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Showing 1 to 12 of 293 entries
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Acitretin : A Review of its Pharmacology and Therapeutic Use.

Drugs

Pilkington T, Brogden RN.
PMID: 28421560
Drugs. 1992 Apr;43(4):597-627. doi: 10.2165/00003495-199243040-00010.

SYNOPSIS: Acitretin (etretin), a second generation monoaromatic retinoid for use in the treatment of severe psoriasis and other dermatoses, is the major active metabolite of etretinate and possesses a similar therapeutic index; i.e. a similar ratio of clinical efficacy...

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Pilkington T, Brogden RN. Acitretin : A Review of its Pharmacology and Therapeutic Use. Drugs. 1992;43(4):597-627doi: 10.2165/00003495-199243040-00010.
Pilkington, T., & Brogden, R. N. (1992). Acitretin : A Review of its Pharmacology and Therapeutic Use. Drugs, 43(4), 597-627. https://doi.org/10.2165/00003495-199243040-00010
Pilkington, Tania, and Brogden, Rex N. "Acitretin : A Review of its Pharmacology and Therapeutic Use." Drugs vol. 43,4 (1992): 597-627. doi: https://doi.org/10.2165/00003495-199243040-00010
Pilkington T, Brogden RN. Acitretin : A Review of its Pharmacology and Therapeutic Use. Drugs. 1992 Apr;43(4):597-627. doi: 10.2165/00003495-199243040-00010. PMID: 28421560.
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Simultaneous targeting of 5-LOX-COX and ODC block NNK-induced lung adenoma progression to adenocarcinoma in A/J mice.

American journal of cancer research

Kumar G, Patlolla JM, Madka V, Mohammed A, Li Q, Zhang Y, Biddick L, Singh A, Gillaspy A, Lightfoot S, Steele VE, Kopelovich L, Rao CV.
PMID: 27293987
Am J Cancer Res. 2016 May 01;6(5):894-909. eCollection 2016.

Lung cancer is the leading cause of cancer deaths worldwide. Targeting complementary pathways will achieve better treatment efficacy than a single agent high-dose strategy that could increase risk of side effects and tumor resistance. To target COX-2, 5-LOX, and...

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Kumar G, Patlolla JM, Madka V, et al. Simultaneous targeting of 5-LOX-COX and ODC block NNK-induced lung adenoma progression to adenocarcinoma in A/J mice. Am J Cancer Res. 2016;6(5):894-909
Kumar, G., Patlolla, J. M., Madka, V., Mohammed, A., Li, Q., Zhang, Y., Biddick, L., Singh, A., Gillaspy, A., Lightfoot, S., Steele, V. E., Kopelovich, L., & Rao, C. V. (2016). Simultaneous targeting of 5-LOX-COX and ODC block NNK-induced lung adenoma progression to adenocarcinoma in A/J mice. American journal of cancer research, 6(5), 894-909.
Kumar, Gaurav, et al. "Simultaneous targeting of 5-LOX-COX and ODC block NNK-induced lung adenoma progression to adenocarcinoma in A/J mice." American journal of cancer research vol. 6,5 (2016): 894-909.
Kumar G, Patlolla JM, Madka V, Mohammed A, Li Q, Zhang Y, Biddick L, Singh A, Gillaspy A, Lightfoot S, Steele VE, Kopelovich L, Rao CV. Simultaneous targeting of 5-LOX-COX and ODC block NNK-induced lung adenoma progression to adenocarcinoma in A/J mice. Am J Cancer Res. 2016 May 01;6(5):894-909. eCollection 2016. PMID: 27293987; PMCID: PMC4889708.
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Polyamines directly promote antizyme-mediated degradation of ornithine decarboxylase by the proteasome.

Microbial cell (Graz, Austria)

Beenukumar RR, Gödderz D, Palanimurugan R, Dohmen RJ.
PMID: 28357293
Microb Cell. 2015 May 20;2(6):197-207. doi: 10.15698/mic2015.06.206.

Ornithine decarboxylase (ODC), a ubiquitin-independent substrate of the proteasome, is a homodimeric protein with a rate-limiting function in polyamine biosynthesis. Polyamines regulate ODC levels by a feedback mechanism mediated by ODC antizyme (OAZ). Higher cellular polyamine levels trigger the...

