메뉴 건너뛰기




Volumn 24, Issue 5, 2010, Pages 1616-1629

Glycoprotein nonmetastatic melanoma protein b, a melanocytic cell marker, is a melanosome-specific and proteolytically released protein

Author keywords

Ectodomain shedding; Glycosylation; Phorbol ester

Indexed keywords

CALCIUM ION; CELL PROTEIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; GLYCOPROTEIN GP 100; GLYCOPROTEIN NONMETASTATIC MELANOMA PROTEIN B; MELAN A; PMEL17; UNCLASSIFIED DRUG; GPNMB PROTEIN, HUMAN; MELANOCYTE LINEAGE SPECIFIC ANTIGEN GP100; MELANOCYTE LINEAGE-SPECIFIC ANTIGEN GP100; MEMBRANE PROTEIN; TUMOR MARKER;

EID: 77952293797     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.09-151019     Document Type: Article
Times cited : (98)

References (74)
  • 1
    • 0029081168 scopus 로고
    • Melanosomes are specialized members of the lysosomal lineage of organelles
    • Orlow, S. J. (1995) Melanosomes are specialized members of the lysosomal lineage of organelles. J. Invest. Dermatol. 105, 3-7
    • (1995) J. Invest. Dermatol. , vol.105 , pp. 3-7
    • Orlow, S.J.1
  • 2
    • 0001259952 scopus 로고
    • Chemical composition and terminology of specialized organelles (melanosomes and melanin granules) in mammalian melanocytes
    • Seiji, M., Fitzpatrick, T. B., Simpson, R. T., and Birbeck, M. S. C. (1963) Chemical composition and terminology of specialized organelles (melanosomes and melanin granules) in mammalian melanocytes. Nature 197, 1082-1084
    • (1963) Nature , vol.197 , pp. 1082-1084
    • Seiji, M.1    Fitzpatrick, T.B.2    Simpson, R.T.3    Birbeck, M.S.C.4
  • 3
    • 67649216556 scopus 로고    scopus 로고
    • Physiological factors that regulate skin pigmentation
    • Yamaguchi, Y., and Hearing, V. J. (2009) Physiological factors that regulate skin pigmentation. BioFactors 35, 193-199
    • (2009) BioFactors , vol.35 , pp. 193-199
    • Yamaguchi, Y.1    Hearing, V.J.2
  • 5
    • 0023573247 scopus 로고
    • A melanocyte-specific complementary DNA clone whose expression is inducible by melanotropin and isobutylmethyl xanthine
    • Kwon, B. S., Halaban, R., Kim, G. S., Usack, L., Pomerantz, S. H., and Haq, A. K. (1987) A melanocyte-specific complementary DNA clone whose expression is inducible by melanotropin and isobutylmethyl xanthine. Mol. Biol. Med. 4, 339-355 (Pubitemid 18029265)
    • (1987) Molecular Biology and Medicine , vol.4 , Issue.6 , pp. 339-355
    • Kwon, B.S.1    Halaban, R.2    Kim, G.S.3    Usack, L.4    Pomerantz, S.5    Haq, A.K.6
  • 7
    • 0035200704 scopus 로고    scopus 로고
    • Pmel17 initiates premelanosome morphogenesis within multivesicular bodies
    • Berson, J. F., Harper, D. C., Tenza, D., Raposo, G., and Marks, M. S. (2001) Pmel17 initiates premelanosome morphogenesis within multivesicular bodies. Mol. Biol. Cell. 12, 3451-3464 (Pubitemid 33108478)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.11 , pp. 3451-3464
    • Berson, J.F.1    Harper, D.C.2    Tenza, D.3    Raposo, G.4    Marks, M.S.5
  • 9
    • 38349177843 scopus 로고    scopus 로고
    • Premelanosome amyloid-like fibrils are composed of only golgi-processed forms of Pmel17 that have been proteolytically processed in endosomes
