Evidence map›Paper›PMID 41732280›Full record

ArticleiScience2026

Kinesin-1 is highly flexible and adopts an open conformation in the absence of cargo.

Evelyn R Smith, Emma D Turner, Mahmoud A S Abdelhamid, Timothy D Craggs, Alison E Twelvetrees

Abstract read
In one paragraph

Article in iScience, 2026. 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
–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

3 citing papers in PubMed.

  1. A Universal Protein Ladder for Standardization of Diverse FRET Assays.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Review
  3. 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

5 authors.

Evelyn R SmithDivision of Neuroscience, School of Medicine and Population Health, Faculty of Health, The University of Sheffield, Glossop Road, Sheffield S10 2HQ, UK.
Emma D TurnerDivision of Neuroscience, School of Medicine and Population Health, Faculty of Health, The University of Sheffield, Glossop Road, Sheffield S10 2HQ, UK.
Mahmoud A S AbdelhamidSchool of Mathematical and Physical Sciences, Faculty of Science, The University of Sheffield, Dainton Building, Brook Hill S3 7HF, UK.
Timothy D CraggsSchool of Mathematical and Physical Sciences, Faculty of Science, The University of Sheffield, Dainton Building, Brook Hill S3 7HF, UK.
Alison E TwelvetreesDivision of Neuroscience, School of Medicine and Population Health, Faculty of Health, The University of Sheffield, Glossop Road, Sheffield S10 2HQ, UK.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kinesin-1 is an essential anterograde microtubule motor protein. The core kinesin motor is a homodimer of two heavy chains; N-terminal motor domains hydrolyze ATP and walk along microtubules, while a long elongated coiled-coil stalk and an intrinsically disordered C-terminal tail region bind cargos. Kinesin autoinhibition is key to preventing futile ATP consumption and occurs, at least in part, through direct interactions between N-terminal motor domains and C-terminal inhibitory motifs. Despite significant advances in our understanding of kinesin walking, little is known about the kinesin-1 conformational landscape of the stalk and tail domains. Here, we apply solution-based biophysical analysis tools to study conformational changes in kinesin-1, with full rotational freedom, and in response to changes in ionic strength, mutations, and the presence of microtubules. This has allowed us to uncover the inherent flexibility in kinesin-1, which gives insights into autoinhibition and the regulation of intracellular transport.

Indexed as

cell biologymolecular biology

Identifiers

PMID41732280
PMCPMC12925526

What OpenQuestion holds

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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.