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Volumn 26, Issue 3, 2006, Pages 209-223

Familial Neurohypophyseal Diabetes Insipidus-An Update

Author keywords

AVP gene; inheritance; mutation; neurohypophyseal diabetes insipidus; pathogenesis

Indexed keywords

ARGIPRESSIN; DESMOPRESSIN; HORMONE PRECURSOR;

EID: 33646497845     PISSN: 02709295     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semnephrol.2006.03.003     Document Type: Article
Times cited : (78)

References (166)
  • 1
    • 0036454214 scopus 로고    scopus 로고
    • The magnocellular neuronal phenotype. Cell-specific gene expression in the hypothalamo-neurohypophysial system
    • Gainer H., Yamashita M., Fields R.L., et al. The magnocellular neuronal phenotype. Cell-specific gene expression in the hypothalamo-neurohypophysial system. Prog Brain Res 139 (2002) 1-14
    • (2002) Prog Brain Res , vol.139 , pp. 1-14
    • Gainer, H.1    Yamashita, M.2    Fields, R.L.3
  • 2
    • 0037322298 scopus 로고    scopus 로고
    • In vivo gene transfer studies on the regulation and function of the vasopressin and oxytocin genes
    • Murphy D., and Wells S. In vivo gene transfer studies on the regulation and function of the vasopressin and oxytocin genes. J Neuroendocrinol 15 (2003) 109-125
    • (2003) J Neuroendocrinol , vol.15 , pp. 109-125
    • Murphy, D.1    Wells, S.2
  • 3
    • 2442545436 scopus 로고    scopus 로고
    • Subcellular vasopressin mRNA trafficking and local translation in dendrites
    • Mohr E., and Richter D. Subcellular vasopressin mRNA trafficking and local translation in dendrites. J Neuroendocrinol 16 (2004) 333-339
    • (2004) J Neuroendocrinol , vol.16 , pp. 333-339
    • Mohr, E.1    Richter, D.2
  • 4
    • 0027175896 scopus 로고
    • Structure and folding properties of neurophysin and its peptide complexes. Biological implications
    • Breslow E. Structure and folding properties of neurophysin and its peptide complexes. Biological implications. Regul Pept 45 (1993) 15-19
    • (1993) Regul Pept , vol.45 , pp. 15-19
    • Breslow, E.1
  • 5
    • 0031884969 scopus 로고    scopus 로고
    • Structure-function relationships of the vasopressin prohormone domains
    • de Bree F.M., and Burbach J.P. Structure-function relationships of the vasopressin prohormone domains. Cell Mol Neurobiol 18 (1998) 173-191
    • (1998) Cell Mol Neurobiol , vol.18 , pp. 173-191
    • de Bree, F.M.1    Burbach, J.P.2
  • 6
    • 0034026833 scopus 로고    scopus 로고
    • Trafficking of the vasopressin and oxytocin prohormone through the regulated secretory pathway
    • de Bree F.M. Trafficking of the vasopressin and oxytocin prohormone through the regulated secretory pathway. J Neuroendocrinol 12 (2000) 589-594
    • (2000) J Neuroendocrinol , vol.12 , pp. 589-594
    • de Bree, F.M.1
  • 7
    • 0024557740 scopus 로고
    • Complete assignment of neurophysin disulfides indicates pairing in two separate domains
    • Burman S., Wellner D., Chait B., et al. Complete assignment of neurophysin disulfides indicates pairing in two separate domains. Proc Natl Acad Sci U S A 86 (1989) 429-433
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 429-433
    • Burman, S.1    Wellner, D.2    Chait, B.3
  • 8
    • 0019731612 scopus 로고
    • Glycosylation of the arginine vasopressin/neurophysin II common precursor
    • Ivell R., Schmale H., and Richter D. Glycosylation of the arginine vasopressin/neurophysin II common precursor. Biochem Biophys Res Commun 102 (1981) 1230-1236
    • (1981) Biochem Biophys Res Commun , vol.102 , pp. 1230-1236
    • Ivell, R.1    Schmale, H.2    Richter, D.3
  • 9
    • 0034636744 scopus 로고    scopus 로고
    • Modulation of dimerization, binding, stability, and folding by mutation of the neurophysin subunit interface
    • Eubanks S., Nguyen T.L., Peyton D., et al. Modulation of dimerization, binding, stability, and folding by mutation of the neurophysin subunit interface. Biochemistry 39 (2000) 8085-8094
    • (2000) Biochemistry , vol.39 , pp. 8085-8094
    • Eubanks, S.1    Nguyen, T.L.2    Peyton, D.3
  • 10
    • 0034705707 scopus 로고    scopus 로고
    • Sorting of the vasopressin prohormone into the regulated secretory pathway
    • de Bree F.M., Knight D., Howell L., et al. Sorting of the vasopressin prohormone into the regulated secretory pathway. FEBS Lett 475 (2000) 175-180
    • (2000) FEBS Lett , vol.475 , pp. 175-180
    • de Bree, F.M.1    Knight, D.2    Howell, L.3
  • 11
    • 0031911681 scopus 로고    scopus 로고
    • Molecular diversity in neurosecretion. Reflections on the hypothalamo-neurohypophysial system
    • Gainer H., and Chin H. Molecular diversity in neurosecretion. Reflections on the hypothalamo-neurohypophysial system. Cell Mol Neurobiol 18 (1998) 211-230
    • (1998) Cell Mol Neurobiol , vol.18 , pp. 211-230
    • Gainer, H.1    Chin, H.2
  • 12
    • 0036014110 scopus 로고    scopus 로고
    • Dynamic processing of neuropeptides. Sequential conformation shaping of neurohypophysial preprohormones during intraneuronal secretory transport
    • Acher R., Chauvet J., and Rouille Y. Dynamic processing of neuropeptides. Sequential conformation shaping of neurohypophysial preprohormones during intraneuronal secretory transport. J Mol Neurosci 18 (2002) 223-228
    • (2002) J Mol Neurosci , vol.18 , pp. 223-228
    • Acher, R.1    Chauvet, J.2    Rouille, Y.3
  • 13
    • 0033003216 scopus 로고    scopus 로고
    • Modulation of vasopressin-elicited water transport by trafficking of aquaporin2-containing vesicles
    • Ward D.T., Hammond T.G., and Harris H.W. Modulation of vasopressin-elicited water transport by trafficking of aquaporin2-containing vesicles. Annu Rev Physiol 61 (1999) 683-697
    • (1999) Annu Rev Physiol , vol.61 , pp. 683-697
    • Ward, D.T.1    Hammond, T.G.2    Harris, H.W.3
  • 14
    • 33644521546 scopus 로고    scopus 로고
    • Molecular biology of hereditary diabetes insipidus
    • Fujiwara T.M., and Bichet D.G. Molecular biology of hereditary diabetes insipidus. J Am Soc Nephrol 16 (2005) 2836-2846
    • (2005) J Am Soc Nephrol , vol.16 , pp. 2836-2846
    • Fujiwara, T.M.1    Bichet, D.G.2
  • 15
    • 0842323932 scopus 로고    scopus 로고
    • Six novel mutations in the arginine vasopressin gene in 15 kindreds with autosomal dominant familial neurohypophyseal diabetes insipidus give further insight into the pathogenesis
    • Christensen J.H., Siggaard C., Corydon T.J., et al. Six novel mutations in the arginine vasopressin gene in 15 kindreds with autosomal dominant familial neurohypophyseal diabetes insipidus give further insight into the pathogenesis. Eur J Hum Genet 12 (2004) 44-51
    • (2004) Eur J Hum Genet , vol.12 , pp. 44-51
    • Christensen, J.H.1    Siggaard, C.2    Corydon, T.J.3
  • 16
    • 0032805975 scopus 로고    scopus 로고
    • Autosomal recessive familial neurohypophyseal diabetes insipidus with continued secretion of mutant weakly active vasopressin
    • Willcutts M.D., Felner E., and White P.C. Autosomal recessive familial neurohypophyseal diabetes insipidus with continued secretion of mutant weakly active vasopressin. Hum Mol Genet 8 (1999) 1303-1307
    • (1999) Hum Mol Genet , vol.8 , pp. 1303-1307
    • Willcutts, M.D.1    Felner, E.2    White, P.C.3
  • 17
    • 0002544593 scopus 로고
    • On hereditary diabetes insipidus with special regard to a sex-linked form
    • Forssman H. On hereditary diabetes insipidus with special regard to a sex-linked form. Acta Med Scand 159 suppl (1945) 1-196
    • (1945) Acta Med Scand , vol.159 , Issue.SUPPL , pp. 1-196
    • Forssman, H.1
  • 19
    • 0031452158 scopus 로고    scopus 로고
    • Genetic basis of familial neurohypophyseal diabetes insipidus
    • Hansen L.K., Rittig S., and Robertson G.L. Genetic basis of familial neurohypophyseal diabetes insipidus. Trends Endocrinol Metab 8 (1997) 363-372
    • (1997) Trends Endocrinol Metab , vol.8 , pp. 363-372
    • Hansen, L.K.1    Rittig, S.2    Robertson, G.L.3
  • 20
    • 0003899962 scopus 로고    scopus 로고
    • A novel X-linked form of familial neurohypophyseal diabetes insipidus
    • (abstr)
    • Habiby R.L., Robertson G.L., Kaplowitz P.B., et al. A novel X-linked form of familial neurohypophyseal diabetes insipidus. J Invest Med 44 (1996) 388A (abstr)
    • (1996) J Invest Med , vol.44
    • Habiby, R.L.1    Robertson, G.L.2    Kaplowitz, P.B.3
  • 21
    • 0022414894 scopus 로고
    • Chromosomal assignment of human sequences encoding arginine vasopressin-neurophysin II and growth hormone releasing factor
    • Riddell D.C., Mallonee R., Phillips J.A., et al. Chromosomal assignment of human sequences encoding arginine vasopressin-neurophysin II and growth hormone releasing factor. Somat Cell Mol Genet 11 (1985) 189-195
    • (1985) Somat Cell Mol Genet , vol.11 , pp. 189-195
    • Riddell, D.C.1    Mallonee, R.2    Phillips, J.A.3
  • 22
    • 0025107546 scopus 로고
    • Linkage relationships of human arginine vasopressin-neurophysin-II and oxytocin-neurophysin-I to prodynorphin and other loci on chromosome 20
    • Summar M.L., Phillips J.A., Battey J., et al. Linkage relationships of human arginine vasopressin-neurophysin-II and oxytocin-neurophysin-I to prodynorphin and other loci on chromosome 20. Mol Endocrinol 4 (1990) 947-950
    • (1990) Mol Endocrinol , vol.4 , pp. 947-950
    • Summar, M.L.1    Phillips, J.A.2    Battey, J.3
  • 23
    • 0026683895 scopus 로고
    • The human gene for oxytocin-neurophysin I (OXT) is physically mapped to chromosome 20p13 by in situ hybridization
    • Rao V.V., Loffler C., Battey J., et al. The human gene for oxytocin-neurophysin I (OXT) is physically mapped to chromosome 20p13 by in situ hybridization. Cytogenet Cell Genet 61 (1992) 271-273
