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Showing 1 to 12 of 138 entries
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Retraction.

DNA repair

Leadon SA.
PMID: 12607554
DNA Repair (Amst). 2003 Mar 01;2(3):361. doi: 10.1016/s1568-7864(02)00236-7.

No abstract available.

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Leadon SA. Retraction. DNA Repair (Amst). 2003;2(3):361doi: 10.1016/s1568-7864(02)00236-7.
Leadon, S. A. (2003). Retraction. DNA repair, 2(3), 361. https://doi.org/10.1016/s1568-7864(02)00236-7
Leadon, Steven A. "Retraction." DNA repair vol. 2,3 (2003): 361. doi: https://doi.org/10.1016/s1568-7864(02)00236-7
Leadon SA. Retraction. DNA Repair (Amst). 2003 Mar 01;2(3):361. doi: 10.1016/s1568-7864(02)00236-7. PMID: 12607554.
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Retraction notice to "The yeast RAD2, but not RAD1, gene is involved in the transcription-coupled repair of thymine glycols" [Mutat. Res. 337 (1995) 169-178].

DNA repair

Friedberg EC.
PMID: 17171811
DNA Repair (Amst). 2006 Dec 09;5(12):1507. doi: 10.1016/j.dnarep.2006.08.004.

No abstract available.

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Friedberg EC. Retraction notice to "The yeast RAD2, but not RAD1, gene is involved in the transcription-coupled repair of thymine glycols" [Mutat. Res. 337 (1995) 169-178]. DNA Repair (Amst). 2006;5(12):1507doi: 10.1016/j.dnarep.2006.08.004.
Friedberg, E. C. (2006). Retraction notice to "The yeast RAD2, but not RAD1, gene is involved in the transcription-coupled repair of thymine glycols" [Mutat. Res. 337 (1995) 169-178]. DNA repair, 5(12), 1507. https://doi.org/10.1016/j.dnarep.2006.08.004
Friedberg, Errol C. "Retraction notice to "The yeast RAD2, but not RAD1, gene is involved in the transcription-coupled repair of thymine glycols" [Mutat. Res. 337 (1995) 169-178]." DNA repair vol. 5,12 (2006): 1507. doi: https://doi.org/10.1016/j.dnarep.2006.08.004
Friedberg EC. Retraction notice to "The yeast RAD2, but not RAD1, gene is involved in the transcription-coupled repair of thymine glycols" [Mutat. Res. 337 (1995) 169-178]. DNA Repair (Amst). 2006 Dec 09;5(12):1507. doi: 10.1016/j.dnarep.2006.08.004. PMID: 17171811.
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WITHDRAWN: Response Letter to the Editor.

DNA repair

Clark AJ.
PMID: 20708441
DNA Repair (Amst). 2010 Aug 12; doi: 10.1016/j.dnarep.2010.07.011. Epub 2010 Aug 12.

This article has been withdrawn at the request of the editor. The Publisher apologizes for any inconvenience this may cause. The full Elsevier Policy on Article Withdrawal can be found at http://www.elsevier.com/locate/withdrawalpolicy.

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Clark AJ. WITHDRAWN: Response Letter to the Editor. DNA Repair (Amst). 2010;doi: 10.1016/j.dnarep.2010.07.011.
Clark, A. J. (2010). WITHDRAWN: Response Letter to the Editor. DNA repair, . https://doi.org/10.1016/j.dnarep.2010.07.011
Clark, Alvin J. "WITHDRAWN: Response Letter to the Editor." DNA repair vol. (2010). doi: https://doi.org/10.1016/j.dnarep.2010.07.011
Clark AJ. WITHDRAWN: Response Letter to the Editor. DNA Repair (Amst). 2010 Aug 12; doi: 10.1016/j.dnarep.2010.07.011. Epub 2010 Aug 12. PMID: 20708441.
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Erratum to "Structure-activity relationships among DNA ligase inhibitors; characterization of a selective uncompetitive DNA ligase I inhibitor" [DNA Repair 60C (2017) 29-39].

DNA repair

Howes TRL, Sallmyr A, Brooks R, Greco GE, Jones DE, Matsumoto Y, Tomkinson AE.
PMID: 29273192
DNA Repair (Amst). 2018 Jan;61:99. doi: 10.1016/j.dnarep.2017.12.001. Epub 2017 Dec 19.

