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Volumn 44, Issue 12, 2005, Pages 4939-4948

Neuropeptide processing profile in mice lacking prohormone convertase-1

Author keywords

[No Author keywords available]

Indexed keywords

BRAIN; CHEMICAL ANALYSIS; HORMONES; IMMUNOLOGY; MASS SPECTROMETRY; MOLECULAR WEIGHT;

EID: 15444366205     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047852m     Document Type: Article
Times cited : (73)

References (59)
  • 3
    • 0026029553 scopus 로고
    • Consensus sequence for processing of peptide precursors at monobasic sites
    • Devi, L. (1991) Consensus sequence for processing of peptide precursors at monobasic sites, FEBS Lett. 280, 189-194.
    • (1991) FEBS Lett. , vol.280 , pp. 189-194
    • Devi, L.1
  • 4
    • 0033597852 scopus 로고    scopus 로고
    • Proteolytic processing in the secretory pathway
    • Zhou, A., Webb, G., Zhu, X., and Steiner, D. F. (1999) Proteolytic processing in the secretory pathway, J. Biol. Chem. 274, 20745-20748.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20745-20748
    • Zhou, A.1    Webb, G.2    Zhu, X.3    Steiner, D.F.4
  • 5
    • 0025284946 scopus 로고
    • DNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: Tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases
    • Seidah, N. G., Gaspar, L., Mion, P., Marcinkiewicz, M., Mbikay, M., and Chretien, M. (1990) cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases, DNA Cell Biol. 9, 415-424.
    • (1990) DNA Cell Biol. , vol.9 , pp. 415-424
    • Seidah, N.G.1    Gaspar, L.2    Mion, P.3    Marcinkiewicz, M.4    Mbikay, M.5    Chretien, M.6
  • 6
    • 0025214491 scopus 로고
    • Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2
    • Smeekens, S. P., and Steiner, D. F. (1990) Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2, J. Biol. Chem. 265, 2997-3000.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2997-3000
    • Smeekens, S.P.1    Steiner, D.F.2
  • 7
    • 0026088633 scopus 로고
    • Identification of a cDNA encoding a second putative prohormone convertase related to PC2 in AtT-20 cells and islets of Langerhans
    • Smeekens, S. P., Avruch, A. S., LaMendola, J., Chan, S. J., and Steiner, D. F. (1991) Identification of a cDNA encoding a second putative prohormone convertase related to PC2 in AtT-20 cells and islets of Langerhans, Proc. Natl. Acad. Sci. U.S.A. 88, 340-344.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 340-344
    • Smeekens, S.P.1    Avruch, A.S.2    LaMendola, J.3    Chan, S.J.4    Steiner, D.F.5
  • 8
    • 0001912912 scopus 로고    scopus 로고
    • Barrett, A. J., Rawlings, N. D., and Woessner, J. F., Eds. Academic Press, San Diego
    • Flicker, L. D. (1998) in Handbook of Proteolytic Enzymes (Barrett, A. J., Rawlings, N. D., and Woessner, J. F., Eds.) pp 1341-1344, Academic Press, San Diego.