    • (1992) Cytogenet Cell Genet , vol.61 , pp. 271-273
    • Rao, V.V.1    Loffler, C.2    Battey, J.3
  • 24
    • 0020069261 scopus 로고
    • Nucleotide sequence of cloned cDNA encoding bovine arginine vasopressin-neurophysin II precursor
    • Land H., Schutz G., Schmale H., et al. Nucleotide sequence of cloned cDNA encoding bovine arginine vasopressin-neurophysin II precursor. Nature 295 (1982) 299-303
    • (1982) Nature , vol.295 , pp. 299-303
    • Land, H.1    Schutz, G.2    Schmale, H.3
  • 25
    • 0022385108 scopus 로고
    • The human vasopressin gene is linked to the oxytocin gene and is selectively expressed in a cultured lung cancer cell line
    • Sausville E., Carney D., and Battey J. The human vasopressin gene is linked to the oxytocin gene and is selectively expressed in a cultured lung cancer cell line. J Biol Chem 260 (1985) 10236-10241
    • (1985) J Biol Chem , vol.260 , pp. 10236-10241
    • Sausville, E.1    Carney, D.2    Battey, J.3
  • 26
    • 0034794075 scopus 로고    scopus 로고
    • Vasopressin gene expression. Experimental models and strategies
    • Gainer H., Fields R.L., and House S.B. Vasopressin gene expression. Experimental models and strategies. Exp Neurol 171 (2001) 190-199
    • (2001) Exp Neurol , vol.171 , pp. 190-199
    • Gainer, H.1    Fields, R.L.2    House, S.B.3
  • 27
    • 0021350786 scopus 로고
    • Structure and comparison of the oxytocin and vasopressin genes from rat
    • Ivell R., and Richter D. Structure and comparison of the oxytocin and vasopressin genes from rat. Proc Natl Acad Sci U S A 81 (1984) 2006-2010
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 2006-2010
    • Ivell, R.1    Richter, D.2
  • 28
    • 0035052523 scopus 로고    scopus 로고
    • Nephrogenic diabetes insipidus
    • Morello J.P., and Bichet D.G. Nephrogenic diabetes insipidus. Annu Rev Physiol 63 (2001) 607-630
    • (2001) Annu Rev Physiol , vol.63 , pp. 607-630
    • Morello, J.P.1    Bichet, D.G.2
  • 29
    • 0024740552 scopus 로고
    • Two isotocin genes are present in the white sucker Catostomus commersoni both lacking introns in their protein coding regions
    • Figueroa J., Morley S.D., Heierhorst J., et al. Two isotocin genes are present in the white sucker Catostomus commersoni both lacking introns in their protein coding regions. EMBO J 8 (1989) 2873-2877
    • (1989) EMBO J , vol.8 , pp. 2873-2877
    • Figueroa, J.1    Morley, S.D.2    Heierhorst, J.3
  • 30
    • 0026773556 scopus 로고
    • Presence of a member of the Tc1-like transposon family from nematodes and Drosophila within the vasotocin gene of a primitive vertebrate, the Pacific hagfish Eptatretus stouti
    • Heierhorst J., Lederis K., and Richter D. Presence of a member of the Tc1-like transposon family from nematodes and Drosophila within the vasotocin gene of a primitive vertebrate, the Pacific hagfish Eptatretus stouti. Proc Natl Acad Sci U S A 89 (1992) 6798-6802
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 6798-6802
    • Heierhorst, J.1    Lederis, K.2    Richter, D.3
  • 31
    • 0030713103 scopus 로고    scopus 로고
    • Australian lungfish neurohypophysial hormone genes encode vasotocin and [Phe2]mesotocin precursors homologous to tetrapod-type precursors
    • Hyodo S., Ishii S., and Joss J.M. Australian lungfish neurohypophysial hormone genes encode vasotocin and [Phe2]mesotocin precursors homologous to tetrapod-type precursors. Proc Natl Acad Sci U S A 94 (1997) 13339-13344
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13339-13344
    • Hyodo, S.1    Ishii, S.2    Joss, J.M.3
  • 32
    • 0034964210 scopus 로고    scopus 로고
    • Gene regulation in the magnocellular hypothalamo-neurohypophysial system
    • Burbach J.P., Luckman S.M., Murphy D., et al. Gene regulation in the magnocellular hypothalamo-neurohypophysial system. Physiol Rev 81 (2001) 1197-1267
    • (2001) Physiol Rev , vol.81 , pp. 1197-1267
    • Burbach, J.P.1    Luckman, S.M.2    Murphy, D.3
  • 33
    • 0027212750 scopus 로고
    • Neurohypophysial peptide systems. Processing machinery, hydroosmotic regulation, adaptation and evolution
    • Acher R. Neurohypophysial peptide systems. Processing machinery, hydroosmotic regulation, adaptation and evolution. Regul Pept 45 (1993) 1-13
    • (1993) Regul Pept , vol.45 , pp. 1-13
    • Acher, R.1
  • 34
    • 0032472216 scopus 로고    scopus 로고
    • Neuropeptide families. Evolutionary perspectives
    • Hoyle C.H. Neuropeptide families. Evolutionary perspectives. Regul Pept 73 (1998) 1-33
    • (1998) Regul Pept , vol.73 , pp. 1-33
    • Hoyle, C.H.1
  • 35
    • 0019133584 scopus 로고
    • Molecular evolution of biologically active polypeptides
    • Acher R. Molecular evolution of biologically active polypeptides. Proc R Soc Lond B Biol Sci 210 (1980) 21-43
    • (1980) Proc R Soc Lond B Biol Sci , vol.210 , pp. 21-43
    • Acher, R.1
  • 36
    • 0033303547 scopus 로고    scopus 로고
    • Single cell reverse transcription-polymerase chain reaction analysis of rat supraoptic magnocellular neurons. Neuropeptide phenotypes and high voltage-gated calcium channel subtypes
    • Glasgow E., Kusano K., Chin H., et al. Single cell reverse transcription-polymerase chain reaction analysis of rat supraoptic magnocellular neurons. Neuropeptide phenotypes and high voltage-gated calcium channel subtypes. Endocrinology 140 (1999) 5391-5401
    • (1999) Endocrinology , vol.140 , pp. 5391-5401
    • Glasgow, E.1    Kusano, K.2    Chin, H.3
  • 37
    • 0033304882 scopus 로고    scopus 로고
    • Quantitative analysis of oxytocin and vasopressin messenger ribonucleic acids in single magnocellular neurons isolated from supraoptic nucleus of rat hypothalamus
    • Xi D., Kusano K., and Gainer H. Quantitative analysis of oxytocin and vasopressin messenger ribonucleic acids in single magnocellular neurons isolated from supraoptic nucleus of rat hypothalamus. Endocrinology 140 (1999) 4677-4682
    • (1999) Endocrinology , vol.140 , pp. 4677-4682
    • Xi, D.1    Kusano, K.2    Gainer, H.3
  • 38
    • 0031678514 scopus 로고    scopus 로고
    • Cell-specific gene expression in oxytocin and vasopressin magnocellular neurons
    • Gainer H. Cell-specific gene expression in oxytocin and vasopressin magnocellular neurons. Adv Exp Med Biol 449 (1998) 15-27
    • (1998) Adv Exp Med Biol , vol.449 , pp. 15-27
    • Gainer, H.1
  • 39
    • 0042821812 scopus 로고    scopus 로고
    • Regulatory domains in the intergenic region of the oxytocin and vasopressin genes that control their hypothalamus-specific expression in vitro
    • Fields R.L., House S.B., and Gainer H. Regulatory domains in the intergenic region of the oxytocin and vasopressin genes that control their hypothalamus-specific expression in vitro. J Neurosci 23 (2003) 7801-7809
    • (2003) J Neurosci , vol.23 , pp. 7801-7809
    • Fields, R.L.1    House, S.B.2    Gainer, H.3
  • 40
    • 0025805918 scopus 로고
    • Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 A determined from the single-wavelength anomalous scattering signal of an incorporated iodine atom
    • Chen L.Q., Rose J.P., Breslow E., et al. Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 A determined from the single-wavelength anomalous scattering signal of an incorporated iodine atom. Proc Natl Acad Sci U S A 88 (1991) 4240-4244
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 4240-4244
    • Chen, L.Q.1    Rose, J.P.2    Breslow, E.3
  • 41
    • 3042656870 scopus 로고    scopus 로고
    • Properties of human vasopressin precursor constructs. Inefficient monomer folding in the absence of copeptin as a potential contributor to diabetes insipidus
    • Barat C., Simpson L., and Breslow E. Properties of human vasopressin precursor constructs. Inefficient monomer folding in the absence of copeptin as a potential contributor to diabetes insipidus. Biochemistry 43 (2004) 8191-8203
    • (2004) Biochemistry , vol.43 , pp. 8191-8203
    • Barat, C.1    Simpson, L.2    Breslow, E.3
  • 42
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R., and Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature 426 (2003) 891-894
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 43
    • 8444242974 scopus 로고    scopus 로고
    • Bi-directional protein transport between the ER and Golgi
    • Lee M.C., Miller E.A., Goldberg J., et al. Bi-directional protein transport between the ER and Golgi. Annu Rev Cell Dev Biol 20 (2004) 87-123
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 87-123
    • Lee, M.C.1    Miller, E.A.2    Goldberg, J.3
  • 44
    • 24944446266 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation
    • Romisch K. Endoplasmic reticulum-associated degradation. Annu Rev Cell Dev Biol 21 (2005) 435-456
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 435-456
    • Romisch, K.1
  • 45
    • 0032526224 scopus 로고    scopus 로고
    • Sorting and storage during secretory granule biogenesis. Looking backward and looking forward
    • Arvan P., and Castle D. Sorting and storage during secretory granule biogenesis. Looking backward and looking forward. Biochem J 332 (1998) 593-610
    • (1998) Biochem J , vol.332 , pp. 593-610
    • Arvan, P.1    Castle, D.2
  • 46
    • 0024344257 scopus 로고
    • The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation
    • Gerdes H.H., Rosa P., Phillips E., et al. The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation. J Biol Chem 264 (1989) 12009-12015
    • (1989) J Biol Chem , vol.264 , pp. 12009-12015
    • Gerdes, H.H.1    Rosa, P.2    Phillips, E.3
  • 47
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat E., and Huttner W.B. Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J Cell Biol 115 (1991) 1505-1519
