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The terminal transcription factors (TFs) of these pathways bind to specific regulatory regions and modulate gene expression through interactions with co-activators and co-repressors [ 2].
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Furin-like convertases can be localized to the TGN, within granules of the regulated secretory pathway, bound to the cell surface or potentially in the extracellular matrix [ 15].
In the canonical pathway Wnts bind to the extracellular domain of Frizzled receptors [3], [4] and through canonical β-catenin or Ca2+/PKC dependent pathways activates Wnt target genes [5].
Moreover, TCF proteins, which function in the canonical Wnt signaling pathway, bind to the DPAGT1 promoter in vivo (Sengupta et al. 2010).
The first traces of IFNβ formed by the TLR3 pathway bind to the Type1 interferon receptor (IFNAR), activating the JAK (Janus kinase) family members JAK1 and TYK2 (tyrosine kinase 2), which phosphorylate STAT1 (signal transducer and activator of transcription 1) and STAT2 [ 11].
In the monomeric pathway monomers bind to the operator site and then recruit another monomer to form a dimer directly on the DNA.
Whilst many of the repair pathway components bind to different domains on the scaffolding proteins, three DNA-end modification proteins PNKP, aprataxin and APLF potentially compete for the same binding sites on XRCC1 and XRCC4.
The ErbB signalling pathway is actually composed of several transmembrane receptors able to trigger several signalling pathways when they bind to an extracellular growth factor molecule.
In the canonical signal transduction pathway Wnt proteins bind to the extracellular domain of Frizzled receptors and consequently recruit Dishevelled (Dsh) to the cell membrane.
In a canonical BMP signaling pathway, dimeric ligands bind to receptors and form a heterotetrameric complex that consists of two Type I and two Type II receptors.
In the canonical Wnt pathway, Wnt proteins bind to a family of Frizzled receptors in a complex with the low-density lipoprotein receptor-related proteins 5 and 6 (LRP5/6) [ 49].
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