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Cytoplasmic maspin may sequester complexes containing HDAC1 and GST and modulating its transport to nucleus and activity.
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These complexes may sequester viral and host sRNAs to engage them in yet unknown mechanisms involved in plant:virus interactions.
Since SLD2 interacts with Ubc9/Hus5 [25] [26], [26], it has been proposed that Rad60 may recruit SUMO-charged Ubc9 to mediate sumoylation of specific proteins, or that it may sequester Ubc9 in an inactive complex to down-regulate sumoylation [1].
The association of P-TEFb with 7SK snRNA and HEXIM proteins may sequester P-TEFb in a complex from which functional P-TEFb can be rapidly recruited to regulate RNA polymerase II transcription [14], [15].
One possible explanation for this behavior is that, at higher concentrations, NKX2-5 may sequester MEIS1 in a direct complex that can bind neither site.
The association of P-TEFb with HEXIM1/7SK may sequester excess P-TEFb in a complex from which functional P-TEFb can be rapidly recruited to regulated RNA polymerase II transcription [14], [15].
Conceivably, LZAP may sequester p38 in the nucleus in a complex with Wip1 as a means of p38 inactivation.
Many such indolent pathogens, including O. anthropi, may sequester in the capsular bag, necessitating its removal [4, 6, 8, 16].
Conceivably, Nullbasic may sequester cellular factors (such as importins) normally required for Rev nucleolar targeting.
This suggests that Pgc may sequester Cdk9 activity away from active promoters.
Ro60 and/or La may sequester Y RNAs and prevent them from functioning in chromosomal DNA replication.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com