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We found that SAP130 binds to Cul1 and that overexpression of SAP130 inhibits binding of the adaptor and substrate receptor module Skp1-Skp2 to Cul1.
This FAK-Src complex facilitates SH3-mediated binding of the adaptor protein p130Cas (breast cancer anti-estrogen resistance protein 1) to FAK and its subsequent phosphorylation.
Interaction between MDP and CARD15 leads to activation of the nuclear factor κB (NFκB) by binding of the adaptor protein RIP2 to CARD15 via caspase recruitment domains (CARDs) on both proteins [5], [6].
The interaction between Nrg3 and ErbB4 activates epidermal growth factor-like signal transduction via binding of the adaptor protein Growth factor receptor bound protein 2 (Grb2), which peaks at the initiation of regeneration.
After binding of the adaptor protein FADD (Fas-associated death domain protein) to the death receptors via the death-domains (DD), the death effector domain (DED) of FADD recruits procaspase-8/procaspase-10 or cFLIP (cellular FLICE-inhibitory protein).
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Domain IV also contains two proline rich domains (prm), which were found capable of binding to the adaptor proteins Crk and Grb2 [ 10]; the latter was also shown to co-immunoprecipitate with the c-Met receptor [ 42].
A variety of exogenous and endogenous ligands can activate TLRs by binding the extracellular domain: This activation induces dimerization of the receptor and binding of either the adaptor protein myeloid differentiation factor 88 (MyD88) or the TIR domain-containing adaptor inducing interferon-β (TRIF -dependent paTRIF -dependentocess culminates in interferon-regulating factor 3 (IRF3) activation.
As a consequence, a high local concentration of the intracellular death domains might be formed, leading to more efficient activation of caspase 8 after binding to the adaptor molecule FADD (Holler et al, 2003).
Moreover, mechanical forces are coupled to electrical signals through multiple binding partners of the adaptor proteins, posttranslational modifications (e.g., phosphorylation), and transport and assembly of channels [ 121].
Short NLS sequences engage only one of the two binding pockets of the adaptor Impα, whereas bipartite ones interact simultaneously with both (Fontes et al, 2000, 2003; Kosugi et al, 2009).
Further, our work suggests that initial binding of the 'bridging adaptor' proteins may contribute to formation of an additional surface for secondary adaptor binding.
More suggestions(16)
binding of the sera
binding of the outbreak
binding of the myosin
binding of the peptide
binding of the fusion
binding of the radiolabel
binding of the radioligand
binding of the heterodimer
binding of the target
binding of the ligand
binding of the karma
binding of the initiator
binding of the nation
binding of the protein
binding of the flavonoid
binding of the rabbit
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Justyna Jupowicz-Kozak
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