ArticlebioRxiv : the preprint server for biology2024
Identification of an intrinsically disordered region (IDR) in arginyltransferase 1 (ATE1).
Misti Cartwright, Rinky Parakra, Ayomide Oduwole, Fangliang Zhang, Daniel J Deredge, Aaron T Smith
Abstract readPreprint
In one paragraphArticle in bioRxiv : the preprint server for biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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4 · The recordCorrections and comments
5 · Who and what moneyAuthors and funding
6 authors.
Misti CartwrightDepartment of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, 21250 USA.
Rinky ParakraDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland, 21201 USA.
Ayomide OduwoleDepartment of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, 21250 USA.
Fangliang ZhangDepartment of Molecular and Cellular Pharmacology, University of Miami, Miller School of Medicine, Miami, Florida, 33136 USA.
Daniel J DeredgeDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland, 21201 USA.
Aaron T SmithDepartment of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, 21250 USA.ORCID 0000-0002-9332-8683 Funding
User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI Gregory L Hura · 2017 to 2026
$28.6MG-RISE at UMBCT32GM144876 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI Rachel Melissa Brewster, Robin Herlands Cresiski · 2022 to 2026
$5.8MGraduate Training at The Chemistry Biology InterfaceT32GM066706 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SELEY-RADTKE, KATHERINE L, SMITH, AARON T · 2004 to 2023
$3.3MDeciphering the Mechanisms of Pathogenic Ferrous Iron Acquisition and Eukaryotic Post-Translational ArginylationR35GM133497 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI Aaron T Smith · 2019 to 2026
$2.9MOxidative stress response and metabolic reprogramming by protein posttranslational arginylationR01GM138557 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI ZHANG, FANGLIANG · 2020 to 2023
$1.3MA Pixel Array Detector System for Small Angle X-ray ScatteringS10OD018483 · OD · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI CLASSEN, SCOTT · 2014 to 2014
$998kNIGMS NIH HHS P30 GM124169NIGMS NIH HHS R01 GM138557NIGMS NIH HHS R35 GM133497NIGMS NIH HHS T32 GM066706NIGMS NIH HHS T32 GM144876NIH HHS S10 OD018483
6 · The paper itselfAbstract
Arginyltransferase 1 (ATE1) catalyzes arginylation, an important post-translational modification (PTM) in eukaryotes that plays a critical role in cellular homeostasis. The disruption of ATE1 function is implicated in mammalian neurodegenerative disorders and cardiovascular maldevelopment, while post-translational arginylation has also been linked to the activities of several important human viruses such as SARS-CoV-2 and HIV. Despite the known significance of ATE1 in mammalian cellular function, past biophysical studies of this enzyme have mainly focused on yeast ATE1, leaving the mechanism of arginylation in mammalian cells unclear. In this study, we sought to structurally and biophysically characterize mouse (
Indexed as
arginyltransferasehydrogen-deuterium exchange mass spectrometryintrinsically disordered regionprotein nucleic acid interactionssmall angle x-ray scattering
Identifiers
PMID39229138
PMCPMC11370617
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