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Jonah Beenstock

Showing results (1-10 of 17) with videos related to

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Nucleic Acids Research|October 6, 2021
The structural and functional workings of KEOPSJonah Beenstock, Frank Sicheri
Trends in Biochemical Sciences|September 6, 2016
How Do Protein Kinases Take a Selfie (Autophosphorylate)?Jonah Beenstock, Navit Mooshayef, David Engelberg
Methods in Enzymology|May 7, 2022
A suite of in vitro and in vivo assays for monitoring the activity of the pseudokinase Bud32Jonah Beenstock, Samara Mishelle Ona, Frank Sicheri
Biochemistry|February 13, 2009
p38alpha is active in vitro and in vivo when monophosphorylated at threonine 180Nadav Askari, Jonah Beenstock, Oded Livnah, et al.
International Journal of Molecular Sciences|August 12, 2023
Differential Modulation of the Phosphoproteome by the MAP Kinases Isoforms p38α and p38βDganit Melamed Kadosh, Jonah Beenstock, David Engelberg, 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.
Structure (London, England : 1993)|May 14, 2021
Bipartite binding of the N terminus of Skp2 to cyclin ASusan Kelso, Stephen Orlicky, Jonah Beenstock, 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.
Molecular and Cellular Biology|March 16, 2016
p38β Mitogen-Activated Protein Kinase Modulates Its Own Basal Activity by Autophosphorylation of the Activating Residue Thr180 and the Inhibitory Residues Thr241 and Ser261Jonah Beenstock, Dganit Melamed, Navit Mooshayef, et al.
Pageof 2

Showing results (1-10 of 17) with videos related to

Sort By:
Pageof 2
Nucleic Acids Research|October 6, 2021
The structural and functional workings of KEOPSJonah Beenstock, Frank Sicheri
Trends in Biochemical Sciences|September 6, 2016
How Do Protein Kinases Take a Selfie (Autophosphorylate)?Jonah Beenstock, Navit Mooshayef, David Engelberg
Methods in Enzymology|May 7, 2022
A suite of in vitro and in vivo assays for monitoring the activity of the pseudokinase Bud32Jonah Beenstock, Samara Mishelle Ona, Frank Sicheri
Biochemistry|February 13, 2009
p38alpha is active in vitro and in vivo when monophosphorylated at threonine 180Nadav Askari, Jonah Beenstock, Oded Livnah, et al.
International Journal of Molecular Sciences|August 12, 2023
Differential Modulation of the Phosphoproteome by the MAP Kinases Isoforms p38α and p38βDganit Melamed Kadosh, Jonah Beenstock, David Engelberg, 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.
Structure (London, England : 1993)|May 14, 2021
Bipartite binding of the N terminus of Skp2 to cyclin ASusan Kelso, Stephen Orlicky, Jonah Beenstock, 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.
Molecular and Cellular Biology|March 16, 2016
p38β Mitogen-Activated Protein Kinase Modulates Its Own Basal Activity by Autophosphorylation of the Activating Residue Thr180 and the Inhibitory Residues Thr241 and Ser261Jonah Beenstock, Dganit Melamed, Navit Mooshayef, et al.
Pageof 2