No abstract available.

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Howes TRL, Sallmyr A, Brooks R, et al. Erratum to "Structure-activity relationships among DNA ligase inhibitors; characterization of a selective uncompetitive DNA ligase I inhibitor" [DNA Repair 60C (2017) 29-39]. DNA Repair (Amst). 2017;61:99doi: 10.1016/j.dnarep.2017.12.001.
Howes, T. R. L., Sallmyr, A., Brooks, R., Greco, G. E., Jones, D. E., Matsumoto, Y., & Tomkinson, A. E. (2018). Erratum to "Structure-activity relationships among DNA ligase inhibitors; characterization of a selective uncompetitive DNA ligase I inhibitor" [DNA Repair 60C (2017) 29-39]. DNA repair, 6199. https://doi.org/10.1016/j.dnarep.2017.12.001
Howes, Timothy R L, et al. "Erratum to "Structure-activity relationships among DNA ligase inhibitors; characterization of a selective uncompetitive DNA ligase I inhibitor" [DNA Repair 60C (2017) 29-39]." DNA repair vol. 61 (2018): 99. doi: https://doi.org/10.1016/j.dnarep.2017.12.001
Howes TRL, Sallmyr A, Brooks R, Greco GE, Jones DE, Matsumoto Y, Tomkinson AE. Erratum to "Structure-activity relationships among DNA ligase inhibitors; characterization of a selective uncompetitive DNA ligase I inhibitor" [DNA Repair 60C (2017) 29-39]. DNA Repair (Amst). 2018 Jan;61:99. doi: 10.1016/j.dnarep.2017.12.001. Epub 2017 Dec 19. PMID: 29273192.
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Toxic R-loops: Cause or consequence of replication stress?.

DNA repair

Kemiha S, Poli J, Lin YL, Lengronne A, Pasero P.
PMID: 34399314
DNA Repair (Amst). 2021 Nov;107:103199. doi: 10.1016/j.dnarep.2021.103199. Epub 2021 Aug 03.

Transcription-replication conflicts (TRCs) represent a potential source of endogenous replication stress (RS) and genomic instability in eukaryotic cells but the mechanisms that underlie this instability remain poorly understood. Part of the problem could come from non-B DNA structures called...

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Kemiha S, Poli J, Lin YL, et al. Toxic R-loops: Cause or consequence of replication stress?. DNA Repair (Amst). 2021;107:103199doi: 10.1016/j.dnarep.2021.103199.
Kemiha, S., Poli, J., Lin, Y. L., Lengronne, A., & Pasero, P. (2021). Toxic R-loops: Cause or consequence of replication stress?. DNA repair, 107103199. https://doi.org/10.1016/j.dnarep.2021.103199
Kemiha, Samira, et al. "Toxic R-loops: Cause or consequence of replication stress?." DNA repair vol. 107 (2021): 103199. doi: https://doi.org/10.1016/j.dnarep.2021.103199
Kemiha S, Poli J, Lin YL, Lengronne A, Pasero P. Toxic R-loops: Cause or consequence of replication stress?. DNA Repair (Amst). 2021 Nov;107:103199. doi: 10.1016/j.dnarep.2021.103199. Epub 2021 Aug 03. PMID: 34399314.
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dCas9 binding inhibits the initiation of base excision repair in vitro.

DNA repair

Antony JS, Roberts SA, Wyrick JJ, Hinz JM.
PMID: 34847381
DNA Repair (Amst). 2021 Nov 20;109:103257. doi: 10.1016/j.dnarep.2021.103257. Epub 2021 Nov 20.

Cas9 targets DNA during genome editing by forming an RNA:DNA heteroduplex (R-loop) between the Cas9-bound guide RNA and the targeted DNA strand. We have recently demonstrated that R-loop formation by catalytically inactive Cas9 (dCas9) is inherently mutagenic, in part,...