    • (1998) Handbook of Proteolytic Enzymes , pp. 1341-1344
    • Flicker, L.D.1
  • 9
    • 0027765503 scopus 로고
    • Differential processing of proenkephalin by prohormone convertases 1(3) and 2 and furin
    • Breslin, M. B., Lindberg, I., Benjannet, S., Mathis, J. P., Lazure, C., and Seidah, N. G. (1993) Differential processing of proenkephalin by prohormone convertases 1(3) and 2 and furin, J. Biol. Chem. 268, 27084-27093.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27084-27093
    • Breslin, M.B.1    Lindberg, I.2    Benjannet, S.3    Mathis, J.P.4    Lazure, C.5    Seidah, N.G.6
  • 10
    • 0027488373 scopus 로고
    • The prohormone convertases PC1 and PC2 mediate distinct endoproteolytic cleavages in a strict temporal order during proopiomelanocortin biosynthetic processing
    • Zhou, A., Bloomquist, B. T., and Mains, R. E. (1993) The prohormone convertases PC1 and PC2 mediate distinct endoproteolytic cleavages in a strict temporal order during proopiomelanocortin biosynthetic processing, J. Biol. Chem. 268, 1763-1769.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1763-1769
    • Zhou, A.1    Bloomquist, B.T.2    Mains, R.E.3
  • 11
    • 0027460523 scopus 로고
    • Purification and characterization of the prohormone convertase PC1 (PC3)
    • Zhou, Y., and Lindberg, I. (1993) Purification and characterization of the prohormone convertase PC1 (PC3), J. Biol. Chem. 268, 5615-5623.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5615-5623
    • Zhou, Y.1    Lindberg, I.2
  • 12
    • 0031985151 scopus 로고    scopus 로고
    • Prodynorphin processing by proprotein convertase 2: Cleavage at single basic residues and enhanced processing in the presence of carboxypeptidase activity
    • Day, R., Lazure, C., Basak, A., Boudreault, A., Limperis, P., Dong, W., and Lindberg, I. (1998) Prodynorphin processing by proprotein convertase 2: Cleavage at single basic residues and enhanced processing in the presence of carboxypeptidase activity, J. Biol. Chem. 273, 829-836.
    • (1998) J. Biol. Chem. , vol.273 , pp. 829-836
    • Day, R.1    Lazure, C.2    Basak, A.3    Boudreault, A.4    Limperis, P.5    Dong, W.6    Lindberg, I.7
  • 13
    • 0028078905 scopus 로고
    • Processing of prodynorphin by the prohormone convertase PC1 results in high molecular weight intermediate forms. Cleavage at a single arginine residue
    • Dupuy, A., Lindberg, I., Zhou, Y., Akil, H., Lazure, C., Chretien, M., Seidah, N. G., and Day, R. (1994) Processing of prodynorphin by the prohormone convertase PC1 results in high molecular weight intermediate forms. Cleavage at a single arginine residue, FEBS Lett. 337, 60-65.
    • (1994) FEBS Lett. , vol.337 , pp. 60-65
    • Dupuy, A.1    Lindberg, I.2    Zhou, Y.3    Akil, H.4    Lazure, C.5    Chretien, M.6    Seidah, N.G.7    Day, R.8
  • 14
    • 0030064542 scopus 로고    scopus 로고
    • Role of PC2 in proenkephalin processing: Antisense and overexpression studies
    • Johanning, K., Mathis, J. P., and Lindberg, I. (1996) Role of PC2 in proenkephalin processing: antisense and overexpression studies, J. Neurochem. 66, 898-907.
    • (1996) J. Neurochem. , vol.66 , pp. 898-907
    • Johanning, K.1    Mathis, J.P.2    Lindberg, I.3
  • 15
    • 0026463542 scopus 로고
    • Posttranslational processing of proenkephalin in AtT-20 cells: Evidence for cleavage at Lys-Lys site
    • Mathis, J. P., and Lindberg, I. (1992) Posttranslational processing of proenkephalin in AtT-20 cells: Evidence for cleavage at Lys-Lys site, Endocrinology 131, 2287-2296.
    • (1992) Endocrinology , vol.131 , pp. 2287-2296
    • Mathis, J.P.1    Lindberg, I.2
  • 16
    • 0030199686 scopus 로고    scopus 로고
    • Peptide biosynthetic processing: Distinguishing prohormone convertases PC1 and PC2
    • Paquet, L., Zhou, A., Chang, E. Y., and Mains, R. E. (1996) Peptide biosynthetic processing: distinguishing prohormone convertases PC1 and PC2, Mol. Cell Endocrinol. 120, 161-168.
