Evidence map›Paper›PMID 10352012›Full record

ArticleThe Journal of cell biology1999

The unstable F-box protein p58-Ctf13 forms the structural core of the CBF3 kinetochore complex.

I D Russell, A S Grancell, P K Sorger

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

54 citing papers in PubMed, 114 citations in OpenAlex.

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  18. Molecular structures and interactions in the yeast kinetochore.Cold Spring Harbor symposia on quantitative biology · 2010
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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 at 1 institution in 1 country.

I D RussellMassachusetts Institute of Technology, Department of Biology, Cambridge, Massachusetts 02139, USA.
A S Grancell
P K Sorger
Massachusetts Institute of Technology · US

Funding

BIOCHEMICAL AND GENETIC ANALYSIS OF YEAST KINETOCHORESR01GM051464 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SORGER, PETER KARL · 1994 to 2010
$3.9M
NIGMS NIH HHS GM51464NIGMS NIH HHS R01 GM051464
6 · The paper itself

Abstract

Kinetochores are smaller and more accessible experimentally in budding yeast than in any other eukaryote. Believing that simple and complex kinetochores have important structural and functional properties in common, we characterized the structure of CBF3, the essential centromere-binding complex that initiates kinetochore formation in Saccharomyces cerevisiae. We find that the four subunits of CBF3 are multimeric in solution: p23(Skp1) and p58(Ctf13) form a heterodimer, and p64(Cep3) and p110(Ndc10) form homodimers. Subcomplexes involving p58 and each of the other CBF3 subunits can assemble in the absence of centromeric DNA. In these subcomplexes, p58 appears to function as a structural core mediating stable interactions among other CBF3 proteins. p58 has a short half-life in yeast, being subject to ubiquitin-dependent proteolysis, but we find that it is much more stable following association with p64. We propose that p23(Skp1)-p58-p64 complexes constitute the primary pool of active p58 in yeast cells. These complexes can either dissociate, reexposing p58 to the degradation pathway, or can bind to p110 and centromeric DNA, forming a functional CBF3 complex in which p58 is fully protected from degradation. This pathway may constitute an editing mechanism preventing the formation of ectopic kinetochores and ensuring the fidelity of chromosome segregation.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceDimerizationDNA-Binding ProteinsFungal ProteinsKinetochoresMolecular Sequence DataNuclear ProteinsPeptide MappingSaccharomyces cerevisiaeCEP3 protein, S cerevisiaeCTF13 protein, S cerevisiaeDNA-Binding ProteinsFungal ProteinsNuclear ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID10352012
PMCPMC2133132
OpenAlexW1995143644

What OpenQuestion holds

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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.