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Tomi P. Mäkelä

Researcher at University of Helsinki

Publications -  134
Citations -  12972

Tomi P. Mäkelä is an academic researcher from University of Helsinki. The author has contributed to research in topics: Cyclin-dependent kinase & Kinase. The author has an hindex of 54, co-authored 130 publications receiving 12390 citations. Previous affiliations of Tomi P. Mäkelä include Helsinki University Central Hospital & Nagoya University.

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Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β are upstream kinases in the AMP-activated protein kinase cascade

TL;DR: These results provide the first description of a physiological substrate for the LKB1 tumor suppressor and suggest that it functions as an upstream regulator of AMPK.
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LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1

TL;DR: The results show that LKB1 functions as a master upstream protein kinase, regulating AMPK‐related kinases as well as AMPK, and may mediate the physiological effects of L KB1, including its tumour suppressor function.
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Lymphatic endothelial reprogramming of vascular endothelial cells by the Prox-1 homeobox transcription factor

TL;DR: It is found that isolated human primary lymphatic and blood vascular endothelial cells show interesting differences in gene expression relevant for their distinct functions in vivo, and overexpression of the homeobox transcription factor Prox‐1 in the BECs is suggested to act as a cell proliferation inducer and a fate determination factor for the LECs.
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FGFR-4, a novel acidic fibroblast growth factor receptor with a distinct expression pattern.

TL;DR: The results suggest that FGFR‐4 along with other fibroblast growth factor receptors performs cell lineage and tissue‐specific functions.
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A novel endothelial cell surface receptor tyrosine kinase with extracellular epidermal growth factor homology domains.

TL;DR: The cloning and characterization of tie is described, a novel type of human endothelial cell surface receptor tyrosine kinase that may have evolved for multiple protein-protein interactions, possibly including cell adhesion to the vascular endothelium.