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Methods in Molecular Biology (Clifton, N.J.)|September 3, 2010
A "molecular evolution" approach for isolation of intrinsically active (MEK-independent) MAP kinasesVered Levin-Salomon, Oded Livnah, David Engelberg
Biochemistry|February 13, 2009
p38alpha is active in vitro and in vivo when monophosphorylated at threonine 180Nadav Askari, Jonah Beenstock, Oded Livnah, et al.
The Journal of Biological Chemistry|May 15, 2013
DEF pocket in p38α facilitates substrate selectivity and mediates autophosphorylationNetanel Tzarum, Nadav Komornik, Dorin Ben Chetrit, et al.
The Journal of Biological Chemistry|October 3, 2008
Isolation of intrinsically active (MEK-independent) variants of the ERK family of mitogen-activated protein (MAP) kinasesVered Levin-Salomon, Konstantin Kogan, Natalie G Ahn, et al.
Plos One|September 18, 2012
Osmostress induces autophosphorylation of Hog1 via a C-terminal regulatory region that is conserved in p38αInbal Maayan, Jonah Beenstock, Irit Marbach, et al.
Bioscience Reports|March 19, 2016
Tighter αC-helix-αL16-helix interactions seem to make p38α less prone to activation by autophosphorylation than Hog1Masha Tesker, Sadiduddin Edbe Selamat, Jonah Beenstock, et al.
The Biochemical Journal|September 10, 2008
When expressed in yeast, mammalian mitogen-activated protein kinases lose proper regulation and become spontaneously phosphorylatedVered Levin-Salomon, Inbal Maayan, Liat Avrahami-Moyal, et al.
The Journal of Biological Chemistry|July 10, 2014
The p38β mitogen-activated protein kinase possesses an intrinsic autophosphorylation activity, generated by a short region composed of the α-G helix and MAPK insertJonah Beenstock, Sheer Ben-Yehuda, Dganit Melamed, et al.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|April 13, 2010
Challenging semi-bootstrapping molecular-replacement strategy reveals intriguing crystal packing of rhizavidinAmit Meir, Oded Livnah
The Journal of Biological Chemistry|July 20, 2023
A conserved arginine within the αC-helix of Erk1/2 is a latch of autoactivation and of oncogenic capabilitiesNadine Soudah, Alexey Baskin, Karin Smorodinsky-Atias, et al.
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