    • (1996) Mol. Cell Endocrinol. , vol.120 , pp. 161-168
    • Paquet, L.1    Zhou, A.2    Chang, E.Y.3    Mains, R.E.4
  • 17
    • 0028276806 scopus 로고
    • Endoproteolytic processing of proopiomelanocortin and prohormone convertases 1 and 2 in neuroendocrine cells overexpressing prohormone convertases 1 or 2
    • Zhou, A., and Mains, R. E. (1994) Endoproteolytic processing of proopiomelanocortin and prohormone convertases 1 and 2 in neuroendocrine cells overexpressing prohormone convertases 1 or 2, J. Biol. Chem. 269, 17440-17447.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17440-17447
    • Zhou, A.1    Mains, R.E.2
  • 18
    • 0025762119 scopus 로고
    • PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues
    • Benjannet, S., Rondeau, N., Day, R., Chretien, M., and Seidah, N. G. (1991) PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues, Proc. Natl. Acad. Sci. U.S.A. 88, 3564-3568.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 3564-3568
    • Benjannet, S.1    Rondeau, N.2    Day, R.3    Chretien, M.4    Seidah, N.G.5
  • 21
    • 0033931620 scopus 로고    scopus 로고
    • VGF: A novel role for this neuronal and neuroendocrine polypeptide in the regulation of energy balance
    • Salton, S. R., Ferri, G. L., Hahm, S., Snyder, S. E., Wilson, A. J., Possenti, R., and Levi, A. (2000) VGF: a novel role for this neuronal and neuroendocrine polypeptide in the regulation of energy balance, Front Neuroendocrinol. 21, 199-219.
    • (2000) Front Neuroendocrinol. , vol.21 , pp. 199-219
    • Salton, S.R.1    Ferri, G.L.2    Hahm, S.3    Snyder, S.E.4    Wilson, A.J.5    Possenti, R.6    Levi, A.7
  • 24
    • 0024851649 scopus 로고
    • Hypothalamic expression of a novel gene product, VGF: Immunocytochemical analysis
    • Van den Pol, A. N., Decavel, C., Levi, A., and Paterson, B. (1989) Hypothalamic expression of a novel gene product, VGF: immunocytochemical analysis, J. Neurosci. 9, 4122-4137.
    • (1989) J. Neurosci. , vol.9 , pp. 4122-4137
    • Van Den Pol, A.N.1    Decavel, C.2    Levi, A.3    Paterson, B.4
  • 26
    • 0035980127 scopus 로고    scopus 로고
    • Inhibitory specificity and potency of proSAAS-derived peptides toward proprotein convertase 1
    • Basak, A., Koch, P., Dupelle, M., Fricker, L. D., Devi, L. A., Chretien, M., and Seidah, N. G. (2001) Inhibitory specificity and potency of proSAAS-derived peptides toward proprotein convertase 1, J. Biol. Chem. 276, 32720-32728.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32720-32728
    • Basak, A.1    Koch, P.2    Dupelle, M.3    Fricker, L.D.4    Devi, L.A.5    Chretien, M.6    Seidah, N.G.7
  • 27
    • 0034604618 scopus 로고    scopus 로고
    • The C-terminal region of proSAAS is a potent inhibitor of prohormone convertase 1
    • Qian, Y., Devi, L. A., Mzhavia, N., Munzer, S., Seidah, N. G., and Fricker, L. D. (2000) The C-terminal region of proSAAS is a potent inhibitor of prohormone convertase 1, J. Biol. Chem. 275, 23596-23601.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23596-23601
    • Qian, Y.1    Devi, L.A.2    Mzhavia, N.3    Munzer, S.4    Seidah, N.G.5    Fricker, L.D.6
  • 28
    • 0034640505 scopus 로고    scopus 로고
    • The SAAS granin exhibits structural and functional homology to 7B2 and contains a highly potent hexapeptide inhibitor of PC1
    • Cameron, A., Fortenberry, Y., and Lindberg, I. (2000) The SAAS granin exhibits structural and functional homology to 7B2 and contains a highly potent hexapeptide inhibitor of PC1, FEBS Lett. 473, 135-138.
