Evidence map›Paper›PMID 29262356›Full record

ArticleBiophysical journal2017

Nanoscale Assembly of High-Mobility Group AT-Hook 2 Protein with DNA Replication Fork.

Natalie Krahn, Markus Meier, Vu To, Evan P Booy, Kevin McEleney, Joe D O'Neil, Sean A McKenna, Trushar R Patel, Jörg Stetefeld

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. 3' UTR-truncated HMGA2 overexpression induces non-malignantMolecular therapy. Methods & clinical development · 2021
    Article
  8. Review
  9. Human DDX17 Unwinds Rift Valley Fever Virus Non-Coding RNAs.International journal of molecular sciences · 2020
    Article
  10. Article
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  12. Article
  13. Review
  14. 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

9 authors at 2 institutions in 1 country.

Natalie KrahnDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Markus MeierDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Vu ToDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Evan P BooyDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Kevin McEleneyDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada; Manitoba Institute for Materials, University of Manitoba, Winnipeg, Manitoba, Canada.
Joe D O'NeilDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Sean A McKennaDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada; Manitoba Institute for Materials, University of Manitoba, Winnipeg, Manitoba, Canada; Department of Biochemistry and Medical Genetics, University of Manitoba, Winnipeg, Manitoba, Canada.
Trushar R PatelAlberta RNA Research and Training Institute, Department of Chemistry and Biochemistry, University of Lethbridge, Lethbridge, Alberta, Canada; Discovery Lab, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada; Department of Microbiology, Immunology and Infectious Diseases, Cumming School of Medicine, University of Calgary, Calgary, Alberta, Canada. Electronic address: trushar.patel@uleth.ca.
Jörg StetefeldDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada; Department of Microbiology, University of Manitoba, Winnipeg, Manitoba, Canada. Electronic address: joerg.stetefeld@umanitoba.ca.
University of Manitoba · CAUniversity of Lethbridge · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High mobility group AT-hook 2 (HMGA2) protein is composed of three AT-hook domains. HMGA2 expresses at high levels in both embryonic stem cells and cancer cells, where it interacts with and stabilizes replication forks (RFs), resulting in elevated cell proliferation rates. In this study, we demonstrated that HMGA2 knockdown reduces cell proliferation. To understand the features required for interaction between HMGA2 and RFs, we studied the solution structure of HMGA2, free and in complex with RFs, using an integrated host of biophysical techniques. Circular dichroism and NMR experiments confirmed the disordered state of unbound HMGA2. Dynamic light scattering and sedimentation velocity experiments demonstrated that HMGA2 and RF are monodisperse in solution, and form an equimolar complex. Small-angle x-ray scattering studies revealed that HMGA2 binds in a side-by-side orientation to RF where 3 AT-hooks act as a clamp to wrap around a distorted RF. Thus, our data provide insights into how HMGA2 interacts with stalled RFs and the function of the process.

Indexed as

DNA ReplicationCell ProliferationDNAGene Knockdown TechniquesHEK293 CellsHMGA2 ProteinHumansModels, MolecularNucleic Acid ConformationProtein BindingProtein ConformationDNAHMGA2 Protein

Identifiers

PMID29262356
PMCPMC5771026
OpenAlexW2779478539

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.