & Yang, W. (2023) · Nature · doi:10.1038/s41586-023-05959-z · Cited by 90
Fischer, J. M. F., Popp, O., Gebhard, D., Veith, S., Fischbach, A., Beneke, S., Leitenstorfer, A., Bergemann, J., Scheffner, M., Ferrando‐May, E., et al. (2014) · The FEBS Journal · doi:10.1111/febs.12885 · Cited by 72
Krasikova, Y. S., Rechkunova, N. I., Maltseva, E. A., Petruseva, I. O., & Lavrik, O. I. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq649 · Cited by 74
Dimerization of Human XPA and Formation of XPA2−RPA Protein Complex
Yang, Z.-G., Liu, Y., Mao, L. Y., Zhang, J.-T., & Zou, Y. (2002) · Biochemistry · doi:10.1021/bi026064z · Cited by 70
Gilljam, K. M., Müller, R., Liabakk, N. B., & Otterlei, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049199 · Cited by 69
Park, C., & Choi, B. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05189.x · Cited by 65
Role of nucleotide excision repair proteins in oxidative DNA damage repair: an updating
Pascucci, B., D’Errico, M., Parlanti, E., Giovannini, S., & Dogliotti, E. (2011) · Biochemistry (Moscow) · doi:10.1134/s0006297911010032 · Cited by 60
Feltes, B. C., & Bonatto, D. (2014) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2014.12.002 · Cited by 53
Fadda, E. (2015) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2015.11.007 · Cited by 57
A key interaction with RPA orients XPA in NER complexes
Topolska‐Woś, A. M., Sugitani, N., Cordoba, J. J., Meur, K. V. L., Meur, R. A. L., Kim, H. S., Yeo, J.-E., Rosenberg, D. J., Hammel, M., Schärer, O. D., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1231 · Cited by 47
Structural insights into the recognition of cisplatin and AAF-dG lesion by Rad14 (XPA)
Koch, S. C., Kuper, J., Gasteiger, K. L., Simon, N., Strasser, R., Eisen, D., Geiger, S., Schneider, S., Kisker, C., & Carell, T. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1508509112 · Cited by 47
Kobayashi, T., Takeuchi, S., Saijo, M., Nakatsu, Y., Tanaka, K., Morioka, H., Otsuka, E., Wakasugi, M., & Nikaido, O. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.20.4662 · Cited by 46
Self-citationAntimony Impairs Nucleotide Excision Repair: XPA and XPE as Potential Molecular Targets
Großkopf, C., Schwerdtle, T., Mullenders, L. H. F., & Hartwig, A. (2010) · Chemical Research in Toxicology · doi:10.1021/tx100106x · Cited by 44
Redefining the DNA-Binding Domain of Human XPA
Sugitani, N., Shell, S. M., Soss, S. E., & Chazin, W. (2014) · Journal of the American Chemical Society · doi:10.1021/ja503020f · Cited by 44
Shell, S. M., Hess, S. Y., Kvaratskhelia, M., & Zou, Y. (2004) · Biochemistry · doi:10.1021/bi048208a · Cited by 42
Identification of Novel Small Molecule Inhibitors of the XPA Protein Using in Silico Based Screening
Neher, T. M., Shuck, S. C., Liu, J., Zhang, J., & Turchi, J. J. (2010) · ACS Chemical Biology · doi:10.1021/cb1000444 · Cited by 40
Saijo, M., Takedachi, A., & Tanaka, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172916 · Cited by 41
Self-citationLee, J. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg683 · Cited by 39
Croteau, D. L., DellaVecchia, M. J., Perera, L., & Houten, B. V. (2008) · DNA repair · doi:10.1016/j.dnarep.2007.11.013 · Cited by 38
Schweizer, U., Hey, T., Lipps, G., & Krauss, G. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.15.3183 · Cited by 38
Chemie und Biologie der DNA‐Reparatur
Schärer, O. D. (2003) · Angewandte Chemie · doi:10.1002/ange.200200523 · Cited by 37
Kim, M., Kim, H.-S., D’Souza, A., Gallagher, K., Jeong, E., Topolska‐Woś, A. M., Meur, K. V. L., Tsai, C.-L., Tsai, M.-S., Kee, M., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2207408119 · Cited by 34
Sim, D. L. C., Yeo, W. M., & Chow, V. T. K. (2002) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00156-x · Cited by 34
