Evidence map›Paper›PMID 21965284›Full record

ArticleMolecular biology of the cell2011

Subunit organization in the Dam1 kinetochore complex and its ring around microtubules.

Vincent H Ramey, Amanda Wong, Jie Fang, Stuart Howes, Georjana Barnes, Eva Nogales

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Structural plasticity of the living kinetochore.The Journal of cell biology · 2017
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Phosphoregulation promotes release of kinetochores from dynamic microtubules via multiple mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  15. Article
  16. Article
  17. 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

6 authors at 3 institutions in 1 country.

Vincent H RameyBiophysics Graduate Group, University of California, Berkeley, Berkeley, CA 94720, USA.
Amanda Wong
Jie Fang
Stuart Howes
Georjana Barnes
Eva Nogales
University of California, Berkeley · USHoward Hughes Medical Institute · USLawrence Berkeley National Laboratory · US

Funding

TUBULIN STRUCTURE BY ELECTRON CRYSTALLOGRAPHYP01GM051487 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI CATE, JAMIE H · 1994 to 2018
$27.6M
XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 1985 to 2011
$17.6M
SACCHAROMYCES CEREVISIAE MICROTUBULE CYTOSKELETONR01GM047842 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BARNES, GEORJANA · 1993 to 2022
$7.5M
Howard Hughes Medical InstituteNCRR NIH HHS P41 RR001081NIGMS NIH HHS 2P01GM51487CNIGMS NIH HHS P01 GM051487NIGMS NIH HHS R01 GM047842NIGMS NIH HHS R01GM47842
6 · The paper itself

Abstract

All eukaryotic cells must segregate their chromosomes equally between two daughter cells at each division. This process needs to be robust, as errors in the form of loss or gain of genetic material have catastrophic effects on viability. Chromosomes are captured, aligned, and segregated to daughter cells via interaction with spindle microtubules mediated by the kinetochore. In Saccharomyces cerevisiae one microtubule attaches to each kinetochore, requiring extreme processivity from this single connection. The yeast Dam1 complex, an essential component of the outer kinetochore, forms rings around microtubules and in vitro recapitulates much of the functionality of a kinetochore-microtubule attachment. To understand the mechanism of the Dam1 complex at the kinetochore, we must know how it binds to microtubules, how it assembles into rings, and how assembly is regulated. We used electron microscopy to map several subunits within the structure of the Dam1 complex and identify the organization of Dam1 complexes within the ring. Of importance, new data strongly support a more passive role for the microtubule in Dam1 ring formation. Integrating this information with previously published data, we generated a structural model for the Dam1 complex assembly that advances our understanding of its function and will direct future experiments.

Indexed as

Cell Cycle ProteinsCell DivisionChromosomesChromosome SegregationKinetochoresMicrotubule-Associated ProteinsMicrotubulesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpindle ApparatusCell Cycle ProteinsDAM1 protein, S cerevisiaeMicrotubule-Associated ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID21965284
PMCPMC3216659
OpenAlexW2155651890

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.