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Showing 1 to 12 of 77 entries
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Tumour-promoting phorbol esters rapidly inhibit bud formation in hydra.

Roux's archives of developmental biology : the official organ of the EDBO

Shiba Y, Yamasaki H, Kanno Y.
PMID: 28305392
Rouxs Arch Dev Biol. 1987 Oct;196(7):445-449. doi: 10.1007/BF00399144.

The effects of tumour promoters and carcinogens on bud formation were investigated in an attempt to clarify the primary process of bud formation in hydra. Treatment with 1.0ng/ml 12-O-tetradecanoylphorbol-13-acetate (TPA), phorbol-12,13-didecanoate (PDD) or mezerein added immediately after feeding rapidly...

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Shiba Y, Yamasaki H, Kanno Y. Tumour-promoting phorbol esters rapidly inhibit bud formation in hydra. Rouxs Arch Dev Biol. 1987;196(7):445-449doi: 10.1007/BF00399144.
Shiba, Y., Yamasaki, H., & Kanno, Y. (1987). Tumour-promoting phorbol esters rapidly inhibit bud formation in hydra. Roux's archives of developmental biology : the official organ of the EDBO, 196(7), 445-449. https://doi.org/10.1007/BF00399144
Shiba, Yoshiki, et al. "Tumour-promoting phorbol esters rapidly inhibit bud formation in hydra." Roux's archives of developmental biology : the official organ of the EDBO vol. 196,7 (1987): 445-449. doi: https://doi.org/10.1007/BF00399144
Shiba Y, Yamasaki H, Kanno Y. Tumour-promoting phorbol esters rapidly inhibit bud formation in hydra. Rouxs Arch Dev Biol. 1987 Oct;196(7):445-449. doi: 10.1007/BF00399144. PMID: 28305392.
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The Neural Cell Adhesion Molecule (N-CAM) Modulates K+ Channels in Cultured Glial Precursor Cells.

The European journal of neuroscience

Sontheimer H, Kettenmann H, Schachner M, Trotter J.
PMID: 12106200
Eur J Neurosci. 1991;3(3):230-236. doi: 10.1111/j.1460-9568.1991.tb00084.x.

Application of antibodies against the neural cell adhesion molecule (N-CAM) to O4-positive murine glial precursor cells in vitro results in a reduction of two distinct K+ currents measured using the whole cell patch clamp technique. Both the A-type and...

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Sontheimer H, Kettenmann H, Schachner M, et al. The Neural Cell Adhesion Molecule (N-CAM) Modulates K+ Channels in Cultured Glial Precursor Cells. Eur J Neurosci. 1991;3(3):230-236doi: 10.1111/j.1460-9568.1991.tb00084.x.
Sontheimer, H., Kettenmann, H., Schachner, M., & Trotter, J. (1991). The Neural Cell Adhesion Molecule (N-CAM) Modulates K+ Channels in Cultured Glial Precursor Cells. The European journal of neuroscience, 3(3), 230-236. https://doi.org/10.1111/j.1460-9568.1991.tb00084.x
Sontheimer, Harald, et al. "The Neural Cell Adhesion Molecule (N-CAM) Modulates K+ Channels in Cultured Glial Precursor Cells." The European journal of neuroscience vol. 3,3 (1991): 230-236. doi: https://doi.org/10.1111/j.1460-9568.1991.tb00084.x
Sontheimer H, Kettenmann H, Schachner M, Trotter J. The Neural Cell Adhesion Molecule (N-CAM) Modulates K+ Channels in Cultured Glial Precursor Cells. Eur J Neurosci. 1991;3(3):230-236. doi: 10.1111/j.1460-9568.1991.tb00084.x. PMID: 12106200.
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The role of hydrogen peroxide and RRR-alpha-tocopherol in smooth muscle cell proliferation.

Cell death and differentiation

Azzi A, Cantoni O, Ozer N, Boscoboinik D, Spycher S.
PMID: 17180058
Cell Death Differ. 1996 Jan;3(1):79-90.

Oxidants can be considered early growth signals, since they have been shown to activate a number of pathways that are also stimulated by growth factors. In particular, H(2)O(2) activates the protein kinase C signal transduction pathway in smooth muscle...

