scholarly journals Design, Synthesis, and Biological Activity of Isophthalic Acid Derivatives Targeted to the C1 Domain of Protein Kinase C

2009 ◽  
Vol 52 (13) ◽  
pp. 3969-3981 ◽  
Author(s):  
Gustav Boije af Gennäs ◽  
Virpi Talman ◽  
Olli Aitio ◽  
Elina Ekokoski ◽  
Moshe Finel ◽  
...  
Keyword(s):  
Biological Activity ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Isophthalic Acid ◽  
Design Synthesis ◽  
Kinase C ◽  
C1 Domain

Alkyl cinnamates as regulator for the C1 domain of protein kinase C isoforms

2012 ◽  
Vol 165 (3) ◽  
pp. 320-330 ◽  
Author(s):  
Narsimha Mamidi ◽  
Sukhamoy Gorai ◽  
Jashobanta Sahoo ◽  
Debasis Manna
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
C1 Domain ◽  
Protein Kinase C Isoforms

scholarly journals Computer-Guided Design, Synthesis, and Protein Kinase C Affinity of a New Salicylate-Based Class of Bryostatin Analogs

2014 ◽  
Vol 16 (19) ◽  
pp. 5136-5139 ◽  
Author(s):  
Paul A. Wender ◽  
Yu Nakagawa ◽  
Katherine E. Near ◽  
Daryl Staveness
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Design Synthesis ◽  
Kinase C

Design, synthesis, and structure–activity relationship of new isobenzofuranone ligands of protein kinase C

2004 ◽  
Vol 14 (11) ◽  
pp. 2963-2967 ◽  
Author(s):  
Yoshiyasu Baba ◽  
Yosuke Ogoshi ◽  
Go Hirai ◽  
Takeshi Yanagisawa ◽  
Kumiko Nagamatsu ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Design Synthesis ◽  
Kinase C ◽  
Structure Activity ◽  
Relationship Of

The C1 Domain of Protein Kinase C as a Lipid Bilayer Surface Sensing Module†

Biochemistry ◽  
2001 ◽  
Vol 40 (34) ◽  
pp. 10334-10341 ◽  
Author(s):  
Cojen Ho ◽  
Simon J. Slater ◽  
Brigid Stagliano ◽  
Christopher D. Stubbs
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Lipid Bilayer ◽  
Kinase C ◽  
Surface Sensing ◽  
C1 Domain

scholarly journals Mechanism of inhibition of protein kinase C by 14-3-3 isoforms. 14-3-3 isoforms do not have phospholipase A2 activity.

1994 ◽  
Vol 299 (3) ◽  
pp. 853-861 ◽  
Author(s):  
K Robinson ◽  
D Jones ◽  
Y Patel ◽  
H Martin ◽  
J Madrazo ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase A2 ◽  
Kinase C ◽  
Mechanism Of Inhibition ◽  
C1 Domain ◽  
Novel Method ◽  
Original Observation ◽  
Cytosolic Pla2 ◽  
Phospholipase A2 Activity

The ability of individual members of the 14-3-3 protein family to inhibit protein kinase C (PKC) has been studied by using a synthetic peptide based on the specific 80 kDa substrate for PKC (MARCKS protein) in two different assay systems. Recombinant 14-3-3 and isoforms renatured by a novel method after separation by reverse-phase h.p.l.c. were studied. The detailed effects of diacylglycerol and the phorbol ester phorbol 12-myristate 13-acetate on the inhibition were also investigated. This suggests that one of the sites of interaction of 14-3-3 may be the cysteine-rich (C1) domain in PKC. Since a region in secreted phospholipase A2 (PLA2) shares similarity with this domain, the ability of 14-3-3 to interact with mammalian PLA2 was studied. Cytosolic PLA2 has some similarity to the C2 region of PKC, and the effect of 14-3-3 on this class of PLA2 was also analysed. In contrast with a previous report, no PLA2 activity was found in brain 14-3-3, nor in any of the recombinant proteins tested. These include zeta 14-3-3 isoform, on which the original observation was made.

Sign in / Sign up

Export Citation Format

Share Document