Testosterone

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(New page: Testosterone Pubchem(6013) A potent androgenic steroid and major product secreted by the LEYDIG CELLS of the TESTIS. Its production is stimulated by LUTEINIZING HORMONE from the PITUITARY ...)
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Activity Androgen
Activity Androgen
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MMDB ID: 15896
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|15896
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PDB ID: 1I37
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|1I37
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Reference: Sack JS, Kish KF, Wang C, Attar RM, Kiefer SE, An Y, Wu GY, Scheffler JE, Salvati ME, Krystek SR Jr, Weinmann R, Einspahr HMCrystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosteroneProc. Natl. Acad. Sci. U. S. A. v98, p.4904-4909
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|Sack JS, Kish KF, Wang C, Attar RM, Kiefer SE, An Y, Wu GY, Scheffler JE, Salvati ME, Krystek SR Jr, Weinmann R, Einspahr HMCrystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosteroneProc. Natl. Acad. Sci. U. S. A. v98, p.4904-4909
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The structures of the ligand-binding domains (LBD) of the wild-type androgen receptor (AR) and the T877A mutant corresponding to that in LNCaP cells, both bound to dihydrotestosterone, have been refined at 2.0 A resolution. In contrast to the homodimer seen in the retinoid-X receptor and estrogen receptor LBD structures, the AR LBD is monomeric, possibly because of the extended C terminus of AR, which lies in a groove at the dimerization interface....
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|15897
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MMDB ID: 15897
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|1I38
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PDB ID: 1I38
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|Sack JS, Kish KF, Wang C, Attar RM, Kiefer SE, An Y, Wu GY, Scheffler JE, Salvati ME, Krystek SR Jr, Weinmann R, Einspahr HMCrystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosteroneProc. Natl. Acad. Sci. U. S. A. v98, p.4904-4909
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Reference: Sack JS, Kish KF, Wang C, Attar RM, Kiefer SE, An Y, Wu GY, Scheffler JE, Salvati ME, Krystek SR Jr, Weinmann R, Einspahr HMCrystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosteroneProc. Natl. Acad. Sci. U. S. A. v98, p.4904-4909
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|-
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The structures of the ligand-binding domains (LBD) of the wild-type androgen receptor (AR) and the T877A mutant corresponding to that in LNCaP cells, both bound to dihydrotestosterone, have been refined at 2.0 A resolution. In contrast to the homodimer seen in the retinoid-X receptor and estrogen receptor LBD structures, the AR LBD is monomeric, possibly because of the extended C terminus of AR, which lies in a groove at the dimerization interface....
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|18740
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|1I9J
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MMDB ID: 18740
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|Valjakka J, Takkinenz K, Teerinen T, Soderlund H, Rouvinen JStructural insights into steroid hormone binding: the crystal structure of a recombinant anti-testosterone Fab fragment in free and testosterone-bound formsJ. Biol. Chem. v277, p.4183-4190
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PDB ID: 1I9J
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Reference: Valjakka J, Takkinenz K, Teerinen T, Soderlund H, Rouvinen JStructural insights into steroid hormone binding: the crystal structure of a recombinant anti-testosterone Fab fragment in free and testosterone-bound formsJ. Biol. Chem. v277, p.4183-4190
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|19484
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The monoclonal anti-testosterone antibody (3-C(4)F(5)) has a relatively high affinity (3 x 10(8) m(-1)) with an overall good specificity profile. However, the earlier characterized binding properties have shown that both the affinity and specificity of this antibody must be improved if it is intended for use in clinical immunoassays....
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|1J96
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|Nahoum V, Gangloff A, Legrand P, Zhu DW, Cantin L, Zhorov BS, Luu-The V, Labrie F, Breton R, Lin SXStructure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolutionJ. Biol. Chem. v276, p.42091-42098
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MMDB ID: 19484
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|-
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PDB ID: 1J96
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|30244
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Reference: Nahoum V, Gangloff A, Legrand P, Zhu DW, Cantin L, Zhorov BS, Luu-The V, Labrie F, Breton R, Lin SXStructure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolutionJ. Biol. Chem. v276, p.42091-42098
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|1Q13
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The first crystallographic structure of human type 3 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD3, AKR1C2), an enzyme playing a critical role in steroid hormone metabolism, has been determined in complex with testosterone and NADP at 1.25-A resolution. The enzyme"s 17beta-HSD activity was studied in comparison with its 3alpha-HSD activity....
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|Couture JF, Legrand P, Cantin L, Labrie F, Luu-The V, Breton RLoop relaxation, a mechanism that explains the reduced specificity of rabbit 20alpha-hydroxysteroid dehydrogenase, a member of the aldo-keto reductase superfamilyJ. Mol. Biol. v339, p.89-102
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MMDB ID: 30244
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|30428
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PDB ID: 1Q13
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|1VPO
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Reference: Couture JF, Legrand P, Cantin L, Labrie F, Luu-The V, Breton RLoop relaxation, a mechanism that explains the reduced specificity of rabbit 20alpha-hydroxysteroid dehydrogenase, a member of the aldo-keto reductase superfamilyJ. Mol. Biol. v339, p.89-102
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|Valjakka J, Hemminki A, Niemi S, Soderlund H, Takkinen K, Rouvinen JCrystal structure of an in vitro affinity- and specificity-matured anti-testosterone Fab in complex with testosterone. Improved affinity results from small structural changes within the variable domainsJ. Biol. Chem. v277, p.44021-44027
