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Antipeptide polyclonal antibodies specifically recognize each human thyroid hormone receptor isoform.

Endocrinology

Falcone M, Miyamoto T, Fierro-Renoy F, Macchia E, DeGroot LJ.
PMID: 1425440
Endocrinology. 1992 Nov;131(5):2419-29. doi: 10.1210/endo.131.5.1425440.

We characterized four antipeptide polyclonal antibodies (abs) able to specifically recognize each thyroid hormone receptor (TR) isoform. The abs immunoprecipitated both the in vitro synthesized receptor and the receptor expressed in E. coli and their specificity was confirmed by...

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Falcone M, Miyamoto T, Fierro-Renoy F, et al. Antipeptide polyclonal antibodies specifically recognize each human thyroid hormone receptor isoform. Endocrinology. 1992;131(5):2419-29doi: 10.1210/endo.131.5.1425440.
Falcone, M., Miyamoto, T., Fierro-Renoy, F., Macchia, E., & DeGroot, L. J. (1992). Antipeptide polyclonal antibodies specifically recognize each human thyroid hormone receptor isoform. Endocrinology, 131(5), 2419-29. https://doi.org/10.1210/endo.131.5.1425440
Falcone, M, et al. "Antipeptide polyclonal antibodies specifically recognize each human thyroid hormone receptor isoform." Endocrinology vol. 131,5 (1992): 2419-29. doi: https://doi.org/10.1210/endo.131.5.1425440
Falcone M, Miyamoto T, Fierro-Renoy F, Macchia E, DeGroot LJ. Antipeptide polyclonal antibodies specifically recognize each human thyroid hormone receptor isoform. Endocrinology. 1992 Nov;131(5):2419-29. doi: 10.1210/endo.131.5.1425440. PMID: 1425440.
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Carbohydrate moiety of follitropin receptor is not required for high affinity hormone-binding or for functional coupling between receptor and guanine nucleotide-binding protein in bovine calf testis membranes.

Endocrinology

Dattatreyamurty B, Reichert LE.
PMID: 1425441
Endocrinology. 1992 Nov;131(5):2437-45. doi: 10.1210/endo.131.5.1425441.

Previously, we have extensively studied FSH-receptor interactions using bovine calf testis membranes, and demonstrated that the high-affinity FSH binding to receptors and coupling of FSH receptors with guanine nucleotide-binding protein (Gs protein) in a GTP-sensitive state are important initial...

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Dattatreyamurty B, Reichert LE. Carbohydrate moiety of follitropin receptor is not required for high affinity hormone-binding or for functional coupling between receptor and guanine nucleotide-binding protein in bovine calf testis membranes. Endocrinology. 1992;131(5):2437-45doi: 10.1210/endo.131.5.1425441.
Dattatreyamurty, B., & Reichert, L. E. (1992). Carbohydrate moiety of follitropin receptor is not required for high affinity hormone-binding or for functional coupling between receptor and guanine nucleotide-binding protein in bovine calf testis membranes. Endocrinology, 131(5), 2437-45. https://doi.org/10.1210/endo.131.5.1425441
Dattatreyamurty, B, and Reichert, L E. "Carbohydrate moiety of follitropin receptor is not required for high affinity hormone-binding or for functional coupling between receptor and guanine nucleotide-binding protein in bovine calf testis membranes." Endocrinology vol. 131,5 (1992): 2437-45. doi: https://doi.org/10.1210/endo.131.5.1425441
Dattatreyamurty B, Reichert LE. Carbohydrate moiety of follitropin receptor is not required for high affinity hormone-binding or for functional coupling between receptor and guanine nucleotide-binding protein in bovine calf testis membranes. Endocrinology. 1992 Nov;131(5):2437-45. doi: 10.1210/endo.131.5.1425441. PMID: 1425441.
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Ultrastructural studies on testicular biopsies from eighteen cases of hypospermatogenesis.

