Evidence map›Paper›PMID 19129233›Full record

ArticleNucleic acids research2009

Mechanism of DNA flexibility enhancement by HMGB proteins.

Jingyun Zhang, Micah J McCauley, L James Maher, Mark C Williams, N E Israeloff

Abstract read
In one paragraph

Article in Nucleic acids research, 2009. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. High-sensitivity C-reactive protein and high mobility group box-1 levels in Parkinson's disease.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2019
    Article
  7. Studying protein-DNA interactions using atomic force microscopy.Seminars in cell & developmental biology · 2018
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. The HMGB1 C-Terminal Tail Regulates DNA Bending.Journal of molecular biology · 2016
    Article
  13. Article
  14. Serum levels of HMGB1 have a diagnostic role in metastatic renal cell cancer.Cancer biomarkers : section A of Disease markers · 2016
    Article
  15. High-resolution mapping of architectural DNA binding protein facilitation of a DNA repression loop in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  16. Article
  17. Review
  18. 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

5 authors.

Jingyun ZhangDepartment of Physics, Northeastern University, Boston, MA 02115, USA.
Micah J McCauley
L James Maher
Mark C Williams
N E Israeloff

Funding

Enhancement of Cellular DNA FlexibilityR01GM075965 · NIGMS · MAYO CLINIC ROCHESTER · PI MAHER, LOUIS JAMES · 2006 to 2018
$4.2M
Single Molecule HIV-1 Replication InteractionsR01GM072462 · NIGMS · NORTHEASTERN UNIVERSITY · PI WILLIAMS, MARK C · 2004 to 2018
$3.9M
NIGMS NIH HHS GM072462NIGMS NIH HHS GM075965NIGMS NIH HHS R01 GM075965PHS HHS DGE-0504331
6 · The paper itself

Abstract

The mechanism by which sequence non-specific DNA-binding proteins enhance DNA flexibility is studied by examining complexes of double-stranded DNA with the high mobility group type B proteins HMGB2 (Box A) and HMGB1 (Box A+B) using atomic force microscopy. DNA end-to-end distances and local DNA bend angle distributions are analyzed for protein complexes deposited on a mica surface. For HMGB2 (Box A) binding we find a mean induced DNA bend angle of 78 degrees, with a standard error of 1.3 degrees and a SD of 23 degrees, while HMGB1 (Box A+B) binding gives a mean bend angle of 67 degrees, with a standard error of 1.3 degrees and a SD of 21 degrees. These results are consistent with analysis of the observed global persistence length changes derived from end-to-end distance measurements, and with results of DNA-stretching experiments. The moderately broad distributions of bend angles induced by both proteins are inconsistent with either a static kink model, or a purely flexible hinge model for DNA distortion by protein binding. Therefore, the mechanism by which HMGB proteins enhance the flexibility of DNA must differ from that of the Escherichia coli HU protein, which in previous studies showed a flat angle distribution consistent with a flexible hinge model.

Indexed as

DNAHMGB1 ProteinHMGB2 ProteinHMGB ProteinsMicroscopy, Atomic ForceNucleic Acid ConformationDNAHMGB1 ProteinHMGB2 ProteinHMGB Proteins

Identifiers

PMID19129233
PMCPMC2651801

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Registered trials

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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.