    • (1991) J Cell Biol , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 48
    • 23944520877 scopus 로고    scopus 로고
    • EGFP-tagged vasopressin precursor protein sorting into large dense core vesicles and secretion from PC12 cells
    • Zhang B.J., Yamashita M., Fields R., et al. EGFP-tagged vasopressin precursor protein sorting into large dense core vesicles and secretion from PC12 cells. Cell Mol Neurobiol 25 (2005) 581-605
    • (2005) Cell Mol Neurobiol , vol.25 , pp. 581-605
    • Zhang, B.J.1    Yamashita, M.2    Fields, R.3
  • 49
    • 0346752249 scopus 로고    scopus 로고
    • The hormone domain of the vasopressin prohormone is required for the correct prohormone trafficking through the secretory pathway
    • de Bree F.M., Van Der Kleij A.A., Nijenhuis M., et al. The hormone domain of the vasopressin prohormone is required for the correct prohormone trafficking through the secretory pathway. J Neuroendocrinol 15 (2003) 1156-1163
    • (2003) J Neuroendocrinol , vol.15 , pp. 1156-1163
    • de Bree, F.M.1    Van Der Kleij, A.A.2    Nijenhuis, M.3
  • 50
    • 33646530412 scopus 로고
    • Mechanisms of intracellular trafficking and processing of pro-proteins
    • Loh Y.P. (Ed), CRC Press, Boca Raton, FL
    • Gainer H. Mechanisms of intracellular trafficking and processing of pro-proteins. In: Loh Y.P. (Ed). Intracellular Protein Trafficking and Proprotein Processing. An Overview (1993), CRC Press, Boca Raton, FL 1-17
    • (1993) Intracellular Protein Trafficking and Proprotein Processing. An Overview , pp. 1-17
    • Gainer, H.1
  • 51
    • 0025284946 scopus 로고
    • cDNA 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., et al. 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 (1990) 415-424
    • (1990) DNA Cell Biol , vol.9 , pp. 415-424
    • Seidah, N.G.1    Gaspar, L.2    Mion, P.3
  • 52
    • 0017325218 scopus 로고
    • Neurophysin biosynthesis. Conversion of a putative precursor during axonal transport
    • Gainer H., Sarne Y., and Brownstein M.J. Neurophysin biosynthesis. Conversion of a putative precursor during axonal transport. Science 195 (1977) 1354-1356
    • (1977) Science , vol.195 , pp. 1354-1356
    • Gainer, H.1    Sarne, Y.2    Brownstein, M.J.3
  • 53
    • 0024985447 scopus 로고
    • Molecular, thermodynamic, and biological aspects of recognition and function in neurophysin-hormone systems. A model system for the analysis of protein-peptide interactions
    • Breslow E., and Burman S. Molecular, thermodynamic, and biological aspects of recognition and function in neurophysin-hormone systems. A model system for the analysis of protein-peptide interactions. Adv Enzymol Relat Areas Mol Biol 63 (1990) 1-67
    • (1990) Adv Enzymol Relat Areas Mol Biol , vol.63 , pp. 1-67
    • Breslow, E.1    Burman, S.2
  • 54
    • 26244467943 scopus 로고    scopus 로고
    • A novel splice site mutation of the arginine vasopressin-neurophysin II gene identified in a kindred with autosomal dominant familial neurohypophyseal diabetes insipidus
    • Tae H.J., Baek K.H., Shim S.M., et al. A novel splice site mutation of the arginine vasopressin-neurophysin II gene identified in a kindred with autosomal dominant familial neurohypophyseal diabetes insipidus. Mol Genet Metab 86 (2005) 307-313
    • (2005) Mol Genet Metab , vol.86 , pp. 307-313
    • Tae, H.J.1    Baek, K.H.2    Shim, S.M.3
  • 55
    • 0029655385 scopus 로고    scopus 로고
    • Identification of 13 new mutations in the vasopressin-neurophysin II gene in 17 kindreds with familial autosomal dominant neurohypophyseal diabetes insipidus
    • Rittig S., Robertson G.L., Siggaard C., et al. Identification of 13 new mutations in the vasopressin-neurophysin II gene in 17 kindreds with familial autosomal dominant neurohypophyseal diabetes insipidus. Am J Hum Genet 58 (1996) 107-117
    • (1996) Am J Hum Genet , vol.58 , pp. 107-117
    • Rittig, S.1    Robertson, G.L.2    Siggaard, C.3
  • 56
    • 23044492523 scopus 로고    scopus 로고
    • Autosomal dominant neurohypophyseal diabetes insipidus with linkage to chromosome 20p13 but without mutations in the AVP-NPII Gene
    • Ye L., Li X., Chen Y., et al. Autosomal dominant neurohypophyseal diabetes insipidus with linkage to chromosome 20p13 but without mutations in the AVP-NPII Gene. J Clin Endocrinol Metab 90 (2005) 4388-4393
    • (2005) J Clin Endocrinol Metab , vol.90 , pp. 4388-4393
    • Ye, L.1    Li, X.2    Chen, Y.3
  • 57
    • 0033775598 scopus 로고    scopus 로고
    • Identification of two distinct mutations at the same nucleotide position, concomitantly with a novel polymorphism in the vasopressin-neurophysin II gene (AVP-NP II) in two Dutch families with familial neurohypophyseal diabetes insipidus
    • Abbes A.P., Bruggeman B., van den Akker E.L., et al. Identification of two distinct mutations at the same nucleotide position, concomitantly with a novel polymorphism in the vasopressin-neurophysin II gene (AVP-NP II) in two Dutch families with familial neurohypophyseal diabetes insipidus. Clin Chem 46 (2000) 1699-1702
    • (2000) Clin Chem , vol.46 , pp. 1699-1702
    • Abbes, A.P.1    Bruggeman, B.2    van den Akker, E.L.3
  • 58
    • 0002393930 scopus 로고
    • Pathogenesis and pathophysiology of familial neurohypophyseal diabetes insipidus
    • Saito T., Kurokawa K., and Yoshida S. (Eds), Elsevier Science B.V, Amsterdam
    • Robertson G.L., Rittig S., Gu W.X., et al. Pathogenesis and pathophysiology of familial neurohypophyseal diabetes insipidus. In: Saito T., Kurokawa K., and Yoshida S. (Eds). Neurohypophysis. Recent Progress of Vasopressin and Oxytocin Research (1995), Elsevier Science B.V, Amsterdam 593-603
    • (1995) Neurohypophysis. Recent Progress of Vasopressin and Oxytocin Research , pp. 593-603
    • Robertson, G.L.1    Rittig, S.2    Gu, W.X.3
  • 59
    • 0030953631 scopus 로고    scopus 로고
    • Molecular basis of autosomal dominant neurohypophyseal diabetes insipidus. Cellular toxicity caused by the accumulation of mutant vasopressin precursors within the endoplasmic reticulum
    • Ito M., and Jameson J.L. Molecular basis of autosomal dominant neurohypophyseal diabetes insipidus. Cellular toxicity caused by the accumulation of mutant vasopressin precursors within the endoplasmic reticulum. J Clin Invest 99 (1997) 1897-1905
    • (1997) J Clin Invest , vol.99 , pp. 1897-1905
    • Ito, M.1    Jameson, J.L.2
  • 60
    • 0033605653 scopus 로고    scopus 로고
    • Mutant vasopressin precursors that cause autosomal dominant neurohypophyseal diabetes insipidus retain dimerization and impair the secretion of wild-type proteins
    • Ito M., Yu R.N., and Jameson J.L. Mutant vasopressin precursors that cause autosomal dominant neurohypophyseal diabetes insipidus retain dimerization and impair the secretion of wild-type proteins. J Biol Chem 274 (1999) 9029-9037
    • (1999) J Biol Chem , vol.274 , pp. 9029-9037
    • Ito, M.1    Yu, R.N.2    Jameson, J.L.3
  • 61
    • 0036668073 scopus 로고    scopus 로고
    • Autophagy in hypothalamic neurones of rats expressing a familial neurohypophysial diabetes insipidus transgene
    • Davies J., and Murphy D. Autophagy in hypothalamic neurones of rats expressing a familial neurohypophysial diabetes insipidus transgene. J Neuroendocrinol 14 (2002) 629-637
    • (2002) J Neuroendocrinol , vol.14 , pp. 629-637
    • Davies, J.1    Murphy, D.2
  • 62
    • 0015253793 scopus 로고
    • Binding properties of bovine neurophysins I and II. An equilibrium dialysis study
    • Breslow E., and Walter R. Binding properties of bovine neurophysins I and II. An equilibrium dialysis study. Mol Pharmacol 8 (1972) 75-81
    • (1972) Mol Pharmacol , vol.8 , pp. 75-81
    • Breslow, E.1    Walter, R.2
  • 63
    • 0023665155 scopus 로고
    • Sequence redesign and the assembly mechanism of the oxytocin/bovine neurophysin I biosynthetic precursor
    • Ando S., McPhie P., and Chaiken I.M. Sequence redesign and the assembly mechanism of the oxytocin/bovine neurophysin I biosynthetic precursor. J Biol Chem 262 (1987) 12962-12969
    • (1987) J Biol Chem , vol.262 , pp. 12962-12969
    • Ando, S.1    McPhie, P.2    Chaiken, I.M.3
  • 64
    • 0029670611 scopus 로고    scopus 로고
    • Thermodynamic role of the pro region of the neurophysin precursor in neurophysin folding. Evidence from the effects of ligand peptides on folding
    • Deeb R., and Breslow E. Thermodynamic role of the pro region of the neurophysin precursor in neurophysin folding. Evidence from the effects of ligand peptides on folding. Biochemistry 35 (1996) 864-873
    • (1996) Biochemistry , vol.35 , pp. 864-873
    • Deeb, R.1    Breslow, E.2
  • 65
    • 0032891340 scopus 로고    scopus 로고
    • Structural basis of neurophysin hormone specificity. Geometry, polarity, and polarizability in aromatic ring interactions
    • Breslow E., Mombouyran V., Deeb R., et al. Structural basis of neurophysin hormone specificity. Geometry, polarity, and polarizability in aromatic ring interactions. Protein Sci 8 (1999) 820-831
    • (1999) Protein Sci , vol.8 , pp. 820-831
    • Breslow, E.1    Mombouyran, V.2    Deeb, R.3
  • 66
    • 0033550069 scopus 로고    scopus 로고
    • Expression, folding, and thermodynamic properties of the bovine oxytocin-neurophysin precursor. Relationships to the intermolecular oxytocin-neurophysin complex
    • Eubanks S., Lu M., Peyton D., et al. Expression, folding, and thermodynamic properties of the bovine oxytocin-neurophysin precursor. Relationships to the intermolecular oxytocin-neurophysin complex. Biochemistry 38 (1999) 13530-13541
    • (1999) Biochemistry , vol.38 , pp. 13530-13541
