Evidence map›Paper›PMID 23990325›Full record

ReviewNucleic acids research2014

The other face of restriction: modification-dependent enzymes.

Wil A M Loenen, Elisabeth A Raleigh

Open access · goldAbstract readReview
In one paragraph

Review in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

114 citing papers in PubMed, 188 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Unlocking genome engineering inMicrobiology spectrum · 2026
    Article
  8. Article
  9. How to Unmask an Unknown: The Restriction-Modification SystemInternational journal of molecular sciences · 2026
    Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. UsingACS synthetic biology · 2025
    Article
  16. Article
  17. Article
  18. Modified DNA substrate selectivity by GmrSD-family Type IV restriction enzyme BrxU.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  19. The extended mobility of plasmids.Nucleic acids research · 2025
    Review
  20. Review

54 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 2 countries.

Wil A M LoenenLeiden University Medical Center, P.O. Box 9600 2300RC Leiden, The Netherlands and New England Biolabs Inc., 240 County Road Ipswich, MA 01938-2723, USA.
Elisabeth A Raleigh
Leiden University Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 1952 observation of host-induced non-hereditary variation in bacteriophages by Salvador Luria and Mary Human led to the discovery in the 1960s of modifying enzymes that glucosylate hydroxymethylcytosine in T-even phages and of genes encoding corresponding host activities that restrict non-glucosylated phage DNA: rglA and rglB (restricts glucoseless phage). In the 1980's, appreciation of the biological scope of these activities was dramatically expanded with the demonstration that plant and animal DNA was also sensitive to restriction in cloning experiments. The rgl genes were renamed mcrA and mcrBC (modified cytosine restriction). The new class of modification-dependent restriction enzymes was named Type IV, as distinct from the familiar modification-blocked Types I-III. A third Escherichia coli enzyme, mrr (modified DNA rejection and restriction) recognizes both methylcytosine and methyladenine. In recent years, the universe of modification-dependent enzymes has expanded greatly. Technical advances allow use of Type IV enzymes to study epigenetic mechanisms in mammals and plants. Type IV enzymes recognize modified DNA with low sequence selectivity and have emerged many times independently during evolution. Here, we review biochemical and structural data on these proteins, the resurgent interest in Type IV enzymes as tools for epigenetic research and the evolutionary pressures on these systems.

Indexed as

DNADNA MethylationDNA Restriction EnzymesEvolution, MolecularProtein MultimerizationDNADNA Restriction Enzymes

Identifiers

PMID23990325
PMCPMC3874153
OpenAlexW2147418524

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.