Results 21 to 30 of about 3,108,795 (391)

Protein tyrosine kinase but not protein kinase C inhibition blocks receptor induced alveolar macrophage activation

open access: yesMediators of Inflammation, 1993
The selective enzyme inhibitors genistein and Ro 31-8220 were used to assess the importance of protein tyrosine kinase (PTK) and protein kinase C (PKC), respectively, in N-formyl-methionyl-leucyl-phenylalanine (FMLP) induced generation of superoxide ...
K. Pollock, M. T. Withnall
doaj   +1 more source

Role of Protein Kinase C in Eosinophil Function

open access: yesAllergology International, 2006
Protein kinase C (PKC) isoforms are being elucidated as an increasingly diverse family of enzymes involved in the downstream signal transduction and cell function in various types of cells.
Takafumi Yamaguchi   +3 more
doaj   +1 more source

Protein kinase C signaling and cell cycle regulation

open access: yesFrontiers in Immunology, 2013
A link between T cell proliferation and the protein kinase C (PKC) family of serine/threonine kinases has been recognized for about thirty years. However, despite the wealth of information on PKC-mediated control of T cell activation, understanding of ...
Adrian R Black, Jennifer D Black
doaj   +1 more source

Novel structural features of CDK inhibition revealed by an ab initio computational method combined with dynamic simulations [PDF]

open access: yesJournal of Medicinal Chemistry 49, 5141-5153 (2006), 2008
The rational development of specific inhibitors for the ~500 protein kinases encoded in the human genome is impeded by a poor understanding of the structural basis for the activity and selectivity of small molecules that compete for ATP binding. Combining classical dynamic simulations with a novel ab initio computational approach linear-scalable to ...
arxiv   +1 more source

Diacylglycerol kinase control of protein kinase C

open access: yesBiochemical Journal, 2019
Abstract The diacylglycerol kinases (DGK) are lipid kinases that transform diacylglycerol (DAG) into phosphatidic acid (PA) in a reaction that terminates DAG-based signals. DGK provide negative regulation to conventional and novel protein kinase C (PKC) enzymes, limiting local DAG availability in a tissue- and subcellular-restricted ...
Isabel Mérida   +3 more
openaire   +4 more sources

Protein Kinases as Drug Development Targets for Heart Disease Therapy

open access: yesPharmaceuticals, 2010
Protein kinases are intimately integrated in different signal transduction pathways for the regulation of cardiac function in both health and disease.
Alison L. Müller, Naranjan S. Dhalla
doaj   +1 more source

Giant Hub Src and Syk Tyrosine Kinase Thermodynamic Profiles Recapitulate Evolution [PDF]

open access: yes, 2016
Thermodynamic scaling theory, previously applied mainly to small proteins, here analyzes quantitative evolution of the titled functional network giant hub enzymes. The broad domain structure identified homologically is confirmed hydropathically using amino acid sequences only.
arxiv   +1 more source

Protein kinase C and cancer: what we know and what we do not

open access: yesOncogene, 2014
Since their discovery in the late 1970s, protein kinase C (PKC) isozymes represent one of the most extensively studied signaling kinases. PKCs signal through multiple pathways and control the expression of genes relevant for cell cycle progression ...
Rachana Garg   +5 more
semanticscholar   +1 more source

Intramolecular C2 Domain-Mediated Autoinhibition of Protein Kinase C βII

open access: yesCell Reports, 2015
The signaling output of protein kinase C (PKC) is exquisitely controlled, with its disruption resulting in pathophysiologies. Identifying the structural basis for autoinhibition is central to developing effective therapies for cancer, where PKC activity ...
Corina E. Antal   +4 more
doaj   +1 more source

Phosphorylation of protein kinase C by casein kinase‐1 [PDF]

open access: yesFEBS Letters, 1989
Because phosphorylation of protein kinase C (PKC) may provide a mechanism for regulation of this enzyme, we have examined the ability of two other kinases to phosphorylate PKC. Our results show that casein kinase 1 (CK‐1), but not casein kinase 2 (CK‐2), can phosphorylate PKC in the absence of Ca2+ and phospholipids.
Michael J. Weber   +4 more
openaire   +3 more sources

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