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Jose M. Lizcano

Researcher at Autonomous University of Barcelona

Publications -  79
Citations -  5903

Jose M. Lizcano is an academic researcher from Autonomous University of Barcelona. The author has contributed to research in topics: Kinase & Amine oxidase. The author has an hindex of 30, co-authored 73 publications receiving 4590 citations. Previous affiliations of Jose M. Lizcano include University of Dundee & University of Barcelona.

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LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1

Jose M. Lizcano, +10 more
- 25 Feb 2004 - 
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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Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Daniel J. Klionsky, +2983 more
- 08 Feb 2021 - 
TL;DR: In this article, the authors present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes.
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The insulin signalling pathway

Jose M. Lizcano, +1 more
- 02 Apr 2002 - 
TL;DR: Although the understanding of the insulin signal transduction pathway is far from being complete, current knowledge of this pathway provides a framework for the development of novel drugs to treat diabetes and it is possible that drugs that mimic the effect that insulin has on its signalling pathway are orally effective.
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Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155.

Jose M. Lizcano, +2 more
- 15 Jul 2000 - 
TL;DR: Ser(155) is identified as a third phosphorylation site on BAD and is the only residue in BAD that becomes phosphorylated when cells are exposed to cAMP-elevating agents, and prevents it from binding to Bcl-X(L) and promotes its interaction with 14-3-3 proteins.
Journal ArticleDOI

Phosphorylation of the Protein Kinase Mutated in Peutz-Jeghers Cancer Syndrome, LKB1/STK11, at Ser431 by p90RSK and cAMP-dependent Protein Kinase, but Not Its Farnesylation at Cys433, Is Essential for LKB1 to Suppress Cell Growth

Gopal P. Sapkota, +8 more
- 01 Jun 2001 - 
TL;DR: It is demonstrated that stimulation of Rat-2 or embryonic stem cells with activators of ERK1/2 or of cAMP-dependent protein kinase induced phosphorylation of endogenously expressed LKB1 at Ser431, and that full-length L KB1 expressed in 293 cells was prenylated by addition of a farnesyl group to Cys433.