Mechanism and regulation of DNA damage recognition in mammalian nucleotide excision repair
Sugasawa, K. (2019) · The Enzymes · doi:10.1016/bs.enz.2019.06.004 · Cited by 33
Maillard, O., Camenisch, U., Blagoev, K. B., & Naegeli, H. (2008) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2008.01.007 · Cited by 36
Molecular mechanisms of xeroderma pigmentosum (XP) proteins
Koch, S. C., Simon, N., Ebert, C., & Carell, T. (2016) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583515000268 · Cited by 33
XPA Gene, Its Product and Biological Roles
Camenisch, U., & Nägeli, H.-P. (2008) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-09599-8_4 · Cited by 31
Tanaka, K., Kamiuchi, S., Ren, Y., Yonemasu, R., Ichikawa, M., Murai, H., Yoshino, M., Takeuchi, S., Saijo, M., Nakatsu, Y., et al. (2001) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(01)00093-8 · Cited by 30
Self-citationMorikawa, K., & Shirakawa, M. (2000) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(00)00031-8 · Cited by 30
Self-citationBuchko, G. W. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.12.2635 · Cited by 29
Camenisch, U., Dip, R., Vitanescu, M., & Naegeli, H. (2007) · DNA repair · doi:10.1016/j.dnarep.2007.07.011 · Cited by 28
DNA repair gets physical: Mapping an XPA-binding site on ERCC1
Croteau, D. L., Ye, P., & Houten, B. V. (2008) · DNA repair · doi:10.1016/j.dnarep.2008.01.018 · Cited by 31
Domains in the XPA protein important in its role as a processivity factor
Bartels, C. L., & Lambert, M. W. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.02.125 · Cited by 27
Mustra, D. J., Warren, A. J., Wilcox, D. E., & Hamilton, J. W. (2007) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2007.04.004 · Cited by 24
Maddukuri, L., Dudzińska, D., & Tudek, B. (2007) · Acta Biochimica Polonica · doi:10.18388/abp.2007_3222 · Cited by 24
Musich, P. R., Li, Z., & Zou, Y. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-56017-5_4 · Cited by 23
Li, S., Xu, K., Gu, D., He, L., Xie, L., Chen, Z., Fan, Z., Zhu, L., Du, M., Chu, H., et al. (2019) · Journal of Gastroenterology · doi:10.1007/s00535-019-01571-z · Cited by 24
A new structural insight into XPA–DNA interactions
Hilton, B., Shkriabai, N., Musich, P. R., Kvaratskhelia, M., Shell, S., & Zou, Y. (2014) · Bioscience Reports · doi:10.1042/bsr20140158 · Cited by 22
The Caenorhabditis elegans XPA Homolog of Human XPA
Park, H., Yook, J.-S., Koo, H., Choi, I. S., & Ahn, B. (2002) · Molecules and Cells · doi:10.1016/s1016-8478(23)15073-4 · Cited by 22
Beckwitt, E. C., Jang, S., Detweiler, I. C., Kuper, J., Sauer, F., Simon, N., Bretzler, J., Watkins, S. C., Carell, T., Kisker, C., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15168-1 · Cited by 23
Chaperoning RPA during DNA metabolism
Li, S., Dong, Z., Yang, S., Feng, J., & Li, Q. (2019) · Current Genetics · doi:10.1007/s00294-019-00945-3 · Cited by 21
Fousteri, M. I., & Lehmann, A. R. (2003) · CRC Press eBooks · doi:10.1201/9780203911709.ch17 · Cited by 21
Saijo, M., Matsuda, T., Kuraoka, I., & Tanaka, K. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.07.030 · Cited by 19
Self-citationSugitani, N., Voehler, M., Roh, M. S., Topolska‐Woś, A. M., & Chazin, W. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.800078 · Cited by 18
Sensing of DNA damage by XPC/Rad4: one protein for many lesions
Sugasawa, K., & Hanaoka, F. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1007-887 · Cited by 18
Hu, J., Hu, Z., Zhang, Y., Gou, X., Mu, Y., Wang, L., & Xie, X. (2016) · Journal of Molecular Modeling · doi:10.1007/s00894-016-3017-x · Cited by 18
Barve, A., Ghaskadbi, S., & Ghaskadbi, S. (2013) · BioMed Research International · doi:10.1155/2013/854745 · Cited by 15
Paul, D., Mu, H., Tavakoli, A., Dai, Q., Chen, X.-J., Chakraborty, S., He, C., Ansari, A., Broyde, S., & Min, J.-H. (2020) · bioRxiv · doi:10.1093/nar/gkaa909 · Cited by 13
