Evidence map›Paper›PMID 33068635›Full record

ArticleJournal of molecular biology2020

Quantifying the Monomer-Dimer Equilibrium of Tubulin with Mass Photometry.

Adam Fineberg, Thomas Surrey, Philipp Kukura

Abstract read
In one paragraph

Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Mass Photometry Analysis of Membrane Proteins in Detergent Micelles.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Article
  4. NIPBL and STAG1 enable loop extrusion by providing differential DNA-cohesin affinity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Label-free methods for opticalPhysical chemistry chemical physics : PCCP · 2021
    Review
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.

Adam FinebergPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, UK.
Thomas SurreyThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK; Centre for Genomic Regulation (CRG), Barcelona Institute of Science and Technology (BIST), Dr Aiguader 88, 08003 Barcelona, Spain; ICREA, Passeig de Lluis Companys 23, 08010 Barcelona, Spain.
Philipp KukuraPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, UK. Electronic address: philipp.kukura@chem.ox.ac.uk.

Funding

Cancer Research UK FC001163Medical Research Council FC001163Wellcome Trust FC001163
6 · The paper itself

Abstract

The αβ-tubulin heterodimer is the fundamental building block of microtubules, making it central to several cellular processes. Despite the apparent simplicity of heterodimerisation, the associated energetics and kinetics remain disputed, largely due to experimental challenges associated with quantifying affinities in the <µM range. We use mass photometry to observe tubulin monomers and heterodimers in solution simultaneously, thereby quantifying the αβ-tubulin dissociation constant (8.48 ± 1.22 nM) and its tightening in the presence of GTP (3.69 ± 0.65 nM), at a dissociation rate >10

Indexed as

Protein ConformationAnimalsGuanosine TriphosphateKineticsPhotometryProtein Interaction MapsProtein MultimerizationThermodynamicsTubulinGuanosine TriphosphateTubulinbinding affinitymass photometrysingle moleculetubulin

Identifiers

PMID33068635
PMCPMC7763485

What Socratic holds

Textmetadata
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 Socratic graph.