Malaria protein kinase CK2 (PfCK2) shows novel mechanisms of regulation [PDF]
Casein kinase 2 (protein kinase CK2) is a conserved eukaryotic serine/theronine kinase with multiple substrates and roles in the regulation of cellular processes such as cellular stress, cell proliferation and apoptosis.
Schmid, Ralf +8 more
core +3 more sources
Structural instability in an autophosphorylating kinase switch [PDF]
We analyse a simple kinase model that exhibits bistability when there is no protein turnover, and show analytically that the property of being bistable is not necessarily conserved when degradation and synthesis of the kinase are taken into ...
Grinfeld, M., Webb, S.D.
core +4 more sources
Phosphoinositide-dependent protein kinase-1 (PDK1)-independent activation of the protein kinase C substrate, protein kinase D [PDF]
Phosphoinoisitide dependent kinase l (PDK1) is proposed to phosphorylate a key threonine residue within the catalytic domain of the protein kinase C (PKC) superfamily that controls the stability and catalytic competence of these kinases.
Kelly, April P. +3 more
core +1 more source
Ets-2 is a target for an Akt (protein kinase B)/Jun N-terminal kinase signaling pathway in macrophages of motheaten-viable mutant mice [PDF]
The transcription factor ets-2 was phosphorylated at residue threonine 72 in a colony-stimulating factor 1 (CSF-1)- and mitogen-activated protein kinase-independent manner in macrophages isolated from motheaten-viable (me-v) mice.
Forsthoefel, David +16 more
core +1 more source
Mechanism of activation of NDR protein kinase by the HMOB1 protein [PDF]
Serine/threonine kinases of the nuclear Dbf2-related (NDR) family are highly conserved throughout the eukaryotic world. Members of this kinase family are implicated in various aspects of the regulation of cell division and cell morphology. It has been
Bichsel, Samuel J.
core +1 more source
Deep evolutionary conservation of an intramolecular protein kinase activation mechanism [PDF]
DYRK-family kinases employ an intramolecular mechanism to autophosphorylate a critical tyrosine residue in the activation loop. Once phosphorylated, DYRKs lose tyrosine kinase activity and function as serine/threonine kinases.
Cleghon Vaughn +31 more
core +1 more source
Regulation of protein kinase B (PKB/Akt) by DNA-dependent protein kinase (DNA-PK) under physiological conditions [PDF]
The serine/threonine protein kinase B (PKB/Akt) is a downstream effector of phosphatidylinositol 3-kinase (PI3K) and a major regulator of a variety of cellular processes, including metabolism, transcription, survival, proliferation, and growth.
Sürücü, Banu
core +1 more source
Modulation of kanamycin B and kanamycin A biosynthesis in Streptomyces kanamyceticus via metabolic engineering. [PDF]
Both kanamycin A and kanamycin B, antibiotic components produced by Streptomyces kanamyceticus, have medical value. Two different pathways for kanamycin biosynthesis have been reported by two research groups. In this study, to obtain an optimal kanamycin
Zheng Wu (344022) +9 more
core +1 more source
Identification of autophosphorylation sites in eukaryotic elongation factor-2 kinase [PDF]
eEF2K [eEF2 (eukaryotic elongation factor 2) kinase] phosphorylates and inactivates the translation elongation factor eEF2. eEF2K is not a member of the main eukaryotic protein kinase superfamily, but instead belongs to a small group of so-called ...
Hussain, Nusrat +16 more
core +1 more source
Oncogenic RET Kinase domain mutations perturb the autophosphorylation trajectory by enhancing substrate presentation in trans [PDF]
To decipher the molecular basis for RET kinase activation and oncogenic deregulation, we defined the temporal sequence of RET autophosphorylation by label-free quantitative mass spectrometry.
Martínez-Torres, R.J. +8 more
core +1 more source

