Evidence map›Paper›PMID 31194673›Full record

ArticleeLife2019

The structure of the yeast Ctf3 complex.

Stephen M Hinshaw, Andrew N Dates, Stephen C Harrison

Abstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. An interdependent Cbf1-CCAN interaction stabilizes the budding yeast kinetochore.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Dual Roads of CENP-A for Centromere Identification.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. CENP-I directly targets centromeric DNA to support CENP-A deposition and centromere maintenance.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Investigating eukaryotic cells with cryo-ET.Molecular biology of the cell · 2020
    Article
  13. 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

3 authors.

Stephen M HinshawDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Howard Hughes Medical Institute, Boston, United States.ORCID 0000-0003-4215-5206
Andrew N DatesHarvard Chemical Biology PhD Program, Harvard University, Boston, United States.
Stephen C HarrisonDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Howard Hughes Medical Institute, Boston, United States.ORCID 0000-0001-7215-9393

Funding

Principles of Scientific Citizenship: Ethics, Communication, and Leadership for ScientistsT32GM095450 · NIGMS · HARVARD UNIVERSITY · PI WALKER, SUZANNE · 2011 to 2020
$3.5M
NIGMS NIH HHS T32 GM095450NIH HHS 5T32GM095450-08
6 · The paper itself

Abstract

Kinetochores are the chromosomal attachment points for spindle microtubules. They are also signaling hubs that control major cell cycle transitions and coordinate chromosome folding. Most well-studied eukaryotes rely on a conserved set of factors, which are divided among two loosely-defined groups, for these functions. Outer kinetochore proteins contact microtubules or regulate this contact directly. Inner kinetochore proteins designate the kinetochore assembly site by recognizing a specialized nucleosome containing the H3 variant Cse4/CENP-A. We previously determined the structure, resolved by cryo-electron microscopy (cryo-EM), of the yeast Ctf19 complex (Ctf19c, homologous to the vertebrate CCAN), providing a high-resolution view of inner kinetochore architecture (Hinshaw and Harrison, 2019). We now extend these observations by reporting a near-atomic model of the Ctf3 complex, the outermost Ctf19c sub-assembly seen in our original cryo-EM density. The model is sufficiently well-determined by the new data to enable molecular interpretation of Ctf3 recruitment and function.

Indexed as

KinetochoresModels, MolecularMultiprotein ComplexesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCtf3 protein, S cerevisiaeMultiprotein ComplexesSaccharomyces cerevisiae ProteinsCryo-EMKinetochoreMitosismolecular biophysicsS. cerevisiaestructural biology

Identifiers

PMID31194673
PMCPMC6602579

What OpenQuestion holds

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LicenceCC BY
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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.