L M Keranen
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Explore the profile of L M Keranen including associated specialties, affiliations and a list of published articles.
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8
Citations
321
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Recent Articles
1.
Keranen L, Newton A
J Biol Chem
. 1997 Nov;
272(41):25959-67.
PMID: 9325330
The regulation of conventional protein kinase Cs by Ca2+ was examined by determining how this cation affects the enzyme's 1) membrane binding and catalytic function and 2) conformation. In the...
2.
Keranen L, Dutil E, Newton A
Curr Biol
. 1995 Dec;
5(12):1394-1403.
PMID: 8749392
Background: Protein kinase Cs are a family of enzymes that transduce the plethora of signals promoting lipid hydrolysis. Here, we show that protein kinase C must first be processed by...
3.
Conrad R, Keranen L, Ellington A, Newton A
J Biol Chem
. 1994 Dec;
269(51):32051-4.
PMID: 7528207
In vitro selection technology has been used to purify RNA aptamers from a random sequence pool that can bind to, and specifically inhibit, protein kinase C beta II. Two of...
4.
Dutil E, Keranen L, DePaoli-Roach A, Newton A
J Biol Chem
. 1994 Nov;
269(47):29359-62.
PMID: 7961910
Dephosphorylation by the catalytic subunits of protein phosphatases 1 (CS1) and 2A (CS2) reveals that mature protein kinase C is phosphorylated at two distinct sites. Treatment of protein kinase C...
5.
Newton A, Keranen L
Biochemistry
. 1994 May;
33(21):6651-8.
PMID: 8204602
The contributions of phospholipid headgroup structure, diacylglycerol, and Ca2+ in regulating the interaction of protein kinase C beta II with membranes or detergent/lipid mixed micelles were examined. Binding measurements revealed...
6.
Orr J, Keranen L, Newton A
J Biol Chem
. 1992 Aug;
267(22):15263-6.
PMID: 1639770
The lipid activators of protein kinase C, phosphatidylserine and diacylglycerol, induce a reversible conformational change that exposes the auto-inhibitory pseudosubstrate domain of the enzyme. The pseudosubstrate domain of beta-II protein...
7.
Murthy P, Pliska-Matyshak G, Keranen L, Lam P, Mueller H, Bhuvarahamurthy N
Plant Physiol
. 1992 Apr;
98(4):1498-501.
PMID: 16668820
The structure of phosphatidylinositol in barley (Hordeum vulgare) aleurone layers was investigated by chemical degradation. In vivo myo-[2-(3)H]inositol-labeled phosphatidylinositol was first converted to glycerophosphoinositol and, subsequently, after removal of the...
8.
Murthy P, Renders J, Keranen L
Plant Physiol
. 1989 Dec;
91(4):1266-9.
PMID: 16667174
Phospholipids of barley (Hordeum vulgare L. cv Himalaya) aleurone layers were labeled with myo-[2-(3)H]inositol or [(32)Pi], extracted, and analyzed by physical (chromatography) and chemical (deacylation) techniques. Three phospholipids were found...