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Antony JS, Roberts SA, Wyrick JJ, et al. dCas9 binding inhibits the initiation of base excision repair in vitro. DNA Repair (Amst). 2021;109:103257doi: 10.1016/j.dnarep.2021.103257.
Antony, J. S., Roberts, S. A., Wyrick, J. J., & Hinz, J. M. (2021). dCas9 binding inhibits the initiation of base excision repair in vitro. DNA repair, 109103257. https://doi.org/10.1016/j.dnarep.2021.103257
Antony, Jacob S, et al. "dCas9 binding inhibits the initiation of base excision repair in vitro." DNA repair vol. 109 (2021): 103257. doi: https://doi.org/10.1016/j.dnarep.2021.103257
Antony JS, Roberts SA, Wyrick JJ, Hinz JM. dCas9 binding inhibits the initiation of base excision repair in vitro. DNA Repair (Amst). 2021 Nov 20;109:103257. doi: 10.1016/j.dnarep.2021.103257. Epub 2021 Nov 20. PMID: 34847381.
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The FAcilitates Chromatin Transcription (FACT) complex: Its roles in DNA repair and implications for cancer therapy.

DNA repair

Bhakat KK, Ray S.
PMID: 34847380
DNA Repair (Amst). 2021 Nov 16;109:103246. doi: 10.1016/j.dnarep.2021.103246. Epub 2021 Nov 16.

Genomic DNA in the nucleus is wrapped around nucleosomes, a repeating unit of chromatin. The nucleosome, consisting of octamer of core histones, is a barrier for several cellular processes that require access to the naked DNA. The FAcilitates Chromatin...

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Bhakat KK, Ray S. The FAcilitates Chromatin Transcription (FACT) complex: Its roles in DNA repair and implications for cancer therapy. DNA Repair (Amst). 2021;109:103246doi: 10.1016/j.dnarep.2021.103246.
Bhakat, K. K., & Ray, S. (2021). The FAcilitates Chromatin Transcription (FACT) complex: Its roles in DNA repair and implications for cancer therapy. DNA repair, 109103246. https://doi.org/10.1016/j.dnarep.2021.103246
Bhakat, Kishor K, and Ray, Sutapa. "The FAcilitates Chromatin Transcription (FACT) complex: Its roles in DNA repair and implications for cancer therapy." DNA repair vol. 109 (2021): 103246. doi: https://doi.org/10.1016/j.dnarep.2021.103246
Bhakat KK, Ray S. The FAcilitates Chromatin Transcription (FACT) complex: Its roles in DNA repair and implications for cancer therapy. DNA Repair (Amst). 2021 Nov 16;109:103246. doi: 10.1016/j.dnarep.2021.103246. Epub 2021 Nov 16. PMID: 34847380.
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DNA polymerase delta Exo domain stabilizes mononucleotide microsatellites in human cells.

DNA repair

Shioi S, Shimamoto A, Song Y, Hidaka K, Nakamura M, Take A, Hayashi N, Takiguchi S, Fujikane R, Hidaka M, Oda S, Nakatsu Y.
PMID: 34530183
DNA Repair (Amst). 2021 Dec;108:103216. doi: 10.1016/j.dnarep.2021.103216. Epub 2021 Sep 03.

In prokaryotes and yeasts, DNA polymerase proofreading (PPR) and DNA mismatch repair (MMR) cooperatively counteracts replication errors leading to repeat sequence destabilization (i.e. insertions/deletions of repeat units). However, PPR has not thus far been regarded as a mechanism stabilizing...

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Shioi S, Shimamoto A, Song Y, et al. DNA polymerase delta Exo domain stabilizes mononucleotide microsatellites in human cells. DNA Repair (Amst). 2021;108:103216doi: 10.1016/j.dnarep.2021.103216.
Shioi, S., Shimamoto, A., Song, Y., Hidaka, K., Nakamura, M., Take, A., Hayashi, N., Takiguchi, S., Fujikane, R., Hidaka, M., Oda, S., & Nakatsu, Y. (2021). DNA polymerase delta Exo domain stabilizes mononucleotide microsatellites in human cells. DNA repair, 108103216. https://doi.org/10.1016/j.dnarep.2021.103216
Shioi, Seijiro, et al. "DNA polymerase delta Exo domain stabilizes mononucleotide microsatellites in human cells." DNA repair vol. 108 (2021): 103216. doi: https://doi.org/10.1016/j.dnarep.2021.103216
Shioi S, Shimamoto A, Song Y, Hidaka K, Nakamura M, Take A, Hayashi N, Takiguchi S, Fujikane R, Hidaka M, Oda S, Nakatsu Y. DNA polymerase delta Exo domain stabilizes mononucleotide microsatellites in human cells. DNA Repair (Amst). 2021 Dec;108:103216. doi: 10.1016/j.dnarep.2021.103216. Epub 2021 Sep 03. PMID: 34530183.
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Damsel in distress calling on her knights: Illuminating the pioneering role of E3 ubiquitin ligases in guarding the genome integrity.

