Results 61 to 70 of about 4,003 (181)
Investigation of IFN signaling in cultured skin fibroblasts from patients with genetically confirmed mitochondrial diseases of diverse origins revealed that altered IFN signaling is an inconsistent feature of these disorders. Cytosolic accumulation of mtDNA and mtRNA was variably detected and showed little correlation with ISG scores.
Manon Marchais +11 more
wiley +1 more source
Human FASTK preferentially binds single‐stranded and G‐rich RNA
Although FASTK is known to play a role in mRNA biology, the mechanism through which it recognizes RNA has yet to be unraveled. Here, we used purified human FASTK to characterize its RNA‐binding properties in vitro. We found that FASTK prefers ssRNA oligonucleotides containing guanines with the potential to form G‐quadruplexes and binds robustly to any ...
Daria M. Dawidziak +7 more
wiley +1 more source
PNPase IN C. ELEGANS: MUTAGENIC ANALYSIS TO COMPLEMENT KNOCKDOWN STUDIES [PDF]
PNPase is a gene implicated as a potential target for cancer therapy; human mutations also present with deafness, myopathies, and neuropathies. In this study, C. elegans was used to investigate the effect of knocking out PNPase in a whole animal.
Seibert, Danielle K.
core +1 more source
Selective RNA processing and stabilization (SRPS) facilitates the differential expression of multiple genes in polycistronic operons. However, how the coordinated actions of SRPS‐related enzymes affect stoichiometric regulation remains unclear.
Daixi Liu +5 more
doaj +1 more source
Al‐Hilfi et al. present a biocatalytic strategy for synthesizing 5‐methyl‐5,6‐dihydrothymidine (5‐MDHT), a sensitive MRI contrast agent. The study demonstrates that recombinant enzyme catalysis offers an efficient, sustainable, and eco‐friendly alternative to traditional chemical synthesis for producing clinically relevant imaging probes.
Aimen Al‐Hilfi +8 more
wiley +1 more source
Domains and structure of PNPase.
(A) Domain organization of PNPase, using the C. crescentus PNPase crystal structure as a reference [44]. The complete PNPase trimer viewed from the (B) top and (C) side, with domains colored the same as in (A). (D) A cut-away view of the RNA-bound trimer
Todd A. Cameron (146712) +2 more
core +1 more source
This review highlights the advances in graphene liquid cell designs for in situ liquid‐phase transmission electron microscopy, spanning veil‐type, well‐type, liquid‐flowing‐type, and mixing‐type configurations. These developments collectively enable real‐time visualization of diverse reactions in liquid environments at atomic resolution, thereby ...
Hyeonjong Ma +2 more
wiley +1 more source
Abstract Ribonuclease E (RNase E) is central to bacterial RNA metabolism. In cyanobacteria, its activity is inhibited by RebA, a key mechanism for controlling cell morphology. Here, we demonstrate that rebA is essential for diazotrophic growth of Anabaena PCC 7120, a filamentous cyanobacterium capable of forming heterocysts—specialized nitrogen‐fixing ...
Sujuan Liu +6 more
wiley +1 more source
Human polynucleotide phosphorylase (PNPase) is an evolutionarily conserved 3′-to-5′ exoribonuclease principally located in mitochondria where it is responsible for RNA turnover and import.
B. Golzarroshan +6 more
semanticscholar +1 more source
Here, we report that mitochondria from rat skeletal muscle contain a select population of nuclear‐encoded protein‐coding and noncoding RNAs, including 3 microRNAs whose expression tended to be altered by exercise training. These findings suggest that mitochondria‐localized nuclear‐encoded RNAs may play a role in mediating the beneficial adaptive ...
Jessica L. Silver +8 more
wiley +1 more source

