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The TOG protein Stu2 is regulated by acetylation

PLoS Genetics(2022)10.1371/journal.pgen.1010358Source: DataRank Database

The TOG protein Stu2 is regulated by acetylation is a research paper published in PLoS Genetics (2022). On theSindex it has a DataRank of 0. It has been cited 5 times.

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0DataRank · unranked

Scored on demand from live citation data

Open Access5 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (7 grants)Impact (FWCI 0.54)OA: goldTopics (55)IDs (PubMed, PMC, OpenAlex)Annotations (2)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (5)

Braden Witt ORCID,Jeremy A. Sabo ORCID,Savannah C. Morris ORCID,Rita K. Miller ORCID,Matt Greenlee

Live enrichment

PubMed:36084134 PMC:PMC9491610 OpenAlex:https://openalex.org/W4295037607

National Institute of General Medical Sciences

Grant: R15GM119117-01

Oklahoma Agricultural Experiment Station

Grant: OKL02961

USDA National Institute of Food and Agriculture -Hatch Project

Grant: 9377

NIGMS NIH HHS

Grant: R15 GM119117

National Institutes of Health

Grant: 1R15GM119117-01

Post-translational regulation of Lis1/Pac1p in dynein function

CASNR/OAES Scholarship

Niblack Research Scholarship

FWCI

0.54

Citation Percentile

0.6%

Citation Trend

2022

2024

2025

goldLicense: cc-by

journalhttps://journals.plos.org/plosgenetics/article/file?id=10.1371/journal.pgen.1010358&type=printable

publisherhttps://journals.plos.org/plosgenetics/article/file?id=10.1371/journal.pgen.1010358&type=printable

publisherhttps://dx.plos.org/10.1371/journal.pgen.1010358

journalhttps://doi.org/10.1371/journal.pgen.1010358

repositoryhttps://pubmed.ncbi.nlm.nih.gov/36084134

Fields of Study

Microtubule and mitosis dynamicsUbiquitin and proteasome pathways14-3-3 protein interactions0301 basic medicine0303 health sciences03 medical and health sciencesAcetylationBenomylChromosomal InstabilityHumansLysineMicrotubule-Associated ProteinsMicrotubulesPerilipin-4Protein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTubulin

MeSH Terms

Perilipin-4AcetylationBenomylHumansLysineMicrotubule-Associated ProteinsMicrotubulesProtein BindingSaccharomyces cerevisiaeTubulinSaccharomyces cerevisiae ProteinsChromosomal Instability

Keywords

AcetylationBiologyMicrotubuleKinetochoreChromosome segregationTubulinCell biologyMutantGeneticsMicrotubule polymerizationBiochemistryChromosomeGeneSaccharomyces cerevisiae ProteinsLysineSaccharomyces cerevisiaeQH426-470Perilipin-4MicrotubulesChromosomal InstabilityHumansBenomylMicrotubule-Associated ProteinsResearch ArticleProtein Binding