fim-1 -"DISCONTINUED" - Citations

fim-1 -"DISCONTINUED" - Citations

View additional product information for fim-1 -"DISCONTINUED" - Citations (F7462)

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Abstract
Time-resolved imaging of protein kinase C activation during sea urchin egg fertilization.
Authorsde Barry J, Kawahara S, Takamura K, Janoshazi A, Kirino Y, Olds JL, Lester DS, Alkon DL, Yoshioka T
JournalExp Cell Res
PubMed ID9223376
'To study protein kinase C (PKC) activation during sea urchin egg fertilization we used three different fluorescent probes specific for PKC, namely, fim-1, which recognizes the catalytic site of the enzyme, and BODIPY- and NBD-phorbol esters interacting with the PKC regulatory domain. We were able to follow PKC activation during ... More
Stimulated increase in free cytosolic Ca(2+) and protein kinase C activity in human cerebrocortical synaptosomes.
AuthorsMoe MC, Berg-Johnsen J, Røste GK, Vinje ML
JournalBrain Res
PubMed ID11744003
'Protein kinase C (PKC) is an important family of kinases regulated by lipid second messengers and cofactors that interact with cellular membranes. Both Ca(2+)-dependent and -independent isoforms of PKC have been described in rat cerebrocortical presynaptic nerve terminals (synaptosomes). In the present study, synaptosomes were prepared from human cerebral cortex ... More
Subcellular distribution of protein kinase C in the living outer hair cell of the guinea pig cochlea.
AuthorsUeda N, Ikeda K, Oshima T, Adachi M, Furukawa M, Takasaka T
JournalHear Res
PubMed ID8789808
Immunohistochemical staining using isoform-specific antibodies and intracellular localization using fluorescent probes for protein kinase C (PKC) were evaluated in the cochlear outer hair cell (OHC). Among three isoforms of classic PKC, PKC alpha was selectively stained in the fixed OHC as well as inner hair cells under a surface preparation ... More
Rapid in vitro conformational changes of the catalytic site of PKC alpha assessed by FIM-1 fluorescence.
AuthorsJanoshazi A, de Barry J
JournalBiochemistry
PubMed ID10529207
To study the activation process of protein kinase C (PKCalpha), we used a fluorescent probe, FIM-1, a bis-indolylmaleimide derivative, which binds to the ATP-binding site on the catalytic domain [Chen, C. S., and Poenie, M. (1993) J. Biol. Chem. 268, 15812]. This enabled us to directly observe the microenvironment of ... More
New fluorescent probes for protein kinase C. Synthesis, characterization, and application.
AuthorsChen CS, Poenie M
JournalJ Biol Chem
PubMed ID8340406
Fluorescent derivatives of the bisindolylmaleimide inhibitors of protein kinase C (PKC) were synthesized and tested with respect to their inhibitory potency, specificity, and usefulness as fluorescent cytological stains for PKC. Several of the fluorescent bisindolylmaleimide derivatives (fim-1, fim-2, and rim-1) acted as ATP-competitive catalytic site inhibitors and retained much of ... More
Reversible protein kinase C activation in PC12 cells: effect of NGF treatment.
AuthorsDupont JL, Janoshazi A, Bellahcene M, Mykita S, de Barry J
JournalEur J Neurosci
PubMed ID10651876
Although protein kinase C (PKC) is a key enzyme in the signal transduction process, there is little information on the mechanism leading to PKC activation in living cells. Using a new fluorescence imaging method, we studied this mechanism and correlated PKC conformational changes with intracellular Ca2+ concentration. PC12 cells were ... More