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The responsiveness of KG-1 cells to IL-18 (in absence of IL-12) is partly due to constitutive expression of both chains of the IL-18R [73], [73], whereas primary NK and T cells require IL-12 stimulation for expression of the binding chain of the IL-18R [74] [77]]–[74] [77]
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IL-1β (as well as IL-1α) binds to the transmembrane ligand-binding chain of the IL-1 receptor (termed IL-1R type I) as well as to the IL-1 receptor type II (IL-1RII), which lacks a cytoplasmic domain and functions as a decoy receptor for IL-1β [ 10, 11].
We engineered an affinity-enhanced variant of the ligand-binding chain of the IFNgamma receptor IFNgammaR1, which enabled us to determine the crystal structure of the complete hexameric (2 2 2) IFNgamma-IFNgammaR1-IFNgammaR2 signalling complex at 3.25A resolution.
IFNGR1, encoding the ligand-binding chain of the receptor for interferon gamma, IFNγR1, is one such gene because interferon gamma is involved in the pathogenesis of the disease.
IFNGR1-rs1327474 polymorphism (NM_000416.2 c.-611G>A) is located near the 5′-end of the IFNGR1 gene [ 17] that codes for the ligand-binding chain of the interferon gamma receptor 1 [ 18].
First the specificity for SP-A, and not for SP-D, and the dependency of the assay on the presence of a complete binding chain consisting of the beads coupled with the anti-goat antibody, and the anti-human-SP-A antibody was shown.
The crystal structure of the IgE Fc FcεRI complex clarified how a 1 1 complex between the antibody and receptor is formed, with the receptor binding each chain of the antibody Fc dimer.
AMPK phosphorylates the cargo-binding light chain of the Kif5 motor protein, leading to dissociation of the phosphatidylinositol 3-Kinase (PI3K) from the motor complex.
The strong preference for hydrophobic residues at I571 as well as V575 in active variants indicates that a hydrophobic surface promotes binding of the polypeptide chain of the acceptor protein.
In tumor cells, cathepsin B redistributes into exocytic vesicles at the cell periphery leading to its secretion and association with the tumor cell surface by binding to the light chain of the annexin II heterotetramer [ 8, 9].
The IFNγR consists of the ligand-binding chain IFNγR1 and the signal-transducing chain IFNγR2.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com