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The aldo-keto reductase rabbit 20alpha-hydroxysteroid dehydrogenase (rb20alpha-HSD; AKR1C5) is less selective than other HSDs, since it exerts its activity both on androgens (C19 steroids) and progestins (C21 steroids). In order to identify the molecular determinants responsible for this reduced selectivity, binary (NADPH) and ternary (NADP(+)/testosterone) complex structures were solved to 1.32A and 2.08A resolution, respectively....
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|54139
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MMDB ID: 30428
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|2Q7I
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PDB ID: 1VPO
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|Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816
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Reference: Valjakka J, Hemminki A, Niemi S, Soderlund H, Takkinen K, Rouvinen JCrystal structure of an in vitro affinity- and specificity-matured anti-testosterone Fab in complex with testosterone. Improved affinity results from small structural changes within the variable domainsJ. Biol. Chem. v277, p.44021-44027
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A highly selective, high affinity recombinant anti-testosterone Fab fragment has been generated by stepwise optimization of the complementarity-determining regions (CDRs) by random mutagenesis and phage display selection of a monoclonal antibody (3-C(4)F(5)). The best mutant (77 Fab) was obtained by evaluating the additivity effects of different independently selected CDR mutations....
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|54140
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|2Q7J
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MMDB ID: 54139
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|Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816
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PDB ID: 2Q7I
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Reference: Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816
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|54141
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The androgen receptor (AR) is transcriptionally activated by high affinity binding of testosterone (T) or its 5alpha-reduced metabolite, dihydrotestosterone (DHT), a more potent androgen required for male reproductive tract development. The molecular basis for the weaker activity of T was investigated by determining T-bound ligand binding domain crystal structures of wild-type AR and a prostate cancer somatic mutant complexed with the AR FXXLF or coactivator LXXLL peptide....
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|2Q7K
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|Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816
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MMDB ID: 54140
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PDB ID: 2Q7J
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|54142
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Reference: Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816
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|2Q7L
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The androgen receptor (AR) is transcriptionally activated by high affinity binding of testosterone (T) or its 5alpha-reduced metabolite, dihydrotestosterone (DHT), a more potent androgen required for male reproductive tract development. The molecular basis for the weaker activity of T was investigated by determining T-bound ligand binding domain crystal structures of wild-type AR and a prostate cancer somatic mutant complexed with the AR FXXLF or coactivator LXXLL peptide....
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|Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816
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MMDB ID: 54141
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|6729
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PDB ID: 2Q7K
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|1AFS
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Reference: Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816
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|Bennett MJ, Albert RH, Jez JM, Ma H, Penning TM, Lewis MSteroid recognition and regulation of hormone action: crystal structure of testosterone and NADP+ bound to 3 alpha-hydroxysteroid/dihydrodiol dehydrogenaseStructure v5, p.799-812
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The androgen receptor (AR) is transcriptionally activated by high affinity binding of testosterone (T) or its 5alpha-reduced metabolite, dihydrotestosterone (DHT), a more potent androgen required for male reproductive tract development. The molecular basis for the weaker activity of T was investigated by determining T-bound ligand binding domain crystal structures of wild-type AR and a prostate cancer somatic mutant complexed with the AR FXXLF or coactivator LXXLL peptide....
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MMDB ID: 54142
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-
PDB ID: 2Q7L
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Reference: Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816
+
-
The androgen receptor (AR) is transcriptionally activated by high affinity binding of testosterone (T) or its 5alpha-reduced metabolite, dihydrotestosterone (DHT), a more potent androgen required for male reproductive tract development. The molecular basis for the weaker activity of T was investigated by determining T-bound ligand binding domain crystal structures of wild-type AR and a prostate cancer somatic mutant complexed with the AR FXXLF or coactivator LXXLL peptide....
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+
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MMDB ID: 6729
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-
PDB ID: 1AFS
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Reference: Bennett MJ, Albert RH, Jez JM, Ma H, Penning TM, Lewis MSteroid recognition and regulation of hormone action: crystal structure of testosterone and NADP+ bound to 3 alpha-hydroxysteroid/dihydrodiol dehydrogenaseStructure v5, p.799-812
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BACKGROUND: Mammalian 3 alpha-hydroxysteroid dehydrogenases (3 alpha-HSDs) modulate the activities of steroid hormones by reversibly reducing their C3 ketone groups. In steroid target tissues, 3 alpha-HSDs act on 5 alpha-dihydrotestosterone, a potent male sex hormone (androgen) implicated in benign prostate hyperplasia and prostate cancer....
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Physical Property  Value  Units  Temp (deg C)  Source
Physical Property  Value  Units  Temp (deg C)  Source

