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Recognition and binding to specific lipids play a central role in targeting reactions, but it remains difficult to analyze the molecular features of such protein-lipid interactions.
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This model could explain the accumulation of DivIVA in a ring-like formation at the site of cell division, without the need for either intrinsic curvature of the protein, binding to specific lipid molecules or the presence of other proteins.
Differences in localization of A-RAF and AR149 can be explained by the existence of two lipid-binding domains in the structure of A-RAF, each domain binding to specific sets of lipids.
Annexins are a family of ubiquitous and Ca2+-dependent membrane-binding proteins whose functions depend on their ability to attach to specific lipid microdomains.
For the PH domain family, binding often occurs in two steps, an initial association is driven by non-specific electrostatic interactions followed by specific binding to anionic lipids (Hurley and Misra, 2000).
They were also named non-specific LTPs (nsLTPs) due to the character of non-specific binding to different lipids.
The overriding property of any StART-like domain is specific binding to a lipid or other hydrophobic ligand.
Individual fatty acid binding proteins show specific lipid-binding profiles and distinct patterns of tissue and cell-type specific expression (Veerkamp et al, 1999; Richieri et al, 2000; Duplus and Forest, 2002).
Thus, v-vesicle clustering is not caused by homo-oligomerization of α-Syn, but requires specific binding of α-Syn to synaptobrevin-2, as well as binding to anionic lipids.
The clustering effect is dependent on specific binding to both anionic lipid membranes and synaptobrevin-2 as revealed by deletion and mutagenesis studies, including the Parkinson's disease mutant A30P that disrupts lipid binding.
(A ) Lam4S2 binding to cellular lipids (see Figure 2A ).
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