Fertility and sterility

Narbaitz R, Tolnai G, Jolly EE, Barwin N, McKay DE.
PMID: 729828
Fertil Steril. 1978 Dec;30(6):679-86. doi: 10.1016/s0015-0282(16)43696-4.

An electron microscopic study was conducted on biopsies from 18 young hypospermatogenic patients. No signs of "tubular blockage" or "germinal disorganization" were found. The relationships between the different components of the germinal epithelium were comparable to those found in...

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Narbaitz R, Tolnai G, Jolly EE, et al. Ultrastructural studies on testicular biopsies from eighteen cases of hypospermatogenesis. Fertil Steril. 1978;30(6):679-86doi: 10.1016/s0015-0282(16)43696-4.
Narbaitz, R., Tolnai, G., Jolly, E. E., Barwin, N., & McKay, D. E. (1978). Ultrastructural studies on testicular biopsies from eighteen cases of hypospermatogenesis. Fertility and sterility, 30(6), 679-86. https://doi.org/10.1016/s0015-0282(16)43696-4
Narbaitz, R, et al. "Ultrastructural studies on testicular biopsies from eighteen cases of hypospermatogenesis." Fertility and sterility vol. 30,6 (1978): 679-86. doi: https://doi.org/10.1016/s0015-0282(16)43696-4
Narbaitz R, Tolnai G, Jolly EE, Barwin N, McKay DE. Ultrastructural studies on testicular biopsies from eighteen cases of hypospermatogenesis. Fertil Steril. 1978 Dec;30(6):679-86. doi: 10.1016/s0015-0282(16)43696-4. PMID: 729828.
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Nonhomologous associations of C-heterochromatin at human male meitoic prophase.

Cytogenetics and cell genetics

Driscoll DJ, Palmer CG, Melman A.
PMID: 761482
Cytogenet Cell Genet. 1979;23(1):23-32. doi: 10.1159/000131298.

In human male meiotic prophase, nonhomologous pairings and connections between C-heterochromatic regions were demonstrated by C-banding and G-11 staining. Approximately 40% of the pachytene stages exhibited bivalent associations at regions of C-heterochromatin. Nonhomologous associations were seen between all possible...

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Driscoll DJ, Palmer CG, Melman A. Nonhomologous associations of C-heterochromatin at human male meitoic prophase. Cytogenet Cell Genet. 1979;23(1):23-32doi: 10.1159/000131298.
Driscoll, D. J., Palmer, C. G., & Melman, A. (1979). Nonhomologous associations of C-heterochromatin at human male meitoic prophase. Cytogenetics and cell genetics, 23(1), 23-32. https://doi.org/10.1159/000131298
Driscoll, D J, et al. "Nonhomologous associations of C-heterochromatin at human male meitoic prophase." Cytogenetics and cell genetics vol. 23,1 (1979): 23-32. doi: https://doi.org/10.1159/000131298
Driscoll DJ, Palmer CG, Melman A. Nonhomologous associations of C-heterochromatin at human male meitoic prophase. Cytogenet Cell Genet. 1979;23(1):23-32. doi: 10.1159/000131298. PMID: 761482.
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Effect of temperature and pregnant mare's serum gonadotropin on testicular function in the spiny-tailed lizard, Uromastix hardwicki.

General and comparative endocrinology

Jalali S, Arslan M, Qureshi S, Qazi MH.
PMID: 992336
Gen Comp Endocrinol. 1976 Oct;30(2):162-70. doi: 10.1016/0016-6480(76)90095-2.

No abstract available.