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Beenukumar RR, Gödderz D, Palanimurugan R, et al. Polyamines directly promote antizyme-mediated degradation of ornithine decarboxylase by the proteasome. Microb Cell. 2015;2(6):197-207doi: 10.15698/mic2015.06.206.
Beenukumar, R. R., Gödderz, D., Palanimurugan, R., & Dohmen, R. J. (2015). Polyamines directly promote antizyme-mediated degradation of ornithine decarboxylase by the proteasome. Microbial cell (Graz, Austria), 2(6), 197-207. https://doi.org/10.15698/mic2015.06.206
Beenukumar, R R, et al. "Polyamines directly promote antizyme-mediated degradation of ornithine decarboxylase by the proteasome." Microbial cell (Graz, Austria) vol. 2,6 (2015): 197-207. doi: https://doi.org/10.15698/mic2015.06.206
Beenukumar RR, Gödderz D, Palanimurugan R, Dohmen RJ. Polyamines directly promote antizyme-mediated degradation of ornithine decarboxylase by the proteasome. Microb Cell. 2015 May 20;2(6):197-207. doi: 10.15698/mic2015.06.206. PMID: 28357293; PMCID: PMC5349141.
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Spermidine is protective against kidney ischemia and reperfusion injury through inhibiting DNA nitration and PARP1 activation.

Anatomy & cell biology

Kim J.
PMID: 29043098
Anat Cell Biol. 2017 Sep;50(3):200-206. doi: 10.5115/acb.2017.50.3.200. Epub 2017 Sep 20.

Kidney ischemia and reperfusion injury (IRI) is associated with a high mortality rate, which is attributed to tubular oxidative and nitrative stresses; however, an effective approach to limit IRI remains elusive. Spermidine, a naturally occurring polyamine, protects yeast cells...

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Kim J. Spermidine is protective against kidney ischemia and reperfusion injury through inhibiting DNA nitration and PARP1 activation. Anat Cell Biol. 2017;50(3):200-206doi: 10.5115/acb.2017.50.3.200.
Kim, J. (2017). Spermidine is protective against kidney ischemia and reperfusion injury through inhibiting DNA nitration and PARP1 activation. Anatomy & cell biology, 50(3), 200-206. https://doi.org/10.5115/acb.2017.50.3.200
Kim, Jinu. "Spermidine is protective against kidney ischemia and reperfusion injury through inhibiting DNA nitration and PARP1 activation." Anatomy & cell biology vol. 50,3 (2017): 200-206. doi: https://doi.org/10.5115/acb.2017.50.3.200
Kim J. Spermidine is protective against kidney ischemia and reperfusion injury through inhibiting DNA nitration and PARP1 activation. Anat Cell Biol. 2017 Sep;50(3):200-206. doi: 10.5115/acb.2017.50.3.200. Epub 2017 Sep 20. PMID: 29043098; PMCID: PMC5639174.
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Hyperhomocysteinemia, Suppressed Immunity, and Altered Oxidative Metabolism Caused by Pathogenic Microbes in Atherosclerosis and Dementia.

Frontiers in aging neuroscience

McCully KS.
PMID: 29056905
Front Aging Neurosci. 2017 Oct 06;9:324. doi: 10.3389/fnagi.2017.00324. eCollection 2017.

Many pathogenic microorganisms have been demonstrated in atherosclerotic plaques and in cerebral plaques in dementia. Hyperhomocysteinemia, which is a risk factor for atherosclerosis and dementia, is caused by dysregulation of methionine metabolism secondary to deficiency of the allosteric regulator,...

