Evidence map›Paper›PMID 22984443›Full record

ArticlePloS one2012

A detailed, hierarchical study of Giardia lamblia's ventral disc reveals novel microtubule-associated protein complexes.

Cindi L Schwartz, John M Heumann, Scott C Dawson, Andreas Hoenger

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.2field-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

36 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Molecular biology of the cell · 2025
    Article
  6. Tubulin Acetylation: A Critical Regulator of Microtubule Function.Results and problems in cell differentiation · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Ultrastructural Alterations of the Human PathogenPathogens (Basel, Switzerland) · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Microtubule organelles in Giardia.Advances in parasitology · 2020
    Review
  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

4 authors at 2 institutions in 1 country.

Cindi L SchwartzBoulder Lab for 3-D Electron Microscopy of Cells, Department of MCD Biology, University of Colorado, Boulder, Colorado, United States of America.
John M Heumann
Scott C Dawson
Andreas Hoenger
University of Colorado Boulder · USUniversity of California, Davis · 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
NCRR NIH HHS P41 RR000592NCRR NIH HHS RR000592
6 · The paper itself

Abstract

Giardia lamblia is a flagellated, unicellular parasite of mammals infecting over one billion people worldwide. Giardia's two-stage life cycle includes a motile trophozoite stage that colonizes the host small intestine and an infectious cyst form that can persist in the environment. Similar to many eukaryotic cells, Giardia contains several complex microtubule arrays that are involved in motility, chromosome segregation, organelle transport, maintenance of cell shape and transformation between the two life cycle stages. Giardia trophozoites also possess a unique spiral microtubule array, the ventral disc, made of approximately 50 parallel microtubules and associated microribbons, as well as a variety of associated proteins. The ventral disc maintains trophozoite attachment to the host intestinal epithelium. With the help of a combined SEM/microtome based slice and view method called 3View® (Gatan Inc., Pleasanton, CA), we present an entire trophozoite cell reconstruction and describe the arrangement of the major cytoskeletal elements. To aid in future analyses of disc-mediated attachment, we used electron-tomography of freeze-substituted, plastic-embedded trophozoites to explore the detailed architecture of ventral disc microtubules and their associated components. Lastly, we examined the disc microtubule array in three dimensions in unprecedented detail using cryo-electron tomography combined with internal sub-tomogram volume averaging of repetitive domains. We discovered details of protein complexes stabilizing microtubules by attachment to their inner and outer wall. A unique tri-laminar microribbon structure is attached vertically to the disc microtubules and is connected to neighboring microribbons via crossbridges. This work provides novel insight into the structure of the ventral disc microtubules, microribbons and associated proteins. Knowledge of the components comprising these structures and their three-dimensional organization is crucial toward understanding how attachment via the ventral disc occurs in vivo.

Indexed as

Giardia lambliaImage Processing, Computer-AssistedMicrotubule-Associated ProteinsMicrotubulesMultiprotein ComplexesProtein MultimerizationProtozoan ProteinsReproducibility of ResultsTomographyTubulinMicrotubule-Associated ProteinsMultiprotein ComplexesProtozoan ProteinsTubulin

Identifiers

PMID22984443
PMCPMC3439489
OpenAlexW1990774856

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.