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The association of ILK with the integrins α2β1 and αIIbβ3 suggest that ILK may have a role in platelet function.
We report here that ILK is present in the liver and localizes at cell-matrix adhesions of cultured hepatocytes.
We further showed that ILK regulates expression of the Wnt receptor frizzled-1 (Fzd1), suggesting the presence of a positive feedback loop between Wnt3a, ILK, and Fzd1.
Our results show that ILK and cell-matrix adhesion proteins play an important role in the process of matrix-induced hepatocyte differentiation.
The findings that ILK phosphorylated both MYPT1 and myosin and the association of ILK with MP suggest that ILK may influence cytoskeletal structure or function.
It has been shown that ILK is expressed preferentially in cardiac and skeletal muscles.
The possibility that ILK may also phosphorylate and regulate MP was investigated.
Together, these results argue that ILK is not a pseudokinase, but an authentic protein kinase.
These data demonstrate that ILK directly phosphorylates physiologically relevant substrates in vitro.
Together, these results suggest that ILK is a more efficient kinase in the presence of manganese.
Hence, this work suggested that ILK is tightly associated with differentiation but not with dedifferentiation and/or carcinogenesis.
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CEO of Professional Science Editing for Scientists @ prosciediting.com