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The Journal of Biological Chemistry|July 31, 2004
Active mutants of the human p38alpha mitogen-activated protein kinaseRon Diskin, Nadav Askari, Ricardo Capone, et al.
Cell Host & Microbe|April 14, 2022
What has been will be again-The story of viral pathogensNetanel Tzarum
The Journal of Biological Chemistry|November 8, 2006
Hyperactive variants of p38alpha induce, whereas hyperactive variants of p38gamma suppress, activating protein 1-mediated transcriptionNadav Askari, Ron Diskin, Michal Avitzour, et al.
Molecular and Cellular Endocrinology|May 5, 2006
MAP-quest: could we produce constitutively active variants of MAP kinases?Nadav Askari, Ron Diskin, Michal Avitzour, 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.
The FEBS Journal|January 24, 2007
Intrinsically active variants of all human p38 isoformsMichal Avitzour, Ron Diskin, Bilha Raboy, 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.
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