Evidence map›Paper›PMID 22815479›Full record

ArticleThe Journal of biological chemistry2012

Uncovering principles that control septin-septin interactions.

Moshe S Kim, Carol D Froese, Hong Xie, William S Trimble

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. The Structural Biology of Septins and Their Filaments: An Update.Frontiers in cell and developmental biology · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Septin Mutations in Human Cancers.Frontiers in cell and developmental biology · 2016
    Review
  15. Article
  16. Article
  17. Article
  18. Lean forward: Genetic analysis of temperature-sensitive mutants unfolds the secrets of oligomeric protein complex assembly.BioEssays : news and reviews in molecular, cellular and developmental biology · 2014
    Article
  19. Article
  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

4 authors at 2 institutions in 1 country.

Moshe S KimProgram in Cell Biology, Department of Biochemistry, Hospital for Sick Children, University of Toronto, Toronto, Ontario M5G 1X8, Canada.
Carol D Froese
Hong Xie
William S Trimble
Hospital for Sick Children · CAUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Septins comprise a conserved family of GTPases important in cytokinesis. These proteins polymerize into filaments from rod-shaped heteromeric septin complexes. Septins interact with one another at two interfaces (NC and G) that alternate within the complex. Here, we show that small mutations at the N terminus greatly enhance the formation of SEPT2 homopolymers. Taking advantage of this mutation to examine polymer formation using SEPT2 alone, we show that both NC and G interfaces are required for filament formation. However, co-expression of wild type SEPT2 with SEPT2 containing mutations at either NC or G interfaces revealed that only the NC mutant suppressed filament formation. NC mutants are able to interact with one another at putative G interfaces, whereas G mutants fail to interact at NC interfaces. In addition, all promiscuous septin pairwise interactions occur at the G interface. These findings suggest that G interface interactions must occur before NC interactions during polymer formation.

Indexed as

MutationAnimalsChlorocebus aethiopsCOS CellsHEK293 CellsHeLa CellsHumansMultiprotein ComplexesProtein MultimerizationProtein Structure, TertiarySeptinsMultiprotein ComplexesSEPTIN2 protein, humanSeptins

Identifiers

PMID22815479
PMCPMC3436290
OpenAlexW2044248178

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.