    • Harper, D. C., Theos, A. C., Herman, K. E., Tenza, D., Raposo, G., and Marks, M. S. (2008) Premelanosome amyloid-like fibrils are composed of only golgi-processed forms of Pmel17 that have been proteolytically processed in endosomes. J. Biol. Chem. 283, 2307-2322
    • (2008) J. Biol. Chem. , vol.283 , pp. 2307-2322
    • Harper, D.C.1    Theos, A.C.2    Herman, K.E.3    Tenza, D.4    Raposo, G.5    Marks, M.S.6
  • 10
    • 33746323972 scopus 로고    scopus 로고
    • The repeat domain of the melanosomal matrix protein PMEL17/GP100 is required for the formation of organellar fibers
    • Hoashi, T., Muller, J., Vieira, W. D., Rouzaud, F., Kikuchi, K., Tamaki, K., and Hearing, V. J. (2006) The repeat domain of the melanosomal matrix protein PMEL17/GP100 is required for the formation of organellar fibers. J. Biol. Chem. 281, 21198-21208
    • (2006) J. Biol. Chem. , vol.281 , pp. 21198-21208
    • Hoashi, T.1    Muller, J.2    Vieira, W.D.3    Rouzaud, F.4    Kikuchi, K.5    Tamaki, K.6    Hearing, V.J.7
  • 14
    • 17144379660 scopus 로고    scopus 로고
    • MART-1 is required for the function of the melanosomal matrix protein Pmel17/gp100 and the maturation of melanosomes
    • Hoashi, T., Watabe, H., Muller, J., Yamaguchi, Y., Vieira, W. D., and Hearing, V. J. (2005) MART-1 is required for the function of the melanosomal matrix protein Pmel17/gp100 and the maturation of melanosomes. J. Biol. Chem. 280, 14006-14016
    • (2005) J. Biol. Chem. , vol.280 , pp. 14006-14016
    • Hoashi, T.1    Watabe, H.2    Muller, J.3    Yamaguchi, Y.4    Vieira, W.D.5    Hearing, V.J.6
  • 19
    • 0036311036 scopus 로고    scopus 로고
    • Coming of age of melanogenesis-related proteins
    • Slominski, A. (2002) Coming of age of melanogenesis-related proteins. Arch. Pathol. Lab. Med. 126, 775-777
    • (2002) Arch. Pathol. Lab. Med. , vol.126 , pp. 775-777
    • Slominski, A.1
  • 20
    • 0036311384 scopus 로고    scopus 로고
    • Tyrosinase expression in malignant melanoma, desmoplastic melanoma, and peripheral nerve tumors; an immunohistochemical study
    • Boyle, J. L., Haupt, H. M., Stern, J. B., and Multhaupt, H. A. B. (2002) Tyrosinase expression in malignant melanoma, desmoplastic melanoma, and peripheral nerve tumors; an immunohistochemical study. Arch. Pathol. Lab. Med. 126, 816-822
    • (2002) Arch. Pathol. Lab. Med. , vol.126 , pp. 816-822
    • Boyle, J.L.1    Haupt, H.M.2    Stern, J.B.3    Multhaupt, H.A.B.4
  • 21
    • 0032886830 scopus 로고    scopus 로고
    • Microphthalmia transcription factor: A sensitive and specific melanocyte marker for melanoma diagnosis
    • King, R. A., Weilbaecher, K. N., McGill, G., Cooley, E., Mihm, M., and Fisher, D. E. (1999) Microphthalmia transcription factor: a sensitive and specific melanocyte marker for melanoma diagnosis. Am. J. Pathol. 155, 731-738 (Pubitemid 29426819)
    • (1999) American Journal of Pathology , vol.155 , Issue.3 , pp. 731-738
    • King, R.1    Weilbaecher, K.N.2    McGill, G.3    Cooley, E.4    Mihm, M.5    Fisher, D.E.6
  • 22
    • 24344439755 scopus 로고    scopus 로고
    • Loss of S100 antigenicity in metastatic melanoma