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Azzi A, Cantoni O, Ozer N, et al. The role of hydrogen peroxide and RRR-alpha-tocopherol in smooth muscle cell proliferation. Cell Death Differ. 1996;3(1):79-90
Azzi, A., Cantoni, O., Ozer, N., Boscoboinik, D., & Spycher, S. (1996). The role of hydrogen peroxide and RRR-alpha-tocopherol in smooth muscle cell proliferation. Cell death and differentiation, 3(1), 79-90.
Azzi, A, et al. "The role of hydrogen peroxide and RRR-alpha-tocopherol in smooth muscle cell proliferation." Cell death and differentiation vol. 3,1 (1996): 79-90.
Azzi A, Cantoni O, Ozer N, Boscoboinik D, Spycher S. The role of hydrogen peroxide and RRR-alpha-tocopherol in smooth muscle cell proliferation. Cell Death Differ. 1996 Jan;3(1):79-90. PMID: 17180058.
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Evidence against roles for phorbol binding protein Munc13-1, ADAM adaptor Eve-1, or vesicle trafficking phosphoproteins Munc18 or NSF as phospho-state-sensitive modulators of phorbol/PKC-activated Alzheimer APP ectodomain shedding.

Molecular neurodegeneration

Ikin AF, Causevic M, Pedrini S, Benson LS, Buxbaum JD, Suzuki T, Lovestone S, Higashiyama S, Mustelin T, Burgoyne RD, Gandy S.
PMID: 18067682
Mol Neurodegener. 2007 Dec 09;2:23. doi: 10.1186/1750-1326-2-23.

BACKGROUND: Shedding of the Alzheimer amyloid precursor protein (APP) ectodomain can be accelerated by phorbol esters, compounds that act via protein kinase C (PKC) or through unconventional phorbol-binding proteins such as Munc13-1. We have previously demonstrated that application of...

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Ikin AF, Causevic M, Pedrini S, et al. Evidence against roles for phorbol binding protein Munc13-1, ADAM adaptor Eve-1, or vesicle trafficking phosphoproteins Munc18 or NSF as phospho-state-sensitive modulators of phorbol/PKC-activated Alzheimer APP ectodomain shedding. Mol Neurodegener. 2007;2:23doi: 10.1186/1750-1326-2-23.
Ikin, A. F., Causevic, M., Pedrini, S., Benson, L. S., Buxbaum, J. D., Suzuki, T., Lovestone, S., Higashiyama, S., Mustelin, T., Burgoyne, R. D., & Gandy, S. (2007). Evidence against roles for phorbol binding protein Munc13-1, ADAM adaptor Eve-1, or vesicle trafficking phosphoproteins Munc18 or NSF as phospho-state-sensitive modulators of phorbol/PKC-activated Alzheimer APP ectodomain shedding. Molecular neurodegeneration, 223. https://doi.org/10.1186/1750-1326-2-23
Ikin, Annat F, et al. "Evidence against roles for phorbol binding protein Munc13-1, ADAM adaptor Eve-1, or vesicle trafficking phosphoproteins Munc18 or NSF as phospho-state-sensitive modulators of phorbol/PKC-activated Alzheimer APP ectodomain shedding." Molecular neurodegeneration vol. 2 (2007): 23. doi: https://doi.org/10.1186/1750-1326-2-23
Ikin AF, Causevic M, Pedrini S, Benson LS, Buxbaum JD, Suzuki T, Lovestone S, Higashiyama S, Mustelin T, Burgoyne RD, Gandy S. Evidence against roles for phorbol binding protein Munc13-1, ADAM adaptor Eve-1, or vesicle trafficking phosphoproteins Munc18 or NSF as phospho-state-sensitive modulators of phorbol/PKC-activated Alzheimer APP ectodomain shedding. Mol Neurodegener. 2007 Dec 09;2:23. doi: 10.1186/1750-1326-2-23. PMID: 18067682; PMCID: PMC2211485.
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Modulation of Neuropeptide-lnduced Membrane Currents by Protein Kinase C in Xenopus Oocytes Injected with GH Pituitary Cell Poly(A) RNA.

Journal of neuroendocrinology

Mahlmann S, Schwarz JR, Meyerhof W.
PMID: 19210484
J Neuroendocrinol. 1989 Feb;1(1):65-9. doi: 10.1111/j.1365-2826.1989.tb00078.x.

