Evidence map›Paper›PMID 14645086›Full record

ArticleBiophysical journal2003

Lipoplex thermodynamics: determination of DNA-cationic lipoid interaction energies.

Edwin Pozharski, Robert C MacDonald

Abstract read
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Intrinsic Structure of Lipoplexes Embedded in Polyelectrolyte Multilayers.Langmuir : the ACS journal of surfaces and colloids · 2026
    Article
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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

2 authors.

Edwin PozharskiDepartment of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500, USA.
Robert C MacDonald

Funding

NEW CATIONIC PHOSPHOLIPIDS FOR TRANSFECTIONR01GM052329 · NIGMS · NORTHWESTERN UNIVERSITY · PI MACDONALD, ROBERT C · 1995 to 2004
$941k
NIGMS NIH HHS GM 52329NIGMS NIH HHS R01 GM052329
6 · The paper itself

Abstract

An experimental study of the cationic lipid-DNA binding affinity is presented. The binding free energy was determined by monitoring lipoplex dissociation under conditions of increasing salt concentration. The primary procedure was based on the extent of quenching by energy transfer of fluorophores on DNA molecules by fluorophore on a lipid as these molecules came into close association in the lipoplex. Titration calorimetry on the Dickerson dodecamer was also done, with results that were in agreement with the fluorescence data. Measurements on short oligonucleotides allowed estimation of the binding energy per nucleotide. The binding free energy is approximately 0.6 kcal/mole nucleotide for the Dickerson dodecamer and declines for longer oligonucleotides. The entropy gained upon complex formation is approximately 1 entropy unit per released counterion. The method was applied to long DNA molecules (herring and lambda-phage DNA) and revealed that complete dissociation occurs at 750 mM NaCl. Likely contributions of macromolecular desolvation and DNA flexibility to the binding energy are discussed.

Indexed as

CalorimetryCationsCell MembraneDNALipidsOligonucleotidesProtein BindingSaltsSodium ChlorideThermodynamicsCationsDNALipidsOligonucleotidesSaltsSodium Chloride

Identifiers

PMID14645086
PMCPMC1303698

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.