    • Aisner, D. L., Maker, A., Rosenberg, S. A., and Berman, D. M. (2005) Loss of S100 antigenicity in metastatic melanoma. Hum. Pathol. 36, 1016-1019
    • (2005) Hum. Pathol. , vol.36 , pp. 1016-1019
    • Aisner, D.L.1    Maker, A.2    Rosenberg, S.A.3    Berman, D.M.4
  • 23
    • 39049163533 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 expression in desmoplastic melanoma
    • Hoashi, T., Kikuchi, K., Watanabe, S., Nanko, H., and Tamaki, K. (2008) Matrix metalloproteinase-9 expression in desmoplastic melanoma. J. Dermatol. 35, 122-123
    • (2008) J. Dermatol. , vol.35 , pp. 122-123
    • Hoashi, T.1    Kikuchi, K.2    Watanabe, S.3    Nanko, H.4    Tamaki, K.5
  • 28
    • 0033555277 scopus 로고    scopus 로고
    • The structure of a PKD domain from polycystin-1: Implications for polycystic kidney disease
    • Bycroft, M., Bateman, A., Clarke, J., Hamill, S. J., Sandford, R., Thomas, R. L., and Chothia, C. (1999) The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease. EMBO J. 18, 297-305
    • (1999) EMBO J. , vol.18 , pp. 297-305
    • Bycroft, M.1    Bateman, A.2    Clarke, J.3    Hamill, S.J.4    Sandford, R.5    Thomas, R.L.6    Chothia, C.7
  • 29
    • 0036005962 scopus 로고    scopus 로고
    • Apolipoprotein (a): Structure-function relationship at the lysine-binding site and plasminogen activator cleavage site
    • Angles-Cano, E., and Rojas, G. (2002) Apolipoprotein (a): structure-function relationship at the lysine-binding site and plasminogen activator cleavage site. Biol. Chem. 383, 93-99
    • (2002) Biol. Chem. , vol.383 , pp. 93-99
    • Angles-Cano, E.1    Rojas, G.2
  • 30
    • 0028948608 scopus 로고
    • Kringle-dependent structural and functional polymorphism of apolipoprotein (a)
    • Scanu, A. M., and Edelstein, C. (1995) Kringle-dependent structural and functional polymorphism of apolipoprotein (a). Biochim. Biophys. Acta 1256, 1-12
    • (1995) Biochim. Biophys. Acta , vol.1256 , pp. 1-12
    • Scanu, A.M.1    Edelstein, C.2
  • 31
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti, E. (1996) RGD and other recognition sequences for integrins. Annu. Rev. Cell. Dev. Biol. 12, 697-715
    • (1996) Annu. Rev. Cell. Dev. Biol. , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 32
    • 66949112599 scopus 로고    scopus 로고
    • Gpnmb is a melanosome-associated glycoprotein that contributes to melanocyte/keratinocyte adhesion in a RGD-dependent fashion
    • Tomihari, M., Hwang, S. H., Chung, J. S., Cruz Jr., P. D., and Ariizumi, K. (2009) Gpnmb is a melanosome-associated glycoprotein that contributes to melanocyte/keratinocyte adhesion in a RGD-dependent fashion. Exp. Dermatol. 18, 586-595
    • (2009) Exp. Dermatol. , vol.18 , pp. 586-595
    • Tomihari, M.1    Hwang, S.H.2    Chung, J.S.3    Cruz Jr., P.D.4    Ariizumi, K.5
  • 34
    • 77952295347 scopus 로고    scopus 로고
    • The secreted form of a melanocyte membrane-bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding
    • E-pub ahead of print doi: 10.1096/fj.09-140921
    • Hoashi, T., Tamaki, K., and Hearing, V. J. (2009) The secreted form of a melanocyte membrane-bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding. [E-pub ahead of print] FASEB. J. doi: 10.1096/fj.09-140921
    • (2009) FASEB. J.