Abstract Protein kinase C was activated in Xenopus laevis oocytes by phorbol ester treatment and its effects on the inositol trisphosphate/Ca(2+) transmembrane signalling pathway analysed. Induction of the pathway was achieved by ligand stimulation of TRH receptors translated from...

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Mahlmann S, Schwarz JR, Meyerhof W. Modulation of Neuropeptide-lnduced Membrane Currents by Protein Kinase C in Xenopus Oocytes Injected with GH Pituitary Cell Poly(A) RNA. J Neuroendocrinol. 1989;1(1):65-9doi: 10.1111/j.1365-2826.1989.tb00078.x.
Mahlmann, S., Schwarz, J. R., & Meyerhof, W. (1989). Modulation of Neuropeptide-lnduced Membrane Currents by Protein Kinase C in Xenopus Oocytes Injected with GH Pituitary Cell Poly(A) RNA. Journal of neuroendocrinology, 1(1), 65-9. https://doi.org/10.1111/j.1365-2826.1989.tb00078.x
Mahlmann, S, et al. "Modulation of Neuropeptide-lnduced Membrane Currents by Protein Kinase C in Xenopus Oocytes Injected with GH Pituitary Cell Poly(A) RNA." Journal of neuroendocrinology vol. 1,1 (1989): 65-9. doi: https://doi.org/10.1111/j.1365-2826.1989.tb00078.x
Mahlmann S, Schwarz JR, Meyerhof W. Modulation of Neuropeptide-lnduced Membrane Currents by Protein Kinase C in Xenopus Oocytes Injected with GH Pituitary Cell Poly(A) RNA. J Neuroendocrinol. 1989 Feb;1(1):65-9. doi: 10.1111/j.1365-2826.1989.tb00078.x. PMID: 19210484.
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Role of mitogen-activated protein kinase in cardiac hypertrophy and heart failure.

Experimental and clinical cardiology

Zhang W, Elimban V, Nijjar MS, Gupta SK, Dhalla NS.
PMID: 19649217
Exp Clin Cardiol. 2003;8(4):173-83.

BACKGROUND: Mitogen-activated protein kinases (MAPKs) are involved in the regulation of various cellular responses including cell proliferation, differentiation and survival. Although MAPKs are activated by MAPK kinase and inactivated by phosphatases, different types of MAPKs, including extracellular signal-regulated kinases...

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Zhang W, Elimban V, Nijjar MS, et al. Role of mitogen-activated protein kinase in cardiac hypertrophy and heart failure. Exp Clin Cardiol. 2003;8(4):173-83
Zhang, W., Elimban, V., Nijjar, M. S., Gupta, S. K., & Dhalla, N. S. (2003). Role of mitogen-activated protein kinase in cardiac hypertrophy and heart failure. Experimental and clinical cardiology, 8(4), 173-83.
Zhang, Weihua, et al. "Role of mitogen-activated protein kinase in cardiac hypertrophy and heart failure." Experimental and clinical cardiology vol. 8,4 (2003): 173-83.
Zhang W, Elimban V, Nijjar MS, Gupta SK, Dhalla NS. Role of mitogen-activated protein kinase in cardiac hypertrophy and heart failure. Exp Clin Cardiol. 2003;8(4):173-83. PMID: 19649217; PMCID: PMC2719157.
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Protein kinases and multidrug resistance.

Cytotechnology

Rumsby MG, Drew L, Warr JR.
PMID: 19002793
Cytotechnology. 1998 Sep;27(1):203-24. doi: 10.1023/A:1008073006495.

The role of protein kinases in the multidrug resistance phenotype of cancer cell lines is discussed with an emphasis on protein kinase C and protein kinase A. Evidence that P-glycoprotein is phosphorylated by these kinases is summarised and the...

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Rumsby MG, Drew L, Warr JR. Protein kinases and multidrug resistance. Cytotechnology. 1998;27(1):203-24doi: 10.1023/A:1008073006495.
Rumsby, M. G., Drew, L., & Warr, J. R. (1998). Protein kinases and multidrug resistance. Cytotechnology, 27(1), 203-24. https://doi.org/10.1023/A:1008073006495
Rumsby, M G, et al. "Protein kinases and multidrug resistance." Cytotechnology vol. 27,1 (1998): 203-24. doi: https://doi.org/10.1023/A:1008073006495
Rumsby MG, Drew L, Warr JR. Protein kinases and multidrug resistance. Cytotechnology. 1998 Sep;27(1):203-24. doi: 10.1023/A:1008073006495. PMID: 19002793; PMCID: PMC3449563.
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Differential regulation of neuropeptide Y and catecholamine production in superior cervical ganglion cultures.