    • (2000) FEBS Lett. , vol.473 , pp. 135-138
    • Cameron, A.1    Fortenberry, Y.2    Lindberg, I.3
  • 31
    • 0035920170 scopus 로고    scopus 로고
    • Severe defect in proglucagon processing in islet A-cells of prohormone convertase 2 null mice
    • Furuta, M., Zhou, A., Webb, G., Carroll, R., Ravazzola, M., Orci, L., and Steiner, D. F. (2001) Severe defect in proglucagon processing in islet A-cells of prohormone convertase 2 null mice, J. Biol. Chem. 276, 27197-27202.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27197-27202
    • Furuta, M.1    Zhou, A.2    Webb, G.3    Carroll, R.4    Ravazzola, M.5    Orci, L.6    Steiner, D.F.7
  • 32
    • 0037022601 scopus 로고    scopus 로고
    • Mortality in 7B2 null mice can be rescued by adrenalectomy: Involvement of dopamine in ACTH hypersecretion
    • Laurent, V., Kimble, A., Peng, B., Zhu, P., Pintar, J. E., Steiner, D. F., and Lindberg, I. (2002) Mortality in 7B2 null mice can be rescued by adrenalectomy: involvement of dopamine in ACTH hypersecretion, Proc. Natl. Acad. Sci. U.S.A. 99, 3087-3092.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 3087-3092
    • Laurent, V.1    Kimble, A.2    Peng, B.3    Zhu, P.4    Pintar, J.E.5    Steiner, D.F.6    Lindberg, I.7
  • 33
    • 0842313106 scopus 로고    scopus 로고
    • Biosynthesis of proopiomelanocortin-derived peptides in prohormone convertase 2 and 7B2 null mice
    • Laurent, V., Jaubert-Miazza, L., Desjardins, R., Day, R., and Lindberg, I. (2004) Biosynthesis of proopiomelanocortin-derived peptides in prohormone convertase 2 and 7B2 null mice, Endocrinology 145, 519-528.
    • (2004) Endocrinology , vol.145 , pp. 519-528
    • Laurent, V.1    Jaubert-Miazza, L.2    Desjardins, R.3    Day, R.4    Lindberg, I.5
  • 34
    • 3843149483 scopus 로고    scopus 로고
    • Altered proglucagon processing in an alpha cell line derived from prohormone convertase 2 null mouse islets
    • Epub ahead of print
    • Webb, G. C., Dey, A., Wang, J., Stein, J., Milewski, M., and Steiner, D. F. (2004) Altered proglucagon processing in an alpha cell line derived from prohormone convertase 2 null mouse islets, J. Biol. Chem. [Epub ahead of print]
    • (2004) J. Biol. Chem.
    • Webb, G.C.1    Dey, A.2    Wang, J.3    Stein, J.4    Milewski, M.5    Steiner, D.F.6
  • 37
    • 0035882519 scopus 로고    scopus 로고
    • Altered processing of pro-orphanin FQ/nociceptin and proopiomelanocortin- derived peptides in the brains of mice expressing defective prohormone convertase 2
    • Allen, R. G., Peng, B., Pellegrino, M. J., Miller, E. D., Grandy, D. K., Lundblad, J. R., Washburn, C. L., and Pintar, J. E. (2001) Altered processing of pro-orphanin FQ/nociceptin and proopiomelanocortin-derived peptides in the brains of mice expressing defective prohormone convertase 2, J. Neurosci. 21, 5864-5870.
