Evidence map›Paper›PMID 32696373›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2020

NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions.

Christopher A Waudby, John Christodoulou

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. A tethering mechanism underlies Pin1-catalyzed prolineProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Multivalency enables unidirectional switch-like competition between intrinsically disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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.

Christopher A WaudbyInstitute of Structural and Molecular Biology, UCL and Birkbeck College, London, UK. c.waudby@ucl.ac.uk.
John ChristodoulouInstitute of Structural and Molecular Biology, UCL and Birkbeck College, London, UK.

Funding

Wellcome Trust 206409Wellcome Trust 206409/Z/17/Z
6 · The paper itself

Abstract

Interactions of intrinsically disordered proteins are central to their cellular functions, and solution-state NMR spectroscopy provides a powerful tool for characterizing both structural and mechanistic aspects of such interactions. Here we focus on the analysis of IDP interactions using NMR titration measurements. Changes in resonance lineshapes in two-dimensional NMR spectra upon titration with a ligand contain rich information on structural changes in the protein and the thermodynamics and kinetics of the interaction, as well as on the microscopic association mechanism. Here we present protocols for the optimal design of titration experiments, data acquisition, and data analysis by two-dimensional lineshape fitting using the TITAN software package.

Indexed as

AutomationHydrogenIntrinsically Disordered ProteinsKineticsNuclear Magnetic Resonance, BiomolecularSoftwareThermodynamicsHydrogenIntrinsically Disordered ProteinsBindingIDPKineticsNuclear magnetic resonanceTitrations

Identifiers

PMID32696373
PMCPMC7116509

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.