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Profil bibliographique

Di Kuang

Informations fournies par OpenAlex. Research Africa ne déduit ni nationalité, ni poste, ni coordonnées personnelles.

4Publications signalées
4Citations signalées
1Affiliations récentes

Les institutions déclarées

Les domaines associés

Mitochondrial Function and PathologyProtein Tyrosine PhosphatasesGenetics, Aging, and Longevity in Model OrganismsMetabolomics and Mass Spectrometry StudiesBioinformatics and Genomic Networks

Les publications récentes

Accès ouvert 2026 preprint OpenAlex

Acetyl-CoA availability regulates neuronal metabolism, growth, and synaptic activity

Eric R. McGregor, Cassandra Joan McGill, Nicholas L. Arp, Josef P. Clark et autres

The metabolite acetyl-CoA plays a central role in cellular metabolic homeostasis. As part of the secretory pathway, acetyl-CoA is imported into the endoplasmic reticulum (ER) by a membrane-bound transporter AT-1 (SLC33A1). AT-1 has been linked to peripheral neuropathy (heterozygous mutations), developmental delay …

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0 citations bioRxiv (Cold Spring Harbor Laboratory)
Accès ouvert 2025 article OpenAlex

Aging-linked systemic lipid signature is reprogrammed by caloric restriction in rhesus monkeys

Salma I Abou Elhassan, Josef P. Clark, Di Kuang, Timothy W. Rhoads et autres

Caloric restriction (CR) without malnutrition delays aging in diverse species, including primates, with metabolic changes implicated in this process. To facilitate exploration of CR metabolism with aging, we developed a 15-minute LC-MS/MS metabolomics and lipidomics method, leveraging monophasic extractions and wide elution-strength …

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1 citation Molecular Systems Biology
Accès ouvert 2022 article OpenAlex

Evolutionary genomic relationships and coupling in MK-STYX and STYX pseudophosphatases

Qi Yi, Di Kuang, Kylan Kelley, William Buchser et autres

The dual specificity phosphatase (DUSP) family has catalytically inactive members, called pseudophosphatases. They have mutations in their catalytic motifs that render them enzymatically inactive. This study analyzes the significance of two pseudophosphatases, MK-STYX [MAPK (mitogen-activated protein kinase phosphoserine/threonine/tyrosine-binding protein]) and STYX (serine/threonine/tyrosine-interacting …

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3 citations Scientific Reports
2021 article OpenAlex

Evolutionary Genomic Relationships and Coupling in Pseudophosphatase MK‐STYX

Qi Yi, Di Kuang, Kylan Kelley, William Buchser et autres

MK‐STYX [MAPK (mitogen‐activated protein kinase) phosphoserine/threonine/tyrosine‐binding protein] is an atypical member of the dual‐specificity family subfamily of protein tyrosine phosphatases. It is catalytically inactive due to mutations at critical histidine and cysteine residues within its signature active motif (HCX5R). Therefore, MK‐STYX is …

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0 citations The FASEB Journal

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