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Assessment of steroidogenic pathways that do not require testosterone as intermediate.

Hormone molecular biology and clinical investigation

Luu-The V.
PMID: 25961251
Horm Mol Biol Clin Investig. 2011 Mar 01;5(3):161-5. doi: 10.1515/HMBCI.2011.007.

Traditional literature and textbooks generally describe that estradiol (E2) and dihydrotestosterone (DHT) are synthesized from the aromatization and 5α-reduction of testosterone (T), respectively, following a pathway in which T is an essential intermediate (Tpath). This pathway implies that the...

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Luu-The V. Assessment of steroidogenic pathways that do not require testosterone as intermediate. Horm Mol Biol Clin Investig. 2011;5(3):161-5doi: 10.1515/HMBCI.2011.007.
Luu-The, V. (2011). Assessment of steroidogenic pathways that do not require testosterone as intermediate. Hormone molecular biology and clinical investigation, 5(3), 161-5. https://doi.org/10.1515/HMBCI.2011.007
Luu-The, Van. "Assessment of steroidogenic pathways that do not require testosterone as intermediate." Hormone molecular biology and clinical investigation vol. 5,3 (2011): 161-5. doi: https://doi.org/10.1515/HMBCI.2011.007
Luu-The V. Assessment of steroidogenic pathways that do not require testosterone as intermediate. Horm Mol Biol Clin Investig. 2011 Mar 01;5(3):161-5. doi: 10.1515/HMBCI.2011.007. PMID: 25961251.
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Expression of Estrogen Sulfotransferase 1E1 and Steroid Sulfatase in Breast Cancer: A Immunohistochemical Study.

Breast cancer : basic and clinical research

Poisson Paré D, Song D, Luu-The V, Han B, Li S, Liu G, Labrie F, Pelletier G.
PMID: 21556246
Breast Cancer (Auckl). 2009 Mar 20;3:9-21. doi: 10.4137/bcbcr.s2012.

It is known that the steroid sulfatase (STS) and the estrogen sulfotransferase (EST1E1) are commonly expressed in human breast carcinomas. STS and EST1E1 combined action could maintain the equilibrium between sulfated (inactive) and unconjugated (active) estrogens, which might have...

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Poisson Paré D, Song D, Luu-The V, et al. Expression of Estrogen Sulfotransferase 1E1 and Steroid Sulfatase in Breast Cancer: A Immunohistochemical Study. Breast Cancer (Auckl). 2009;3:9-21doi: 10.4137/bcbcr.s2012.
Poisson Paré, D., Song, D., Luu-The, V., Han, B., Li, S., Liu, G., Labrie, F., & Pelletier, G. (2009). Expression of Estrogen Sulfotransferase 1E1 and Steroid Sulfatase in Breast Cancer: A Immunohistochemical Study. Breast cancer : basic and clinical research, 39-21. https://doi.org/10.4137/bcbcr.s2012
Poisson Paré, D, et al. "Expression of Estrogen Sulfotransferase 1E1 and Steroid Sulfatase in Breast Cancer: A Immunohistochemical Study." Breast cancer : basic and clinical research vol. 3 (2009): 9-21. doi: https://doi.org/10.4137/bcbcr.s2012
Poisson Paré D, Song D, Luu-The V, Han B, Li S, Liu G, Labrie F, Pelletier G. Expression of Estrogen Sulfotransferase 1E1 and Steroid Sulfatase in Breast Cancer: A Immunohistochemical Study. Breast Cancer (Auckl). 2009 Mar 20;3:9-21. doi: 10.4137/bcbcr.s2012. PMID: 21556246; PMCID: PMC3086308.
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Expression of 5α-reductase type 1 in breast cancer and adjacent non-malignant tissue: an immunohistochemical study.

Hormone molecular biology and clinical investigation

Zhao G, Lu L, Luu-The V, Fan Z, Labrie F, Pelletier G.
PMID: 25961212
Horm Mol Biol Clin Investig. 2010 Dec 01;3(2):411-5. doi: 10.1515/HMBCI.2010.046.

Intratumoral biosynthesis of sex steroids is thought to play a role in the pathogenesis and development of human breast cancer. There is evidence that androgens can inhibit the development and progression of breast cancer. Among the enzymes involved in...