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McCully KS. Hyperhomocysteinemia, Suppressed Immunity, and Altered Oxidative Metabolism Caused by Pathogenic Microbes in Atherosclerosis and Dementia. Front Aging Neurosci. 2017;9:324doi: 10.3389/fnagi.2017.00324.
McCully, K. S. (2017). Hyperhomocysteinemia, Suppressed Immunity, and Altered Oxidative Metabolism Caused by Pathogenic Microbes in Atherosclerosis and Dementia. Frontiers in aging neuroscience, 9324. https://doi.org/10.3389/fnagi.2017.00324
McCully, Kilmer S. "Hyperhomocysteinemia, Suppressed Immunity, and Altered Oxidative Metabolism Caused by Pathogenic Microbes in Atherosclerosis and Dementia." Frontiers in aging neuroscience vol. 9 (2017): 324. doi: https://doi.org/10.3389/fnagi.2017.00324
McCully KS. Hyperhomocysteinemia, Suppressed Immunity, and Altered Oxidative Metabolism Caused by Pathogenic Microbes in Atherosclerosis and Dementia. Front Aging Neurosci. 2017 Oct 06;9:324. doi: 10.3389/fnagi.2017.00324. eCollection 2017. PMID: 29056905; PMCID: PMC5635055.
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A comparison of RNA concentrations and ornithine decarboxylase activity in Atlantic salmon (Salmo salar) muscle tissue, with respect to specific growth rates and diel variations.

Fish physiology and biochemistry

Arndt SK, Benfey TJ, Cunjak RA.
PMID: 24197142
Fish Physiol Biochem. 1994 Dec;13(6):463-71. doi: 10.1007/BF00004329.

RNA concentrations and enzyme activities are often used as indices of recent growth in fish, but few studies have used both methods to assess the same fish. This study measured RNA concentrations and ornithine decarboxylase (ODC) activity in muscle...

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Arndt SK, Benfey TJ, Cunjak RA. A comparison of RNA concentrations and ornithine decarboxylase activity in Atlantic salmon (Salmo salar) muscle tissue, with respect to specific growth rates and diel variations. Fish Physiol Biochem. 1994;13(6):463-71doi: 10.1007/BF00004329.
Arndt, S. K., Benfey, T. J., & Cunjak, R. A. (1994). A comparison of RNA concentrations and ornithine decarboxylase activity in Atlantic salmon (Salmo salar) muscle tissue, with respect to specific growth rates and diel variations. Fish physiology and biochemistry, 13(6), 463-71. https://doi.org/10.1007/BF00004329
Arndt, S K, et al. "A comparison of RNA concentrations and ornithine decarboxylase activity in Atlantic salmon (Salmo salar) muscle tissue, with respect to specific growth rates and diel variations." Fish physiology and biochemistry vol. 13,6 (1994): 463-71. doi: https://doi.org/10.1007/BF00004329
Arndt SK, Benfey TJ, Cunjak RA. A comparison of RNA concentrations and ornithine decarboxylase activity in Atlantic salmon (Salmo salar) muscle tissue, with respect to specific growth rates and diel variations. Fish Physiol Biochem. 1994 Dec;13(6):463-71. doi: 10.1007/BF00004329. PMID: 24197142.
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Ornithine decarboxylase and ribosomal RNA synthesis during the stimulation of lymphocytes by phytohaemagglutinin.

FEBS letters

Kay JE, Cooke A.
PMID: 11945886
FEBS Lett. 1971 Jul 15;16(1):9-12. doi: 10.1016/0014-5793(71)80671-3.

No abstract available.

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Kay JE, Cooke A. Ornithine decarboxylase and ribosomal RNA synthesis during the stimulation of lymphocytes by phytohaemagglutinin. FEBS Lett. 1971;16(1):9-12doi: 10.1016/0014-5793(71)80671-3.
Kay, J. E., & Cooke, A. (1971). Ornithine decarboxylase and ribosomal RNA synthesis during the stimulation of lymphocytes by phytohaemagglutinin. FEBS letters, 16(1), 9-12. https://doi.org/10.1016/0014-5793(71)80671-3
Kay, John E., and Cooke, Anne. "Ornithine decarboxylase and ribosomal RNA synthesis during the stimulation of lymphocytes by phytohaemagglutinin." FEBS letters vol. 16,1 (1971): 9-12. doi: https://doi.org/10.1016/0014-5793(71)80671-3
Kay JE, Cooke A. Ornithine decarboxylase and ribosomal RNA synthesis during the stimulation of lymphocytes by phytohaemagglutinin. FEBS Lett. 1971 Jul 15;16(1):9-12. doi: 10.1016/0014-5793(71)80671-3. PMID: 11945886.
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Cessation of Long-term Alcohol Administration and Two-day Cycling of Exposure Respectively Promote and Inhibit Hepatocarcinogenesis in Rats.

