Results 161 to 170 of about 267,872 (264)

RNF138‐Mediated Ubiquitination and Degradation of NS5 Restricts Tick‐Borne Encephalitis Virus Infection

open access: yesAdvanced Science, EarlyView.
Host‐specific compatibility between RNF138‐like proteins and flavivirus NS5 determines NS5 stability. Mammalian RNF138 but not arthropod homologs recognizes and induces conserved NS5/RdRp K48‐linked ubiquitination and proteasomal degradation, thereby restricting viral replication. Ectopic RNF138 in mice attenuates TBEV‐induced pathogenesis. (Created in
Jialiang Sun   +6 more
wiley   +1 more source

Cerebrospinal Fluid Metabolome in Central Nervous System Infections: A Study of Diagnostic Accuracy. [PDF]

open access: yesAnn Neurol
Staal SL   +7 more
europepmc   +1 more source

PRMT9 Aggravated Dopaminergic Neurodegeneration in Parkinson's Disease Model by Facilitating the Degradation of DUSP26 and Inducing Mitochondrial Dysfunction

open access: yesAdvanced Science, EarlyView.
In the pathological state of PD induced by MPP+, the upregulated PRMT9 in dopaminergic neurons translocates into mitochondrion and interacts with DUSP26 and catalyzes its arginine methylation, leading to the ubiquitin‐proteasomal degradation of DUSP26 mediated by Trim32.
Tengfei Liu   +13 more
wiley   +1 more source

ZNF33B Promotes Japanese Encephalitis Virus Infection by Regulating the Stability of M6A‐Modified Trim25 to Control the Autophagy Process

open access: yesAdvanced Science, EarlyView.
Upon JEV infection, ZNF33B recruits METTL14 to stabilize the METTL3‐METTL14 m6A methyltransferase complex, leading to increased m6A modification of host transcripts, including Trim25 mRNA. ZNF33B selectively binds m6A‐modified sites on Trim25 mRNA and accelerates its decay, resulting in reduced TRIM25 protein abundance.
Jian Du   +9 more
wiley   +1 more source

Review of the aetiologies of central nervous system infections in Vietnam. [PDF]

open access: yesFront Public Health
Brindle HE   +7 more
europepmc   +1 more source

RNA‐Binding Protein RBM25 Targets the mRNA Stability of GTPase Rab22a to Restrict Viral Entry and Infection

open access: yesAdvanced Science, EarlyView.
This study identifies RNA‐binding protein RBM25 as a broad‐spectrum antiviral factor acting independently of type I interferon. It blocks viral entry by suppressing GTPase Rab22a via the RC3H1‐mediated destabilization of Rab22a mRNA. Viral downregulation of RBM25 enhances GTPase Rab22a expression and viral entry, revealing an unreported post ...
Yingying Ding   +13 more
wiley   +1 more source

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