    • (2001) J. Neurosci. , vol.21 , pp. 5864-5870
    • Allen, R.G.1    Peng, B.2    Pellegrino, M.J.3    Miller, E.D.4    Grandy, D.K.5    Lundblad, J.R.6    Washburn, C.L.7    Pintar, J.E.8
  • 39
    • 0036678101 scopus 로고    scopus 로고
    • Severe block in processing of proinsulin to insulin accompanied by elevation of des-64,65 proinsulin intermediates in islets of mice lacking prohormone convertase 1/3
    • Zhu, X., Orci, L., Carroll, R., Norrbom, C., Ravazzola, M., and Steiner, D. F. (2002) Severe block in processing of proinsulin to insulin accompanied by elevation of des-64,65 proinsulin intermediates in islets of mice lacking prohormone convertase 1/3, Proc. Natl. Acad. Sci. U.S.A. 99, 10299-10304.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10299-10304
    • Zhu, X.1    Orci, L.2    Carroll, R.3    Norrbom, C.4    Ravazzola, M.5    Steiner, D.F.6
  • 40
    • 0038013621 scopus 로고    scopus 로고
    • Biological processing of the cocaine and amphetamine-regulated transcript precursors by prohormone convertases, PC2 and PC1/3
    • Dey, A., Xhu, X., Carroll, R., Turck, C. W., Stein, J., and Steiner, D. F. (2003) Biological processing of the cocaine and amphetamine-regulated transcript precursors by prohormone convertases, PC2 and PC1/3, J. Biol. Chem. 278, 15007-15014.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15007-15014
    • Dey, A.1    Xhu, X.2    Carroll, R.3    Turck, C.W.4    Stein, J.5    Steiner, D.F.6
  • 42
    • 1942487781 scopus 로고    scopus 로고
    • Genetic inactivation of prohormone convertase (PC1) causes a reduction in cholecystokinin (CCK) levels in the hippocampus, amygdala, pons and medulla in mouse brain that correlates with the degree of colocalization of PC1 and CCK mRNA in these structures in rat brain
    • Cain, B. M., Connolly, K., Blum, A. C., Vishnuvardhan, D., Marchand, J. E., Zhu, X., Steiner, D. F., and Beinfeld, M. C. (2004) Genetic inactivation of prohormone convertase (PC1) causes a reduction in cholecystokinin (CCK) levels in the hippocampus, amygdala, pons and medulla in mouse brain that correlates with the degree of colocalization of PC1 and CCK mRNA in these structures in rat brain, J. Neurochem. 89, 307-313.
    • (2004) J. Neurochem. , vol.89 , pp. 307-313
    • Cain, B.M.1    Connolly, K.2    Blum, A.C.3    Vishnuvardhan, D.4    Marchand, J.E.5    Zhu, X.6    Steiner, D.F.7    Beinfeld, M.C.8
  • 43
    • 1442274636 scopus 로고    scopus 로고
    • Impaired intestinal proglucagon processing in mice lacking prohormone convertase 1
    • Ugleholdt, R., Zhu, X., Deacon, C. F., Orskov, C., Steiner, D. F., and Holst, J. J. (2004) Impaired intestinal proglucagon processing in mice lacking prohormone convertase 1, Endocrinology 145, 1349-1355.
    • (2004) Endocrinology , vol.145 , pp. 1349-1355
    • Ugleholdt, R.1    Zhu, X.2    Deacon, C.F.3    Orskov, C.4    Steiner, D.F.5    Holst, J.J.6
  • 45
    • 0036523809 scopus 로고    scopus 로고
    • Minimizing resolution of isotopically coded peptides in comparative proteomics
    • Zhang, R., and Regnier, F. E. (2002) Minimizing resolution of isotopically coded peptides in comparative proteomics, J. Proteome Res. 1, 139-147.
    • (2002) J. Proteome Res. , vol.1 , pp. 139-147
    • Zhang, R.1    Regnier, F.E.2
  • 46
    • 14744275484 scopus 로고    scopus 로고
    • fat/fat mouse pituitary using stable isotopic tags and mass spectrometry
    • fat/fat mouse pituitary using stable isotopic tags and mass spectrometry, J. Mass Spectrom. 40, 227-237.
