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Page 1
Showing results for sapintoxin
Search for Supinoxin instead (1 results)
Synergistic Gene Expression Signature Observed in TK6 Cells upon Co-Exposure to UVC-Irradiation and Protein Kinase C-Activating Tumor Promoters.
Glover KP, Chen Z, Markell LK, Han X. Glover KP, et al. PLoS One. 2015 Oct 2;10(10):e0139850. doi: 10.1371/journal.pone.0139850. eCollection 2015. PLoS One. 2015. PMID: 26431317 Free PMC article.
The 17 gene signature derived from this model was confirmed with other PKC-activating tumor promoters including phorbol-12,13-dibutyrate, sapintoxin D, mezerein, (-)-Indolactam V and resiniferonol 9,13,14-ortho-phenylacetate (ROPA) with quantitative real-time PCR (QPCR). . …
The 17 gene signature derived from this model was confirmed with other PKC-activating tumor promoters including phorbol-12,13-dibutyrate, …
Some phorbol esters might partially resemble bryostatin 1 in their actions on LNCaP prostate cancer cells and U937 leukemia cells.
Kedei N, Lubart E, Lewin NE, Telek A, Lim L, Mannan P, Garfield SH, Kraft MB, Keck GE, Kolusheva S, Jelinek R, Blumberg PM. Kedei N, et al. Chembiochem. 2011 May 16;12(8):1242-51. doi: 10.1002/cbic.201100064. Epub 2011 May 3. Chembiochem. 2011. PMID: 21542090 Free PMC article.
Dose-response curves ranged from monophasic for indolactam V to markedly biphasic for sapintoxin D. The divergent patterns of response, however, correlated neither to lipophilicity, to plasma membrane translocation of PKCdelta, nor to the ability to interact with model mem …
Dose-response curves ranged from monophasic for indolactam V to markedly biphasic for sapintoxin D. The divergent patterns of respons …
Binding of curcumin and its long chain derivatives to the activator binding domain of novel protein kinase C.
Majhi A, Rahman GM, Panchal S, Das J. Majhi A, et al. Bioorg Med Chem. 2010 Feb 15;18(4):1591-8. doi: 10.1016/j.bmc.2009.12.075. Epub 2010 Jan 6. Bioorg Med Chem. 2010. PMID: 20100661 Free PMC article.
Fluorescence emission maxima of 1 and 4 were blue shifted and the fluorescence anisotropy values were increased in the presence of the C1B domains in a manner similar to that shown by the fluorescent analog of TPA, sapintoxin-D, confirming that they were bound to the prote …
Fluorescence emission maxima of 1 and 4 were blue shifted and the fluorescence anisotropy values were increased in the presence of the C1B d …
Propofol activates and allosterically modulates recombinant protein kinase C epsilon.
Wickley PJ, Yuge R, Martin BA, Meyer JS, Damron DS. Wickley PJ, et al. Anesthesiology. 2009 Jul;111(1):36-43. doi: 10.1097/ALN.0b013e3181a3274b. Anesthesiology. 2009. PMID: 19512879 Free PMC article.
Spectral shifts in fluorescence emission maxima of the C1B subdomain of PKC epsilon in combination with the fluorescent phorbol ester, sapintoxin D, was used to identify molecular interactions between propofol and the phorbol ester/diacylglycerol binding site on the enzyme …
Spectral shifts in fluorescence emission maxima of the C1B subdomain of PKC epsilon in combination with the fluorescent phorbol ester, sa
PKC epsilon has an alcohol-binding site in its second cysteine-rich regulatory domain.
Das J, Pany S, Rahman GM, Slater SJ. Das J, et al. Biochem J. 2009 Jul 15;421(3):405-13. doi: 10.1042/BJ20082271. Biochem J. 2009. PMID: 19432558
Ethanol, butanol and octanol increased the binding affinity of a fluorescent phorbol ester SAPD (sapintoxin-D) to PKC epsilon C1B in a concentration-dependent manner with EC50 values of 78 mM, 8 mM and 340 microM respectively, suggesting the presence of an allosteric alcoh …
Ethanol, butanol and octanol increased the binding affinity of a fluorescent phorbol ester SAPD (sapintoxin-D) to PKC epsilon C1B in …
Identification of a general anesthetic binding site in the diacylglycerol-binding domain of protein kinase Cdelta.
Das J, Addona GH, Sandberg WS, Husain SS, Stehle T, Miller KW. Das J, et al. J Biol Chem. 2004 Sep 3;279(36):37964-72. doi: 10.1074/jbc.M405137200. Epub 2004 Jul 2. J Biol Chem. 2004. PMID: 15234976 Free article.
To test this hypothesis, we expressed, purified, and characterized the high affinity phorbol-binding subdomain, C1B, of mouse protein kinase Cdelta, and studied its interaction with general anesthetic alcohols. When the fluorescent phorbol ester, sapintoxin-D, bound to PKC …
To test this hypothesis, we expressed, purified, and characterized the high affinity phorbol-binding subdomain, C1B, of mouse protein kinase …
The C1 domain of protein kinase C as a lipid bilayer surface sensing module.
Ho C, Slater SJ, Stagliano B, Stubbs CD. Ho C, et al. Biochemistry. 2001 Aug 28;40(34):10334-41. doi: 10.1021/bi002839x. Biochemistry. 2001. PMID: 11513612
In addition, the rotational correlation time of both PKCalpha and PKCdelta C1-domain-associated sapintoxin D, a fluorescent phorbol ester, was also a biphasic function of membrane lipid PE content. ...
In addition, the rotational correlation time of both PKCalpha and PKCdelta C1-domain-associated sapintoxin D, a fluorescent phorbol e …
Down-modulation through protein kinase C-alpha of lipopolysaccharide-induced expression of membrane CD14 in mouse bone marrow granulocytes.
Pedron T, Girard R, Chaby R. Pedron T, et al. Biochem Pharmacol. 2000 Dec 15;60(12):1837-43. doi: 10.1016/s0006-2952(00)00499-8. Biochem Pharmacol. 2000. PMID: 11108799
The observations that a selective activator of protein kinase C (PKC)-alpha (sapintoxin D) mimics the PMA effect, whereas a selective PKC-alpha inhibitor (Ro-320432) antagonizes this effect, suggest a regulatory role of PKC-alpha in the LPS signaling pathway in mouse BMC.. …
The observations that a selective activator of protein kinase C (PKC)-alpha (sapintoxin D) mimics the PMA effect, whereas a selective …
28 results