Evidence map›Paper›PMID 20111687›Full record

ReviewInternational journal of molecular sciences2009

Analysis of cooperativity by isothermal titration calorimetry.

Alan Brown

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

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  15. Cooperativity and Allostery in RNA Systems.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  16. Article
  17. 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

1 author.

Alan BrownDepartment of Biochemistry, University of Cambridge, UK. alan@cryst.bioc.cam.ac.uk

Funding

Wellcome Trust RG44650
6 · The paper itself

Abstract

Cooperative binding pervades Nature. This review discusses the use of isothermal titration calorimetry (ITC) in the identification and characterisation of cooperativity in biological interactions. ITC has broad scope in the analysis of cooperativity as it determines binding stiochiometries, affinities and thermodynamic parameters, including enthalpy and entropy in a single experiment. Examples from the literature are used to demonstrate the applicability of ITC in the characterisation of cooperative systems.

Indexed as

CalorimetryLigandsArchaeal ProteinsDNADNA-Binding ProteinsFatty Acid-Binding ProteinsGastrointestinal HormonesHumansKineticsMagnetic Resonance SpectroscopyProtein BindingThermodynamicsThioredoxin-Disulfide ReductaseArchaeal ProteinsDNADNA-Binding Proteinsfatty acid-binding protein 6Fatty Acid-Binding ProteinsGastrointestinal HormonesLigandsSac7 protein, SulfolobusThioredoxin-Disulfide Reductasecooperativityglobal analysisisothermal titration calorimetrymultiprotein complexesNMRstoichiometrythermodynamics

Identifiers

PMID20111687
PMCPMC2812830

What OpenQuestion holds

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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.