    • Hoashi, T.1    Tamaki, K.2    Hearing, V.J.3
  • 35
    • 0037986392 scopus 로고    scopus 로고
    • Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis
    • Berson, J. F., Theos, A. C., Harper, D. C., Tenza, D., Raposo, G., and Marks, M. S. (2003) Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J. Cell Biol. 161, 521-533
    • (2003) J. Cell Biol. , vol.161 , pp. 521-533
    • Berson, J.F.1    Theos, A.C.2    Harper, D.C.3    Tenza, D.4    Raposo, G.5    Marks, M.S.6
  • 36
    • 3142546894 scopus 로고    scopus 로고
    • Epitope mapping of the melanosomal matrix protein gp100 (PMEL17): Rapid processing in the endoplasmic reticulum and glycosylation in the early Golgi compartment
    • Yasumoto, K., Watabe, H., Valencia, J. C., Kushimoto, T., Kobayashi, T., Appella, E., and Hearing, V. J. (2004) Epitope mapping of the melanosomal matrix protein gp100 (PMEL17): Rapid processing in the endoplasmic reticulum and glycosylation in the early Golgi compartment. J. Biol. Chem. 279, 28330-28338
    • (2004) J. Biol. Chem. , vol.279 , pp. 28330-28338
    • Yasumoto, K.1    Watabe, H.2    Valencia, J.C.3    Kushimoto, T.4    Kobayashi, T.5    Appella, E.6    Hearing, V.J.7
  • 38
    • 0023818435 scopus 로고
    • Identification of a secreted Mr 95,000 glycoprotein in human melanocytes and melanomas by a melanocyte-specific monoclonal antibody
    • Vogel, A. M., and Esclamodo, R. M. (1988) Identification of a secreted Mr 95,000 glycoprotein in human melanocytes and melanomas by a melanocyte-specific monoclonal antibody. Cancer Res. 48, 1286-1294
    • (1988) Cancer Res. , vol.48 , pp. 1286-1294
    • Vogel, A.M.1    Esclamodo, R.M.2
  • 39
    • 59049094283 scopus 로고    scopus 로고
    • Formation of Pmel17 amyloid is regulated by juxtamembrane metalloproteinase cleavage, and the resulting C-terminal fragment is a substrate for gamma-secretase
    • Kummer, M. P., Maruyama, H., Huelsmann, C., Baches, S., Weggen, S., and Koo, E. H. (2009) Formation of Pmel17 amyloid is regulated by juxtamembrane metalloproteinase cleavage, and the resulting C-terminal fragment is a substrate for gamma-secretase. J. Biol. Chem. 284, 2296-2306
    • (2009) J. Biol. Chem. , vol.284 , pp. 2296-2306
    • Kummer, M.P.1    Maruyama, H.2    Huelsmann, C.3    Baches, S.4    Weggen, S.5    Koo, E.H.6
  • 40
    • 0034876636 scopus 로고    scopus 로고
    • The AP-3-dependent targeting of the melanosomal glycoprotein QNR-71 requires a di-leucine-based sorting signal
    • Le Borgne, R., Planque, N., Martin, P., Dewitte, F., Saule, S., and Hoflack, B. (2001) The AP-3-dependent targeting of the melanosomal glycoprotein QNR-71 requires a di-leucine-based sorting signal. J. Cell Sci. 114, 2831-2841
    • (2001) J. Cell Sci. , vol.114 , pp. 2831-2841
    • Le Borgne, R.1    Planque, N.2    Martin, P.3    Dewitte, F.4    Saule, S.5    Hoflack, B.6
  • 41
    • 0035185649 scopus 로고    scopus 로고
    • Cloning and characterization of osteoactivin, a novel cDNA expressed in osteoblasts
    • Safadi, F. F., Xu, J., Smock, S. L., Rico, M. C., Owen, T. A., and Popoff, S. N. (2001) Cloning and characterization of osteoactivin, a novel cDNA expressed in osteoblasts. J. Cell Biochem. 84, 12-26
    • (2001) J. Cell Biochem. , vol.84 , pp. 12-26
    • Safadi, F.F.1    Xu, J.2    Smock, S.L.3    Rico, M.C.4    Owen, T.A.5    Popoff, S.N.6
  • 44
    • 42049100127 scopus 로고    scopus 로고
    • Osteoactivin is a novel osteoclastic protein and plays a key role in osteoclast differentiation and activity
    • Sheng, M. H., Wergedal, J. E., Mohan, S., and Lau, K. H. (2008) Osteoactivin is a novel osteoclastic protein and plays a key role in osteoclast differentiation and activity. FEBS. Lett. 582, 1451-1458
    • (2008) FEBS. Lett. , vol.582 , pp. 1451-1458
    • Sheng, M.H.1    Wergedal, J.E.2    Mohan, S.3    Lau, K.H.4
  • 46
    • 0035896629 scopus 로고    scopus 로고
