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Volumn 26, Issue 3, 2013, Pages 300-315

PMEL: A pigment cell-specific model for functional amyloid formation

Author keywords

Alzheimer Disease; Fibrils; Melanosome; Multivesicular body; Pmel17; Proprotein processing; Silver

Indexed keywords

AMYLOID; GLYCOPROTEIN; METALLOPROTEINASE; MONOCLONAL ANTIBODY; OLIGOSACCHARIDE; PMEL PROTEIN; SIGNAL PEPTIDASE; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

EID: 84876816383     PISSN: 17551471     EISSN: 1755148X     Source Type: Journal    
DOI: 10.1111/pcmr.12067     Document Type: Article
Times cited : (147)

References (120)
  • 1
    • 83755205906 scopus 로고    scopus 로고
    • Coat color dilution in mice because of inactivation of the melanoma antigen MART-1
    • Aydin, I.T., Hummler, E., Smit, N.P., and Beermann, F. (2012). Coat color dilution in mice because of inactivation of the melanoma antigen MART-1. Pigment Cell Melanoma Res. 25, 37-46.
    • (2012) Pigment Cell Melanoma Res. , vol.25 , pp. 37-46
    • Aydin, I.T.1    Hummler, E.2    Smit, N.P.3    Beermann, F.4
  • 2
    • 79960743373 scopus 로고    scopus 로고
    • MVB vesicle formation: ESCRT-dependent, ESCRT-independent and everything in between
    • Babst, M. (2011). MVB vesicle formation: ESCRT-dependent, ESCRT-independent and everything in between. Curr. Opin. Cell Biol. 23, 452-457.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 452-457
    • Babst, M.1
  • 3
    • 0035200704 scopus 로고    scopus 로고
    • Pmel17 initiates premelanosome morphogenesis within multivesicular bodies
    • Berson, J.F., Harper, D., Tenza, D., Raposo, G., and Marks, M.S. (2001). Pmel17 initiates premelanosome morphogenesis within multivesicular bodies. Mol. Biol. Cell 12, 3451-3464.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3451-3464
    • Berson, J.F.1    Harper, D.2    Tenza, D.3    Raposo, G.4    Marks, M.S.5
  • 4
    • 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
  • 5
    • 0005144016 scopus 로고
    • Electron microscopy of melanocytes: the fine structure of hair-bulb premelanosomes
    • Birbeck, M.S.C. (1963). Electron microscopy of melanocytes: the fine structure of hair-bulb premelanosomes. Ann. N. Y. Acad. Sci. 100, 540-547.
    • (1963) Ann. N. Y. Acad. Sci. , vol.100 , pp. 540-547
    • Birbeck, M.S.C.1
  • 9
    • 33750603074 scopus 로고    scopus 로고
    • A missense mutation in PMEL17 is associated with the Silver coat color in the horse
    • Brunberg, E., Andersson, L., Cothran, G., Sandberg, K., Mikko, S., and Lindgren, G. (2006). A missense mutation in PMEL17 is associated with the Silver coat color in the horse. BMC Genet. 7, 46.
    • (2006) BMC Genet. , vol.7 , pp. 46
    • Brunberg, E.1    Andersson, L.2    Cothran, G.3    Sandberg, K.4    Mikko, S.5    Lindgren, G.6
  • 10
    • 84863988708 scopus 로고    scopus 로고
    • A molecular history of the amyloidoses
    • Buxbaum, J.N., and Linke, R.P. (2012). A molecular history of the amyloidoses. J. Mol. Biol. 421, 142-159.
    • (2012) J. Mol. Biol. , vol.421 , pp. 142-159
    • Buxbaum, J.N.1    Linke, R.P.2
  • 11
    • 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
  • 13
    • 0029912354 scopus 로고    scopus 로고
    • Polymerization of 5,6-dihydroxyindole-2-carboxylic acid to melanin by the pmel 17/silver locus protein
    • Chakraborty, A.K., Platt, J.T., Kim, K.K., Kwon, B.S., Bennett, D.C., and Pawelek, J.M. (1996). Polymerization of 5, 6-dihydroxyindole-2-carboxylic acid to melanin by the pmel 17/silver locus protein. Eur. J. Biochem. 236, 180-188.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 180-188
    • Chakraborty, A.K.1    Platt, J.T.2    Kim, K.K.3    Kwon, B.S.4    Bennett, D.C.5    Pawelek, J.M.6
  • 15
    • 0035890055 scopus 로고    scopus 로고
    • Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca2 + stabilization
    • Chen, C.-D., Huff, M.E., Matteson, J., Page, L.J., Phillips, R., Kelly, J.W., and Balch, W.E. (2001). Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca2 + stabilization. EMBO J. 20, 6277-6287.
    • (2001) EMBO J. , vol.20 , pp. 6277-6287
    • Chen, C.-D.1    Huff, M.E.2    Matteson, J.3    Page, L.J.4    Phillips, R.5    Kelly, J.W.6    Balch, W.E.7
  • 17
    • 0029810922 scopus 로고    scopus 로고
    • Anti-melanoma monoclonal antibody HMB-45 on enhanced chemiluminescence-western blotting recognizes a 30-35 kDa melanosome-associated sialated glycoprotein
