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Proteolytic cleavage plays an essential role in the control of numerous biological processes, including protein localization, fate and activity as well as the processing of cellular information.
This paper presents a concise review of current techniques employed for the transduction and processing of cellular signals.
The RNA exosome is a multisubunit 3′ to 5′ exoribonuclease complex that participates in degradation and processing of cellular RNA.
Additionally, NS1 protein inhibits the processing of cellular mRNA in the nucleus by binding with the cellular factor CPSF30 and PABPII that are involved in transcriptional termination and polyadenylation (Chen et al., 1999; Nemeroff et al., 1998).
Perhaps the most plausible explanation is that while the primary function of SOX and muSOX is to induce degradation of mRNAs, dysregulation of transcription and/or processing of cellular messages are secondary effects of host shutoff.
Both these proteases can proteolytically activate SERA5, which triggers downstream processing of cellular substrates [ 103, 104].
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The truncation results in the loss of the NS1 nuclear localization signal, a PI3K-binding motif, and binding domains that support interactions with the cellular nuclear proteins CPSF and poly (A -binding protein II (PA -bindingo factors that function in the 3'-end-proteinIIg of cellular PABIIRNAs [ 14, 15].
In addition, time and space must be fundamentally discrete or must emerge from the discrete processing of the cellular automaton.
The Golgi complex constitutes a central way station of the eukaryotic endomembrane system, an intricate network of organelles engaged in control of membrane trafficking and the processing of various cellular components.
The end result of either pathway is the activation of the caspase cascade and the proteolytic processing of specific cellular substrates, resulting in apoptotic cell death [ 56, 57].
Thus, dysfunction of genes and their protein products involved in the recognition and processing of the cellular radiation damage could be a possible molecular basis underlying the adverse radiotoxic reactions in healthy tissue.
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