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In this system, transiently transfected wild type tyrosinase is translocated into the ER where the glycosylated polypeptide chain folds in the presence of calnexin/calreticulin into an export competent protein that exits the ER.
The released, export competent BR mRNP moves randomly by diffusion through the interchromatin space.
Export competent pre-ribosomal particles are separately transported through nuclear pore complexes (NPCs) into the cytoplasm by multiple export factors.
The intranuclear mRNP enters the NPC via the basket as an export competent mRNP, and during translocation, conformational and compositional changes are triggered.
These mechanisms involve both transcription and different pre-mRNA processing steps and thus connect these processes to the formation of export competent mRNPs.
Pre-mRNAs, synthesised by transcription of protein-coding genes, are assembled into pre-mRNA protein (pre-mRNA proteinxes, processed, transformed into export competent mRNA–protein (mRNP) complexes and exprocessed transformedsm.
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Studies of this mechanism in Escherichia coli have identified numerous transient protein-protein interactions that guide export-competent proteins through the Tat pathway.
Following mRNA maturation and processing, the export-competent mRNP must travel through the nuclear pore complex (NPC) to reach the cytoplasm.
The observation that Ccr4-Not interacts both with methylated, export-competent hnRNPs and NPC nuclear basket components is consistent with a model in which Ccr4-Not selectively interacts with methylated hnRNPs as they chaperone their mRNA cargoes through the NPC.
The final maturation and release of export-competent mRNPs from the transcription site requires in mammalian cells the carboxy terminal domain (CTD) of the large subunit of Pol-II [27].
The nuclear steps required for gene expression are highly integrated and are controlled by evolutionarily conserved factors and mechanisms which package an mRNA molecule into an export-competent ribonucleoprotein (mRNP) complex [1], [2], [3].
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