Evidence map›Paper›PMID 36065637›Full record

ArticleeLife2022

Structural model of microtubule dynamics inhibition by kinesin-4 from the crystal structure of KLP-12 -tubulin complex.

Shinya Taguchi, Juri Nakano, Tsuyoshi Imasaki, Tomoki Kita, Yumiko Saijo-Hamano, Naoki Sakai, Hideki Shigematsu, Hiromichi Okuma, Takahiro Shimizu, Eriko Nitta and 4 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. 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
1.9field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Microtubule Engagement by the WD40-Containing Tail of Kinesin-4 KIF21B.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Kinesins inOpen biology · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. TUBB3 and KIF21A in neurodevelopment and disease.Frontiers in neuroscience · 2023
    Review
  11. 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

14 authors at 3 institutions in 1 country.

Shinya Taguchi *Division of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.ORCID 0000-0002-9868-0651
Juri Nakano *Graduate School of Life Sciences, Tohoku University, Sendai, Japan.
Tsuyoshi Imasaki *Division of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.ORCID 0000-0001-5462-1820
Tomoki KitaDepartment of Applied Physics, Graduate School of Engineering, Tohoku University, Sendai, Japan.
Yumiko Saijo-HamanoDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
Naoki SakaiRIKEN SPring-8 Center, Sayo, Japan.
Hideki ShigematsuRIKEN SPring-8 Center, Sayo, Japan.ORCID 0000-0003-3951-8651
Hiromichi OkumaDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
Takahiro ShimizuDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
Eriko NittaDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
Satoshi KikkawaDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
Satoshi MizobuchiDivision of Anesthesiology, Kobe University Graduate School of Medicine, Kobe, Japan.
Shinsuke NiwaGraduate School of Life Sciences, Tohoku University, Sendai, Japan.ORCID 0000-0002-8367-9228
Ryo NittaDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.ORCID 0000-0002-6537-9272
Kobe University · JPTohoku University · JPSPring-8 · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kinesin superfamily proteins are microtubule-based molecular motors driven by the energy of ATP hydrolysis. Among them, the kinesin-4 family is a unique motor that inhibits microtubule dynamics. Although mutations of kinesin-4 cause several diseases, its molecular mechanism is unclear because of the difficulty of visualizing the high-resolution structure of kinesin-4 working at the microtubule plus-end. Here, we report that KLP-12, a

Indexed as

KinesinsTubulinAnimalsCaenorhabditis elegansMicrotubulesModels, StructuralKinesinsTubulinC. elegansKIF21AKIF21Bkinesin-4KLP-12microtubulemolecular biophysicsneurosciencestructural biologytubulin

Identifiers

PMID36065637
PMCPMC9451533
OpenAlexW4294991327

What OpenQuestion 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 OpenQuestion graph.