    • Eubanks, S.1    Lu, M.2    Peyton, D.3
  • 67
    • 0037035520 scopus 로고    scopus 로고
    • NMR analysis of the monomeric form of a mutant unliganded bovine neurophysin. Comparison with the crystal structure of a neurophysin dimer
    • Nguyen T.L., and Breslow E. NMR analysis of the monomeric form of a mutant unliganded bovine neurophysin. Comparison with the crystal structure of a neurophysin dimer. Biochemistry 41 (2002) 5920-5930
    • (2002) Biochemistry , vol.41 , pp. 5920-5930
    • Nguyen, T.L.1    Breslow, E.2
  • 68
    • 24344464881 scopus 로고    scopus 로고
    • NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I. Demonstration of dimerization-induced changes at the hormone-binding site
    • Naik M.T., Lee H., Bracken C., et al. NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I. Demonstration of dimerization-induced changes at the hormone-binding site. Biochemistry 44 (2005) 11766-11776
    • (2005) Biochemistry , vol.44 , pp. 11766-11776
    • Naik, M.T.1    Lee, H.2    Bracken, C.3
  • 69
    • 0030026190 scopus 로고    scopus 로고
    • Crystal structure of the neurophysin-oxytocin complex
    • Rose J.P., Wu C.K., Hsiao C.D., et al. Crystal structure of the neurophysin-oxytocin complex. Nat Struct Biol 3 (1996) 163-169
    • (1996) Nat Struct Biol , vol.3 , pp. 163-169
    • Rose, J.P.1    Wu, C.K.2    Hsiao, C.D.3
  • 70
    • 0034842483 scopus 로고    scopus 로고
    • Structures of an unliganded neurophysin and its vasopressin complex. Implications for binding and allosteric mechanisms
    • Wu C.K., Hu B., Rose J.P., et al. Structures of an unliganded neurophysin and its vasopressin complex. Implications for binding and allosteric mechanisms. Protein Sci 10 (2001) 1869-1880
    • (2001) Protein Sci , vol.10 , pp. 1869-1880
    • Wu, C.K.1    Hu, B.2    Rose, J.P.3
  • 71
    • 0026781949 scopus 로고
    • Identification of the unstable neurophysin disulfide and localization to the hormone-binding site. Relationship to folding-unfolding pathways
    • Huang H.B., and Breslow E. Identification of the unstable neurophysin disulfide and localization to the hormone-binding site. Relationship to folding-unfolding pathways. J Biol Chem 267 (1992) 6750-6756
    • (1992) J Biol Chem , vol.267 , pp. 6750-6756
    • Huang, H.B.1    Breslow, E.2
  • 72
    • 0021858508 scopus 로고
    • Molecular properties of the oxytocin/bovine neurophysin biosynthetic precursor. Studies using a semisynthetic precursor
    • Kanmera T., and Chaiken I.M. Molecular properties of the oxytocin/bovine neurophysin biosynthetic precursor. Studies using a semisynthetic precursor. J Biol Chem 260 (1985) 8474-8482
    • (1985) J Biol Chem , vol.260 , pp. 8474-8482
    • Kanmera, T.1    Chaiken, I.M.2
  • 73
    • 0023723001 scopus 로고
    • Structural requirements of peptide hormone binding for peptide-potentiated self-association of bovine neurophysin II
    • Fassina G., and Chaiken I.M. Structural requirements of peptide hormone binding for peptide-potentiated self-association of bovine neurophysin II. J Biol Chem 263 (1988) 13539-13543
    • (1988) J Biol Chem , vol.263 , pp. 13539-13543
    • Fassina, G.1    Chaiken, I.M.2
  • 74
    • 0018097609 scopus 로고
    • Importance of neurophysin dimer and of tyrosine-49 in the binding of neurohypophyseal peptides
    • Nicolas P., Wolff J., Camier M., et al. Importance of neurophysin dimer and of tyrosine-49 in the binding of neurohypophyseal peptides. J Biol Chem 253 (1978) 2633-2639
    • (1978) J Biol Chem , vol.253 , pp. 2633-2639
    • Nicolas, P.1    Wolff, J.2    Camier, M.3
  • 75
    • 0035839456 scopus 로고    scopus 로고
    • Effects of diabetes insipidus mutations on neurophysin folding and function
    • Eubanks S., Nguyen T.L., Deeb R., et al. Effects of diabetes insipidus mutations on neurophysin folding and function. J Biol Chem 276 (2001) 29671-29680
    • (2001) J Biol Chem , vol.276 , pp. 29671-29680
    • Eubanks, S.1    Nguyen, T.L.2    Deeb, R.3
  • 76
    • 0040131905 scopus 로고
    • Die erbpathologie des diabetes insipidus
    • Julius Springer, Berlin
    • Hanhart E. Die erbpathologie des diabetes insipidus. in Handbuch der Erbbiologie des Menschen (1940), Julius Springer, Berlin 798-823
    • (1940) in Handbuch der Erbbiologie des Menschen , pp. 798-823
    • Hanhart, E.1
  • 77
    • 0039540372 scopus 로고
    • Über den diabetes insipidus
    • Gaupp R. Über den diabetes insipidus. Z ges Neurol Psychiat 171 (1941) 514-546
    • (1941) Z ges Neurol Psychiat , vol.171 , pp. 514-546
    • Gaupp, R.1
  • 78
    • 0014125477 scopus 로고
    • Hereditary and idiopathic types of diabetes insipidus
    • Green J.R., Buchan G.C., Alvord E.C.J., et al. Hereditary and idiopathic types of diabetes insipidus. Brain 90 (1967) 707-714
    • (1967) Brain , vol.90 , pp. 707-714
    • Green, J.R.1    Buchan, G.C.2    Alvord, E.C.J.3
  • 79
    • 0000594624 scopus 로고
    • Hereditary idiopathic diabetes insipidus. A case report with autopsy findings
    • Braverman L.E., Mancini J.P., and McGoldrick D.M. Hereditary idiopathic diabetes insipidus. A case report with autopsy findings. Ann Intern Med 63 (1965) 503-508
    • (1965) Ann Intern Med , vol.63 , pp. 503-508
    • Braverman, L.E.1    Mancini, J.P.2    McGoldrick, D.M.3
  • 80
    • 0026011671 scopus 로고
    • Hereditary diabetes insipidus. An immunohistochemical study of the hypothalamus and pituitary gland
    • Bergeron C., Kovacs K., Ezrin C., et al. Hereditary diabetes insipidus. An immunohistochemical study of the hypothalamus and pituitary gland. Acta Neuropathol 81 (1991) 345-348
    • (1991) Acta Neuropathol , vol.81 , pp. 345-348
    • Bergeron, C.1    Kovacs, K.2    Ezrin, C.3
  • 81
    • 84995826008 scopus 로고
    • Familial neurohypophyseal diabetes insipidus associated with a signal peptide mutation
    • McLeod J.F., Kovacs L., Gaskill M.B., et al. Familial neurohypophyseal diabetes insipidus associated with a signal peptide mutation. J Clin Endocrinol Metab 77 (1993) 599A-599G
    • (1993) J Clin Endocrinol Metab , vol.77
    • McLeod, J.F.1    Kovacs, L.2    Gaskill, M.B.3
  • 82
    • 2442475348 scopus 로고    scopus 로고
    • Degradation of wild-type vasopressin precursor and pathogenic mutants by the proteasome
    • Friberg M.A., Spiess M., and Rutishauser J. Degradation of wild-type vasopressin precursor and pathogenic mutants by the proteasome. J Biol Chem 279 (2004) 19441-19447
    • (2004) J Biol Chem , vol.279 , pp. 19441-19447
    • Friberg, M.A.1    Spiess, M.2    Rutishauser, J.3
  • 83
    • 23244440884 scopus 로고    scopus 로고
    • Expression of three different mutations in the arginine vasopressin gene suggests genotype-phenotype correlation in familial neurohypophyseal diabetes insipidus kindreds
    • Siggaard C., Christensen J.H., Corydon T.J., et al. Expression of three different mutations in the arginine vasopressin gene suggests genotype-phenotype correlation in familial neurohypophyseal diabetes insipidus kindreds. Clin Endocrinol (Oxf) 63 (2005) 207-216
    • (2005) Clin Endocrinol (Oxf) , vol.63 , pp. 207-216
    • Siggaard, C.1    Christensen, J.H.2    Corydon, T.J.3
  • 84
    • 0025727290 scopus 로고
    • Magnetic resonance imaging in familial central diabetes insipidus
    • Miyamoto S., Sasaki N., and Tanabe Y. Magnetic resonance imaging in familial central diabetes insipidus. Neuroradiology 33 (1991) 272-273
    • (1991) Neuroradiology , vol.33 , pp. 272-273
    • Miyamoto, S.1    Sasaki, N.2    Tanabe, Y.3
  • 85
    • 0034859255 scopus 로고    scopus 로고
    • Hyperintensity of posterior pituitary on MR T1WI in a boy with central diabetes insipidus caused by missense mutation of neurophysin II gene
    • Kubota T., Yamamoto T., Ozono K., et al. Hyperintensity of posterior pituitary on MR T1WI in a boy with central diabetes insipidus caused by missense mutation of neurophysin II gene. Endocr J 48 (2001) 459-463
    • (2001) Endocr J , vol.48 , pp. 459-463
    • Kubota, T.1    Yamamoto, T.2    Ozono, K.3
  • 86
    • 0036172574 scopus 로고    scopus 로고
    • Effects of aging on vasopressin production in a kindred with autosomal dominant neurohypophyseal diabetes insipidus due to the DeltaE47 neurophysin mutation
    • Mahoney C.P., Weinberger E., Bryant C., et al. Effects of aging on vasopressin production in a kindred with autosomal dominant neurohypophyseal diabetes insipidus due to the DeltaE47 neurophysin mutation. J Clin Endocrinol Metab 87 (2002) 870-876
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 870-876
    • Mahoney, C.P.1    Weinberger, E.2    Bryant, C.3
  • 87
    • 0029801679 scopus 로고    scopus 로고
    • Heterologous expression of human vasopressin-neurophysin precursors in a pituitary cell line. Defective transport of a mutant protein from patients with familial diabetes insipidus
    • Olias G., Richter D., and Schmale H. Heterologous expression of human vasopressin-neurophysin precursors in a pituitary cell line. Defective transport of a mutant protein from patients with familial diabetes insipidus. DNA Cell Biol 15 (1996) 929-935
    • (1996) DNA Cell Biol , vol.15 , pp. 929-935
    • Olias, G.1    Richter, D.2    Schmale, H.3
  • 88
    • 0033516578 scopus 로고    scopus 로고
    • Mechanism of endoplasmic reticulum retention of mutant vasopressin precursor caused by a signal peptide truncation associated with diabetes insipidus
    • Beuret N., Rutishauser J., Bider M.D., et al. Mechanism of endoplasmic reticulum retention of mutant vasopressin precursor caused by a signal peptide truncation associated with diabetes insipidus. J Biol Chem 274 (1999) 18965-18972
    • (1999) J Biol Chem , vol.274 , pp. 18965-18972
