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The decapeptides described herein bind to and transfer isotope (32P) to cell lines derived from several colorectal carcinomas.
Previously, it had never been shown or suspected that this substrate, when labeled with a tumor-ablating material such as 32P, could bind to and transfer the radioisotope to a cell line after one to two hours of incubation.
Previously, we reported the discovery of nine different 32P-labeled decapeptides, each varying from one another by only one to three amino acids, that exhibited widely disparate abilities to bind to and transfer radioisotope permanently to proteins in cell lines established from a panel of colon adenocarcinomas.
The Suf system is composed of two subcomplexes: One is SufBCD that can bind to and transfer the [4Fe 4S] cluster to proteins.
We have previously demonstrated that high mobility group box 1 (HMGB1) can bind to and transfer LPS, consequently increasing LPS-induced TNF-α production in human peripheral blood mononuclear cells (PBMCs).
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PLTP is able to bind to and facilitate the transfer of several types of phospholipids, including phosphatidylcholine, phosphatidylethanolamine, and phosphatidylinositol, as well as sphingomyeline [13].
A potential future application that would be specific for Ga-gallium citrate arises from the fact that certain chemotherapeutic agents such as cisplatin also bind to transferrin and transfer to cancer cells through transferrin receptors.
We previously found that HMGB1 can bind to LPS and transfer it to CD14 thereby enhancing LPS-mediated inflammation, demonstrating that HMGB1 plays a role in LPS-mediated TNF-α production [ 14].
In a similar way, CD14 could be a "shuttle" that takes monomers of diacylglycerol ligands, which are bound to CD36, and transfer them to TLR2/TLR6.
This is due to the flexible coordination chemistry and redox reactivity of iron, which allow it to associate with proteins and bind to oxygen, transfer electrons or mediate catalytic reactions [ 1].
Thus, the main function of CD36 is to bind and transfer diacylglycerol ligands onto TLR2, in a CD14-dependent manner.
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