Evidence map›Paper›PMID 20025975›Full record

ArticleJournal of structural biology2010

Cryo-electron tomography of microtubule-kinesin motor complexes.

Julia Cope, Susan Gilbert, Ivan Rayment, David Mastronarde, Andreas Hoenger

Open access · greenAbstract read
In one paragraph

Article in Journal of structural biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025
    Review
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  17. Limiting factors in single particle cryo electron tomography.Computational and structural biotechnology journal · 2012
    Review
  18. Article
  19. Article
  20. 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 at 3 institutions in 1 country.

Julia CopeThe Boulder Laboratory for 3-D Microscopy of Cells, University of Colorado at Boulder, Department of Molecular, Cellular, and Developmental Biology, Boulder, CO 80309-0347, USA.
Susan Gilbert
Ivan Rayment
David Mastronarde
Andreas Hoenger
University of Colorado Boulder · USRensselaer Polytechnic Institute · USUniversity of Wisconsin–Madison · US

Funding

WORKSHOPS AND TRAINING FOR IMAGE ANALYSIS USING IMODP41RR000592 · NCRR · UNIVERSITY OF COLORADO AT BOULDER · PI BASS, PETER W. · 1985 to 2011
$11.9M
Predoctoral Training Molecular BiophysicsT32GM065103 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI FALKE, JOSEPH J · 2002 to 2021
$4.3M
NCRR NIH HHS P41 RR000592NIGMS NIH HHS T32 GM-065103PHS HHS P41-000592
6 · The paper itself

Abstract

Microtubules complexed with molecular motors of the kinesin family or non-motor microtubule associated proteins (MAPs) such as tau or EB1 have been the subject of cryo-electron microcopy based 3-D studies for several years. Most of these studies that targeted complexes with intact microtubules have been carried out by helical 3-D reconstruction, while few were analyzed by single particle approaches or from 2-D crystalline arrays. Helical reconstruction of microtubule-MAP or motor complexes has been extremely successful but by definition, all helical 3-D reconstruction attempts require perfectly helical assemblies, which presents a serious limitation and confines the attempts to 15- or 16-protofilament microtubules, microtubule configurations that are very rare in nature. The rise of cryo-electron tomography within the last few years has now opened a new avenue towards solving 3-D structures of microtubule-MAP complexes that do not form helical assemblies, most importantly for the subject here, all microtubules that exhibit a lattice seam. In addition, not all motor domains or MAPs decorate the microtubule surface regularly enough to match the underlying microtubule lattice, or they adopt conformations that deviate from helical symmetry. Here we demonstrate the power and limitation of cryo-electron tomography using two kinesin motor domains, the monomeric Eg5 motor domain, and the heterodimeric Kar3Vik1 motor. We show here that tomography does not exclude the possibility of post-tomographic averaging when identical sub-volumes can be extracted from tomograms and in both cases we were able to reconstruct 3-D maps of conformations that are not possible to obtain using helical or other averaging-based methods.

Indexed as

Protein ConformationAnimalsCattleCryoelectron MicroscopyElectron Microscope TomographyFungal ProteinsHumansKinesinsMicrotubule-Associated ProteinsMicrotubulesModels, MolecularMultiprotein ComplexesSaccharomyces cerevisiae ProteinsFungal ProteinsKAR3 protein, S cerevisiaeKIF11 protein, humanKinesinsMicrotubule-Associated ProteinsMultiprotein ComplexesSaccharomyces cerevisiae ProteinsVIK1 protein, S cerevisiae

Identifiers

PMID20025975
PMCPMC2856765
OpenAlexW2127754605

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.