    • Beuret, N.1    Rutishauser, J.2    Bider, M.D.3
  • 89
    • 0033334318 scopus 로고    scopus 로고
    • Clinical and molecular evidence of abnormal processing and trafficking of the vasopressin preprohormone in a large kindred with familial neurohypophyseal diabetes insipidus due to a signal peptide mutation
    • Siggaard C., Rittig S., Corydon T.J., et al. Clinical and molecular evidence of abnormal processing and trafficking of the vasopressin preprohormone in a large kindred with familial neurohypophyseal diabetes insipidus due to a signal peptide mutation. J Clin Endocrinol Metab 84 (1999) 2933-2941
    • (1999) J Clin Endocrinol Metab , vol.84 , pp. 2933-2941
    • Siggaard, C.1    Rittig, S.2    Corydon, T.J.3
  • 90
    • 0033597771 scopus 로고    scopus 로고
    • Mutations in the vasopressin prohormone involved in diabetes insipidus impair endoplasmic reticulum export but not sorting
    • Nijenhuis M., Zalm R., and Burbach J.P. Mutations in the vasopressin prohormone involved in diabetes insipidus impair endoplasmic reticulum export but not sorting. J Biol Chem 274 (1999) 21200-21208
    • (1999) J Biol Chem , vol.274 , pp. 21200-21208
    • Nijenhuis, M.1    Zalm, R.2    Burbach, J.P.3
  • 91
    • 0034715063 scopus 로고    scopus 로고
    • A diabetes insipidus vasopressin prohormone altered outside the central core of neurophysin accumulates in the endoplasmic reticulum
    • Nijenhuis M., Zalm R., and Burbach J.P. A diabetes insipidus vasopressin prohormone altered outside the central core of neurophysin accumulates in the endoplasmic reticulum. Mol Cell Endocrinol 167 (2000) 55-67
    • (2000) Mol Cell Endocrinol , vol.167 , pp. 55-67
    • Nijenhuis, M.1    Zalm, R.2    Burbach, J.P.3
  • 92
    • 0034913945 scopus 로고    scopus 로고
    • Familial neurohypophysial diabetes insipidus in a large Dutch kindred. Effect of the onset of diabetes on growth in children and cell biological defects of the mutant vasopressin prohormone
    • Nijenhuis M., van den Akker E.L., Zalm R., et al. Familial neurohypophysial diabetes insipidus in a large Dutch kindred. Effect of the onset of diabetes on growth in children and cell biological defects of the mutant vasopressin prohormone. J Clin Endocrinol Metab 86 (2001) 3410-3420
    • (2001) J Clin Endocrinol Metab , vol.86 , pp. 3410-3420
    • Nijenhuis, M.1    van den Akker, E.L.2    Zalm, R.3
  • 93
    • 0842330810 scopus 로고    scopus 로고
    • Impaired trafficking of mutated AVP prohormone in cells expressing rare disease genes causing autosomal dominant familial neurohypophyseal diabetes insipidus
    • Christensen J.H., Siggaard C., Corydon T.J., et al. Impaired trafficking of mutated AVP prohormone in cells expressing rare disease genes causing autosomal dominant familial neurohypophyseal diabetes insipidus. Clin Endocrinol (Oxf) 60 (2004) 125-136
    • (2004) Clin Endocrinol (Oxf) , vol.60 , pp. 125-136
    • Christensen, J.H.1    Siggaard, C.2    Corydon, T.J.3
  • 94
    • 4544278346 scopus 로고    scopus 로고
    • Differential cellular handling of defective arginine vasopressin (AVP) prohormones in cells expressing mutations of the AVP gene associated with autosomal dominant and recessive familial neurohypophyseal diabetes insipidus
    • Christensen J.H., Siggaard C., Corydon T.J., et al. Differential cellular handling of defective arginine vasopressin (AVP) prohormones in cells expressing mutations of the AVP gene associated with autosomal dominant and recessive familial neurohypophyseal diabetes insipidus. J Clin Endocrinol Metab 89 (2004) 4521-4531
    • (2004) J Clin Endocrinol Metab , vol.89 , pp. 4521-4531
    • Christensen, J.H.1    Siggaard, C.2    Corydon, T.J.3
  • 95
    • 0347600942 scopus 로고    scopus 로고
    • A murine model of autosomal dominant neurohypophyseal diabetes insipidus reveals progressive loss of vasopressin-producing neurons
    • Russell T.A., Ito M., Ito M., et al. A murine model of autosomal dominant neurohypophyseal diabetes insipidus reveals progressive loss of vasopressin-producing neurons. J Clin Invest 112 (2003) 1697-1706
    • (2003) J Clin Invest , vol.112 , pp. 1697-1706
    • Russell, T.A.1    Ito, M.2    Ito, M.3
  • 96
    • 0033822702 scopus 로고    scopus 로고
    • Endoplasmic reticulum derangement in hypothalamic neurons of rats expressing a familial neurohypophyseal diabetes insipidus mutant vasopressin transgene
    • Si-Hoe S., de Bree F.M., Nijenhuis M., et al. Endoplasmic reticulum derangement in hypothalamic neurons of rats expressing a familial neurohypophyseal diabetes insipidus mutant vasopressin transgene. FASEB J 14 (2000) 1680-1684
    • (2000) FASEB J , vol.14 , pp. 1680-1684
    • Si-Hoe, S.1    de Bree, F.M.2    Nijenhuis, M.3
  • 97
    • 20444459545 scopus 로고    scopus 로고
    • Autophagy is a prosurvival mechanism in cells expressing an autosomal dominant familial neurohypophyseal diabetes insipidus mutant vasopressin transgene
    • Castino R., Davies J., Beaucourt S., et al. Autophagy is a prosurvival mechanism in cells expressing an autosomal dominant familial neurohypophyseal diabetes insipidus mutant vasopressin transgene. FASEB J 19 (2005) 1021-1023
    • (2005) FASEB J , vol.19 , pp. 1021-1023
    • Castino, R.1    Davies, J.2    Beaucourt, S.3
  • 98
    • 20444493589 scopus 로고    scopus 로고
    • Autophagy-dependent cell survival and cell death in an autosomal dominant familial neurohypophyseal diabetes insipidus in vitro model
    • Castino R., Isidoro C., and Murphy D. Autophagy-dependent cell survival and cell death in an autosomal dominant familial neurohypophyseal diabetes insipidus in vitro model. FASEB J 19 (2005) 1024-1026
    • (2005) FASEB J , vol.19 , pp. 1024-1026
    • Castino, R.1    Isidoro, C.2    Murphy, D.3
  • 99
    • 0027055355 scopus 로고
    • Hepatic endoplasmic reticulum storage diseases
    • Callea F., Brisigotti M., Fabbretti G., et al. Hepatic endoplasmic reticulum storage diseases. Liver 12 (1992) 357-362
    • (1992) Liver , vol.12 , pp. 357-362
    • Callea, F.1    Brisigotti, M.2    Fabbretti, G.3
  • 100
    • 0032432673 scopus 로고    scopus 로고
    • Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases. Disorders of protein trafficking and the role of ER molecular chaperones
    • Kim P.S., and Arvan P. Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases. Disorders of protein trafficking and the role of ER molecular chaperones. Endocr Rev 19 (1998) 173-202
    • (1998) Endocr Rev , vol.19 , pp. 173-202
    • Kim, P.S.1    Arvan, P.2
  • 101
    • 0030481624 scopus 로고    scopus 로고
    • Congenital hypothyroid goiter with deficient thyroglobulin. Identification of an endoplasmic reticulum storage disease with induction of molecular chaperones
    • Medeiros-Neto G., Kim P.S., Yoo S.E., et al. Congenital hypothyroid goiter with deficient thyroglobulin. Identification of an endoplasmic reticulum storage disease with induction of molecular chaperones. J Clin Invest 98 (1996) 2838-2844
    • (1996) J Clin Invest , vol.98 , pp. 2838-2844
    • Medeiros-Neto, G.1    Kim, P.S.2    Yoo, S.E.3
  • 102
    • 0028902639 scopus 로고
    • Endoplasmic reticulum-mediated quality control of type I collagen production by cells from osteogenesis imperfecta patients with mutations in the pro alpha 1 (I) chain carboxyl-terminal propeptide which impair subunit assembly
    • Lamande S.R., Chessler S.D., Golub S.B., et al. Endoplasmic reticulum-mediated quality control of type I collagen production by cells from osteogenesis imperfecta patients with mutations in the pro alpha 1 (I) chain carboxyl-terminal propeptide which impair subunit assembly. J Biol Chem 270 (1995) 8642-8649
    • (1995) J Biol Chem , vol.270 , pp. 8642-8649
    • Lamande, S.R.1    Chessler, S.D.2    Golub, S.B.3
  • 103
    • 0023140956 scopus 로고
    • The Lebanese allele at the low density lipoprotein receptor locus. Nonsense mutation produces truncated receptor that is retained in endoplasmic reticulum
    • Lehrman M.A., Schneider W.J., Brown M.S., et al. The Lebanese allele at the low density lipoprotein receptor locus. Nonsense mutation produces truncated receptor that is retained in endoplasmic reticulum. J Biol Chem 262 (1987) 401-410
    • (1987) J Biol Chem , vol.262 , pp. 401-410
    • Lehrman, M.A.1    Schneider, W.J.2    Brown, M.S.3
  • 104
    • 17944398616 scopus 로고    scopus 로고
    • A common W556S mutation in the LDL receptor gene of Danish patients with familial hypercholesterolemia encodes a transport-defective protein
    • Jensen H.K., Holst H., Jensen L.G., et al. A common W556S mutation in the LDL receptor gene of Danish patients with familial hypercholesterolemia encodes a transport-defective protein. Atherosclerosis 131 (1997) 67-72
    • (1997) Atherosclerosis , vol.131 , pp. 67-72
    • Jensen, H.K.1    Holst, H.2    Jensen, L.G.3
  • 105
    • 0034721773 scopus 로고    scopus 로고
    • Grp78 is involved in retention of mutant low density lipoprotein receptor protein in the endoplasmic reticulum
    • Jorgensen M.M., Jensen O.N., Holst H.U., et al. Grp78 is involved in retention of mutant low density lipoprotein receptor protein in the endoplasmic reticulum. J Biol Chem 275 (2000) 33861-33868
    • (2000) J Biol Chem , vol.275 , pp. 33861-33868
    • Jorgensen, M.M.1    Jensen, O.N.2    Holst, H.U.3
  • 106
    • 0036319618 scopus 로고    scopus 로고
    • Autosomal dominant neurohypophyseal diabetes insipidus due to substitution of histidine for tyrosine(2) in the vasopressin moiety of the hormone precursor
    • Rittig S., Siggaard C., Ozata M., et al. Autosomal dominant neurohypophyseal diabetes insipidus due to substitution of histidine for tyrosine(2) in the vasopressin moiety of the hormone precursor. J Clin Endocrinol Metab 87 (2002) 3351-3355