Molecular and cellular neurosciences

Marek KL, Mains RE.
PMID: 19912776
Mol Cell Neurosci. 1990 Dec;1(3):262-9. doi: 10.1016/1044-7431(90)90008-r.

Primary cultures of newborn rat superior cervical ganglion (SCG) neurons grown in complete serum-free medium have been used to study the regulation of catecholamine and neuropeptide Y (NPY) production. The levels of mRNA for preproNPY and for tyrosine hydroxylase...

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Marek KL, Mains RE. Differential regulation of neuropeptide Y and catecholamine production in superior cervical ganglion cultures. Mol Cell Neurosci. 1990;1(3):262-9doi: 10.1016/1044-7431(90)90008-r.
Marek, K. L., & Mains, R. E. (1990). Differential regulation of neuropeptide Y and catecholamine production in superior cervical ganglion cultures. Molecular and cellular neurosciences, 1(3), 262-9. https://doi.org/10.1016/1044-7431(90)90008-r
Marek, K L, and Mains, R E. "Differential regulation of neuropeptide Y and catecholamine production in superior cervical ganglion cultures." Molecular and cellular neurosciences vol. 1,3 (1990): 262-9. doi: https://doi.org/10.1016/1044-7431(90)90008-r
Marek KL, Mains RE. Differential regulation of neuropeptide Y and catecholamine production in superior cervical ganglion cultures. Mol Cell Neurosci. 1990 Dec;1(3):262-9. doi: 10.1016/1044-7431(90)90008-r. PMID: 19912776.
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Involvement of protein kinase C in prostaglandin D(2) synthesis by cultured astrocytes.

Neurochemistry international

Gebicke-Haerter PJ, Seregi A, Schobert A, Hertting G.
PMID: 20501306
Neurochem Int. 1988;13(4):475-80. doi: 10.1016/0197-0186(88)90077-0.

The role of protein kinase C (PKC) and calcium in the stimulation of prostaglandin D(2) (PGD(2)) synthesis was investigated in primary rat astroglial cultures using the phorbol esters phorbol 12-myristate, 13-acetate (PMA), phorbol 12,13-dibutyrate (PDB) and the calcium ionophore...

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Gebicke-Haerter PJ, Seregi A, Schobert A, et al. Involvement of protein kinase C in prostaglandin D(2) synthesis by cultured astrocytes. Neurochem Int. 1988;13(4):475-80doi: 10.1016/0197-0186(88)90077-0.
Gebicke-Haerter, P. J., Seregi, A., Schobert, A., & Hertting, G. (1988). Involvement of protein kinase C in prostaglandin D(2) synthesis by cultured astrocytes. Neurochemistry international, 13(4), 475-80. https://doi.org/10.1016/0197-0186(88)90077-0
Gebicke-Haerter, P J, et al. "Involvement of protein kinase C in prostaglandin D(2) synthesis by cultured astrocytes." Neurochemistry international vol. 13,4 (1988): 475-80. doi: https://doi.org/10.1016/0197-0186(88)90077-0
Gebicke-Haerter PJ, Seregi A, Schobert A, Hertting G. Involvement of protein kinase C in prostaglandin D(2) synthesis by cultured astrocytes. Neurochem Int. 1988;13(4):475-80. doi: 10.1016/0197-0186(88)90077-0. PMID: 20501306.
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Expression and regulation of the 67-kda laminin-binding protein and its precursor gene in lymphoid-cells.

International journal of oncology

Suzuki H, Zhang X, Sobel M, Kondoh N, Papas T, Bhat N.
PMID: 21573471
Int J Oncol. 1993 Dec;3(6):1049-56. doi: 10.3892/ijo.3.6.1049.

The 67-kDa laminin-binding protein is a non-integrin laminin-binding protein that mediates cancer cell adhesion and migration. The expression of the 67-kDa laminin-binding protein and of its putative precursor, a 37-kDa polypeptide, was studied in peripheral T-cells and T-lymphoma cell...

