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Cited by 210

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Modularity and Specialization in Superfamily 1 and 2 Helicases

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Singleton, Martin R., Wigley, Dale B.·2002·Journal of Bacteriology

Abstract

The family of nucleic acid (NA) strand separation enzymes known as helicases are found in all organisms and participate in a wide variety of cellular processes. The central reaction catalyzed is always the same: hydrolysis of a nucleoside triphosphate (NTP; usually ATP) is coupled to the separation of an NA duplex, be it DNA-DNA, DNA-RNA, or RNA-RNA. This central process is required in almost every aspect of NA metabolism in the cell, including chromosomal and plasmid replication, transcription, translation, RNA processing, and DNA recombination and repair (30, 46). This widespread usage may be seen by examining the cellular complement of helicases; for example, at least 12 putative DNA helicases have been identified in the genome of Escherichia coli, while it has been estimated that more than 2% of the Saccharomyces cerevisiae genome encodes helicase-related proteins (48).

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Crossref · 10.1128/jb.184.7.1819-1826.2002

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Metadata

Authors
Singleton, M. R., & Wigley, D. B.
Venue
Journal of Bacteriology
Published
2002-04
Volume
184
Issue
7
Pages
1819-1826
ISSN
  • 0021-9193 (ISSN-L)
  • 1098-5530
OpenAlex
W2147805925
Cited by
210
References
2
FWCI
6.16
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Modularity and Specialization in Superfamily 1 and 2 Helicases. https://app.cochat.ai/papers/10.1128/jb.184.7.1819-1826.2002
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Singleton, M. R., & Wigley, D. B. (2002). Modularity and Specialization in Superfamily 1 and 2 Helicases. Journal of Bacteriology. https://doi.org/10.1128/jb.184.7.1819-1826.2002

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.