Evidence map›Paper›PMID 18439894›Full record

ArticleMolecular cell2008

Architecture of a serine recombinase-DNA regulatory complex.

Kent W Mouw, Sally-J Rowland, Mark M Gajjar, Martin R Boocock, W Marshall Stark, Phoebe A Rice

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Structural basis of directionality control in large serine integrases.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Snapshots of a molecular swivel in action.Nucleic acids research · 2018
    Article
  7. Article
  8. Review
  9. Gene stacking by recombinases.Plant biotechnology journal · 2016
    Review
  10. Article
  11. Serine Resolvases.Microbiology spectrum · 2015
    Review
  12. Article
  13. The ins and outs of serine integrase site-specific recombination.Current opinion in structural biology · 2014
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Kent W MouwDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
Sally-J Rowland
Mark M Gajjar
Martin R Boocock
W Marshall Stark
Phoebe A Rice
University of Chicago · USUniversity of Glasgow · GB

Funding

Understanding DNA specificity in the IHF/HU familyR01GM066011 · NIGMS · UNIVERSITY OF CHICAGO · PI RICE, PHOEBE A · 2002 to 2005
$1.0M
Structural Biology of a Serine DNA RecombinaseR56GM066011 · NIGMS · UNIVERSITY OF CHICAGO · PI RICE, PHOEBE A · 2007 to 2007
$261k
Biotechnology and Biological Sciences Research Council BB/E022200/1NIGMS NIH HHS GM066011NIGMS NIH HHS R01 GM066011NIGMS NIH HHS R56 GM066011PHS HHS 5 T32 G07281Wellcome TrustWellcome Trust 072552
6 · The paper itself

Abstract

An essential feature of many site-specific recombination systems is their ability to regulate the direction and topology of recombination. Resolvases from the serine recombinase family assemble an interwound synaptic complex that harnesses negative supercoiling to drive the forward reaction and promote recombination between properly oriented sites. To better understand the interplay of catalytic and regulatory functions within these synaptic complexes, we have solved the structure of the regulatory site synapse in the Sin resolvase system. It reveals an unexpected synaptic interface between helix-turn-helix DNA-binding domains that is also highlighted in a screen for synapsis mutants. The tetramer defined by this interface provides the foundation for a robust model of the synaptic complex, assembled entirely from available crystal structures, that gives insight into how the catalytic activity of Sin and other serine recombinases may be regulated.

Indexed as

Models, MolecularRecombination, GeneticBacterial ProteinsBinding SitesCatalysisCrystallizationCrystallography, X-RayDimerizationDNADNA NucleotidyltransferasesMutationProtein ConformationBacterial ProteinsDNADNA Nucleotidyltransferasessin protein, Staphylococcus aureus

Identifiers

PMID18439894
PMCPMC2428073
OpenAlexW2020484563

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.