The DOI matches its Crossref record; 163 of the 164 references it cites were found in a registry or an index.
Eukaryotic DNA Polymerases
Abstract
▪ Abstract Any living cell is faced with the fundamental task of keeping the genome intact in order to develop in an organized manner, to function in a complex environment, to divide at the right time, and to die when it is appropriate. To achieve this goal, an efficient machinery is required to maintain the genetic information encoded in DNA during cell division, DNA repair, DNA recombination, and the bypassing of damage in DNA. DNA polymerases (pols) α, β, γ, δ, and ϵ are the key enzymes required to maintain the integrity of the genome under all these circumstances. In the last few years the number of known pols, including terminal transferase and telomerase, has increased to at least 19. A particular pol might have more than one functional task in a cell and a particular DNA synthetic event may require more than one pol, which suggests that nature has provided various safety mechanisms. This multi-functional feature is especially valid for the variety of novel pols identified in the last three years. These are the lesion-replicating enzymes pol ζ, pol η, pol ι, pol κ, and Rev1, and a group of pols called pol θ, pol λ, pol μ, pol σ, and pol φ that fulfill a variety of other tasks.
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In the citing paper
“To perform these tasks, cells harbor multiple DNA polymerases (2,3), many of which have only been discovered in the past 5 years and whose cellular functions are not fully understood.”
From DNA Replication Fidelity (2004) · cites this paper as [2]
In the citing paper
“Although many (e.g. at least 10 of 15 template-dependent human) polymerases lack intrinsic proofreading activity (2, 3), it is possible that dissociation from DNA after misinsertion may allow proofreading by the exonuclease activity intrinsic to another replication or repair protein, such as Pol ␦, Pol ⑀, or apurinic/apyrimidinic endonuclease (50).”
From DNA Replication Fidelity (2004) · cites this paper as [2]
Citations
Cites
DNA Replication in Eukaryotic Cells
Bell, S. P., & Dutta, A. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135425 · Cited by 2,065
Lindahl, T. L., & Wood, R. D. (1999) · Science · doi:10.1126/science.286.5446.1897 · Cited by 1,521
The Cell as a Collection of Protein Machines: Preparing the Next Generation of Molecular Biologists
Alberts, B. (1998) · Cell · doi:10.1016/s0092-8674(00)80922-8 · Cited by 1,411
Telomere states and cell fates
Blackburn, E. H. (2000) · Nature · doi:10.1038/35040500 · Cited by 1,395
The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase η
Masutani, C., Kusumoto, R., Yamada, A., Dohmae, N., Yokoi, M., Yuasa, M., Araki, M., Iwai, S., Takio, K., & Hanaoka, F. (1999) · Nature · doi:10.1038/21447 · Cited by 1,292
Kunkel, T. A., & Bebenek, K. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.497 · Cited by 1,003
Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
Krishna, T. S. R., Kong, X., Gary, S. L., Burgers, P., & Kuriyan, J. (1994) · Cell · doi:10.1016/0092-8674(94)90014-0 · Cited by 902
The Y-Family of DNA Polymerases
Ohmori, H., Friedberg, E. C., Fuchs, R. P., Goodman, M. F., Hanaoka, F., Hinkle, D. C., Kunkel, T. A., Lawrence, C. W., Livneh, Z., Nohmi, T., et al. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00278-7 · Cited by 882
Eukaryotic DNA mismatch repair
Kolodner, R. D., & Marsischky, G. (1999) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(99)80013-6 · Cited by 861
DNA Polymerases: Structural Diversity and Common Mechanisms
Steitz, T. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17395 · Cited by 848
Research works printed but not linked: 4
Cited by
Sorted by citations
Proliferating cell nuclear antigen (PCNA): a dancer with many partners
Maga, G., & Hübscher, U. (2003) · Journal of Cell Science · doi:10.1242/jcs.00653 · Cited by 1,121
Self-citationKunkel, T. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400006200 · Cited by 754
Wang, F., Lü, C., & Willner, I. (2014) · Chemical Reviews · doi:10.1021/cr400354z · Cited by 647
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
Lange, S. S., Takata, K.-I., & Wood, R. D. (2011) · Nature Reviews Cancer · doi:10.1038/nrc2998 · Cited by 615
Metadata
- Authors
- Hübscher, U., Maga, G., & Spadari, S.
- Affiliations
- University of Zurich (CH)
- ORCID
- Maga, Giovanni
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2002-06
- Volume
- 71
- Issue
- 1
- Pages
- 133-163
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2163221081
- Semantic Scholar
- ac3d6c3b8ed17b4d96d5bade9bc385a4743991c6
- Cited by
- 691
- References
- 164
- Citations by year
- 2026: 6 · 2025: 4 · 2024: 6 · 2023: 7 · 2022: 5 · 2021: 15 · 2020: 18 · 2019: 15 · 2018: 10 · 2017: 16 · 2016: 20 · 2015: 16 · 2014: 25 · 2013: 41 · 2012: 47
- FWCI
- 4.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- eukaryotic DNA polymerases, genome stability, DNA replication, DNA repair, DNA recombination, DNA damage bypass, Pol eta, Rev1, telomerase, terminal transferase
- MeSH terms
- Animals, Binding Sites, DNA, DNA-Directed DNA Polymerase, DNA Repair, DNA Replication, DNA-Binding Proteins, Humans, Models, Molecular, Recombination, Genetic, Protein Structure, Tertiary, Proliferating Cell Nuclear Antigen, Telomerase, Protein Subunits, Replication Protein C
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