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The ubiquitination process requires the product of the von Hippel-Lindau tumor suppressor gene (VHL), which functions as a substrate recognition component of an E3 ubiquitin ligase complex [5], [6], [7], [8].
We identify SOCS6 as a substrate recognition factor targeting YAP for degradation.
As a substrate recognition protein of the SCF complex, Fbs1 binding leads to polyubiquitination and finally degradation of its substrates.
S-phase kinase-associated protein 2 (SKP2) is an F-box protein that functions as a substrate recognition unit of the Skp1-Clu1-F-box ubiquitin ligase complex.
These effects are consistent with the most-studied function of VHL as a substrate recognition unit of an ubiquitin ligase complex that targets HIFα for proteasomal degradation (Maxwell et al, 1999).
Recent studies have identified ERLIN2 both as a novel component of lipid raft domains in the ER membrane and as a substrate recognition factor during ERAD of activated inositol triphosphate receptors (IP3R) as well as other substrates [ 34- 36].
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In association with a RING finger E3 and a substrate recognition protein such as F-box proteins, they form Cullin-RING-Ligases (CRLs).
We called these proteins 'substrate receptors' that can act as a substrate-recognition subunit of E3 ligase complex or as E3 ligase alone.
This inhibitor was found potent and considerably selective to DAPK1 as it made direct contact with the ATP binding sites as well as substrate recognition motifs: Gly-Glu-Leu (GEL) and Pro-Glu-Asn (PEN).
The disintegrin domain can selectively interact with different integrins [ 4]; together with the cysteine-rich domain, it may modulate cell-cell and cell-matrix adhesion [ 4- 6], as well as substrate recognition by the metalloproteinase domain [ 7, 8].
The TH-mediated control is highly specific with respect to protein protein interactions, as well as on acyl substrate recognition.
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