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Jalali S, Arslan M, Qureshi S, et al. Effect of temperature and pregnant mare's serum gonadotropin on testicular function in the spiny-tailed lizard, Uromastix hardwicki. Gen Comp Endocrinol. 1976;30(2):162-70doi: 10.1016/0016-6480(76)90095-2.
Jalali, S., Arslan, M., Qureshi, S., & Qazi, M. H. (1976). Effect of temperature and pregnant mare's serum gonadotropin on testicular function in the spiny-tailed lizard, Uromastix hardwicki. General and comparative endocrinology, 30(2), 162-70. https://doi.org/10.1016/0016-6480(76)90095-2
Jalali, S, et al. "Effect of temperature and pregnant mare's serum gonadotropin on testicular function in the spiny-tailed lizard, Uromastix hardwicki." General and comparative endocrinology vol. 30,2 (1976): 162-70. doi: https://doi.org/10.1016/0016-6480(76)90095-2
Jalali S, Arslan M, Qureshi S, Qazi MH. Effect of temperature and pregnant mare's serum gonadotropin on testicular function in the spiny-tailed lizard, Uromastix hardwicki. Gen Comp Endocrinol. 1976 Oct;30(2):162-70. doi: 10.1016/0016-6480(76)90095-2. PMID: 992336.
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Changes in testicular morphology in boars actively immunized against gonadotropin hormone-releasing hormone.

Journal of andrology

Awoniyi CA, Chandrashekar V, Arthur RD, Schanbacher BD, Falvo RE.
PMID: 3042729
J Androl. 1988 May-Jun;9(3):160-71. doi: 10.1002/j.1939-4640.1988.tb01028.x.
Free Article

Alterations in testicular morphology were studied in boars actively immunized against gonadotropin hormone releasing hormone (GnRH). Ten boars were divided equally into two experimental groups (five GnRH-immunized, and five controls). Antibody production was achieved by conjugating GnRH to human...

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Awoniyi CA, Chandrashekar V, Arthur RD, et al. Changes in testicular morphology in boars actively immunized against gonadotropin hormone-releasing hormone. J Androl. 1988;9(3):160-71doi: 10.1002/j.1939-4640.1988.tb01028.x.
Awoniyi, C. A., Chandrashekar, V., Arthur, R. D., Schanbacher, B. D., & Falvo, R. E. (1988). Changes in testicular morphology in boars actively immunized against gonadotropin hormone-releasing hormone. Journal of andrology, 9(3), 160-71. https://doi.org/10.1002/j.1939-4640.1988.tb01028.x
Awoniyi, C A, et al. "Changes in testicular morphology in boars actively immunized against gonadotropin hormone-releasing hormone." Journal of andrology vol. 9,3 (1988): 160-71. doi: https://doi.org/10.1002/j.1939-4640.1988.tb01028.x
Awoniyi CA, Chandrashekar V, Arthur RD, Schanbacher BD, Falvo RE. Changes in testicular morphology in boars actively immunized against gonadotropin hormone-releasing hormone. J Androl. 1988 May-Jun;9(3):160-71. doi: 10.1002/j.1939-4640.1988.tb01028.x. PMID: 3042729.
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[Ultrastructural study of the testis in 22 persons based on the effect of gossypol].

Zhonghua bing li xue za zhi = Chinese journal of pathology

YU TW.
PMID: 2957085
Zhonghua Bing Li Xue Za Zhi. 1987 Mar;16(1):60-1.

No abstract available.

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YU TW. [Ultrastructural study of the testis in 22 persons based on the effect of gossypol]. Zhonghua Bing Li Xue Za Zhi. 1987;16(1):60-1
YU, T. W. (1987). [Ultrastructural study of the testis in 22 persons based on the effect of gossypol]. Zhonghua bing li xue za zhi = Chinese journal of pathology, 16(1), 60-1.
YU, T W. "[Ultrastructural study of the testis in 22 persons based on the effect of gossypol]." Zhonghua bing li xue za zhi = Chinese journal of pathology vol. 16,1 (1987): 60-1.
YU TW. [Ultrastructural study of the testis in 22 persons based on the effect of gossypol]. Zhonghua Bing Li Xue Za Zhi. 1987 Mar;16(1):60-1. Chinese. PMID: 2957085.
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Inhibition of spermatogenesis.

Basic life sciences

Frick J, Bartsch G.
PMID: 4447575
Basic Life Sci. 1974;4:259-71. doi: 10.1007/978-1-4684-2889-6_17.

No abstract available.

