BIOMAT Database Logo BIOMAT Database Logo

Lipid activation of protein kinase C. 1991

R M Bell, and D J Burns
Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D011493 Protein Kinase C An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters. Calcium Phospholipid-Dependent Protein Kinase,Calcium-Activated Phospholipid-Dependent Kinase,PKC Serine-Threonine Kinase,Phospholipid-Sensitive Calcium-Dependent Protein Kinase,Protein Kinase M,Calcium Activated Phospholipid Dependent Kinase,Calcium Phospholipid Dependent Protein Kinase,PKC Serine Threonine Kinase,Phospholipid Sensitive Calcium Dependent Protein Kinase,Phospholipid-Dependent Kinase, Calcium-Activated,Serine-Threonine Kinase, PKC
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D050356 Lipid Metabolism Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS. Metabolism, Lipid

Related Publications

R M Bell, and D J Burns
Activation of protein kinase C in lipid monolayers.
January 1991, The Journal of biological chemistry,
R M Bell, and D J Burns
Protein kinase C activation and lipid peroxidation by doxorubicin analogues.
August 1989, Tumori,
R M Bell, and D J Burns
Activation of protein kinase C from B lymphocytes by lipid A.
April 1988, Biochemical and biophysical research communications,
R M Bell, and D J Burns
Lipid-dependent activation of protein kinase C-alpha by normal alcohols.
November 1999, The Journal of biological chemistry,
R M Bell, and D J Burns
Activation of rat brain protein kinase C by lipid oxidation products.
September 1988, Biochemical and biophysical research communications,
R M Bell, and D J Burns
[Protein kinase C activation].
November 2010, Nihon rinsho. Japanese journal of clinical medicine,
R M Bell, and D J Burns
Lipid activators of protein kinase C.
January 1990, Life sciences,
R M Bell, and D J Burns
Analyzing protein kinase C activation.
January 2002, Methods in enzymology,
R M Bell, and D J Burns
Lipid mediators and protein kinase C activation for the intracellular signaling network.
June 1994, Journal of biochemistry,
R M Bell, and D J Burns
Calcium- and lipid-independent protein kinase C autophosphorylation. Activation by low pH.
August 1989, The Journal of biological chemistry,
Copied contents to your clipboard!