Asian Pacific journal of cancer prevention : APJCP

Tanaka T, Hirota Y, Kuriyama M, Nishiguchi S, Otani S.
PMID: 12716308
Asian Pac J Cancer Prev. 2000;1(4):325-328.

The effects of different patterns of alcohol administration on hepatocarcinogenesis induced by diethylnitrosamine (DEN) in male Wistar rats were assessed using a modified Ito's medium-term bioassay system. Carcinogenic potential was scored by comparing numbers and areas of glutathione S...

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Tanaka T, Hirota Y, Kuriyama M, et al. Cessation of Long-term Alcohol Administration and Two-day Cycling of Exposure Respectively Promote and Inhibit Hepatocarcinogenesis in Rats. Asian Pac J Cancer Prev. 2000;1(4):325-328
Tanaka, T., Hirota, Y., Kuriyama, M., Nishiguchi, S., & Otani, S. (2000). Cessation of Long-term Alcohol Administration and Two-day Cycling of Exposure Respectively Promote and Inhibit Hepatocarcinogenesis in Rats. Asian Pacific journal of cancer prevention : APJCP, 1(4), 325-328.
Tanaka, Takashi, et al. "Cessation of Long-term Alcohol Administration and Two-day Cycling of Exposure Respectively Promote and Inhibit Hepatocarcinogenesis in Rats." Asian Pacific journal of cancer prevention : APJCP vol. 1,4 (2000): 325-328.
Tanaka T, Hirota Y, Kuriyama M, Nishiguchi S, Otani S. Cessation of Long-term Alcohol Administration and Two-day Cycling of Exposure Respectively Promote and Inhibit Hepatocarcinogenesis in Rats. Asian Pac J Cancer Prev. 2000;1(4):325-328. PMID: 12716308.
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Studies on ornithine decarboxylase activity in normal and T2-infected Escherichia coli.

FEBS letters

Bachrach U, Ben-Joseph M.
PMID: 11945817
FEBS Lett. 1971 Jun 02;15(1):75-77. doi: 10.1016/0014-5793(71)80082-0.

No abstract available.

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Bachrach U, Ben-Joseph M. Studies on ornithine decarboxylase activity in normal and T2-infected Escherichia coli. FEBS Lett. 1971;15(1):75-77doi: 10.1016/0014-5793(71)80082-0.
Bachrach, U., & Ben-Joseph, M. (1971). Studies on ornithine decarboxylase activity in normal and T2-infected Escherichia coli. FEBS letters, 15(1), 75-77. https://doi.org/10.1016/0014-5793(71)80082-0
Bachrach, U, and Ben-Joseph, M. "Studies on ornithine decarboxylase activity in normal and T2-infected Escherichia coli." FEBS letters vol. 15,1 (1971): 75-77. doi: https://doi.org/10.1016/0014-5793(71)80082-0
Bachrach U, Ben-Joseph M. Studies on ornithine decarboxylase activity in normal and T2-infected Escherichia coli. FEBS Lett. 1971 Jun 02;15(1):75-77. doi: 10.1016/0014-5793(71)80082-0. PMID: 11945817.
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Polyamine depletion induces G1 and S phase arrest in human retinoblastoma Y79 cells.

Cancer cell international

Ueda A, Araie M, Kubota S.
PMID: 18208615
Cancer Cell Int. 2008 Jan 21;8:2. doi: 10.1186/1475-2867-8-2.

BACKGROUND: Polyamines and ornithine decarboxylase (ODC) are essential for cell proliferation. DL-alpha-difluoromethylornithine (DFMO), a synthetic inhibitor of ODC, induces G1 arrest through dephosphorylation of retinoblastoma protein (pRb). The effect of DFMO on cell growth of pRb deficient cells is...