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Frick J, Bartsch G. Inhibition of spermatogenesis. Basic Life Sci. 1974;4:259-71doi: 10.1007/978-1-4684-2889-6_17.
Frick, J., & Bartsch, G. (1974). Inhibition of spermatogenesis. Basic life sciences, 4259-71. https://doi.org/10.1007/978-1-4684-2889-6_17
Frick, J, and Bartsch, G. "Inhibition of spermatogenesis." Basic life sciences vol. 4 (1974): 259-71. doi: https://doi.org/10.1007/978-1-4684-2889-6_17
Frick J, Bartsch G. Inhibition of spermatogenesis. Basic Life Sci. 1974;4:259-71. doi: 10.1007/978-1-4684-2889-6_17. PMID: 4447575.
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Dictyosome-like structures from guinea-pig testes lack galactosyltransferase, a Golgi apparatus marker.

Cell and tissue research

Morré DJ, Matyas GR, Mollenhauer HH.
PMID: 3922620
Cell Tissue Res. 1985;240(1):35-40. doi: 10.1007/BF00217555.

More than twenty different enzyme activities of fractions containing dictyosome-like structures (DLS) as a dominant cell component were monitored. Plasma membrane vesicles were a major contaminant of the DLS fractions, which, presumably as a consequence, were enriched somewhat in...

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Morré DJ, Matyas GR, Mollenhauer HH. Dictyosome-like structures from guinea-pig testes lack galactosyltransferase, a Golgi apparatus marker. Cell Tissue Res. 1985;240(1):35-40doi: 10.1007/BF00217555.
Morré, D. J., Matyas, G. R., & Mollenhauer, H. H. (1985). Dictyosome-like structures from guinea-pig testes lack galactosyltransferase, a Golgi apparatus marker. Cell and tissue research, 240(1), 35-40. https://doi.org/10.1007/BF00217555
Morré, D J, et al. "Dictyosome-like structures from guinea-pig testes lack galactosyltransferase, a Golgi apparatus marker." Cell and tissue research vol. 240,1 (1985): 35-40. doi: https://doi.org/10.1007/BF00217555
Morré DJ, Matyas GR, Mollenhauer HH. Dictyosome-like structures from guinea-pig testes lack galactosyltransferase, a Golgi apparatus marker. Cell Tissue Res. 1985;240(1):35-40. doi: 10.1007/BF00217555. PMID: 3922620.
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[Morphology of peritubular structures of the seminiferous tubule in children. An electron microscopic study].

Zeitschrift fur mikroskopisch-anatomische Forschung

Seguchi H, Hadziselimovic F.
PMID: 4466145
Z Mikrosk Anat Forsch. 1974;88(6):1149-60.

No abstract available.

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Seguchi H, Hadziselimovic F. Morphologie der peritubulären Strukturen des Tubulus seminiferus bei Kindern. Eine elektronenmikroskopische Studie [Morphology of peritubular structures of the seminiferous tubule in children. An electron microscopic study]. Z Mikrosk Anat Forsch. 1974;88(6):1149-60
Seguchi, H., & Hadziselimovic, F. (1974). Morphologie der peritubulären Strukturen des Tubulus seminiferus bei Kindern. Eine elektronenmikroskopische Studie [Morphology of peritubular structures of the seminiferous tubule in children. An electron microscopic study]. Zeitschrift fur mikroskopisch-anatomische Forschung, 88(6), 1149-60.
Seguchi, H, and Hadziselimovic, F. "Morphologie der peritubulären Strukturen des Tubulus seminiferus bei Kindern. Eine elektronenmikroskopische Studie" [Morphology of peritubular structures of the seminiferous tubule in children. An electron microscopic study]. Zeitschrift fur mikroskopisch-anatomische Forschung vol. 88,6 (1974): 1149-60.
Seguchi H, Hadziselimovic F. Morphologie der peritubulären Strukturen des Tubulus seminiferus bei Kindern. Eine elektronenmikroskopische Studie [Morphology of peritubular structures of the seminiferous tubule in children. An electron microscopic study]. Z Mikrosk Anat Forsch. 1974;88(6):1149-60. German. PMID: 4466145.
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Three Drosophila beta-tubulin sequences: a developmentally regulated isoform (beta 3), the testis-specific isoform (beta 2), and an assembly-defective mutation of the testis-specific isoform (B2t8) reveal both an ancient divergence in metazoan isotypes and structural constraints for beta-tubulin function.