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 3351-3355
    • Rittig, S.1    Siggaard, C.2    Ozata, M.3
  • 107
    • 1942536608 scopus 로고    scopus 로고
    • A novel mutation in the preprovasopressin gene identified in a kindred with autosomal dominant neurohypophyseal diabetes insipidus
    • Wahlstrom J.T., Fowler M.J., Nicholson W.E., et al. A novel mutation in the preprovasopressin gene identified in a kindred with autosomal dominant neurohypophyseal diabetes insipidus. J Clin Endocrinol Metab 89 (2004) 1963-1968
    • (2004) J Clin Endocrinol Metab , vol.89 , pp. 1963-1968
    • Wahlstrom, J.T.1    Fowler, M.J.2    Nicholson, W.E.3
  • 108
    • 0017762406 scopus 로고
    • Interactions of oxytocin with bovine neurophysins I and II. Use of 13C nuclear magnetic resonance and hormones specifically enriched with 13C in the glycinamide-9 and half-cystine-1 positions
    • Blumenstein M., and Hruby V.J. Interactions of oxytocin with bovine neurophysins I and II. Use of 13C nuclear magnetic resonance and hormones specifically enriched with 13C in the glycinamide-9 and half-cystine-1 positions. Biochemistry 16 (1977) 5169-5177
    • (1977) Biochemistry , vol.16 , pp. 5169-5177
    • Blumenstein, M.1    Hruby, V.J.2
  • 109
    • 33644486769 scopus 로고
    • De la polydipsie. L'experiance
    • Lacombe U. De la polydipsie. L'experiance. J Med Chir 7 (1841) 323-339
    • (1841) J Med Chir , vol.7 , pp. 323-339
    • Lacombe, U.1
  • 110
    • 0010322825 scopus 로고
    • Ueber die hereditaere Form des Diabetes insipidus
    • Weil A. Ueber die hereditaere Form des Diabetes insipidus. Virchows Arch Path Anat 95 (1884) 70-95
    • (1884) Virchows Arch Path Anat , vol.95 , pp. 70-95
    • Weil, A.1
  • 111
    • 0001690320 scopus 로고
    • Notes on some cases of diabetes insipidus with marked family and hereditary tendencies
    • McIlraith C.H. Notes on some cases of diabetes insipidus with marked family and hereditary tendencies. Lancet ii (1892) 767-768
    • (1892) Lancet , vol.ii , pp. 767-768
    • McIlraith, C.H.1
  • 112
    • 0141728373 scopus 로고    scopus 로고
    • Progressive decline of vasopressin secretion in familial autosomal dominant neurohypophyseal diabetes insipidus presenting a novel mutation in the vasopressin-neurophysin II gene
    • Elias P.C., Elias L.L., Torres N., et al. Progressive decline of vasopressin secretion in familial autosomal dominant neurohypophyseal diabetes insipidus presenting a novel mutation in the vasopressin-neurophysin II gene. Clin Endocrinol (Oxf) 59 (2003) 511-518
    • (2003) Clin Endocrinol (Oxf) , vol.59 , pp. 511-518
    • Elias, P.C.1    Elias, L.L.2    Torres, N.3
  • 113
    • 0030067123 scopus 로고    scopus 로고
    • A novel point mutation in the translation initiation codon of the pre- pro-vasopressin-neurophysin II gene. cosegregation with morphological abnormalities and clinical symptoms in autosomal dominant neurohypophyseal diabetes insipidus
    • Rutishauser J., Boni-Schnetzler M., Boni J., et al. A novel point mutation in the translation initiation codon of the pre- pro-vasopressin-neurophysin II gene. cosegregation with morphological abnormalities and clinical symptoms in autosomal dominant neurohypophyseal diabetes insipidus. J Clin Endocrinol Metab 81 (1996) 192-198
    • (1996) J Clin Endocrinol Metab , vol.81 , pp. 192-198
    • Rutishauser, J.1    Boni-Schnetzler, M.2    Boni, J.3
  • 114
    • 0031765316 scopus 로고    scopus 로고
    • Identification of mutations of the arginine vasopressin-neurophysin II gene in two kindreds with familial central diabetes insipidus
    • Heppner C., Kotzka J., Bullmann C., et al. Identification of mutations of the arginine vasopressin-neurophysin II gene in two kindreds with familial central diabetes insipidus. J Clin Endocrinol Metab 83 (1998) 693-696
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 693-696
    • Heppner, C.1    Kotzka, J.2    Bullmann, C.3
  • 115
    • 0031025127 scopus 로고    scopus 로고
    • Heterogeneity in clinical manifestation of autosomal dominant neurohypophyseal diabetes insipidus caused by a mutation encoding Ala-1- ->Val in the signal peptide of the arginine vasopressin/neurophysin II/copeptin precursor
    • Repaske D.R., Medlej R., Gultekin E.K., et al. Heterogeneity in clinical manifestation of autosomal dominant neurohypophyseal diabetes insipidus caused by a mutation encoding Ala-1- ->Val in the signal peptide of the arginine vasopressin/neurophysin II/copeptin precursor. J Clin Endocrinol Metab 82 (1997) 51-56
    • (1997) J Clin Endocrinol Metab , vol.82 , pp. 51-56
    • Repaske, D.R.1    Medlej, R.2    Gultekin, E.K.3
  • 116
    • 0023248327 scopus 로고
    • Diabetes insipidus in pregnancy
    • Durr J.A. Diabetes insipidus in pregnancy. Am J Kidney Dis 9 (1987) 276-283
    • (1987) Am J Kidney Dis , vol.9 , pp. 276-283
    • Durr, J.A.1
  • 117
    • 0024217917 scopus 로고
    • Differential diagnosis of polyuria
    • Robertson G.L. Differential diagnosis of polyuria. Annu Rev Med 39 (1988) 425-442
    • (1988) Annu Rev Med , vol.39 , pp. 425-442
    • Robertson, G.L.1
  • 118
    • 0030030466 scopus 로고    scopus 로고
    • Three novel AVPR2 mutations in three Japanese families with X-linked nephrogenic diabetes insipidus
    • Tajima T., Nakae J., Takekoshi Y., et al. Three novel AVPR2 mutations in three Japanese families with X-linked nephrogenic diabetes insipidus. Pediatr Res 39 (1996) 522-526
    • (1996) Pediatr Res , vol.39 , pp. 522-526
    • Tajima, T.1    Nakae, J.2    Takekoshi, Y.3
  • 119
    • 0030717492 scopus 로고    scopus 로고
    • Biochemical basis of partial nephrogenic diabetes insipidus phenotypes
    • Sadeghi H., Robertson G.L., Bichet D.G., et al. Biochemical basis of partial nephrogenic diabetes insipidus phenotypes. Mol Endocrinol 11 (1997) 1806-1813
    • (1997) Mol Endocrinol , vol.11 , pp. 1806-1813
    • Sadeghi, H.1    Robertson, G.L.2    Bichet, D.G.3
  • 120
    • 0031429315 scopus 로고    scopus 로고
    • Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12 families with congenital nephrogenic diabetes insipidus
    • Vargas-Poussou R., Forestier L., Dautzenberg M.D., et al. Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12 families with congenital nephrogenic diabetes insipidus. J Am Soc Nephrol 8 (1997) 1855-1862
    • (1997) J Am Soc Nephrol , vol.8 , pp. 1855-1862
    • Vargas-Poussou, R.1    Forestier, L.2    Dautzenberg, M.D.3
  • 121
    • 0034457168 scopus 로고    scopus 로고
    • Functional characterization of the molecular defects causing nephrogenic diabetes insipidus in eight families
    • Pasel K., Schulz A., Timmermann K., et al. Functional characterization of the molecular defects causing nephrogenic diabetes insipidus in eight families. J Clin Endocrinol Metab 85 (2000) 1703-1710
    • (2000) J Clin Endocrinol Metab , vol.85 , pp. 1703-1710
    • Pasel, K.1    Schulz, A.2    Timmermann, K.3
  • 122
    • 0035140394 scopus 로고    scopus 로고
    • The property of a novel v2 receptor mutant in a patient with nephrogenic diabetes insipidus
    • Inaba S., Hatakeyama H., Taniguchi N., et al. The property of a novel v2 receptor mutant in a patient with nephrogenic diabetes insipidus. J Clin Endocrinol Metab 86 (2001) 381-385
    • (2001) J Clin Endocrinol Metab , vol.86 , pp. 381-385
    • Inaba, S.1    Hatakeyama, H.2    Taniguchi, N.3
  • 124
    • 16644376868 scopus 로고    scopus 로고
    • Clinical characteristics of eight patients with congenital nephrogenic diabetes insipidus
    • Mizuno H., Sugiyama Y., Ohro Y., et al. Clinical characteristics of eight patients with congenital nephrogenic diabetes insipidus. Endocrine 24 (2004) 55-59
    • (2004) Endocrine , vol.24 , pp. 55-59
    • Mizuno, H.1    Sugiyama, Y.2    Ohro, Y.3
  • 125
    • 27944468721 scopus 로고    scopus 로고
    • Minor disturbances in central nervous system function in familial neurohypophysial diabetes insipidus
    • Bruins J., Kovacs G.L., Abbes A.P., et al. Minor disturbances in central nervous system function in familial neurohypophysial diabetes insipidus. Psychoneuroendocrinology 31 (2006) 80-91
    • (2006) Psychoneuroendocrinology , vol.31 , pp. 80-91
    • Bruins, J.1    Kovacs, G.L.2    Abbes, A.P.3
  • 126
    • 23644447753 scopus 로고    scopus 로고
    • Current perspective on the pathogenesis of central diabetes insipidus
    • Ghirardello S., Malattia C., Scagnelli P., et al. Current perspective on the pathogenesis of central diabetes insipidus. J Pediatr Endocrinol Metab 18 (2005) 631-645
    • (2005) J Pediatr Endocrinol Metab , vol.18 , pp. 631-645
    • Ghirardello, S.1    Malattia, C.2    Scagnelli, P.3
  • 127
    • 0036113787 scopus 로고    scopus 로고
    • Clinical and molecular analysis of three families with autosomal dominant neurohypophyseal diabetes insipidus associated with a novel and recurrent mutations in the vasopressin-neurophysin II gene
    • Rutishauser J., Kopp P., Gaskill M.B., et al. Clinical and molecular analysis of three families with autosomal dominant neurohypophyseal diabetes insipidus associated with a novel and recurrent mutations in the vasopressin-neurophysin II gene. Eur J Endocrinol 146 (2002) 649-656
    • (2002) Eur J Endocrinol , vol.146 , pp. 649-656
    • Rutishauser, J.1    Kopp, P.2    Gaskill, M.B.3
  • 128
    • 0141480203 scopus 로고    scopus 로고
    • Oral DDAVP is a good alternative therapy for patients with central diabetes insipidus. Experience of five-year treatment
    • Fukuda I., Hizuka N., and Takano K. Oral DDAVP is a good alternative therapy for patients with central diabetes insipidus. Experience of five-year treatment. Endocr J 50 (2003) 437-443