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Zhao G, Lu L, Luu-The V, et al. Expression of 5α-reductase type 1 in breast cancer and adjacent non-malignant tissue: an immunohistochemical study. Horm Mol Biol Clin Investig. 2010;3(2):411-5doi: 10.1515/HMBCI.2010.046.
Zhao, G., Lu, L., Luu-The, V., Fan, Z., Labrie, F., & Pelletier, G. (2010). Expression of 5α-reductase type 1 in breast cancer and adjacent non-malignant tissue: an immunohistochemical study. Hormone molecular biology and clinical investigation, 3(2), 411-5. https://doi.org/10.1515/HMBCI.2010.046
Zhao, Gang, et al. "Expression of 5α-reductase type 1 in breast cancer and adjacent non-malignant tissue: an immunohistochemical study." Hormone molecular biology and clinical investigation vol. 3,2 (2010): 411-5. doi: https://doi.org/10.1515/HMBCI.2010.046
Zhao G, Lu L, Luu-The V, Fan Z, Labrie F, Pelletier G. Expression of 5α-reductase type 1 in breast cancer and adjacent non-malignant tissue: an immunohistochemical study. Horm Mol Biol Clin Investig. 2010 Dec 01;3(2):411-5. doi: 10.1515/HMBCI.2010.046. PMID: 25961212.
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Target deletion of the bifunctional type 12 17β-hydroxysteroid dehydrogenase in mice results in reduction of androgen and estrogen levels in heterozygotes and embryonic lethality in homozygotes.

Hormone molecular biology and clinical investigation

Bellemare V, Phaneuf D, Luu-The V.
PMID: 25961203
Horm Mol Biol Clin Investig. 2010 Aug 01;2(3):311-8. doi: 10.1515/HMBCI.2010.036.

17β-Hydroxysteroid dehydrogenases (17β-HSDs) are enzymes issued from convergent evolution of activity from various ancestral genes having different functions. Type 12 17β-HSD (17β-HSD12) was described as a bifunctional enzyme, involved in the biosynthesis of estradiol (E2) and the elongation of...

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Bellemare V, Phaneuf D, Luu-The V. Target deletion of the bifunctional type 12 17β-hydroxysteroid dehydrogenase in mice results in reduction of androgen and estrogen levels in heterozygotes and embryonic lethality in homozygotes. Horm Mol Biol Clin Investig. 2010;2(3):311-8doi: 10.1515/HMBCI.2010.036.
Bellemare, V., Phaneuf, D., & Luu-The, V. (2010). Target deletion of the bifunctional type 12 17β-hydroxysteroid dehydrogenase in mice results in reduction of androgen and estrogen levels in heterozygotes and embryonic lethality in homozygotes. Hormone molecular biology and clinical investigation, 2(3), 311-8. https://doi.org/10.1515/HMBCI.2010.036
Bellemare, Véronique, et al. "Target deletion of the bifunctional type 12 17β-hydroxysteroid dehydrogenase in mice results in reduction of androgen and estrogen levels in heterozygotes and embryonic lethality in homozygotes." Hormone molecular biology and clinical investigation vol. 2,3 (2010): 311-8. doi: https://doi.org/10.1515/HMBCI.2010.036
Bellemare V, Phaneuf D, Luu-The V. Target deletion of the bifunctional type 12 17β-hydroxysteroid dehydrogenase in mice results in reduction of androgen and estrogen levels in heterozygotes and embryonic lethality in homozygotes. Horm Mol Biol Clin Investig. 2010 Aug 01;2(3):311-8. doi: 10.1515/HMBCI.2010.036. PMID: 25961203.
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Sequential transformation of 4-androstenedione into dihydrotestosterone in prostate carcinoma (DU-145) cells indicates that 4-androstenedione and not testosterone is the substrate of 5α-reductase.

Hormone molecular biology and clinical investigation

Samson M, Labrie F, Luu-The V.
PMID: 25961972
Horm Mol Biol Clin Investig. 2010 Jan 01;1(2):67-72. doi: 10.1515/HMBCI.2010.009.

BACKGROUND: Although it is well recognized that 5α-reductases possess higher affinity for 4-androstenedione than testosterone, and the affinity of 4-androstenedione is higher for 5α-reductases than 17β-hydroxysteroid dehydrogenases, it is generally believed that dihydrotestosterone is necessarily produced by the transformation...

