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The cysteine-rich domain of SEP15, a selenoprotein co-chaperone of the ER chaperone, UDP-glucose:glycoprotein glucosyltransferase, adopts a novel fold

bioRxiv (Cold Spring Harbor Laboratory)(2025)10.1101/2025.08.11.669745Source: DataRank Database

The cysteine-rich domain of SEP15, a selenoprotein co-chaperone of the ER chaperone, UDP-glucose:glycoprotein glucosyltransferase, adopts a novel fold is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2025). On theSindex it has a DataRank of 0.

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Enrichment:Funding (5 grants)OA: greenTopics (23)IDs (PubMed, OpenAlex)Annotations (1)SDGs (1)

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)

Kevin P. Guay ORCID,Owen Hurlbut Lesk,Daniel N. Hebert ORCID,Lila M. Gierasch ORCID,Robert V. Williams ORCID

Live enrichment

PubMed:40832263 OpenAlex:https://openalex.org/W4413128451

NIGMS NIH HHS

Grant: R35 GM118161

NIGMS NIH HHS

Grant: R01 GM086874

NIGMS NIH HHS

Grant: F32 GM156016

NIGMS NIH HHS

Grant: T32 GM008515

NIGMS NIH HHS

Grant: P41 GM111135

greenLicense: cc-by-nc-nd

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2025/08/13/2025.08.11.669745.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2025.08.11.669745

repositoryhttps://doi.org/10.1101/2025.08.11.669745

repositoryhttps://pubmed.ncbi.nlm.nih.gov/40832263

Fields of Study

Endoplasmic Reticulum Stress and DiseaseHeat shock proteins researchEnzyme Structure and Function

Keywords

GlucosyltransferaseEndoplasmic reticulumBiochemistryChaperone (clinical)CalnexinGlycoproteinProtein disulfide-isomeraseChemistryGroELCell biologyCysteineDsbAProtein foldingBiologyPeriplasmic spaceEnzymeCalreticulinGenedisulfideselenoprotein

Sustainable Development Goals

SDG 0: Clean water and sanitation

The cysteine-rich domain of SEP15, a selenoprotein co-chaperone of the ER chaperone, UDP-glucose:glycoprotein glucosyltransferase, adopts a novel fold

FAIR Checklist

Authors (5)

Funding (5 grants)

Open Access

Topics

Annotations (Europe PMC)