Evidence map›Paper›PMID 21281594›Full record

ArticleBiophysical journal2011

HU protein induces incoherent DNA persistence length.

Guy Nir, Moshe Lindner, Heidelinde R C Dietrich, Olga Girshevitz, Constantinos E Vorgias, Yuval Garini

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.1field-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

12 citing papers in PubMed, 29 citations in OpenAlex.

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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

6 authors at 3 institutions in 3 countries.

Guy NirPhysics Department, Bar Ilan University, Ramat-Gan, Israel; Institute for Nanotechnology, Bar Ilan University, Ramat-Gan, Israel.
Moshe LindnerPhysics Department, Bar Ilan University, Ramat-Gan, Israel; Institute for Nanotechnology, Bar Ilan University, Ramat-Gan, Israel.
Heidelinde R C DietrichDepartment of Imaging Science and Technology, Delft University of Technology, Delft, The Netherlands.
Olga GirshevitzInstitute for Nanotechnology, Bar Ilan University, Ramat-Gan, Israel.
Constantinos E VorgiasDepartment of Biochemistry and Molecular Biology, Faculty of Biology, National and Kapodistrian University of Athens, Athens, Greece.
Yuval GariniPhysics Department, Bar Ilan University, Ramat-Gan, Israel; Institute for Nanotechnology, Bar Ilan University, Ramat-Gan, Israel. Electronic address: gariniy@mail.biu.ac.il.
Bar-Ilan University · ILDelft University of Technology · NLNational and Kapodistrian University of Athens · GR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HU is a highly conserved protein that is believed to play an important role in the architecture and dynamic compaction of bacterial DNA. Its ability to control DNA bending is crucial for functions such as transcription and replication. The effects of HU on the DNA structure have been studied so far mainly by single molecule methods that require us to apply stretching forces on the DNA and therefore may perturb the DNA-protein interaction. To overcome this hurdle, we study the effect of HU on the DNA structure without applying external forces by using an improved tethered particle motion method. By combining the results with DNA curvature analysis from atomic force microscopy measurements we find that the DNA consists of two different curvature distributions and the measured persistence length is determined by their interplay. As a result, the effective persistence length adopts a bimodal property that depends primarily on the HU concentration. The results can be explained according to a recently suggested model that distinguishes single protein binding from cooperative protein binding.

Indexed as

Bacterial ProteinsDNA, BacterialDNA-Binding ProteinsGeobacillus stearothermophilusMicroscopy, Atomic ForceMicrospheresBacterial ProteinsDNA, BacterialDNA-Binding Proteinshistone-like protein HU, bacteria

Identifiers

PMID21281594
PMCPMC3030240
OpenAlexW2119230112

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.