Evidence map›Paper›PMID 42086734›Full record

ArticleCommunications biology2026

KLP-6 is a kinesin superfamily protein resistant to ADP inhibition.

Tomoki Kita, Taisei Watanabe, Shinsuke Niwa

Abstract read
In one paragraph

Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Tomoki KitaGraduate School of Life Sciences, Tohoku University, Sendai, Miyagi, Japan. tomoki.kita.p3@dc.tohoku.ac.jp.ORCID http://orcid.org/0000-0002-1531-565X
Taisei WatanabeGraduate School of Life Sciences, Tohoku University, Sendai, Miyagi, Japan.
Shinsuke NiwaGraduate School of Life Sciences, Tohoku University, Sendai, Miyagi, Japan. shinsuke.niwa.c8@tohoku.ac.jp.ORCID http://orcid.org/0000-0002-8367-9228

Funding

MEXT | Japan Society for the Promotion of Science (JSPS) JP23H02472MEXT | Japan Society for the Promotion of Science (JSPS) JP23KJ0168
6 · The paper itself

Abstract

Product inhibition is a common regulatory feature of ATPases, in which the hydrolysis product suppresses further enzymatic activity. Kinesins are microtubule-dependent ATPases that typically undergo inhibition by ADP, the product of ATP hydrolysis. Here, we show that the Caenorhabditis elegans kinesin-3 KLP-6 is unusually resistant to product inhibition by ADP and continues to move along microtubules at an unreduced speed even in the presence of high ADP concentrations. Kinetic measurements of the Michaelis constant for Mg·ATP (K

Indexed as

Adenosine DiphosphateCaenorhabditis elegansCaenorhabditis elegans ProteinsKinesinsAdenosine TriphosphateAmino Acid SequenceAnimalsKineticsMicrotubulesMolecular Dynamics SimulationAdenosine DiphosphateAdenosine TriphosphateCaenorhabditis elegans ProteinsKinesins

Identifiers

PMID42086734
PMCPMC13346673

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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.