    • (2003) Endocr J , vol.50 , pp. 437-443
    • Fukuda, I.1    Hizuka, N.2    Takano, K.3
  • 129
    • 0031912872 scopus 로고    scopus 로고
    • Effect of food intake on the pharmacokinetics and antidiuretic activity of oral desmopressin (DDAVP) in hydrated normal subjects
    • Rittig S., Jensen A.R., Jensen K.T., et al. Effect of food intake on the pharmacokinetics and antidiuretic activity of oral desmopressin (DDAVP) in hydrated normal subjects. Clin Endocrinol (Oxf) 48 (1998) 235-241
    • (1998) Clin Endocrinol (Oxf) , vol.48 , pp. 235-241
    • Rittig, S.1    Jensen, A.R.2    Jensen, K.T.3
  • 130
    • 33646497138 scopus 로고    scopus 로고
    • A pharmacodynamic study in children with primary nocturnal enuresis using a new "melt" orodispersible formulation of desmopressin
    • (abstr)
    • Bogaert G., Vande Walle J., Mattson S., et al. A pharmacodynamic study in children with primary nocturnal enuresis using a new "melt" orodispersible formulation of desmopressin. Neurourol Urodyn 24 (2005) 578-579 (abstr)
    • (2005) Neurourol Urodyn , vol.24 , pp. 578-579
    • Bogaert, G.1    Vande Walle, J.2    Mattson, S.3
  • 131
    • 0031465261 scopus 로고    scopus 로고
    • Long-term gene therapy in the CNS. Reversal of hypothalamic diabetes insipidus in the Brattleboro rat by using an adenovirus expressing arginine vasopressin
    • Geddes B.J., Harding T.C., Lightman S.L., et al. Long-term gene therapy in the CNS. Reversal of hypothalamic diabetes insipidus in the Brattleboro rat by using an adenovirus expressing arginine vasopressin. Nat Med 3 (1997) 1402-1404
    • (1997) Nat Med , vol.3 , pp. 1402-1404
    • Geddes, B.J.1    Harding, T.C.2    Lightman, S.L.3
  • 132
    • 0347917177 scopus 로고    scopus 로고
    • Persistent phenotypic correction of central diabetes insipidus using adeno-associated virus vector expressing arginine-vasopressin in brattleboro rats
    • Ideno J., Mizukami H., Honda K., et al. Persistent phenotypic correction of central diabetes insipidus using adeno-associated virus vector expressing arginine-vasopressin in brattleboro rats. Mol Ther 8 (2003) 895-902
    • (2003) Mol Ther , vol.8 , pp. 895-902
    • Ideno, J.1    Mizukami, H.2    Honda, K.3
  • 133
    • 0038190879 scopus 로고    scopus 로고
    • Long-term replacement of a mutated nonfunctional CNS gene. Reversal of hypothalamic diabetes insipidus using an EIAV-based lentiviral vector expressing arginine vasopressin
    • Bienemann A.S., Martin-Rendon E., Cosgrave A.S., et al. Long-term replacement of a mutated nonfunctional CNS gene. Reversal of hypothalamic diabetes insipidus using an EIAV-based lentiviral vector expressing arginine vasopressin. Mol Ther 7 (2003) 588-596
    • (2003) Mol Ther , vol.7 , pp. 588-596
    • Bienemann, A.S.1    Martin-Rendon, E.2    Cosgrave, A.S.3
  • 134
    • 1042275335 scopus 로고    scopus 로고
    • Gene therapy for central diabetes insipidus. Effective antidiuresis by muscle-targeted gene transfer
    • Yoshida M., Iwasaki Y., Asai M., et al. Gene therapy for central diabetes insipidus. Effective antidiuresis by muscle-targeted gene transfer. Endocrinology 145 (2004) 261-268
    • (2004) Endocrinology , vol.145 , pp. 261-268
    • Yoshida, M.1    Iwasaki, Y.2    Asai, M.3
  • 135
    • 33646172978 scopus 로고    scopus 로고
    • Conivaptan. A selective vasopressin antagonist for the treatment of heart failure
    • Schwarz E.R., and Sanghi P. Conivaptan. A selective vasopressin antagonist for the treatment of heart failure. Expert Rev Cardiovasc Ther 4 (2006) 17-23
    • (2006) Expert Rev Cardiovasc Ther , vol.4 , pp. 17-23
    • Schwarz, E.R.1    Sanghi, P.2
  • 136
    • 0027311315 scopus 로고
    • Possible involvement of inefficient cleavage of preprovasopressin by signal peptidase as a cause for familial central diabetes insipidus
    • Ito M., Oiso Y., Murase T., et al. Possible involvement of inefficient cleavage of preprovasopressin by signal peptidase as a cause for familial central diabetes insipidus. J Clin Invest 91 (1993) 2565-2571
    • (1993) J Clin Invest , vol.91 , pp. 2565-2571
    • Ito, M.1    Oiso, Y.2    Murase, T.3
  • 137
    • 0038947728 scopus 로고
    • Familial neurogenic diabetes insipidus in 5 Danish kindreds
    • Gross P., Richter D., and Robertson G.L. (Eds), John Libbey Eurotext, Paris
    • Rittig S., Kovacs L., Gregersen N., et al. Familial neurogenic diabetes insipidus in 5 Danish kindreds. In: Gross P., Richter D., and Robertson G.L. (Eds). Vasopressin (1993), John Libbey Eurotext, Paris 600
    • (1993) Vasopressin , pp. 600
    • Rittig, S.1    Kovacs, L.2    Gregersen, N.3
  • 138
    • 0029885492 scopus 로고    scopus 로고
    • Recurrent mutations in the vasopressin-neurophysin II gene cause autosomal dominant neurohypophyseal diabetes insipidus
    • Repaske D.R., Summar M.L., Krishnamani M.R., et al. Recurrent mutations in the vasopressin-neurophysin II gene cause autosomal dominant neurohypophyseal diabetes insipidus. J Clin Endocrinol Metab 81 (1996) 2328-2334
    • (1996) J Clin Endocrinol Metab , vol.81 , pp. 2328-2334
    • Repaske, D.R.1    Summar, M.L.2    Krishnamani, M.R.3
  • 139
    • 0031765306 scopus 로고    scopus 로고
    • Identification of a novel nonsense mutation and a missense substitution in the vasopressin-neurophysin II gene in two Spanish kindreds with familial neurohypophyseal diabetes insipidus
    • Calvo B., Bilbao J.R., Urrutia I., et al. Identification of a novel nonsense mutation and a missense substitution in the vasopressin-neurophysin II gene in two Spanish kindreds with familial neurohypophyseal diabetes insipidus. J Clin Endocrinol Metab 83 (1998) 995-997
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 995-997
    • Calvo, B.1    Bilbao, J.R.2    Urrutia, I.3
  • 140
    • 0037236853 scopus 로고    scopus 로고
    • A signal peptide mutation of the arginine vasopressin gene in monozygotic twins
    • Boson W.L., Sarubi J.C., D'Alva C.B., et al. A signal peptide mutation of the arginine vasopressin gene in monozygotic twins. Clin Endocrinol (Oxf) 58 (2003) 108-110
    • (2003) Clin Endocrinol (Oxf) , vol.58 , pp. 108-110
    • Boson, W.L.1    Sarubi, J.C.2    D'Alva, C.B.3
  • 141
    • 0036947762 scopus 로고    scopus 로고
    • Familial central diabetes insipidus detected by nocturnal enuresis
    • Kanemitsu N., Kawauchi A., Nishida M., et al. Familial central diabetes insipidus detected by nocturnal enuresis. Pediatr Nephrol 17 (2002) 1063-1065
    • (2002) Pediatr Nephrol , vol.17 , pp. 1063-1065
    • Kanemitsu, N.1    Kawauchi, A.2    Nishida, M.3
  • 142
    • 0026567519 scopus 로고
    • A missense mutation in the vasopressin-neurophysin precursor gene cosegregates with human autosomal dominant neurohypophyseal diabetes insipidus
    • Bahnsen U., Oosting P., Swaab D.F., et al. A missense mutation in the vasopressin-neurophysin precursor gene cosegregates with human autosomal dominant neurohypophyseal diabetes insipidus. EMBO J 11 (1992) 19-23
    • (1992) EMBO J , vol.11 , pp. 19-23
    • Bahnsen, U.1    Oosting, P.2    Swaab, D.F.3
  • 143
    • 0034876541 scopus 로고    scopus 로고
    • A novel AVP-neurophysin gene mutation in familial neurohypophyseal diabetes insipidus presenting with nocturnal enuresis
    • Goking N.Q., Chertow B.S., Robertson G.L., et al. A novel AVP-neurophysin gene mutation in familial neurohypophyseal diabetes insipidus presenting with nocturnal enuresis. J Endocrine Genetics 2 (2001) 105-113
    • (2001) J Endocrine Genetics , vol.2 , pp. 105-113
    • Goking, N.Q.1    Chertow, B.S.2    Robertson, G.L.3
  • 144
    • 0033305374 scopus 로고    scopus 로고
    • Molecular analysis in familial neurohypophyseal diabetes insipidus. Early diagnosis of an asymptomatic carrier
    • Calvo B., Bilbao J.R., Rodriguez A., et al. Molecular analysis in familial neurohypophyseal diabetes insipidus. Early diagnosis of an asymptomatic carrier. J Clin Endocrinol Metab 84 (1999) 3351-3354
    • (1999) J Clin Endocrinol Metab , vol.84 , pp. 3351-3354
    • Calvo, B.1    Bilbao, J.R.2    Rodriguez, A.3
  • 145
    • 0030670882 scopus 로고    scopus 로고
    • Autosomal dominant neurohypophyseal diabetes insipidus associated with a missense mutation encoding Gly23->Val in neurophysin II
    • Gagliardi P.C., Bernasconi S., and Repaske D.R. Autosomal dominant neurohypophyseal diabetes insipidus associated with a missense mutation encoding Gly23->Val in neurophysin II. J Clin Endocrinol Metab 82 (1997) 3643-3646
    • (1997) J Clin Endocrinol Metab , vol.82 , pp. 3643-3646
    • Gagliardi, P.C.1    Bernasconi, S.2    Repaske, D.R.3
  • 146
    • 0028123040 scopus 로고
    • A de novo mutation in the coding sequence for neurophysin-II (Pro24- >Leu) is associated with onset and transmission of autosomal dominant neurohypophyseal diabetes insipidus
    • Repaske D.R., and Browning J.E. A de novo mutation in the coding sequence for neurophysin-II (Pro24- >Leu) is associated with onset and transmission of autosomal dominant neurohypophyseal diabetes insipidus. J Clin Endocrinol Metab 79 (1994) 421-427
    • (1994) J Clin Endocrinol Metab , vol.79 , pp. 421-427
    • Repaske, D.R.1    Browning, J.E.2
  • 147
    • 0042386243 scopus 로고    scopus 로고
    • A new missense mutation of the vasopressin-neurophysin II gene in a family with neurohypophyseal diabetes insipidus
    • Wolf M.T., Dotsch J., Metzler M., et al. A new missense mutation of the vasopressin-neurophysin II gene in a family with neurohypophyseal diabetes insipidus. Horm Res 60 (2003) 143-147
    • (2003) Horm Res , vol.60 , pp. 143-147
    • Wolf, M.T.1    Dotsch, J.2    Metzler, M.3
