Evidence map›Paper›PMID 28303166›Full record

ReviewBiophysical reviews2017

Single-molecule studies of high-mobility group B architectural DNA bending proteins.

Divakaran Murugesapillai, Micah J McCauley, L James Maher, Mark C Williams

Open access · hybridAbstract readReview
In one paragraph

Review in Biophysical reviews, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 38 citations in OpenAlex.

  1. MicroRNAs in Sepsis.Biomedicines · 2024
    Review
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  9. Review
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  14. The Role of Nucleic Acid Sensing in Controlling Microbial and Autoimmune Disorders.International review of cell and molecular biology · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Characterization of circRNA-Associated-ceRNA Networks in a Senescence-Accelerated Mouse Prone 8 Brain.Molecular therapy : the journal of the American Society of Gene Therapy · 2017
    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.

Divakaran MurugesapillaiDepartment of Physics, Northeastern University, Boston, MA 02115 USA.
Micah J McCauleyDepartment of Physics, Northeastern University, Boston, MA 02115 USA.
L James MaherDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, MN 55905 USA.
Mark C WilliamsDepartment of Physics, Northeastern University, Boston, MA 02115 USA.
Northeastern University · USMayo Clinic · US

Funding

Enhancement of Cellular DNA FlexibilityR01GM075965 · NIGMS · MAYO CLINIC ROCHESTER · PI MAHER, LOUIS JAMES · 2006 to 2018
$4.2M
NIGMS NIH HHS R01 GM075965
6 · The paper itself

Abstract

Protein-DNA interactions can be characterized and quantified using single molecule methods such as optical tweezers, magnetic tweezers, atomic force microscopy, and fluorescence imaging. In this review, we discuss studies that characterize the binding of high-mobility group B (HMGB) architectural proteins to single DNA molecules. We show how these studies are able to extract quantitative information regarding equilibrium binding as well as non-equilibrium binding kinetics. HMGB proteins play critical but poorly understood roles in cellular function. These roles vary from the maintenance of chromatin structure and facilitation of ribosomal RNA transcription (yeast high-mobility group 1 protein) to regulatory and packaging roles (human mitochondrial transcription factor A). We describe how these HMGB proteins bind, bend, bridge, loop and compact DNA to perform these functions. We also describe how single molecule experiments observe multiple rates for dissociation of HMGB proteins from DNA, while only one rate is observed in bulk experiments. The measured single-molecule kinetics reveals a local, microscopic mechanism by which HMGB proteins alter DNA flexibility, along with a second, much slower macroscopic rate that describes the complete dissociation of the protein from DNA.

Indexed as

BendingBindingDNAHMGBKineticsProtein

Identifiers

PMID28303166
PMCPMC5331113
OpenAlexW2551988658

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.