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Ueda A, Araie M, Kubota S. Polyamine depletion induces G1 and S phase arrest in human retinoblastoma Y79 cells. Cancer Cell Int. 2008;8:2doi: 10.1186/1475-2867-8-2.
Ueda, A., Araie, M., & Kubota, S. (2008). Polyamine depletion induces G1 and S phase arrest in human retinoblastoma Y79 cells. Cancer cell international, 82. https://doi.org/10.1186/1475-2867-8-2
Ueda, Akiko, et al. "Polyamine depletion induces G1 and S phase arrest in human retinoblastoma Y79 cells." Cancer cell international vol. 8 (2008): 2. doi: https://doi.org/10.1186/1475-2867-8-2
Ueda A, Araie M, Kubota S. Polyamine depletion induces G1 and S phase arrest in human retinoblastoma Y79 cells. Cancer Cell Int. 2008 Jan 21;8:2. doi: 10.1186/1475-2867-8-2. PMID: 18208615; PMCID: PMC2259317.
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Effects of a high soy protein diet on intestinal polyamines and ornithine decarboxylase activity in rats.

The Journal of nutritional biochemistry

Meziani K, Benamouzig R, Mahé S, Martin A, Bouras M, Rautureau J, Tomé D.
PMID: 15539316
J Nutr Biochem. 1999 Jul;10(7):405-10. doi: 10.1016/s0955-2863(99)00019-4.

This study was performed to determine whether intestinal luminal polyamine concentrations are affected by a high soy protein diet when compared with a high casein diet or a normoprotein casein diet. We also determined the effects of these diets,...

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Meziani K, Benamouzig R, Mahé S, et al. Effects of a high soy protein diet on intestinal polyamines and ornithine decarboxylase activity in rats. J Nutr Biochem. 1999;10(7):405-10doi: 10.1016/s0955-2863(99)00019-4.
Meziani, K., Benamouzig, R., Mahé, S., Martin, A., Bouras, M., Rautureau, J., & Tomé, D. (1999). Effects of a high soy protein diet on intestinal polyamines and ornithine decarboxylase activity in rats. The Journal of nutritional biochemistry, 10(7), 405-10. https://doi.org/10.1016/s0955-2863(99)00019-4
Meziani, K, et al. "Effects of a high soy protein diet on intestinal polyamines and ornithine decarboxylase activity in rats." The Journal of nutritional biochemistry vol. 10,7 (1999): 405-10. doi: https://doi.org/10.1016/s0955-2863(99)00019-4
Meziani K, Benamouzig R, Mahé S, Martin A, Bouras M, Rautureau J, Tomé D. Effects of a high soy protein diet on intestinal polyamines and ornithine decarboxylase activity in rats. J Nutr Biochem. 1999 Jul;10(7):405-10. doi: 10.1016/s0955-2863(99)00019-4. PMID: 15539316.
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Ornithine decarboxylase, polyamines, and pyrrolizidine alkaloids in senecio and crotalaria.

Plant physiology

Birecka H, Birecki M, Cohen EJ, Bitonti AJ, McCann PP.
PMID: 16665870
Plant Physiol. 1988 Jan;86(1):224-30. doi: 10.1104/pp.86.1.224.

When tested for ornithine and arginine decarboxylases, pyrrolizidine alkaloid-bearing Senecio riddellii, S. longilobus (Compositae), and Crotalaria retusa (Leguminosae) plants exhibited only ornithine decarboxylase activity. This contrasts with previous studies of four species of pyrrolizidine alkaloid-bearing Heliotropium (Boraginaceae) in which...

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Birecka H, Birecki M, Cohen EJ, et al. Ornithine decarboxylase, polyamines, and pyrrolizidine alkaloids in senecio and crotalaria. Plant Physiol. 1988;86(1):224-30doi: 10.1104/pp.86.1.224.
Birecka, H., Birecki, M., Cohen, E. J., Bitonti, A. J., & McCann, P. P. (1988). Ornithine decarboxylase, polyamines, and pyrrolizidine alkaloids in senecio and crotalaria. Plant physiology, 86(1), 224-30. https://doi.org/10.1104/pp.86.1.224
Birecka, H, et al. "Ornithine decarboxylase, polyamines, and pyrrolizidine alkaloids in senecio and crotalaria." Plant physiology vol. 86,1 (1988): 224-30. doi: https://doi.org/10.1104/pp.86.1.224
Birecka H, Birecki M, Cohen EJ, Bitonti AJ, McCann PP. Ornithine decarboxylase, polyamines, and pyrrolizidine alkaloids in senecio and crotalaria. Plant Physiol. 1988 Jan;86(1):224-30. doi: 10.1104/pp.86.1.224. PMID: 16665870; PMCID: PMC1054458.
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Showing 1 to 12 of 293 entries