DNA repair

Sahay O, Barik GK, Sharma T, Pillai AD, Rapole S, Santra MK.
PMID: 34920250
DNA Repair (Amst). 2022 Jan;109:103261. doi: 10.1016/j.dnarep.2021.103261. Epub 2021 Dec 10.

The maintenance of genomic integrity is of utmost importance for the organisms to survive and to accurately inherit traits to their progenies. Any kind of DNA damage either due to defect in DNA duplication and/ or uncontrolled cell division...

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Sahay O, Barik GK, Sharma T, et al. Damsel in distress calling on her knights: Illuminating the pioneering role of E3 ubiquitin ligases in guarding the genome integrity. DNA Repair (Amst). 2021;109:103261doi: 10.1016/j.dnarep.2021.103261.
Sahay, O., Barik, G. K., Sharma, T., Pillai, A. D., Rapole, S., & Santra, M. K. (2022). Damsel in distress calling on her knights: Illuminating the pioneering role of E3 ubiquitin ligases in guarding the genome integrity. DNA repair, 109103261. https://doi.org/10.1016/j.dnarep.2021.103261
Sahay, Osheen, et al. "Damsel in distress calling on her knights: Illuminating the pioneering role of E3 ubiquitin ligases in guarding the genome integrity." DNA repair vol. 109 (2022): 103261. doi: https://doi.org/10.1016/j.dnarep.2021.103261
Sahay O, Barik GK, Sharma T, Pillai AD, Rapole S, Santra MK. Damsel in distress calling on her knights: Illuminating the pioneering role of E3 ubiquitin ligases in guarding the genome integrity. DNA Repair (Amst). 2022 Jan;109:103261. doi: 10.1016/j.dnarep.2021.103261. Epub 2021 Dec 10. PMID: 34920250.
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Structure, function and evolution of the Helix-hairpin-Helix DNA glycosylase superfamily: Piecing together the evolutionary puzzle of DNA base damage repair mechanisms.

DNA repair

Trasviña-Arenas CH, Demir M, Lin WJ, David SS.
PMID: 34649144
DNA Repair (Amst). 2021 Dec;108:103231. doi: 10.1016/j.dnarep.2021.103231. Epub 2021 Sep 25.

The Base Excision Repair (BER) pathway is a highly conserved DNA repair system targeting chemical base modifications that arise from oxidation, deamination and alkylation reactions. BER features lesion-specific DNA glycosylases (DGs) which recognize and excise modified or inappropriate DNA...

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Trasviña-Arenas CH, Demir M, Lin WJ, et al. Structure, function and evolution of the Helix-hairpin-Helix DNA glycosylase superfamily: Piecing together the evolutionary puzzle of DNA base damage repair mechanisms. DNA Repair (Amst). 2021;108:103231doi: 10.1016/j.dnarep.2021.103231.
Trasviña-Arenas, C. H., Demir, M., Lin, W. J., & David, S. S. (2021). Structure, function and evolution of the Helix-hairpin-Helix DNA glycosylase superfamily: Piecing together the evolutionary puzzle of DNA base damage repair mechanisms. DNA repair, 108103231. https://doi.org/10.1016/j.dnarep.2021.103231
Trasviña-Arenas, C H, et al. "Structure, function and evolution of the Helix-hairpin-Helix DNA glycosylase superfamily: Piecing together the evolutionary puzzle of DNA base damage repair mechanisms." DNA repair vol. 108 (2021): 103231. doi: https://doi.org/10.1016/j.dnarep.2021.103231
Trasviña-Arenas CH, Demir M, Lin WJ, David SS. Structure, function and evolution of the Helix-hairpin-Helix DNA glycosylase superfamily: Piecing together the evolutionary puzzle of DNA base damage repair mechanisms. DNA Repair (Amst). 2021 Dec;108:103231. doi: 10.1016/j.dnarep.2021.103231. Epub 2021 Sep 25. PMID: 34649144.
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The Sm core components of small nuclear ribonucleoproteins promote homologous recombination repair.