    • Molecular cloning of a dendritic cell-associated transmembrane protein, DC-HIL, that promotes RGD-dependent adhesion of endothelial cells through recognition of heparan sulfate proteoglycans
    • Shikano, S., Bonkobara, M., Zukas, P. K., and Ariizumi, K. (2001) Molecular cloning of a dendritic cell-associated transmembrane protein, DC-HIL, that promotes RGD-dependent adhesion of endothelial cells through recognition of heparan sulfate proteoglycans. J. Biol. Chem. 276, 8125-8134
    • (2001) J. Biol. Chem. , vol.276 , pp. 8125-8134
    • Shikano, S.1    Bonkobara, M.2    Zukas, P.K.3    Ariizumi, K.4
  • 47
    • 34248226374 scopus 로고    scopus 로고
    • Gpnmb is induced in macrophages by IFN-γ and lipopolysaccharide and acts as a feedback regulator of proinflammatory responses
    • Ripoll, V. M., Irvine, K. M., Ravasi, T., Sweet, M. J., and Hume, D. A. (2007) Gpnmb is induced in macrophages by IFN-γ and lipopolysaccharide and acts as a feedback regulator of proinflammatory responses. J. Immunol. 178, 6557-6566
    • (2007) J. Immunol. , vol.178 , pp. 6557-6566
    • Ripoll, V.M.1    Irvine, K.M.2    Ravasi, T.3    Sweet, M.J.4    Hume, D.A.5
  • 48
    • 43649099521 scopus 로고    scopus 로고
    • Pharmacologically enhanced expression of GPNMB increases the sensitivity of melanoma cells to the CR011-vcMMAE antibody-drug conjugate
    • Qian, X., Mills, E., Torgov, M., LaRochelle, W. J., and Jeffers, M. (2008) Pharmacologically enhanced expression of GPNMB increases the sensitivity of melanoma cells to the CR011-vcMMAE antibody-drug conjugate. Mol. Oncol. 2, 81-93
    • (2008) Mol. Oncol. , vol.2 , pp. 81-93
    • Qian, X.1    Mills, E.2    Torgov, M.3    LaRochelle, W.J.4    Jeffers, M.5
  • 53
    • 0035911146 scopus 로고    scopus 로고
    • Distinct protein sorting and localization to pre-melanosomes, melanosomes and lysosomes in pigmented melanocytic cells
    • Raposo, G., Tenza, D., Murphy, D. M., Berson, J. F., and Marks, M. S. (2001) Distinct protein sorting and localization to pre-melanosomes, melanosomes and lysosomes in pigmented melanocytic cells. J. Cell Biol. 152, 809-823
    • (2001) J. Cell Biol. , vol.152 , pp. 809-823
    • Raposo, G.1    Tenza, D.2    Murphy, D.M.3    Berson, J.F.4    Marks, M.S.5
  • 56
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R. D., Donaldson, J. G., and Lippincott-Schwartz, J. (1992) Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116, 1071-1080
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 57
    • 33644532558 scopus 로고    scopus 로고
    • A lumenal domain-dependent pathway for sorting to intralumenal vesicles of multivesicular endosomes involved in organelle morphogenesis
    • Theos, A. C., Truschel, S. T., Tenza, D., Hurbain, I., Harper, D. C., Berson, J. F., Thomas, P. C., Raposo, G., and Marks, M. S. (2006) A lumenal domain-dependent pathway for sorting to intralumenal vesicles of multivesicular endosomes involved in organelle morphogenesis. Dev. Cell 10, 343-354
    • (2006) Dev. Cell , vol.10 , pp. 343-354
    • Theos, A.C.1    Truschel, S.T.2    Tenza, D.3    Hurbain, I.4    Harper, D.C.5    Berson, J.F.6    Thomas, P.C.7    Raposo, G.8    Marks, M.S.9
  • 58
    • 0019377631 scopus 로고
    • Synthesis and processing of asparagine-linked oligosaccharides
    • Hubbard, S. C., and Ivatt, R. J. (1981) Synthesis and processing of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 50, 555-583
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 555-583
    • Hubbard, S.C.1    Ivatt, R.J.2
  • 59
    • 57649221135 scopus 로고    scopus 로고
    • Amyloid precursor protein trafficking, processing, and function
    • Thinakaran, G., and Koo, E. H. (2008) Amyloid precursor protein trafficking, processing, and function. J. Biol. Chem. 283, 29615-29619
    • (2008) J. Biol. Chem. , vol.283 , pp. 29615-29619
    • Thinakaran, G.1    Koo, E.H.2
  • 61
    • 0028921581 scopus 로고
    • Calmodulin-binding domains: Just two faced or multi-faceted?
