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We identified β1 and β3 integrins as the principal binding partners for tTG on the cell surface, and showed a major role of the integrin-tTG complexes in cell-ECM interactions and outside-in signaling [20], [21], [55].
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While low levels of αvβ3 integrin in the NIH3T3-tTG fibroblasts [55], [56] precluded analysis of its intracellular interaction with tTG, we identified the internalized α5β1 integrin as a key binding partner for tTG inside the PNRC vesicles and showed that de novo synthesized tTG is externalized as a complex with this integrin via the long recycling route.
To identify the binding partners for secreted tTG in these cellular fractions, cell surface-bound Fab fragment of mAb 4G3 [21] was used to pull-down externalized tTG together with associated proteins (Fig. 5F).
Although fibronectin and heparan sulphate proteoglycans, two extracellular binding partners of tTG, and its own transamidating activity, were all proposed to affect its secretion [25], [32], [33], they likely impact the retention of tTG on the surface rather than its outbound trafficking inside the cell.
Oxidized derivatives of cholesterol with biological activity, for example, as binding partners for nuclear receptors.
Identifying binding partners for ALK1 will help to understand its cellular function.
We used yeast two-hybrid analysis to identify potential protein binding partners for human TTP (hTTP).
These two proteins may represent novel binding partners for Tspan9.
Electrostatic interactions can facilitate macromolecular recognition by enhancing the collision frequency of the binding partners and by orienting the binding partners for subsequent short-range interactions.
At least 20 proteins (besides G-alpha subunits) have now been identified as direct binding partners for RGS proteins, and additional binding partners remain to be found [ 4].
The yeast two-hybrid method was used to identify potential binding partners for psoriasin.
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