    • (2005) J. Mass Spectrom. , vol.40 , pp. 227-237
    • Che, F.-Y.1    Fricker, L.D.2
  • 47
    • 14744270672 scopus 로고    scopus 로고
    • Quantitative peptidomics of mouse pituitary: Comparison of different stable isotopic tags
    • Che, F.-Y., and Fricker, L. D. Quantitative peptidomics of mouse pituitary: Comparison of different stable isotopic tags. J. Mass Spectrom. 40, 238-249.
    • J. Mass Spectrom. , vol.40 , pp. 238-249
    • Che, F.-Y.1    Fricker, L.D.2
  • 48
    • 0028020110 scopus 로고
    • Peptide V: A VGF-derived neuropeptide purified from bovine posterior pituitary
    • Liu, J. W., Andrews, P. C., Mershon, J. L., Yan, C., Allen, D. L., and Ben Jonathan, N. (1994) Peptide V: a VGF-derived neuropeptide purified from bovine posterior pituitary, Endocrinology 135, 2742-2748.
    • (1994) Endocrinology , vol.135 , pp. 2742-2748
    • Liu, J.W.1    Andrews, P.C.2    Mershon, J.L.3    Yan, C.4    Allen, D.L.5    Ben Jonathan, N.6
  • 49
    • 0029075455 scopus 로고
    • 7B2 facilitates the maturation of proPC2 in neuroendocrine cells and is required for the expression of enzymatic activity
    • Zhu, X., and Lindberg, I. (1995) 7B2 facilitates the maturation of proPC2 in neuroendocrine cells and is required for the expression of enzymatic activity, J. Cell Biol. 129, 1641-1650.
    • (1995) J. Cell Biol. , vol.129 , pp. 1641-1650
    • Zhu, X.1    Lindberg, I.2
  • 50
    • 0028021246 scopus 로고
    • 7B2 is a neuroendocrine chaperone that transiently interacts with prohormone convertase PC2 in the secretory pathway
    • Braks, J. A. M. and Martens, G. J. M. (1994) 7B2 is a neuroendocrine chaperone that transiently interacts with prohormone convertase PC2 in the secretory pathway, Cell 78, 263-273.
    • (1994) Cell , vol.78 , pp. 263-273
    • Braks, J.A.M.1    Martens, G.J.M.2
  • 51
    • 0032411480 scopus 로고    scopus 로고
    • Neuroendocrine protein 7B2 is essential for proteolytic conversion and activation of proprotein convertase 2 in vivo
    • Seidel, B., Dong, W., Savaria, D., Zheng, M., Pintar, J. E., and Day, R. (1998) Neuroendocrine protein 7B2 is essential for proteolytic conversion and activation of proprotein convertase 2 in vivo, DNA Cell Biol. 17, 1017-1029.
    • (1998) DNA Cell Biol. , vol.17 , pp. 1017-1029
    • Seidel, B.1    Dong, W.2    Savaria, D.3    Zheng, M.4    Pintar, J.E.5    Day, R.6
  • 52
    • 0029054053 scopus 로고
    • Identification of the region within the neuroendocrine polypeptide 7B2 responsible for the inhibition of prohormone convertase PC2
    • Van Horssen, A. M., van den Hurk, W. H., Bailyes, E. M., Hutton, J. C., Martens, G. J., and Lindberg, I. (1995) Identification of the region within the neuroendocrine polypeptide 7B2 responsible for the inhibition of prohormone convertase PC2, J. Biol. Chem. 270, 14292-14296.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14292-14296
    • Van Horssen, A.M.1    Van Den Hurk, W.H.2    Bailyes, E.M.3    Hutton, J.C.4    Martens, G.J.5    Lindberg, I.6
  • 53
    • 0029022254 scopus 로고
    • Enzymatic characterization of immunopurified prohormone convertase 2: Potent inhibition by a 7B2 peptide fragment
    • Lindberg, I., van den Hurk, W. H., Bui, C., and Batie, C. J. (1995) Enzymatic characterization of immunopurified prohormone convertase 2: potent inhibition by a 7B2 peptide fragment, Biochemistry 34, 5486-5493.