DNA repair

Li Y, Kardell MB, Wang F, Wang L, Zhu S, Bessho T, Peng A.
PMID: 34768043
DNA Repair (Amst). 2021 Dec;108:103244. doi: 10.1016/j.dnarep.2021.103244. Epub 2021 Nov 02.

DNA Double strand breaks (DSBs) are highly hazardous to the cell, and are repaired predominantly via non-homologous end joining (NHEJ) and homologous recombination (HR). Using DSB-mimicking DNA templates, our proteomic studies identified a group of Sm core proteins of...

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Li Y, Kardell MB, Wang F, et al. The Sm core components of small nuclear ribonucleoproteins promote homologous recombination repair. DNA Repair (Amst). 2021;108:103244doi: 10.1016/j.dnarep.2021.103244.
Li, Y., Kardell, M. B., Wang, F., Wang, L., Zhu, S., Bessho, T., & Peng, A. (2021). The Sm core components of small nuclear ribonucleoproteins promote homologous recombination repair. DNA repair, 108103244. https://doi.org/10.1016/j.dnarep.2021.103244
Li, Yanqiu, et al. "The Sm core components of small nuclear ribonucleoproteins promote homologous recombination repair." DNA repair vol. 108 (2021): 103244. doi: https://doi.org/10.1016/j.dnarep.2021.103244
Li Y, Kardell MB, Wang F, Wang L, Zhu S, Bessho T, Peng A. The Sm core components of small nuclear ribonucleoproteins promote homologous recombination repair. DNA Repair (Amst). 2021 Dec;108:103244. doi: 10.1016/j.dnarep.2021.103244. Epub 2021 Nov 02. PMID: 34768043; PMCID: PMC8720265.
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Interaction of Wwox with Brca1 and associated complex proteins prevents premature resection at double-strand breaks and aberrant homologous recombination.

DNA repair

Park D, Gharghabi M, Schrock MS, Plow R, Druck T, Yungvirt C, Aldaz CM, Huebner K.
PMID: 34998176
DNA Repair (Amst). 2021 Dec 26;110:103264. doi: 10.1016/j.dnarep.2021.103264. Epub 2021 Dec 26.

Down regulation of Wwox protein expression occurs in many cancers, contributing to insensitivity to ionizing radiation (IR) and platinum drug treatments. Patients with reduced Wwox expression in their cancer tissue show decreased overall survival following these treatments, in accord...

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Park D, Gharghabi M, Schrock MS, et al. Interaction of Wwox with Brca1 and associated complex proteins prevents premature resection at double-strand breaks and aberrant homologous recombination. DNA Repair (Amst). 2021;110:103264doi: 10.1016/j.dnarep.2021.103264.
Park, D., Gharghabi, M., Schrock, M. S., Plow, R., Druck, T., Yungvirt, C., Aldaz, C. M., & Huebner, K. (2021). Interaction of Wwox with Brca1 and associated complex proteins prevents premature resection at double-strand breaks and aberrant homologous recombination. DNA repair, 110103264. https://doi.org/10.1016/j.dnarep.2021.103264
Park, Dongju, et al. "Interaction of Wwox with Brca1 and associated complex proteins prevents premature resection at double-strand breaks and aberrant homologous recombination." DNA repair vol. 110 (2021): 103264. doi: https://doi.org/10.1016/j.dnarep.2021.103264
Park D, Gharghabi M, Schrock MS, Plow R, Druck T, Yungvirt C, Aldaz CM, Huebner K. Interaction of Wwox with Brca1 and associated complex proteins prevents premature resection at double-strand breaks and aberrant homologous recombination. DNA Repair (Amst). 2021 Dec 26;110:103264. doi: 10.1016/j.dnarep.2021.103264. Epub 2021 Dec 26. PMID: 34998176.
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Showing 1 to 12 of 138 entries