Evidence map›Paper›PMID 15882618›Full record

ArticleCell2005

Transition from nonspecific to specific DNA interactions along the substrate-recognition pathway of dam methyltransferase.

John R Horton, Kirsten Liebert, Stanley Hattman, Albert Jeltsch, Xiaodong Cheng

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

56 citing papers in PubMed, 110 citations in OpenAlex.

  1. Inhibition ofACS omega · 2025
    Article
  2. Inhibition ofbioRxiv : the preprint server for biology · 2025
    Article
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  4. Article
  5. Article
  6. Article
  7. Article
  8. Multiple modes of DNA compaction by protamine.bioRxiv : the preprint server for biology · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Structural insights into DNA NCell discovery · 2023
    Article
  13. Systematic Design of Adenosine Analogs as Inhibitors of aJournal of medicinal chemistry · 2023
    Article
  14. Article
  15. N6-methyladenine: A Rare and Dynamic DNA Mark.Advances in experimental medicine and biology · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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

5 authors at 3 institutions in 2 countries.

John R HortonDepartment of Biochemistry, Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA 30322, USA.
Kirsten Liebert
Stanley Hattman
Albert Jeltsch
Xiaodong Cheng
Constructor University · DEEmory University · USUniversity of Rochester · US

Funding

THREE-DIMENSIONAL STRUCTURE OF HHAI METHYLASER01GM049245 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI CHENG, XIAODONG · 1993 to 2017
$6.6M
NIGMS NIH HHS GM 29227NIGMS NIH HHS GM 49245NIGMS NIH HHS R01 GM049245
6 · The paper itself

Abstract

DNA methyltransferases methylate target bases within specific nucleotide sequences. Three structures are described for bacteriophage T4 DNA-adenine methyltransferase (T4Dam) in ternary complexes with partially and fully specific DNA and a methyl-donor analog. We also report the effects of substitutions in the related Escherichia coli DNA methyltransferase (EcoDam), altering residues corresponding to those involved in specific interaction with the canonical GATC target sequence in T4Dam. We have identified two types of protein-DNA interactions: discriminatory contacts, which stabilize the transition state and accelerate methylation of the cognate site, and antidiscriminatory contacts, which do not significantly affect methylation of the cognate site but disfavor activity at noncognate sites. These structures illustrate the transition in enzyme-DNA interaction from nonspecific to specific interaction, suggesting that there is a temporal order for formation of specific contacts.

Indexed as

Models, MolecularAdenineAdenosineAmino Acid SequenceAmino Acid SubstitutionBacteriophage T4Base SequenceBinding SitesCatalysisCatalytic DomainCrystallography, X-RayDNAEscherichia coliEscherichia coli ProteinsKineticsMolecular Sequence DataAdenineAdenosineDam methyltransferasedam protein, Bacteriophage T4dam protein, E coliDNAEscherichia coli ProteinsOligonucleotidesS-AdenosylhomocysteinesinefunginSite-Specific DNA-Methyltransferase (Adenine-Specific)Viral Proteins

Identifiers

PMID15882618
PMCPMC2656680
OpenAlexW2080102916

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.