    • (1995) Biochemistry , vol.34 , pp. 5486-5493
    • Lindberg, I.1    Van Den Hurk, W.H.2    Bui, C.3    Batie, C.J.4
  • 54
    • 0029954032 scopus 로고    scopus 로고
    • Internal cleavage of the inhibitory 7B2 carboxyl-terminal peptide by PC2: A potential mechanism for its inactivation
    • Zhu, X., Rouille, Y., Lamango, N. S., Steiner, D. F., and Lindberg, I. (1996) Internal cleavage of the inhibitory 7B2 carboxyl-terminal peptide by PC2: a potential mechanism for its inactivation, Proc. Natl. Acad. Sci. U.S.A. 93, 4919-4924.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 4919-4924
    • Zhu, X.1    Rouille, Y.2    Lamango, N.S.3    Steiner, D.F.4    Lindberg, I.5
  • 56
    • 0031672594 scopus 로고    scopus 로고
    • Oxytocin, vasopressin, and the neuroendocrine basis of pair bond formation
    • Insel, T. R., Winslow, J. T., Wang, Z., and Young, L. J. (1998) Oxytocin, vasopressin, and the neuroendocrine basis of pair bond formation, Adv. Exp. Med. Biol. 449, 215-224.
    • (1998) Adv. Exp. Med. Biol. , vol.449 , pp. 215-224
    • Insel, T.R.1    Winslow, J.T.2    Wang, Z.3    Young, L.J.4
  • 57
    • 0036553050 scopus 로고    scopus 로고
    • The social deficits of the oxytocin knockout mouse
    • Winslow, J. T., and Insel, T. R. (2002) The social deficits of the oxytocin knockout mouse, Neuropeptides 36, 221-229.
    • (2002) Neuropeptides , vol.36 , pp. 221-229
    • Winslow, J.T.1    Insel, T.R.2
  • 58
    • 0031031519 scopus 로고    scopus 로고
    • Cellular localization of the prohormone convertases in the hypothalamic paraventricular and supraoptic nuclei: Selective regulation of PC1 in corticotrophin-releasing hormone parvocellular neurons mediated by glucocorticoids
    • Dong, W., Seidel, B., Marcinkiewicz, M., Chretien, M., Seidah, N. G., and Day, R. (1997) Cellular localization of the prohormone convertases in the hypothalamic paraventricular and supraoptic nuclei: selective regulation of PC1 in corticotrophin-releasing hormone parvocellular neurons mediated by glucocorticoids, J. Neurosci. 17, 563-575.
    • (1997) J. Neurosci. , vol.17 , pp. 563-575
    • Dong, W.1    Seidel, B.2    Marcinkiewicz, M.3    Chretien, M.4    Seidah, N.G.5    Day, R.6
  • 59
    • 0037397005 scopus 로고    scopus 로고
    • Genetic disruption of gamma-melanocyte-stimulating hormone signaling leads to salt-sensitive hypertension in the mouse
    • Ni, X. P., Pearce, D., Butler, A. A., Cone, R. D., and Humphreys, M. H. (2003) Genetic disruption of gamma-melanocyte-stimulating hormone signaling leads to salt-sensitive hypertension in the mouse, J. Clin. Invest. 111, 1251-1258.
    • (2003) J. Clin. Invest. , vol.111 , pp. 1251-1258
    • Ni, X.P.1    Pearce, D.2    Butler, A.A.3    Cone, R.D.4    Humphreys, M.H.5


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