Evidence map›Paper›PMID 9700165›Full record

ArticleThe Journal of cell biology1998

Recruitment of the gamma-tubulin ring complex to Drosophila salt-stripped centrosome scaffolds.

M Moritz, Y Zheng, B M Alberts, K Oegema

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

99 citing papers in PubMed, 232 citations in OpenAlex.

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  5. Structure of the γ-tubulin ring complex-capped microtubule.Nature structural & molecular biology · 2024
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39 more citing papers are in PubMed but not listed here.

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.

M MoritzDepartment of Biochemistry and Biophysics, University of California, San Francisco, California 94143-0448, USA.
Y Zheng
B M Alberts
K Oegema
National Academy of Sciences · USHarvard University · US

Funding

GENETIC AND BIOCHEMICAL ANALYSIS OF CYTOKINESISR01GM023928 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1985 to 2010
$3.6M
NIGMS NIH HHS GM23928NIGMS NIH HHS R01 GM023928
6 · The paper itself

Abstract

Extracting isolated Drosophila centrosomes with 2 M KI generates salt-resistant scaffolds that lack the centrosomal proteins CP190, CP60, centrosomin, and gamma-tubulin. To clarify the role of these proteins in microtubule nucleation by centrosomes and to identify additional centrosome components required for nucleation, we have developed an in vitro complementation assay for centrosome function. Centrosome aster formation is reconstituted when these inactive, salt-stripped centrosome scaffolds are supplemented with a soluble fraction of a Drosophila embryo extract. The CP60 and CP190 can be removed from this extract without effect, whereas removing the gamma-tubulin destroys the complementing activity. Consistent with these results, we find no evidence that these three proteins form a complex together. Instead, gamma-tubulin is found in two distinct protein complexes of 240,000 and approximately 3,000,000 D. The larger complex, which is analogous to the Xenopus gamma-tubulin ring complex (gammaTuRC) (Zheng, Y., M.L. Wong, B. Alberts, and T. Mitchison. 1995. Nature. 378:578-583), is necessary but not sufficient for complementation. An additional factor found in the extract is required. These results provide the first evidence that the gammaTuRC is required for microtubule nucleation at the centrosome.

Indexed as

Drosophila ProteinsAnimalsCell Cycle ProteinsCentrosomeDrosophilaIodatesMicrotubule-Associated ProteinsMicrotubulesNuclear ProteinsPotassium CompoundsSaltsTubulinXenopusCell Cycle ProteinsCP190 protein, DrosophilaDrosophila ProteinsIodatesMap60 protein, DrosophilaMicrotubule-Associated ProteinsNuclear ProteinsPotassium Compoundspotassium iodateSaltsTubulin

Identifiers

PMID9700165
PMCPMC2148159
OpenAlexW2063734769

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.