Results 21 to 30 of about 1,883,043 (318)

Malaria protein kinase CK2 (PfCK2) shows novel mechanisms of regulation [PDF]

, 2013
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.
Mahmood Alam, Schmid, Ralf, Alam, Mahmood M, Cullis, Paul M, Andrew B. Tobin (7589429), Lev Solyakov (122244), Solyakov, Lev, Andrew R Bottrill, Andrew B Tobin, G. Burley (7653734), Graciotti, Michele, Burley, Glenn, Lev Solyakov, Tobin, Andrew B., Bottrill, Andrew R, Mahmood Alam (540985), Andrew R. Bottrill, Andrew B. Tobin, Doerig, Christian D, Alam, Mahmood, Paul Cullis, Bottrill, Andrew, Paul Cullis (540988), Doerig, Christian, Michele Graciotti, Ralf Schmid (45614), Michele Graciotti (540984), Burley, Glenn Ashley, C. Doerig (7646465), Glenn Burley, Andrew R. Bottrill (540987), Tobin, Andrew, Christian Doerig, Bottrill, Andrew R., Tobin, Andrew B, Cullis, Paul, Ralf Schmid   +36 more
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Historical data on cardiovascular health in Surinamese men

BMC Research Notes, 2018
Objectives Cardiovascular risk factor burden was recently reported to be high in the Caribbean country Suriname. However, historical data for comparison were lacking.
Lizzy M. Brewster, Jules Brewster
doaj   +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]

, 2000
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, Ostrowski, M C, Hartman, M, Schaffner, A E, Smith, James L., Hume, D A, Smith, J L, Ostrowski, Michael C., Wei, G, Hofmeister, Joseph K., Hofmeister, J K, Schaffner, Alicia E., Wei, Guo, Hume, David A., Hartman, Matthew, Hartman, Matthew Hartman, Forsthoefel, D   +16 more
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Mediation of PKM2-dependent glycolytic and non-glycolytic pathways by ENO2 in head and neck cancer development

Journal of Experimental & Clinical Cancer Research, 2023
Background Enolase 2 (ENO2) is a crucial glycolytic enzyme in cancer metabolic process and acts as a “moonlighting” protein to play various functions in diverse cellular processes unrelated to glycolysis.
Lixia Gao, Fan Yang, Dianyong Tang, Zhigang Xu, Yan Tang, Donglin Yang, Deping Sun, Zhongzhu Chen, Yong Teng   +8 more
doaj   +1 more source

Mechanism of activation of NDR protein kinase by the HMOB1 protein [PDF]

, 2005
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

Identification of autophosphorylation sites in eukaryotic elongation factor-2 kinase [PDF]

, 2012
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, Proud, Christopher G, Proud, C., Wang, Xuemin, Rider, M., Rider, Mark H, Pyr Dit Ruys, S., Vertommen, D., Rider, Mark, Pyr Dit Ruys, Sébastien, Herinckx, Gaëtan, Vertommen, Didier, Herinckx, G., Smith, Ewan M, Wang, X., Smith, E., Hussain, N.   +16 more
core   +1 more source

Crystal structure of methyl 2-(4-(3-iodopyrazolo[1,5-a]pyrimidin-6-yl)phenyl)acetate, C15H12IN3O2

Zeitschrift für Kristallographie - New Crystal Structures, 2020
C15H12IN3O2, triclinic, P1̄ (no. 2), a = 4.511(2) Å, b = 11.891(6) Å, c = 14.557(7) Å, α = 109.709(9)°, β = 96.971(9)°, γ = 97.054(9)°, V = 718.4(6) Å3, Z = 2, Rgt(F) = 0.0449, wRref(F2) = 0.1052, T = 293(2) K.
Fang Bo, Jiang Fang Fang, Meng Jiang Ping   +2 more
doaj   +1 more source

Deep evolutionary conservation of an intramolecular protein kinase activation mechanism [PDF]

, 2012
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, Aman Singh (191216), Cleghon, V., Nathan Luebbering (191210), Sibbet Gary, Jingfen Han, Luebbering Nathan, Nathan Luebbering, Michael A J Ferguson, Singh, A., Aman Singh, Ferguson, M.A.J., Ferguson Michael A. J., Hong, W., Diego Miranda-Saavedra (36622), Michael A. J. Ferguson (166662), Jingfen Han, Han, J., Gary Sibbet (191221), Vaughn Cleghon (191224), Miranda-Saavedra Diego, Sibbet, G., Ferguson, M.A.J.; id_orcid, Han Jingfen, Miranda-Saavedra, D., Gary Sibbet, Luebbering, N., Diego Miranda-Saavedra, Michael A. J. Ferguson, Vaughn Cleghon, Singh Aman, Jingfen Han (191204)   +31 more
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Regulation of protein kinase B (PKB/Akt) by DNA-dependent protein kinase (DNA-PK) under physiological conditions [PDF]

, 2010
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

Kinases and Cancer [PDF]

Cancers, 2018
Protein kinases are a large family of enzymes catalyzing protein phosphorylation. The human genome contains 518 protein kinase genes, 478 of which belong to the classical protein kinase family and 40 are atypical protein kinases [...]
Jonas Cicenas, Egle Zalyte, Amos Bairoch, Pascale Gaudet   +3 more
openaire   +5 more sources