    • James, P., Vorherr, T., and Carafoli, E. (1995) Calmodulin-binding domains: just two faced or multi-faceted?. Trends Biochem. Sci. 20, 38-42
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 38-42
    • James, P.1    Vorherr, T.2    Carafoli, E.3
  • 64
    • 38049005632 scopus 로고    scopus 로고
    • Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain
    • Lambert, D. W., Clarke, N. E., Hooper, N. M., and Turner, A. J. (2008) Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain. FEBS Lett. 582, 385-390
    • (2008) FEBS Lett. , vol.582 , pp. 385-390
    • Lambert, D.W.1    Clarke, N.E.2    Hooper, N.M.3    Turner, A.J.4
  • 65
    • 13144250144 scopus 로고    scopus 로고
    • The distal ectodomain of angiotensin-converting enzyme regulates its cleavage-secretion from the cell surface
    • Sadhukhan, R., Sen, G. C., Ramchandran, R., and Sen, I. (1998) The distal ectodomain of angiotensin-converting enzyme regulates its cleavage-secretion from the cell surface. Proc. Natl. Acad. Sci. U. S. A. 95, 138-143
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 138-143
    • Sadhukhan, R.1    Sen, G.C.2    Ramchandran, R.3    Sen, I.4
  • 67
    • 0036882397 scopus 로고    scopus 로고
    • Protein ectodomain shedding
    • Arribas, J., and Borroto, A. (2002) Protein ectodomain shedding. Chem. Rev. 102, 4627-4638
    • (2002) Chem. Rev. , vol.102 , pp. 4627-4638
    • Arribas, J.1    Borroto, A.2
  • 68
    • 0029559949 scopus 로고
    • Topical W-7 inhibits ultraviolet radiation-induced melanogenesis in Skh:HR2 pigmented hairless mice
    • Dowdy, J. C., Anthony, F. A., and Costlow, M. E. (1995) Topical W-7 inhibits ultraviolet radiation-induced melanogenesis in Skh:HR2 pigmented hairless mice. Photodermatol. Photoimmunol. Photomed. 11, 143-148
    • (1995) Photodermatol. Photoimmunol. Photomed. , vol.11 , pp. 143-148
    • Dowdy, J.C.1    Anthony, F.A.2    Costlow, M.E.3
  • 70
    • 0034723418 scopus 로고    scopus 로고
    • Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network
    • Skovronsky, D. M., Moore, D. B., Milla, M. E., Doms, R. W., and Lee, V. M. (2000) Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network. J. Biol. Chem. 275, 2568-2575
    • (2000) J. Biol. Chem. , vol.275 , pp. 2568-2575
    • Skovronsky, D.M.1    Moore, D.B.2    Milla, M.E.3    Doms, R.W.4    Lee, V.M.5
  • 72
    • 25444456658 scopus 로고    scopus 로고
    • The Silver locus product Pmel17/gp100/Silv/ME20: Controversial in name and in function
    • Theos, A. C., Truschel, S. T., Raposo, G., and Marks, M. S. (2005) The Silver locus product Pmel17/gp100/Silv/ME20: controversial in name and in function. Pigment Cell Res. 18, 322-336
    • (2005) Pigment Cell Res. , vol.18 , pp. 322-336
    • Theos, A.C.1    Truschel, S.T.2    Raposo, G.3    Marks, M.S.4
  • 74
    • 0021674392 scopus 로고
    • Determination of DOPA, dopamine, and 5-S-cysteinyl-DOPA in plasma, urine, and tissue samples by high-performance liquid chromatography with electrochemical detection
    • Ito, S., Kato, T., Maruta, K., Fujita, K., and Kurahashi, T. (1984) Determination of DOPA, dopamine, and 5-S-cysteinyl-DOPA in plasma, urine, and tissue samples by high-performance liquid chromatography with electrochemical detection. J. Chromatogr. 311, 154-159 (Pubitemid 15219665)
    • (1984) Journal of Chromatography - Biomedical Applications , vol.311 , Issue.1 , pp. 154-159
    • Ito, S.1    Kato, T.2    Maruta, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.