Evidence map›Paper›PMID 25573261›Full record

ReviewMethods (San Diego, Calif.)2015

Global ITC fitting methods in studies of protein allostery.

Lee Freiburger, Karine Auclair, Anthony Mittermaier

Abstract readReview
In one paragraph

Review in Methods (San Diego, Calif.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. 4-Ethyl phenyl sulfate binding to human serum albumin.Protein science : a publication of the Protein Society · 2026
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  9. Isothermal Titration Calorimetry.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  10. CALX-CBD1 CaBiophysical journal · 2020
    Article
  11. Review
  12. 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

3 authors.

Lee FreiburgerTechnische Universität München, Chair of Biomolecular NMR Spectroscopy, Germany.
Karine AuclairMcGill University, Chemistry Department, Canada.
Anthony MittermaierMcGill University, Chemistry Department, Canada.

Funding

CIHR 85062CIHR MOP-89784
6 · The paper itself

Abstract

Allostery is a nearly ubiquitous feature of biological systems in which ligand binding or covalent modification at one site alters the activities of distant sites in a macromolecule or macromolecular complex. The molecular mechanisms underlying this phenomenon have been studied for decades. Nevertheless there are many aspects that remain poorly understood. ITC yields detailed information on the thermodynamics of biomacromolecular interactions and their coupling to additional equilibria, therefore in principle it is a powerful tool for better understanding how allostery is achieved. A particularly powerful approach involves simultaneously fitting multiple ITC data sets together with those of complementary techniques, especially nuclear magnetic resonance and circular dichroism spectroscopies. In this review, we describe several group-fitting methods for discriminating between different binding models and for improving the accuracy of thermodynamic parameters extracted from variable-temperature ITC data. The techniques were applied to the antibiotic resistance-causing enzyme aminoglycoside-6'-acetyltransferase Ii, uncovering the existence of competition between opposing mechanisms and ligand-dependent switching of the underlying mechanism. These novel observations underline the potential of combining ITC and spectroscopic techniques to study allostery.

Indexed as

LigandsBinding SitesCalorimetryModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein BindingProtein FoldingProteinsThermodynamicsLigandsProteinsAminoglycoside acetyltransferaseCDCooperativityITCNMR

Identifiers

PMID25573261
PMCPMC5182068

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.