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The small GTPases coordinate functions of actin binding proteins at the cell cortex.
2) It interacts with 5 known subunits of MICOS and known MICOS binding proteins at the outer membrane.
Our approach provides an easy route to the characterization of UBA domain binding proteins at the level of the whole proteome, its application will unfold the important roles that p62's UBA domain plays.
This could lead to physico-chemical alterations of the membrane or create new ligands for carbohydrate binding proteins at the surface of the cells that would mediate the binding.
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The Notch intracellular domain translocates to the nucleus, binds to the DNA-binding protein RBP-J (recombinant recognition sequence binding protein at the Jκ site; also named CSL or CBF1), and activates Notch target genes such as Hes and Hey.
NICD is subsequently translocated to the nucleus where it interacts via its RAM domain with the DNA-binding protein recombinant recognition sequence binding protein at the Jκ site (RBP-J, also named CSL or CBF1).
Recombinant recognition sequence binding protein at the Jκ site (RBP-J, also named CSL or CBF1) is the central nuclear mediator of canonical Notch signaling whose activation leads to transcription of Notch target genes.
In both trypanosomatids the metal ion is acquired by endocytosis, following its binding to Tf which has a receptor (or binding protein) at the plasma membrane [14], [41], [42].
Recently we have shown that GNE interacts with α-actinin 1, an actin binding protein, at the M line and juxtaposed to the Z line in mouse muscle [32].
The recombinant protein MBP-DGAT1-His (rDGAT1) contained a MBP (maltose binding protein) at the amino terminus and 6 histidine residues (His) at the carboxyl terminus.
The recombinant protein MBP-DGAT1-His (rDGAT1) contained MBP (maltose binding protein) at the amino terminus and 6 histidine residues (His) at the carboxyl terminus.
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