Evidence map›Paper›PMID 10037793›Full record

ArticleThe Journal of cell biology1999

Characterization of two related Drosophila gamma-tubulin complexes that differ in their ability to nucleate microtubules.

K Oegema, C Wiese, O C Martin, R A Milligan, A Iwamatsu, T J Mitchison, Y Zheng

Open access · bronzeAbstract readComparative Study
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 148 papers.

0numbers the graph read from it
0cells of the map it votes in
148citing papers in PubMed
7.8field-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

148 citing papers in PubMed, 310 citations in OpenAlex.

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  10. Structure of the γ-tubulin ring complex-capped microtubule.Nature structural & molecular biology · 2024
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88 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

7 authors at 4 institutions in 2 countries.

K OegemaDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA. Karen.Omega@EMBL-Heidelburg.DE
C Wiese
O C Martin
R A Milligan
A Iwamatsu
T J Mitchison
Y Zheng
Harvard University · USKirin (Japan) · JPScripps Research Institute · USDepartment of Embryology · US

Funding

The function and assembly of the lamin-B spindle sheathR01GM056312 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI ZHENG, YIXIAN · 1997 to 2014
$2.7M
NIGMS NIH HHS R01 GM056312NIGMS NIH HHS R01-GM56312-01
6 · The paper itself

Abstract

gamma-tubulin exists in two related complexes in Drosophila embryo extracts (Moritz, M., Y. Zheng, B.M. Alberts, and K. Oegema. 1998. J. Cell Biol. 142:1- 12). Here, we report the purification and characterization of both complexes that we name gamma-tubulin small complex (gammaTuSC; approximately 280,000 D) and Drosophila gammaTuRC ( approximately 2,200,000 D). In addition to gamma-tubulin, the gammaTuSC contains Dgrip84 and Dgrip91, two proteins homologous to the Spc97/98p protein family. The gammaTuSC is a structural subunit of the gammaTuRC, a larger complex containing about six additional polypeptides. Like the gammaTuRC isolated from Xenopus egg extracts (Zheng, Y., M.L. Wong, B. Alberts, and T. Mitchison. 1995. Nature. 378:578-583), the Drosophila gammaTuRC can nucleate microtubules in vitro and has an open ring structure with a diameter of 25 nm. Cryo-electron microscopy reveals a modular structure with approximately 13 radially arranged structural repeats. The gammaTuSC also nucleates microtubules, but much less efficiently than the gammaTuRC, suggesting that assembly into a larger complex enhances nucleating activity. Analysis of the nucleotide content of the gammaTuSC reveals that gamma-tubulin binds preferentially to GDP over GTP, rendering gamma-tubulin an unusual member of the tubulin superfamily.

Indexed as

Amino Acid SequenceAnimalsCryoelectron MicroscopyDrosophilaGuanosine DiphosphateGuanosine TriphosphateInsect ProteinsMacromolecular SubstancesMicrotubulesMolecular Sequence DataMolecular WeightProtein BindingTubulinXenopusGuanosine DiphosphateGuanosine TriphosphateInsect ProteinsMacromolecular SubstancesTubulin

Identifiers

PMID10037793
PMCPMC2132928
OpenAlexW2033018905

What OpenQuestion holds

Texttitle and abstract
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.