    • Chiamenti, A.M., Vella, F., Bonetti, F., Pea, M., Ferrari, S., Martignoni, G., Benedetti, A., and Suzuki, H. (1996). Anti-melanoma monoclonal antibody HMB-45 on enhanced chemiluminescence-western blotting recognizes a 30-35 kDa melanosome-associated sialated glycoprotein. Melanoma Res. 6, 291-298.
    • (1996) Melanoma Res. , vol.6 , pp. 291-298
    • Chiamenti, A.M.1    Vella, F.2    Bonetti, F.3    Pea, M.4    Ferrari, S.5    Martignoni, G.6    Benedetti, A.7    Suzuki, H.8
  • 18
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., and Dobson, C.M. (2006). Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 19
    • 79954609544 scopus 로고    scopus 로고
    • Role of matrix metalloproteinase 3-mediated alpha-synuclein cleavage in dopaminergic cell death
    • Choi, D.H., Kim, Y.J., Kim, Y.G., Joh, T.H., Beal, M.F., and Kim, Y.S. (2011). Role of matrix metalloproteinase 3-mediated alpha-synuclein cleavage in dopaminergic cell death. J. Biol. Chem. 286, 14168-14177.
    • (2011) J. Biol. Chem. , vol.286 , pp. 14168-14177
    • Choi, D.H.1    Kim, Y.J.2    Kim, Y.G.3    Joh, T.H.4    Beal, M.F.5    Kim, Y.S.6
  • 20
    • 31944436548 scopus 로고    scopus 로고
    • Retrotransposon insertion in SILV is responsible for merle patterning of the domestic dog
    • Clark, L.A., Wahl, J.M., Rees, C.A., and Murphy, K.E. (2006). Retrotransposon insertion in SILV is responsible for merle patterning of the domestic dog. Proc. Natl Acad. Sci. USA 103, 1376-1381.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 1376-1381
    • Clark, L.A.1    Wahl, J.M.2    Rees, C.A.3    Murphy, K.E.4
  • 21
    • 70449725586 scopus 로고    scopus 로고
    • AP-1 and KIF13A coordinate endosomal sorting and positioning during melanosome biogenesis
    • Delevoye, C., Hurbain, I., Tenza, D. et al. (2009). AP-1 and KIF13A coordinate endosomal sorting and positioning during melanosome biogenesis. J. Cell Biol. 187, 247-264.
    • (2009) J. Cell Biol. , vol.187 , pp. 247-264
    • Delevoye, C.1    Hurbain, I.2    Tenza, D.3
  • 23
    • 0028926923 scopus 로고
    • Lysosomal hydrolases are present in melanosomes and are elevated in melanizing cells
    • Diment, S., Eidelman, M., Rodriguez, G.M., and Orlow, S.J. (1995). Lysosomal hydrolases are present in melanosomes and are elevated in melanizing cells. J. Biol. Chem. 270, 4213-4215.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4213-4215
    • Diment, S.1    Eidelman, M.2    Rodriguez, G.M.3    Orlow, S.J.4
  • 24
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C.M. (2003). Protein folding and misfolding. Nature 426, 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 25
    • 0029134535 scopus 로고
    • Interaction of melanosomal proteins with melanin
    • Donatien, P.D., and Orlow, S.J. (1995). Interaction of melanosomal proteins with melanin. Eur. J. Biochem. 232, 159-164.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 159-164
    • Donatien, P.D.1    Orlow, S.J.2
  • 26
    • 0038628127 scopus 로고
    • The silver mouse: a recessive color variation
    • Dunn, L.C., and Thigpen, L.W. (1930). The silver mouse: a recessive color variation. J. Heredity 21, 495-498.
    • (1930) J. Heredity , vol.21 , pp. 495-498
    • Dunn, L.C.1    Thigpen, L.W.2
  • 27
    • 0022546741 scopus 로고
    • Unique proteins defined by monoclonal antibodies specific for human melanoma
    • Esclamado, R.M., Gown, A.M., and Vogel, A.M. (1986). Unique proteins defined by monoclonal antibodies specific for human melanoma. Am. J. Surg. 152, 376-385.
    • (1986) Am. J. Surg. , vol.152 , pp. 376-385
    • Esclamado, R.M.1    Gown, A.M.2    Vogel, A.M.3
  • 28
    • 0036727125 scopus 로고    scopus 로고
    • Gamma-secretase-mediated proteolysis in cell-surface-receptor signalling
    • Fortini, M.E. (2002). Gamma-secretase-mediated proteolysis in cell-surface-receptor signalling. Nat. Rev. Mol. Cell Biol. 3, 673-684.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 673-684
    • Fortini, M.E.1
  • 31
    • 0023864209 scopus 로고
    • Carboxypeptidase E
    • Fricker, L.D. (1988). Carboxypeptidase E. Annu. Rev. Physiol. 50, 309-321.
    • (1988) Annu. Rev. Physiol. , vol.50 , pp. 309-321
    • Fricker, L.D.1
  • 33
    • 70449419701 scopus 로고    scopus 로고
