Evidence map›Paper›PMID 11557810›Full record

ReviewNucleic acids research2001

AdoMet-dependent methylation, DNA methyltransferases and base flipping.

X Cheng, R J Roberts

Open access · bronzeAbstract readReview
In one paragraph

Review in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers.

0numbers the graph read from it
0cells of the map it votes in
154citing papers in PubMed
11.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

154 citing papers in PubMed, 478 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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  9. Article
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  11. Article
  12. Advances in the structure and function of the nucleolar protein fibrillarin.Frontiers in cell and developmental biology · 2024
    Review
  13. Article
  14. Base Dynamics in theThe journal of physical chemistry. B · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. The roles of NOP56 in cancer and SCA36.Pathology oncology research : POR · 2023
    Review
  20. Review

94 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

X ChengEmory University School of Medicine, Department of Biochemistry, 1510 Clifton Road, Atlanta, GA 30322, USA. xcheng@emory.edu
R J Roberts
Emory University · US

Funding

THREE-DIMENSIONAL STRUCTURE OF HHAI METHYLASER01GM049245 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI CHENG, XIAODONG · 1993 to 2017
$6.6M
PROTEIN ARGININE METHYLATION--STRUCTURES AND FUNCTIONSR01GM061355 · NIGMS · EMORY UNIVERSITY · PI CHENG, XIAODONG · 2000 to 2004
$992k
STUDIES OF M5-CYTOSINE METHYLASESR01GM046127 · NIGMS · NEW ENGLAND BIOLABS, INC. · PI ROBERTS, RICHARD J. · 1991 to 1998
–
NIGMS NIH HHS GM46127NIGMS NIH HHS GM49245NIGMS NIH HHS GM61355NIGMS NIH HHS R01 GM049245NIGMS NIH HHS R01 GM061355
6 · The paper itself

Abstract

Twenty AdoMet-dependent methyltransferases (MTases) have been characterized structurally by X-ray crystallography and NMR. These include seven DNA MTases, five RNA MTases, four protein MTases and four small molecule MTases acting on the carbon, oxygen or nitrogen atoms of their substrates. The MTases share a common core structure of a mixed seven-stranded beta-sheet (6 downward arrow 7 upward arrow 5 downward arrow 4 downward arrow 1 downward arrow 2 downward arrow 3 downward arrow) referred to as an 'AdoMet-dependent MTase fold', with the exception of a protein arginine MTase which contains a compact consensus fold lacking the antiparallel hairpin strands (6 downward arrow 7 upward arrow). The consensus fold is useful to identify hypothetical MTases during structural proteomics efforts on unannotated proteins. The same core structure works for very different classes of MTase including those that act on substrates differing in size from small molecules (catechol or glycine) to macromolecules (DNA, RNA and protein). DNA MTases use a 'base flipping' mechanism to deliver a specific base within a DNA molecule into a typically concave catalytic pocket. Base flipping involves rotation of backbone bonds in double-stranded DNA to expose an out-of-stack nucleotide, which can then be a substrate for an enzyme-catalyzed chemical reaction. The phenomenon is fully established for DNA MTases and for DNA base excision repair enzymes, and is likely to prove general for enzymes that require access to unpaired, mismatched or damaged nucleotides within base-paired regions in DNA and RNA. Several newly discovered MTase families in eukaryotes (DNA 5mC MTases and protein arginine and lysine MTases) offer new challenges in the MTase field.

Indexed as

DNA MethylationBinding SitesDNAMethyltransferasesNucleic Acid ConformationProtein ConformationS-AdenosylmethionineDNAMethyltransferasesS-Adenosylmethionine

Identifiers

PMID11557810
PMCPMC55914
OpenAlexW2018512856

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.