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Suzuki H, Zhang X, Sobel M, et al. Expression and regulation of the 67-kda laminin-binding protein and its precursor gene in lymphoid-cells. Int J Oncol. 1993;3(6):1049-56doi: 10.3892/ijo.3.6.1049.
Suzuki, H., Zhang, X., Sobel, M., Kondoh, N., Papas, T., & Bhat, N. (1993). Expression and regulation of the 67-kda laminin-binding protein and its precursor gene in lymphoid-cells. International journal of oncology, 3(6), 1049-56. https://doi.org/10.3892/ijo.3.6.1049
Suzuki, H, et al. "Expression and regulation of the 67-kda laminin-binding protein and its precursor gene in lymphoid-cells." International journal of oncology vol. 3,6 (1993): 1049-56. doi: https://doi.org/10.3892/ijo.3.6.1049
Suzuki H, Zhang X, Sobel M, Kondoh N, Papas T, Bhat N. Expression and regulation of the 67-kda laminin-binding protein and its precursor gene in lymphoid-cells. Int J Oncol. 1993 Dec;3(6):1049-56. doi: 10.3892/ijo.3.6.1049. PMID: 21573471.
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Mapping of QTLs for Seed Phorbol Esters, a Toxic Chemical in Jatropha curcas (L.).

Genes

Amkul K, Laosatit K, Somta P, Shim S, Lee SH, Tanya P, Srinives P.
PMID: 28820491
Genes (Basel). 2017 Aug 18;8(8). doi: 10.3390/genes8080205.

Jatropha (

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Amkul K, Laosatit K, Somta P, et al. Mapping of QTLs for Seed Phorbol Esters, a Toxic Chemical in Jatropha curcas (L.). Genes (Basel). 2017;8(8)doi: 10.3390/genes8080205.
Amkul, K., Laosatit, K., Somta, P., Shim, S., Lee, S. H., Tanya, P., & Srinives, P. (2017). Mapping of QTLs for Seed Phorbol Esters, a Toxic Chemical in Jatropha curcas (L.). Genes, 8(8), . https://doi.org/10.3390/genes8080205
Amkul, Kitiya, et al. "Mapping of QTLs for Seed Phorbol Esters, a Toxic Chemical in Jatropha curcas (L.)." Genes vol. 8,8 (2017). doi: https://doi.org/10.3390/genes8080205
Amkul K, Laosatit K, Somta P, Shim S, Lee SH, Tanya P, Srinives P. Mapping of QTLs for Seed Phorbol Esters, a Toxic Chemical in Jatropha curcas (L.). Genes (Basel). 2017 Aug 18;8(8). doi: 10.3390/genes8080205. PMID: 28820491; PMCID: PMC5575668.
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Substitution of soybean meal with detoxified .

Asian-Australasian journal of animal sciences

Li Y, Chen L, Zhang Y, Wu J, Lin Y, Fang Z, Che L, Xu S, Wu.
PMID: 29103279
Asian-Australas J Anim Sci. 2018 Jun;31(6):888-898. doi: 10.5713/ajas.17.0499. Epub 2017 Nov 03.

OBJECTIVE: The study was conducted to investigate the effects of replacing soybean meal (SBM) with different levels of detoxified METHODS: A total of 144 pigs with initial body weight of 20.47±1.44 kg, were randomly allocated to 6 dietary treatments...

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Li Y, Chen L, Zhang Y, et al. Substitution of soybean meal with detoxified . Asian-Australas J Anim Sci. 2017;31(6):888-898doi: 10.5713/ajas.17.0499.
Li, Y., Chen, L., Zhang, Y., Wu, J., Lin, Y., Fang, Z., Che, L., Xu, S., & Wu. (2018). Substitution of soybean meal with detoxified . Asian-Australasian journal of animal sciences, 31(6), 888-898. https://doi.org/10.5713/ajas.17.0499
Li, Yang, et al. "Substitution of soybean meal with detoxified ." Asian-Australasian journal of animal sciences vol. 31,6 (2018): 888-898. doi: https://doi.org/10.5713/ajas.17.0499
Li Y, Chen L, Zhang Y, Wu J, Lin Y, Fang Z, Che L, Xu S, Wu. Substitution of soybean meal with detoxified . Asian-Australas J Anim Sci. 2018 Jun;31(6):888-898. doi: 10.5713/ajas.17.0499. Epub 2017 Nov 03. PMID: 29103279; PMCID: PMC5933988.
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Showing 1 to 12 of 77 entries