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CryoEM analysis of the essential native UDP-glucose pyrophosphorylase from Aspergillus nidulans reveals key conformations for activity regulation and function

mBio(2023)10.1128/mbio.00414-23Source: DataRank Database

CryoEM analysis of the essential native UDP-glucose pyrophosphorylase from Aspergillus nidulans reveals key conformations for activity regulation and function is a research paper published in mBio (2023). On theSindex it has a DataRank of 0. It has been cited 6 times.

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Open Access6 citations

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datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (10 grants)Impact (FWCI 0.64)OA: goldTopics (43)IDs (PubMed, PMC, OpenAlex)Annotations (1)SDGs (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 (12)

Cecilia D’Angelo ORCID,Ainara Otamendi ORCID,Javier O. Cifuente ORCID,Elisa de Astigarraga,Borja Ochoa-Lizarralde ORCID

Live enrichment

PubMed:37409813 PMC:PMC10470519 OpenAlex:https://openalex.org/W4383302053

Ministerio de Asuntos Económicos y Transformación Digital, Gobierno de España

Grant: PID2021-122705OB-I00

Ministerio de Asuntos Económicos y Transformación Digital, Gobierno de España (MINECO)

Grant: CTQ201782222-R

Basque Government

Grant: IT1662-22

Basque Government

Grant: KK-2022/00107

HHS | National Institutes of Health

Grant: R01AI149297

Basque Government

Grant: KK-2019/00076

Ministerio de Asuntos Económicos y Transformación Digital, Gobierno de España

Grant: PID2019-105649RB-I00

Basque Government

Grant: PIBA-2020-1-0032-GVB0

Basque Government

Grant: KK-2021-00034

National Institutes of Health

Grant: 5R01AI149297-02

Rationalizing glycoengineering strategies for immunotherapeutic antibodies

FWCI

0.64

Citation Percentile

0.6%

Citation Trend

2024

2025

2026

goldLicense: cc-by

journalhttps://doi.org/10.1128/mbio.00414-23

publisherhttps://doi.org/10.1128/mbio.00414-23

repositoryhttps://pubmed.ncbi.nlm.nih.gov/37409813

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/10470519

repositoryhttps://doaj.org/article/232e426a0a684ce694dd55e5be755b6b

Fields of Study

Glycosylation and Glycoproteins ResearchEnzyme Production and CharacterizationCarbohydrate Chemistry and Synthesis0301 basic medicine0303 health sciences03 medical and health sciencesAspergillus nidulansUTP-Glucose-1-Phosphate UridylyltransferaseCryoelectron MicroscopyProtein ConformationModels, MolecularFungal ProteinsCell WallUridine Diphosphate Glucose

MeSH Terms

Aspergillus nidulansCell WallFungal ProteinsUTP-Glucose-1-Phosphate UridylyltransferaseModels, MolecularProtein ConformationUridine Diphosphate GlucoseCryoelectron Microscopy

Keywords

Aspergillus fumigatusAspergillus nidulansProtein subunitBiochemistryBiologyEnzymeCell wallFungal proteinChemistryMicrobiologySaccharomyces cerevisiaeYeastGeneAspergillosisEnzyme MechanismCell Wall BiosynthesisCryoemEnzyme SpecificityUdp-glucose PyrophosphorylasesQR1-502Research Article

Sustainable Development Goals

SDG 3: 3. Good healthSDG 0: Life in Land