Revision as of 05:46, 30 October 2008

Testosterone Pubchem(6013) A potent androgenic steroid and major product secreted by the LEYDIG CELLS of the TESTIS. Its production is stimulated by LUTEINIZING HORMONE from the PITUITARY GLAND. In turn, testosterone exerts feedback control of the pituitary LH and FSH secretion. Depending on the tissues, testosterone can be further converted to DIHYDROTESTOSTERONE or ESTRADIOL.

KEGG Pathway(C00535,D00075) Androgen and estrogen metabolism Prostate cancer Activity Androgen

|15896 |1I37 |Sack JS, Kish KF, Wang C, Attar RM, Kiefer SE, An Y, Wu GY, Scheffler JE, Salvati ME, Krystek SR Jr, Weinmann R, Einspahr HMCrystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosteroneProc. Natl. Acad. Sci. U. S. A. v98, p.4904-4909 |- |15897 |1I38 |Sack JS, Kish KF, Wang C, Attar RM, Kiefer SE, An Y, Wu GY, Scheffler JE, Salvati ME, Krystek SR Jr, Weinmann R, Einspahr HMCrystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosteroneProc. Natl. Acad. Sci. U. S. A. v98, p.4904-4909 |- |18740 |1I9J |Valjakka J, Takkinenz K, Teerinen T, Soderlund H, Rouvinen JStructural insights into steroid hormone binding: the crystal structure of a recombinant anti-testosterone Fab fragment in free and testosterone-bound formsJ. Biol. Chem. v277, p.4183-4190 |- |19484 |1J96 |Nahoum V, Gangloff A, Legrand P, Zhu DW, Cantin L, Zhorov BS, Luu-The V, Labrie F, Breton R, Lin SXStructure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolutionJ. Biol. Chem. v276, p.42091-42098 |- |30244 |1Q13 |Couture JF, Legrand P, Cantin L, Labrie F, Luu-The V, Breton RLoop relaxation, a mechanism that explains the reduced specificity of rabbit 20alpha-hydroxysteroid dehydrogenase, a member of the aldo-keto reductase superfamilyJ. Mol. Biol. v339, p.89-102 |- |30428 |1VPO |Valjakka J, Hemminki A, Niemi S, Soderlund H, Takkinen K, Rouvinen JCrystal structure of an in vitro affinity- and specificity-matured anti-testosterone Fab in complex with testosterone. Improved affinity results from small structural changes within the variable domainsJ. Biol. Chem. v277, p.44021-44027 |- |54139 |2Q7I |Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816 |- |54140 |2Q7J |Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816 |- |54141 |2Q7K |Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816 |- |54142 |2Q7L |Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816 |- |6729 |1AFS |Bennett MJ, Albert RH, Jez JM, Ma H, Penning TM, Lewis MSteroid recognition and regulation of hormone action: crystal structure of testosterone and NADP+ bound to 3 alpha-hydroxysteroid/dihydrodiol dehydrogenaseStructure v5, p.799-812 |-

Physical Property Value Units Temp (deg C) Source Melting Point 155 deg C EXP log P (octanol-water) 3.32 (none) EXP Water Solubility 23.4 mg/L 25 EXP Vapor Pressure 2.23E-08 mm Hg 25 EST Henry's Law Constant 3.53E-09 atm-m3/mole 25 EST Atmospheric OH Rate Constant 1.07E-10 cm3/molecule-sec 25 EST

Organism Test Type Route Reported Dose (Normalized Dose) Effect Source mammal (species unspecified) LD50 oral > 5gm/kg (5000mg/kg) Toksikologicheskii Vestnik. Vol. (2), Pg. 6, 1996. rat LDLo intraperitoneal 326mg/kg (326mg/kg) LUNGS, THORAX, OR RESPIRATION: OTHER CHANGES Proceedings of the Society for Experimental Biology and Medicine. Vol. 46, Pg. 116, 1941.

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