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Cited by 429

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

The DNA (cytosine-5) methyltransferases

Open access
Kumar, Sanjay, Cheng, Xiaodong, Klimasauskas, Saulius, Sha, Mi, Posfai, Janos, Roberts, Richard J., Wilson, Geoffrey G.·1994·Nucleic Acids Research

Abstract

The m5C-MTases form a closely-knit family of enzymes in which common amino acid sequence motifs almost certainly translate into common structural and functional elements. These common elements are located predominantly in a single structural domain that performs the chemistry of the reaction. Sequence-specific DNA recognition is accomplished by a separate domain that contains recognition elements not seen in other structures. This, combined with the novel and unexpected mechanistic feature of trapping a base out of the DNA helix, makes the m5C-MTases an intriguing class of enzymes for further study. The reaction pathway has suddenly become more complicated because of the base-flipping and much remains to be learned about the DNA recognition elements in the family members for which structural information is not yet available.

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Metadata

Authors
Kumar, S., Cheng, X., Klimasauskas, S., Sha, M., Posfai, J., Roberts, R. J., & Wilson, G. G.
Venue
Nucleic Acids Research
Published
1994
Volume
22
Issue
1
Pages
1-10
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
OpenAlex
W2055565613
Cited by
429
References
2
FWCI
7.84
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: The DNA (cytosine-5) methyltransferases. https://app.cochat.ai/papers/10.1093/nar/22.1.1
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Kumar, S., Cheng, X., Klimasauskas, S., Sha, M., Posfai, J., Roberts, R. J., & Wilson, G. G. (1994). The DNA (cytosine-5) methyltransferases. Nucleic Acids Research. https://doi.org/10.1093/nar/22.1.1

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