Molecular and cellular biology

Rudolph JE, Kimble M, Hoyle HD, Subler MA, Raff EC.
PMID: 3037352
Mol Cell Biol. 1987 Jun;7(6):2231-42. doi: 10.1128/mcb.7.6.2231-2242.1987.
Free PMC Article

The genomic DNA sequence and deduced amino acid sequence are presented for three Drosophila melanogaster beta-tubulins: a developmentally regulated isoform beta 3-tubulin, the wild-type testis-specific isoform beta 2-tubulin, and an ethyl methanesulfonate-induced assembly-defective mutation of the testis isoform, B2t8....

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Rudolph JE, Kimble M, Hoyle HD, et al. Three Drosophila beta-tubulin sequences: a developmentally regulated isoform (beta 3), the testis-specific isoform (beta 2), and an assembly-defective mutation of the testis-specific isoform (B2t8) reveal both an ancient divergence in metazoan isotypes and structural constraints for beta-tubulin function. Mol Cell Biol. 1987;7(6):2231-42doi: 10.1128/mcb.7.6.2231-2242.1987.
Rudolph, J. E., Kimble, M., Hoyle, H. D., Subler, M. A., & Raff, E. C. (1987). Three Drosophila beta-tubulin sequences: a developmentally regulated isoform (beta 3), the testis-specific isoform (beta 2), and an assembly-defective mutation of the testis-specific isoform (B2t8) reveal both an ancient divergence in metazoan isotypes and structural constraints for beta-tubulin function. Molecular and cellular biology, 7(6), 2231-42. https://doi.org/10.1128/mcb.7.6.2231-2242.1987
Rudolph, J E, et al. "Three Drosophila beta-tubulin sequences: a developmentally regulated isoform (beta 3), the testis-specific isoform (beta 2), and an assembly-defective mutation of the testis-specific isoform (B2t8) reveal both an ancient divergence in metazoan isotypes and structural constraints for beta-tubulin function." Molecular and cellular biology vol. 7,6 (1987): 2231-42. doi: https://doi.org/10.1128/mcb.7.6.2231-2242.1987
Rudolph JE, Kimble M, Hoyle HD, Subler MA, Raff EC. Three Drosophila beta-tubulin sequences: a developmentally regulated isoform (beta 3), the testis-specific isoform (beta 2), and an assembly-defective mutation of the testis-specific isoform (B2t8) reveal both an ancient divergence in metazoan isotypes and structural constraints for beta-tubulin function. Mol Cell Biol. 1987 Jun;7(6):2231-42. doi: 10.1128/mcb.7.6.2231-2242.1987. PMID: 3037352; PMCID: PMC365347.
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Local regulation of testicular function.

International review of cytology

de Kretser DM.
PMID: 3323108
Int Rev Cytol. 1987;109:89-112. doi: 10.1016/s0074-7696(08)61720-9.

No abstract available.

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de Kretser DM. Local regulation of testicular function. Int Rev Cytol. 1987;109:89-112doi: 10.1016/s0074-7696(08)61720-9.
de Kretser, D. M. (1987). Local regulation of testicular function. International review of cytology, 10989-112. https://doi.org/10.1016/s0074-7696(08)61720-9
de Kretser, D M. "Local regulation of testicular function." International review of cytology vol. 109 (1987): 89-112. doi: https://doi.org/10.1016/s0074-7696(08)61720-9
de Kretser DM. Local regulation of testicular function. Int Rev Cytol. 1987;109:89-112. doi: 10.1016/s0074-7696(08)61720-9. PMID: 3323108.
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Showing 1 to 12 of 2257 entries