Gavande, N. S., VanderVere-Carozza, P. S., Mishra, A. K., Vernon, T. L., Pawelczak, K. S., & Turchi, J. J. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00780 · Cited by 15
Lutz, P. B., & Bayse, C. A. (2016) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2016.01.013 · Cited by 14
Comparative insight into nucleotide excision repair components of Plasmodium falciparum
Tajedin, L., Anwar, M., Gupta, D. K., & Tuteja, R. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.02.009 · Cited by 14
Structural characterization of the redefined DNA-binding domain of human XPA
Lian, F., Yang, X., Yang, W., Jiang, Y., & Qian, C. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.05.050 · Cited by 14
The XPA Protein—Life under Precise Control
Krasikova, Y. S., Lavrik, O. I., & Rechkunova, N. I. (2022) · Cells · doi:10.3390/cells11233723 · Cited by 12
Buchko, G. W., Isern, N., Spicer, L. D., & Kennedy, M. A. (2001) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(01)00072-6 · Cited by 12
Buchko, G. W., Iakoucheva, L. M., Kennedy, M. A., Ackerman, E. J., & Hess, N. J. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9890 · Cited by 12
Zhou, C., Wang, Y., He, L., Zhu, J., Li, J., Tang, Y., Zhou, H., He, J., & Wu, H. (2020) · Molecular Therapy — Oncolytics · doi:10.1016/j.omto.2020.12.004 · Cited by 11
Silva, W. G. M. D., McCarthy, B. Y., Han, J. Z. R., Yang, C., Holland, A. J. A., Stern, H. S., Dixon, K. M., Tang, E. K. Y., Tuckey, R. C., Rybchyn, M. S., et al. (2023) · Metabolites · doi:10.3390/metabo13070775 · Cited by 12
Lian, F., Yang, X., Jiang, Y., Yang, F., Li, C., Yang, W., & Qian, C. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.01.169 · Cited by 11
Nucleotide Excision Repair in Eukaryotes
Friedberg, E. C., Walker, G. C., Siede, W., Wood, R. D., Schultz, R. A., & Ellenberger, T. (2014) · ASM Press eBooks · doi:10.1128/9781555816704.ch8 · Cited by 11
Vasilenko, N. L., & Nevinsky, G. A. (2003) · Molecular Biology · doi:10.1023/b:mbil.0000008347.64141.bc · Cited by 10
Pyrimidine Dimers: UV‐Induced DNA Damage
Iwai, S. (2008) · Wiley eBooks · doi:10.1002/9783527623112.ch5 · Cited by 9
Modelling DNA Repair Pathways: Recent Advances and Future Directions
Gentile, F., Tuszyński, J. A., & Barakat, K. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666160420141435 · Cited by 8
Metadata
- Authors
- Ikegami, T., Kuraoka, I., Saijo, M., Kodo, N., Kyogoku, Y., Morikawa, K., Tanaka, K., & Shirakawa, M.
- Affiliations
- Nara Institute of Science and Technology (JP)
- The University of Osaka (JP)
- Institute for Protein Research, The University of Osaka (JP)
- Biomolecular Engineering Research Institute (Japan) (JP)
- Corresponding author
- Shirakawa, Masahiro
- Venue
- Nature Structural & Molecular Biology
- Published
- 1998-08
- Volume
- 5
- Issue
- 8
- Pages
- 701-706
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- DOI
- 10.1038/1400
- OpenAlex
- W2020761966
- Cited by
- 139
- References
- 27
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 3 · 2023: 4 · 2022: 3 · 2021: 2 · 2020: 4 · 2019: 8 · 2018: 5 · 2017: 8 · 2016: 7 · 2015: 4 · 2014: 9 · 2013: 2 · 2012: 2
- FWCI
- 2.44
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- XPA, nucleotide excision repair, DNA repair, replication protein A, DNA binding, alpha/beta fold, protein structure, solution structure, protein-DNA complex
- MeSH terms
- Amino Acid Sequence, Binding Sites, DNA Repair, DNA-Binding Proteins, Humans, Metalloproteins, Models, Molecular, Molecular Sequence Data, Protein Conformation, Xeroderma Pigmentosum, Zinc, RNA-Binding Proteins, Sequence Homology, Amino Acid, Nuclear Magnetic Resonance, Biomolecular, Replication Protein A, Xeroderma Pigmentosum Group A Protein
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review