Evidence map›Paper›PMID 20576476›Full record

ReviewPhysics of life reviews2010

Biophysical characterization of DNA binding from single molecule force measurements.

Kathy R Chaurasiya, Thayaparan Paramanathan, Micah J McCauley, Mark C Williams

Abstract readReview
In one paragraph

Review in Physics of life reviews, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
12.9field-weighted citation impact, top 1% 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

67 citing papers in PubMed, 190 citations in OpenAlex.

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  13. Optical Tweezers to Study Viruses.Sub-cellular biochemistry · 2024
    Review
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7 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Kathy R ChaurasiyaDepartment of Physics, Northeastern University, 111 Dana Research Center, Boston, MA 02115, USA.
Thayaparan Paramanathan
Micah J McCauley
Mark C Williams
Northeastern University · USDana (United States) · US

Funding

Single Molecule HIV-1 Replication InteractionsR01GM072462 · NIGMS · NORTHEASTERN UNIVERSITY · PI WILLIAMS, MARK C · 2004 to 2018
$3.9M
NIGMS NIH HHS R01 GM072462NIGMS NIH HHS R01GM072462
6 · The paper itself

Abstract

Single molecule force spectroscopy is a powerful method that uses the mechanical properties of DNA to explore DNA interactions. Here we describe how DNA stretching experiments quantitatively characterize the DNA binding of small molecules and proteins. Small molecules exhibit diverse DNA binding modes, including binding into the major and minor grooves and intercalation between base pairs of double-stranded DNA (dsDNA). Histones bind and package dsDNA, while other nuclear proteins such as high mobility group proteins bind to the backbone and bend dsDNA. Single-stranded DNA (ssDNA) binding proteins slide along dsDNA to locate and stabilize ssDNA during replication. Other proteins exhibit binding to both dsDNA and ssDNA. Nucleic acid chaperone proteins can switch rapidly between dsDNA and ssDNA binding modes, while DNA polymerases bind both forms of DNA with high affinity at distinct binding sites at the replication fork. Single molecule force measurements quantitatively characterize these DNA binding mechanisms, elucidating small molecule interactions and protein function.

Indexed as

Microscopy, Atomic ForceBiophysicsDNADNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA, Single-StrandedMolecular ChaperonesDNADNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA, Single-StrandedMolecular Chaperones

Identifiers

PMID20576476
PMCPMC2930095
OpenAlexW2107773011

What OpenQuestion holds

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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.