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In this scenario, BIRC3, an E3 ligase, ubiquitinates receptor interacting protein 1 (RIP1) and enables its interaction with the TAK1/TAB2/3 (TGFβ-activated kinase 1/ TAK1 -binding protein 2/3) complex, which in turn activates I kappa B kinase (IKK), and thus NF- κB.
This is primarily achieved by phosphorylation of p53, which renders it resistant to Mdm2-mediated ubiquitination and enables its interaction with transcriptional co-activators.
PIN1 binds to threonine-phosphorylated p73 upon DNA damage-induced c-Abl activation and enables its interaction with p300.
Such phosphorylation of p53 enables its interaction with activated Smad2/3 to regulate target genes that are important for TGFβ cytostatic program [ 36].
Upon an increase in Ca2+ concentration during extracellular stimulation, CaM activation caused by Ca2+ binding enables its interaction with the CaM binding domain in CNA and removes the AI domain from the catalytic site, resulting in CN activation.
Here, we show that a switch from cyclic to unidirectional vesicular traffic of EGFR enables its interaction with spatially organized PTPs to suppress spontaneous auto-activation while allowing for ligand-induced signal propagation.
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This movement both deepens and widens the DRY-cavity, thus enabling its interaction with downstream G-proteins.
In this configuration, TGF-β is not active but requires cleavage or dissociation from LAP to enable its interaction with its cognate receptor complex, TβRII and TβRI [ 32].
RIPK1 is also recruited to form TNFR1 Complex I, and the cIAP proteins then conjugate K11- and K63-linked polyubiquitin chains to RIPK1 enabling its interaction with the IKK complex and activation of the NF κB signalling pathway; this in turn results in transcription of genes, which predominantly encode pro-survival (including FLIP and cIAP1) and pro-inflammatory proteins.
The interaction between SRPK1 and SRSF1 has been well documented; SRPK1 phosphorylates SRSF1 enabling its nuclear localisation and interaction with cellular pre-mRNA (Ghosh and Adams, 2011).
It is assumed that recycling of free b1 follows dissociation of B.b1, enabling its re-use in subsequent interactions and ballistic B* generation.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com