Results 191 to 200 of about 409,167 (281)

Lactylation Enhances the Activity of Lactate Dehydrogenase A and Promotes the Chemoresistance to Cisplatin Through Facilitating DNA Nonhomologous End Junction in Lung Adenocarcinoma

open access: yesAdvanced Science, EarlyView.
Lactylation, linked to glycolysis, is poorly understood in regulation. It is found that LDHA is lactylated at Lys81/Lys318 by AARS1, boosting its activity and cellular lactylation via positive feedback in LUAD. Lactylation regulates NHEJ‐related proteins; their delactylation impairs NHEJ and increases cisplatin sensitivity, offering anticancer insights.
Jizhuo Li   +11 more
wiley   +1 more source

Sex-specific cardiac dysfunction in mice with chronic kidney disease. [PDF]

open access: yesNephrol Dial Transplant
Zhao Y   +8 more
europepmc   +1 more source

Purine metabolism in cultured endothelial cells [PDF]

open access: yes, 1980
Gerbes, Alexander L.   +4 more
core   +1 more source

Proteogenomic Characterization Reveals Metabolic Vulnerabilities and Aberrant Phosphorylation in Colorectal Metastasis to Liver

open access: yesAdvanced Science, EarlyView.
This study provides a multi‐omics landscape of treatment‐naïve colorectal liver metastasis and reveals dysregulated molecules and cellular pathways. SHMT1 and NDRG1 Ser330 phosphorylation are demonstrated to display crucial roles in tumorigenesis and liver metastasis. Two proteomics subtypes (metabolism and RNA function) with distinct clinical outcomes
Wensi Zhao   +20 more
wiley   +1 more source

Erucic Acid, Derived by Lactobacillus Crispatus, Induces Ferroptosis in Cervical Cancer Organoids Through the PPAR‐δ Signaling Pathway

open access: yesAdvanced Science, EarlyView.
Utilizing PDO, cell lines and cervical cancer xenograft (CDX) models, the study demonstrate both in vitro and in vivo that the metabolite of L. crispatus, erucic acid, can modulate the proliferation, migration and invasion of cervical cancer by activating the PPAR‐δ pathway.
Qianwei Zhen   +8 more
wiley   +1 more source

Distinct Phage‐Encoded Enzymes for Substitution of Deoxythymidine by Deoxyuridine in Phage Genomes

open access: yesAdvanced Science, EarlyView.
Distinct enzymes including dCTP deaminases (Dcds), dTMP phosphatases (Dtms), and dTTP pyrophosphatases (Dtt) are found to be responsible for dU‐DNA biosynthesis in the phages PBS1, DSS3_VP1, and PhiR1‐37. Both PhiR1‐37‐derived and synthetic dU‐DNA are resistant to cleavage by restriction enzymes and Cas12a nuclease targeting dT‐containing sites.
Yating Li   +7 more
wiley   +1 more source

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