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Samson M, Labrie F, Luu-The V. Sequential transformation of 4-androstenedione into dihydrotestosterone in prostate carcinoma (DU-145) cells indicates that 4-androstenedione and not testosterone is the substrate of 5α-reductase. Horm Mol Biol Clin Investig. 2010;1(2):67-72doi: 10.1515/HMBCI.2010.009.
Samson, M., Labrie, F., & Luu-The, V. (2010). Sequential transformation of 4-androstenedione into dihydrotestosterone in prostate carcinoma (DU-145) cells indicates that 4-androstenedione and not testosterone is the substrate of 5α-reductase. Hormone molecular biology and clinical investigation, 1(2), 67-72. https://doi.org/10.1515/HMBCI.2010.009
Samson, Melanie, et al. "Sequential transformation of 4-androstenedione into dihydrotestosterone in prostate carcinoma (DU-145) cells indicates that 4-androstenedione and not testosterone is the substrate of 5α-reductase." Hormone molecular biology and clinical investigation vol. 1,2 (2010): 67-72. doi: https://doi.org/10.1515/HMBCI.2010.009
Samson M, Labrie F, Luu-The V. Sequential transformation of 4-androstenedione into dihydrotestosterone in prostate carcinoma (DU-145) cells indicates that 4-androstenedione and not testosterone is the substrate of 5α-reductase. Horm Mol Biol Clin Investig. 2010 Jan 01;1(2):67-72. doi: 10.1515/HMBCI.2010.009. PMID: 25961972.
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Human type 3 5α-reductase is expressed in peripheral tissues at higher levels than types 1 and 2 and its activity is potently inhibited by finasteride and dutasteride.

Hormone molecular biology and clinical investigation

Yamana K, Labrie F, Luu-The V.
PMID: 25961201
Horm Mol Biol Clin Investig. 2010 Aug 01;2(3):293-9. doi: 10.1515/HMBCI.2010.035.

5α-Reductases are crucial enzymes involved in the biosynthesis of dihydrotestosterone, the most potent natural androgen. To date, three types of 5α-reductases, chronologically named types 1, 2 and 3 5α-reductases (SRD5a-1, 2 and 3) have been described. In the present...

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Yamana K, Labrie F, Luu-The V. Human type 3 5α-reductase is expressed in peripheral tissues at higher levels than types 1 and 2 and its activity is potently inhibited by finasteride and dutasteride. Horm Mol Biol Clin Investig. 2010;2(3):293-9doi: 10.1515/HMBCI.2010.035.
Yamana, K., Labrie, F., & Luu-The, V. (2010). Human type 3 5α-reductase is expressed in peripheral tissues at higher levels than types 1 and 2 and its activity is potently inhibited by finasteride and dutasteride. Hormone molecular biology and clinical investigation, 2(3), 293-9. https://doi.org/10.1515/HMBCI.2010.035
Yamana, Kazutoshi, et al. "Human type 3 5α-reductase is expressed in peripheral tissues at higher levels than types 1 and 2 and its activity is potently inhibited by finasteride and dutasteride." Hormone molecular biology and clinical investigation vol. 2,3 (2010): 293-9. doi: https://doi.org/10.1515/HMBCI.2010.035
Yamana K, Labrie F, Luu-The V. Human type 3 5α-reductase is expressed in peripheral tissues at higher levels than types 1 and 2 and its activity is potently inhibited by finasteride and dutasteride. Horm Mol Biol Clin Investig. 2010 Aug 01;2(3):293-9. doi: 10.1515/HMBCI.2010.035. PMID: 25961201.
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Microbiological Safety of Ready-to-Eat Foods in Hospital and University Canteens in Hanoi, Vietnam.

Journal of food protection

Luu-Thi H, Michiels CW.
PMID: 34189563
J Food Prot. 2021 Nov 01;84(11):1915-1921. doi: 10.4315/JFP-20-324.

No abstract available.

