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The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC)

eLife(2022)10.7554/elife.80053Source: DataRank Database

The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC) is a research paper published in eLife (2022). On theSindex it has a DataRank of 0.733. It has been cited 24 times, with 15 citing works in its 1-hop citation network.

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0.733DataRank · unranked

Scored on demand from live citation data

Deposits data Open Access24 citations · 15 citing works in its network

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Data for: The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC) · Dryad

pdb

Data availability

Repositories this paper deposited data in (declared in PubMed).

Dryad10.5061/dryad.gb5mkkwt3

DataRank reads this dataset's downstream impact straight off the citation graph — no black box, no proprietary weighting. How is this computed?

›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (12 grants)Impact (FWCI 2.04)OA: goldTopics (47)Linked Datasets (1)DataCite Reuse (1)IDs (PubMed, PMC, OpenAlex)Annotations (1)SDGs (1)

FAIR Checklist

Context only (not used in score)

Findable (2/2)

Has DOI
Indexed in repositories

Accessible (1/2)

Open Access

Interoperable (2/2)

DataCite relations
Linked datasets

Reusable (0/3)

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DataRank Breakdown

Base Score 66%Citation Network 34%

Base Score Contribution

0.483

From this paper's citation signal

Citation Network Contribution

0.250

From 10 citing papers with measurable signal

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Top 5 citers driving the network score

Ranked by each citer's contribution to N(p) — log1p(C_q) divided by its reference count — out of 15 citers.

Autoinhibitory mechanism controls binding of centrosomin motif 1 to γ-tubulin ring complex
The Journal of Cell Biology202313 citations46 referencesContributes 0.057
Transition of human γ-tubulin ring complex into a closed conformation during microtubule nucleation
Science202443 citations81 referencesContributes 0.047
CAMSAPs and nucleation-promoting factors control microtubule release from γ-TuRC
Nature Cell Biology202443 citations94 referencesContributes 0.040
Partial closure of the γ-tubulin ring complex by CDK5RAP2 activates microtubule nucleation
Developmental Cell202423 citations96 referencesContributes 0.033
γ-TuRC asymmetry induces local protofilament mismatch at the RanGTP-stimulated microtubule minus end
The EMBO Journal202418 citations94 referencesContributes 0.031

Authors (5)

Brianna Romer ORCID,Brian P. Mahon ORCID,Sophie M. Travis ORCID,Sabine Petry ORCID,Michael J Rale ORCID

Live enrichment

PubMed:36515268 PMC:PMC9859039 OpenAlex:https://openalex.org/W4311399222

Howard Hughes Medical Institute

Grant: Gilliam Graduate Student Fellowship

National Science Foundation

Grant: Graduate Research Fellowship

National Institutes of Health

Grant: New Innovator Award

Pew Charitable Trusts

Grant: Pew Scholars Program in the Biomedical Sciences

David and Lucile Packard Foundation

Grant: 2014-40376

National Institutes of Health

Grant: 1DP2GM123493

NIGMS NIH HHS

Grant: DP2 GM123493

NIH HHS

Grant: New Innovator Award,1DP2GM123493

NIGMS NIH HHS

Grant: T32 GM007388

National Science Foundation

Grant: 2011750

Princeton Center for Complex Materials

Fundação para a Ciência e a Tecnologia, I.P.

Grant: PTDC/CCI-INF/6762/2020

MS3: New foundations for micro-services and serverless systems

National Institutes of Health

Grant: 1DP2GM123493-01

Building the Chromosome Segregation Machinery from Scratch

FWCI

2.04

Citation Percentile

0.9%

Influential Citations

Citation Trend

2022

2023

2024

2025

2026

goldLicense: cc-by

journalhttps://doi.org/10.7554/elife.80053

GOLDhttps://doi.org/10.7554/elife.80053

publisherhttps://doi.org/10.7554/elife.80053

publisherhttps://cdn.elifesciences.org/articles/80053/elife-80053-v2.pdf

publisherhttps://cdn.elifesciences.org/articles/80053/elife-80053-v2.xml

Fields of Study

Microtubule and mitosis dynamicsAdvanced Electron Microscopy Techniques and ApplicationsUbiquitin and proteasome pathwaysMedicineBiology0301 basic medicine03 medical and health sciences

MeSH Terms

AnimalsMicrotubule-Associated ProteinsMicrotubulesTubulinXenopus laevisCentrosomeMicrotubule-Organizing Center

Keywords

MicrotubuleTunaCentrosomeXenopusTubulinCell biologyMicrotubule nucleationBiologyActivator (genetics)CytoplasmActinChemistryBiophysicsBiochemistryCellGeneFisheryMicrotubulesChemical BiologyCdk5rap2Gamma-tubulin Ring ComplexSingle Molecule TirfQH301-705.5ScienceQRXenopus laevisBiochemistry and Chemical BiologyMedicineAnimalsBiology (General)Microtubule-Associated ProteinsMicrotubule-Organizing Center

Sustainable Development Goals

SDG 3: 3. Good health

Data for: The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC)

10.5061/dryad.gb5mkkwt3Dryad

The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC)

FAIR Checklist

DataRank Breakdown

Top 5 citers driving the network score

Authors (5)

Funding (12 grants)

Impact

Open Access

Topics

Linked Datasets (1)

Annotations (Europe PMC)