Evidence map›Paper›PMID 31110044›Full record

ArticleThe Journal of biological chemistry2019

All tubulins are not alike: Heterodimer dissociation differs among different biological sources.

Felipe Montecinos-Franjola, Sumit K Chaturvedi, Peter Schuck, Dan L Sackett

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 24% of its field
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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Missense variants in TUBA4A cause myo-tubulinopathies.Brain : a journal of neurology · 2026
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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

4 authors at 2 institutions in 2 countries.

Felipe Montecinos-FranjolaFrom the Division of Basic and Translational Biophysics, NICHD, and.
Sumit K ChaturvediDynamics of Macromolecular Assembly Section, Laboratory of Cellular Imaging and Macromolecular Biophysics, NIBIB, National Institutes of Health, Bethesda, Maryland 20892.
Peter SchuckDynamics of Macromolecular Assembly Section, Laboratory of Cellular Imaging and Macromolecular Biophysics, NIBIB, National Institutes of Health, Bethesda, Maryland 20892.
Dan L SackettFrom the Division of Basic and Translational Biophysics, NICHD, and sackettd@mail.nih.gov.ORCID 0000-0002-3492-1866
National Institutes of Health · USInstitute of Molecular Biology and Biophysics · RU

Funding

Microtubule regulation by small molecules.ZIAHD008765 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI SACKETT, DAN L · 2009 to 2025
$8.9M
Biophysical Characterization Of MacromoleculesZIAEB000008 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2009 to 2019
$1.7M
6 · The paper itself

Abstract

Tubulin, the subunit of microtubules, is a noncovalent heterodimer composed of one α- and one β-tubulin monomer. Both tubulins are encoded by multiple genes or composed of different isotypes, which are differentially expressed in different tissues and in development. Tubulin αβ dimers are found throughout the eukaryotes and, although very similar, are known to differ among organisms. We seek to investigate tubulins from different tissues and different organisms for a basic physical characteristic: heterodimer stability and monomer exchange between heterodimers. We previously showed that mammalian brain tubulin heterodimers reversibly dissociate, following the mass action law. Dissociation yields native monomers that can exchange with added tubulin to form new heterodimers. Here, we compared the dissociation of tubulins from multiple sources, including mammalian (rat) brain, cultured human cells (HeLa cells), chicken brain, chicken erythrocytes, and the protozoan

Indexed as

Protein MultimerizationAmino Acid SequenceAnimalsBrainChickensErythrocytesHumansLeishmaniaModels, MolecularProtein ConformationRatsSequence HomologyTubulinTubulinanalytical ultracentrifugationcytoskeletondimerizationdissociation constantfluorescenceheterologous dimerizationmonomernon-interacting surface (NIS)protein conformationtubulin

Identifiers

PMID31110044
PMCPMC6664194
OpenAlexW2946483023

What Socratic 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 Socratic graph.