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Luu-Thi H, Michiels CW. Microbiological Safety of Ready-to-Eat Foods in Hospital and University Canteens in Hanoi, Vietnam. J Food Prot. 2021;84(11):1915-1921doi: 10.4315/JFP-20-324.
Luu-Thi, H., & Michiels, C. W. (2021). Microbiological Safety of Ready-to-Eat Foods in Hospital and University Canteens in Hanoi, Vietnam. Journal of food protection, 84(11), 1915-1921. https://doi.org/10.4315/JFP-20-324
Luu-Thi, Hue, and Michiels, Chris W. "Microbiological Safety of Ready-to-Eat Foods in Hospital and University Canteens in Hanoi, Vietnam." Journal of food protection vol. 84,11 (2021): 1915-1921. doi: https://doi.org/10.4315/JFP-20-324
Luu-Thi H, Michiels CW. Microbiological Safety of Ready-to-Eat Foods in Hospital and University Canteens in Hanoi, Vietnam. J Food Prot. 2021 Nov 01;84(11):1915-1921. doi: 10.4315/JFP-20-324. PMID: 34189563.
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Neurosteroid biosynthesis in the brain of amphibians.

Frontiers in endocrinology

Vaudry H, Do Rego JL, Burel D, Luu-The V, Pelletier G, Vaudry D, Tsutsui K.
PMID: 22649387
Front Endocrinol (Lausanne). 2011 Nov 30;2:79. doi: 10.3389/fendo.2011.00079. eCollection 2011.

Amphibians have been widely used to investigate the synthesis of biologically active steroids in the brain and the regulation of neurosteroid production by neurotransmitters and neuropeptides. The aim of the present review is to summarize the current knowledge regarding...

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Vaudry H, Do Rego JL, Burel D, et al. Neurosteroid biosynthesis in the brain of amphibians. Front Endocrinol (Lausanne). 2011;2:79doi: 10.3389/fendo.2011.00079.
Vaudry, H., Do Rego, J. L., Burel, D., Luu-The, V., Pelletier, G., Vaudry, D., & Tsutsui, K. (2011). Neurosteroid biosynthesis in the brain of amphibians. Frontiers in endocrinology, 279. https://doi.org/10.3389/fendo.2011.00079
Vaudry, Hubert, et al. "Neurosteroid biosynthesis in the brain of amphibians." Frontiers in endocrinology vol. 2 (2011): 79. doi: https://doi.org/10.3389/fendo.2011.00079
Vaudry H, Do Rego JL, Burel D, Luu-The V, Pelletier G, Vaudry D, Tsutsui K. Neurosteroid biosynthesis in the brain of amphibians. Front Endocrinol (Lausanne). 2011 Nov 30;2:79. doi: 10.3389/fendo.2011.00079. eCollection 2011. PMID: 22649387; PMCID: PMC3355965.
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Regulation of neurosteroid biosynthesis by neurotransmitters and neuropeptides.

Frontiers in endocrinology

Do Rego JL, Seong JY, Burel D, Leprince J, Vaudry D, Luu-The V, Tonon MC, Tsutsui K, Pelletier G, Vaudry H.
PMID: 22654849
Front Endocrinol (Lausanne). 2012 Jan 24;3:4. doi: 10.3389/fendo.2012.00004. eCollection 2012.

The enzymatic pathways leading to the synthesis of bioactive steroids in the brain are now almost completely elucidated in various groups of vertebrates and, during the last decade, the neuronal mechanisms involved in the regulation of neurosteroid production have...

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Do Rego JL, Seong JY, Burel D, et al. Regulation of neurosteroid biosynthesis by neurotransmitters and neuropeptides. Front Endocrinol (Lausanne). 2012;3:4doi: 10.3389/fendo.2012.00004.
Do Rego, J. L., Seong, J. Y., Burel, D., Leprince, J., Vaudry, D., Luu-The, V., Tonon, M. C., Tsutsui, K., Pelletier, G., & Vaudry, H. (2012). Regulation of neurosteroid biosynthesis by neurotransmitters and neuropeptides. Frontiers in endocrinology, 34. https://doi.org/10.3389/fendo.2012.00004
Do Rego, Jean Luc, et al. "Regulation of neurosteroid biosynthesis by neurotransmitters and neuropeptides." Frontiers in endocrinology vol. 3 (2012): 4. doi: https://doi.org/10.3389/fendo.2012.00004
Do Rego JL, Seong JY, Burel D, Leprince J, Vaudry D, Luu-The V, Tonon MC, Tsutsui K, Pelletier G, Vaudry H. Regulation of neurosteroid biosynthesis by neurotransmitters and neuropeptides. Front Endocrinol (Lausanne). 2012 Jan 24;3:4. doi: 10.3389/fendo.2012.00004. eCollection 2012. PMID: 22654849; PMCID: PMC3356045.
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