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PACAP (both forms) bind to three different receptors: PAC1, which specifically interacts with PACAP, and VPAC1 and VPAC2, which bind PACAP and VIP with approximately equal affinity [67].
Available literature indicate that omeprazole gets converted to its sulfenic acid and sulfenamide derivative in acidic environment and these forms bind to the Cys 813 sulfhydral group by making a covalent disulfide linkage [18, 19].
Both forms bind to RANK, the receptor of RANKL.
When compared in a phage display assay, the two PR forms bind to distinct subgroups of peptides.
Thus, both SI and SA forms bind to site I in the subdomain IIA of BSA.
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Using principal component analysis and generalized masked Delaunay analysis, an examination of the conformational space of TcdB in its apo form as well as forms bound to the peptides and UDP-Glucose was performed.
We found that, regardless of whether cell lysates containing exogenous or endogenous AID were examined, one of two mouse AID forms bound to agarose alone.
NFI-C (wild type or mutant forms) bound to the oligonucleotides was detected by SDS-PAGE and immunoblotting using the mouse monoclonal anti-NFI-C antibody.
The TGF-β protein is secreted into the extracellular matrix (ECM) in its inactive form bound to latent TGF-β binding proteins (LTBPs) [51].
TGF-β1 is secreted in an inactive form bound to a latency associated peptide (LAP), but binding of αvβ6 to the LAP part of the LAP-TGF-β1 complex, allows TGF-β1 to interact with its receptor [ 20].
In our DNA binding assays we also found that the ZF - KTS form bound to most WT1 sites in the WT1 promoter, while the ZF + KTS isoform only bound to sites between nucleotides -212 and -21.
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