Evidence map›Paper›PMID 24727830›Full record

ArticleNature cell biology2014

Structural mechanism of the dynein power stroke.

Jianfeng Lin, Kyoko Okada, Milen Raytchev, Maria C Smith, Daniela Nicastro

Abstract readVideo-Audio Media
In one paragraph

Article in Nature cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing 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

75 citing papers in PubMed.

  1. Review
  2. Article
  3. The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025
    Article
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15 more citing papers are in PubMed but not listed here.

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.

Jianfeng LinBiology Department and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham Massachusetts 02454-9110, USA.
Kyoko OkadaBiology Department and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham Massachusetts 02454-9110, USA.
Milen RaytchevBiology Department and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham Massachusetts 02454-9110, USA.
Maria C SmithBiology Department and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham Massachusetts 02454-9110, USA.
Daniela NicastroBiology Department and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham Massachusetts 02454-9110, USA.

Funding

Structure and Function of Complexes that Regulate Ciliary MotilityR01GM083122 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI Daniela Nicastro · 2007 to 2026
$6.2M
NIGMS NIH HHS GM083122NIGMS NIH HHS R01 GM083122
6 · The paper itself

Abstract

Dyneins are large microtubule motor proteins required for mitosis, intracellular transport and ciliary and flagellar motility. They generate force through a power-stroke mechanism, which is an ATP-consuming cycle of pre- and post-power-stroke conformational changes that cause relative motion between different dynein domains. However, key structural details of dynein's force generation remain elusive. Here, using cryo-electron tomography of intact, active (that is, beating), rapidly frozen sea urchin sperm flagella, we determined the in situ three-dimensional structures of all domains of both pre- and post-power-stroke dynein, including the previously unresolved linker and stalk of pre-power-stroke dynein. Our results reveal that the rotation of the head relative to the linker is the key action in dynein movement, and that there are at least two distinct pre-power-stroke conformations: pre-I (microtubule-detached) and pre-II (microtubule-bound). We provide three-dimensional reconstructions of native dyneins in three conformational states, in situ, allowing us to propose a molecular model of the structural cycle underlying dynein movement.

Indexed as

Adenosine TriphosphateAnimalsDyneinsEnergy MetabolismFlagellaHydrolysisMaleMicrotubulesModels, BiologicalModels, MolecularMotionProtein ConformationSea UrchinsSpermatozoaAdenosine TriphosphateDyneins

Identifiers

PMID24727830
PMCPMC4102432

What OpenQuestion holds

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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.