Evidence map›Paper›PMID 31879896›Full record

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

In Vitro Reconstitution Assays of Microtubule Amplification and Lattice Repair by the Microtubule-Severing Enzymes Katanin and Spastin.

Annapurna Vemu, Ewa Szczesna, Antonina Roll-Mecak

Abstract read
PubMed Full text at PMC Publisher
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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.0field-weighted citation impact, top 19% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Tubulin flux at spastin-induced nanodamage sites regulates microtubule rescue frequency and EB1 lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Nucleus (Austin, Tex.) · 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

3 authors at 2 institutions in 1 country.

Annapurna VemuCell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, Bethesda, MD, USA.
Ewa SzczesnaCell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, Bethesda, MD, USA.
Antonina Roll-MecakCell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, Bethesda, MD, USA. Antonina@mail.nih.gov.
National Institute of Neurological Disorders and Stroke · USNational Heart Lung and Blood Institute · US

Funding

Mechanisms of molecular machines that regulate the neuronal cytoskeletonZIANS003122 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI ROLL-MECAK, ANTONINA · 2010 to 2016
$9.9M
Mechanism of microtubule severing enzymesZIANS003165 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI ROLL-MECAK, ANTONINA · 2017 to 2025
$9.2M
Intramural NIH HHS ZIA NS003122Intramural NIH HHS ZIA NS003165
6 · The paper itself

Abstract

Microtubules are non-covalent dynamic polymers essential for the life of all eukaryotic cells. Their dynamic behavior is regulated by a large array of cellular effectors. In vitro microtubule assays have been instrumental in dissecting the mechanism of microtubule-associated proteins. In this chapter, we focus on microtubule-severing enzymes katanin and spastin. They are AAA ATPases that generate internal breaks in microtubules by extracting tubulin dimers out of the microtubule lattice. We present protocols for TIRF microscopy-based assays that were instrumental in proving that these enzymes not only sever microtubules but also remodel the microtubule lattice by promoting the exchange of lattice GDP-tubulin with GTP-tubulin from the soluble pool. This activity can modulate microtubule dynamics and support microtubule-dependent microtubule amplification in the absence of a nucleating factor.

Indexed as

Adenosine TriphosphatasesBiological AssayGuanosine TriphosphateKataninMicrotubule-Associated ProteinsMicrotubulesModels, MolecularRecombinant ProteinsSpastinTubulinAdenosine TriphosphatasesGuanosine TriphosphateKataninMicrotubule-Associated ProteinsRecombinant ProteinsSpastinTubulinAAA ATPaseCytoskeletonGTP-tubulinKataninMicrotubuleMicrotubule dynamicsMicrotubule repairMicrotubule severingRescueSpastin

Identifiers

PMID31879896
PMCPMC7153568
OpenAlexW2997960916

What OpenQuestion holds

Textmetadata
LicenceTDM
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.