  • 148
    • 0033679763 scopus 로고    scopus 로고
    • A novel arginine vasopressin-neurophysin II mutation causes autosomal dominant neurohypophyseal diabetes insipidus and morphologic pituitary changes
    • Skordis N., Patsalis P.C., Hettinger J.A., et al. A novel arginine vasopressin-neurophysin II mutation causes autosomal dominant neurohypophyseal diabetes insipidus and morphologic pituitary changes. Horm Res 53 (2000) 239-245
    • (2000) Horm Res , vol.53 , pp. 239-245
    • Skordis, N.1    Patsalis, P.C.2    Hettinger, J.A.3
  • 149
    • 0034817342 scopus 로고    scopus 로고
    • Autosomal dominant neurohypophyseal diabetes insipidus in a Swiss family, caused by a novel mutation (C59Delta/A60W) in the neurophysin moiety of prepro-vasopressin-neurophysin II (AVP-NP II)
    • Fluck C.E., Deladoey J., Nayak S., et al. Autosomal dominant neurohypophyseal diabetes insipidus in a Swiss family, caused by a novel mutation (C59Delta/A60W) in the neurophysin moiety of prepro-vasopressin-neurophysin II (AVP-NP II). Eur J Endocrinol 145 (2001) 439-444
    • (2001) Eur J Endocrinol , vol.145 , pp. 439-444
    • Fluck, C.E.1    Deladoey, J.2    Nayak, S.3
  • 150
    • 0027381580 scopus 로고
    • Glu-47, which forms a salt bridge between neurophysin-II and arginine vasopressin, is deleted in patients with familial central diabetes insipidus
    • Yuasa H., Ito M., Nagasaki H., et al. Glu-47, which forms a salt bridge between neurophysin-II and arginine vasopressin, is deleted in patients with familial central diabetes insipidus. J Clin Endocrinol Metab 77 (1993) 600-604
    • (1993) J Clin Endocrinol Metab , vol.77 , pp. 600-604
    • Yuasa, H.1    Ito, M.2    Nagasaki, H.3
  • 151
    • 13444278558 scopus 로고    scopus 로고
    • Novel mutant vasopressin-neurophysin II gene associated with familial neurohypophyseal diabetes insipidus
    • Miyakoshi M., Kamoi K., Murase T., et al. Novel mutant vasopressin-neurophysin II gene associated with familial neurohypophyseal diabetes insipidus. Endocr J 51 (2004) 551-556
    • (2004) Endocr J , vol.51 , pp. 551-556
    • Miyakoshi, M.1    Kamoi, K.2    Murase, T.3
  • 152
    • 0031732499 scopus 로고    scopus 로고
    • Two novel mutations of the vasopressin gene associated with familial diabetes insipidus and identification of an asymptomatic carrier infant
    • Grant F.D., Ahmadi A., Hosley C.M., et al. Two novel mutations of the vasopressin gene associated with familial diabetes insipidus and identification of an asymptomatic carrier infant. J Clin Endocrinol Metab 83 (1998) 3958-3964
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 3958-3964
    • Grant, F.D.1    Ahmadi, A.2    Hosley, C.M.3
  • 153
    • 0025973553 scopus 로고
    • A single base substitution in the coding region for neurophysin II associated with familial central diabetes insipidus
    • Ito M., Mori Y., Oiso Y., et al. A single base substitution in the coding region for neurophysin II associated with familial central diabetes insipidus. J Clin Invest 87 (1991) 725-728
    • (1991) J Clin Invest , vol.87 , pp. 725-728
    • Ito, M.1    Mori, Y.2    Oiso, Y.3
  • 154
    • 0036236722 scopus 로고    scopus 로고
    • Identification of a novel mutation in the arginine vasopressin-neurophysin II gene in familial central diabetes insipidus
    • Bullmann C., Kotzka J., Grimm T., et al. Identification of a novel mutation in the arginine vasopressin-neurophysin II gene in familial central diabetes insipidus. Exp Clin Endocrinol Diabetes 110 (2002) 134-137
    • (2002) Exp Clin Endocrinol Diabetes , vol.110 , pp. 134-137
    • Bullmann, C.1    Kotzka, J.2    Grimm, T.3
  • 155
    • 0028948492 scopus 로고
    • Two novel mutations in the coding region for neurophysin-II associated with familial central diabetes insipidus
    • Nagasaki H., Ito M., Yuasa H., et al. Two novel mutations in the coding region for neurophysin-II associated with familial central diabetes insipidus. J Clin Endocrinol Metab 80 (1995) 1352-1356
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 1352-1356
    • Nagasaki, H.1    Ito, M.2    Yuasa, H.3
  • 156
    • 0030032680 scopus 로고    scopus 로고
    • A novel mutation in the coding region for neurophysin-II is associated with autosomal dominant neurohypophyseal diabetes insipidus
    • Rauch F., Lenzner C., Nurnberg P., et al. A novel mutation in the coding region for neurophysin-II is associated with autosomal dominant neurohypophyseal diabetes insipidus. Clin Endocrinol (Oxf) 44 (1996) 45-51
    • (1996) Clin Endocrinol (Oxf) , vol.44 , pp. 45-51
    • Rauch, F.1    Lenzner, C.2    Nurnberg, P.3
  • 157
    • 9344256023 scopus 로고    scopus 로고
    • A new type of familial central diabetes insipidus caused by a single base substitution in the neurophysin II coding region of the vasopressin gene
    • Ueta Y., Taniguchi S., Yoshida A., et al. A new type of familial central diabetes insipidus caused by a single base substitution in the neurophysin II coding region of the vasopressin gene. J Clin Endocrinol Metab 81 (1996) 1787-1790
    • (1996) J Clin Endocrinol Metab , vol.81 , pp. 1787-1790
    • Ueta, Y.1    Taniguchi, S.2    Yoshida, A.3
  • 158
    • 0032801459 scopus 로고    scopus 로고
    • A novel mutation (R97C) in the neurophysin moiety of prepro-vasopressin-neurophysin II associated with autosomal-dominant neurohypophyseal diabetes insipidus
    • Rutishauser J., Kopp P., Gaskill M.B., et al. A novel mutation (R97C) in the neurophysin moiety of prepro-vasopressin-neurophysin II associated with autosomal-dominant neurohypophyseal diabetes insipidus. Mol Genet Metab 67 (1999) 89-92
    • (1999) Mol Genet Metab , vol.67 , pp. 89-92
    • Rutishauser, J.1    Kopp, P.2    Gaskill, M.B.3
  • 159
    • 0035665143 scopus 로고    scopus 로고
    • A new mutation of the arginine vasopressin-neurophysin II gene in a family with autosomal dominant neurohypophyseal diabetes insipidus
    • Mundschenk J., Rittig S., Siggaard C., et al. A new mutation of the arginine vasopressin-neurophysin II gene in a family with autosomal dominant neurohypophyseal diabetes insipidus. Exp Clin Endocrinol Diabetes 109 (2001) 406-409
    • (2001) Exp Clin Endocrinol Diabetes , vol.109 , pp. 406-409
    • Mundschenk, J.1    Rittig, S.2    Siggaard, C.3
  • 160
    • 0035715968 scopus 로고    scopus 로고
    • A missense mutation encoding cys(67) -> gly in neurophysin II is associated with early onset autosomal dominant neurohypophyseal diabetes insipidus
    • DiMeglio L.A., Gagliardi P.C., Browning J.E., et al. A missense mutation encoding cys(67) -> gly in neurophysin II is associated with early onset autosomal dominant neurohypophyseal diabetes insipidus. Mol Genet Metab 72 (2001) 39-44
    • (2001) Mol Genet Metab , vol.72 , pp. 39-44
    • DiMeglio, L.A.1    Gagliardi, P.C.2    Browning, J.E.3
  • 161
    • 9444283785 scopus 로고    scopus 로고
    • Identification of a novel mutation in the arginine vasopressin-neurophysin II gene affecting the sixth intrachain disulfide bridge of the neurophysin II moiety
    • Baglioni S., Corona G., Maggi M., et al. Identification of a novel mutation in the arginine vasopressin-neurophysin II gene affecting the sixth intrachain disulfide bridge of the neurophysin II moiety. Eur J Endocrinol 151 (2004) 605-611
    • (2004) Eur J Endocrinol , vol.151 , pp. 605-611
    • Baglioni, S.1    Corona, G.2    Maggi, M.3
  • 162
    • 27744562983 scopus 로고    scopus 로고
    • Clinical features, diagnosis and molecular studies of familial central diabetes insipidus
    • Davies J.H., Penney M., Abbes A.P., et al. Clinical features, diagnosis and molecular studies of familial central diabetes insipidus. Horm Res 64 (2005) 231-237
    • (2005) Horm Res , vol.64 , pp. 231-237
    • Davies, J.H.1    Penney, M.2    Abbes, A.P.3
  • 163
    • 0036395154 scopus 로고    scopus 로고
    • A missense mutation encoding Cys73Phe in neurophysin II is associated with autosomal dominant neurohypophyseal diabetes insipidus
    • Santiprabhob J., Browning J., and Repaske D. A missense mutation encoding Cys73Phe in neurophysin II is associated with autosomal dominant neurohypophyseal diabetes insipidus. Mol Genet Metab 77 (2002) 112-118
    • (2002) Mol Genet Metab , vol.77 , pp. 112-118
    • Santiprabhob, J.1    Browning, J.2    Repaske, D.3
  • 164
    • 0034145489 scopus 로고    scopus 로고
    • Familial neurohypophyseal diabetes insipidus associated with a novel mutation in the vasopressin-neurophysin II gene
    • Fujii H., Iida S., and Moriwaki K. Familial neurohypophyseal diabetes insipidus associated with a novel mutation in the vasopressin-neurophysin II gene. Int J Mol Med 5 (2000) 229-234
    • (2000) Int J Mol Med , vol.5 , pp. 229-234
    • Fujii, H.1    Iida, S.2    Moriwaki, K.3
  • 165
    • 0034643646 scopus 로고    scopus 로고
    • [Identification of a new mutation (CysII6Gly) in a family with neurogenic diabetes insipidus.]
    • van den Akker E.L., de Groot M.R., Abbes A.P., et al. [Identification of a new mutation (CysII6Gly) in a family with neurogenic diabetes insipidus.]. Ned Tijdschr Geneeskd 144 (2000) 941-945
    • (2000) Ned Tijdschr Geneeskd , vol.144 , pp. 941-945
    • van den Akker, E.L.1    de Groot, M.R.2    Abbes, A.P.3
  • 166
    • 0033987736 scopus 로고    scopus 로고
    • Mutation nomenclature extensions and suggestions to describe complex mutations. A discussion
    • den Dunnen J.T., and Antonarakis S.E. Mutation nomenclature extensions and suggestions to describe complex mutations. A discussion. Hum Mutat 15 (2000) 7-12
    • (2000) Hum Mutat , vol.15 , pp. 7-12
    • den Dunnen, J.T.1    Antonarakis, S.E.2


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