    • The Ocular Albinism type 1 (OA1) G-protein coupled receptor functions with MART-1 at early stages of melanogenesis to control melanosome identity and composition
    • Giordano, F., Bonetti, C., Surace, E.M., Marigo, V., and Raposo, G. (2009). The Ocular Albinism type 1 (OA1) G-protein coupled receptor functions with MART-1 at early stages of melanogenesis to control melanosome identity and composition. Hum. Mol. Genet. 18, 4530-4545.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 4530-4545
    • Giordano, F.1    Bonetti, C.2    Surace, E.M.3    Marigo, V.4    Raposo, G.5
  • 34
    • 79961090102 scopus 로고    scopus 로고
    • The ocular albinism type 1 (OA1) GPCR is ubiquitinated and its traffic requires endosomal sorting complex responsible for transport (ESCRT) function
    • Giordano, F., Simoes, S., and Raposo, G. (2011). The ocular albinism type 1 (OA1) GPCR is ubiquitinated and its traffic requires endosomal sorting complex responsible for transport (ESCRT) function. Proc. Natl Acad. Sci. USA 108, 11906-11911.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 11906-11911
    • Giordano, F.1    Simoes, S.2    Raposo, G.3
  • 35
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • Goldschmidt, L., Teng, P.K., Riek, R., and Eisenberg, D. (2010). Identifying the amylome, proteins capable of forming amyloid-like fibrils. Proc. Natl Acad. Sci. USA 107, 3487-3492.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 36
    • 77957782470 scopus 로고    scopus 로고
    • Biology of amyloid: structure, function, and regulation
    • Greenwald, J., and Riek, R. (2010). Biology of amyloid: structure, function, and regulation. Structure 18, 1244-1260.
    • (2010) Structure , vol.18 , pp. 1244-1260
    • Greenwald, J.1    Riek, R.2
  • 37
    • 85027473447 scopus 로고
    • A study of the physiological properties of melanophores with special reference to their role in feather coloration
    • Hamilton, H. (1940). A study of the physiological properties of melanophores with special reference to their role in feather coloration. Anat. Rec. 78, 525-548.
    • (1940) Anat. Rec. , vol.78 , pp. 525-548
    • Hamilton, H.1
  • 39
    • 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
  • 40
    • 80053436599 scopus 로고    scopus 로고
    • Inactivation of the Pmel gene alters melanosome shape but has only a subtle effect on visible pigmentation
    • Hellström, A.R., Watt, B., Fard, S.S. et al. (2011). Inactivation of the Pmel gene alters melanosome shape but has only a subtle effect on visible pigmentation. PLoS Genet. 7, e1002285.
    • (2011) PLoS Genet. , vol.7
    • Hellström, A.R.1    Watt, B.2    Fard, S.S.3
  • 41
    • 0020494253 scopus 로고
    • Origin of melanosome structures and cytochemical localizations of tyrosinase activity in differentiating epidermal melanocytes of newborn mouse skin
    • Hirobe, T. (1982). Origin of melanosome structures and cytochemical localizations of tyrosinase activity in differentiating epidermal melanocytes of newborn mouse skin. J. Exp. Zool. 224, 355-363.
    • (1982) J. Exp. Zool. , vol.224 , pp. 355-363
    • Hirobe, T.1
  • 42
    • 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
  • 43
    • 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, 21198-22208.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21198-22208
    • Hoashi, T.1    Muller, J.2    Vieira, W.D.3    Rouzaud, F.4    Kikuchi, K.5    Tamaki, K.6    Hearing, V.J.7
  • 44
    • 77952295347 scopus 로고    scopus 로고
    • The secreted form of a melanocyte membrane-bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding
    • Hoashi, T., Tamaki, K., and Hearing, V.J. (2010). The secreted form of a melanocyte membrane-bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding. FASEB J. 24, 916-930.
    • (2010) FASEB J. , vol.24 , pp. 916-930
    • Hoashi, T.1    Tamaki, K.2    Hearing, V.J.3
  • 45
    • 80455164835 scopus 로고    scopus 로고
    • Segmental polymorphism in a functional amyloid
    • Hu, K.N., McGlinchey, R.P., Wickner, R.B., and Tycko, R. (2011). Segmental polymorphism in a functional amyloid. Biophys. J. 101, 2242-2450.
    • (2011) Biophys. J. , vol.101 , pp. 2242-2450
    • Hu, K.N.1    McGlinchey, R.P.2    Wickner, R.B.3    Tycko, R.4
  • 47
    • 58149376474 scopus 로고    scopus 로고
    • Electron tomography of early melanosomes: implications for melanogenesis and the generation of fibrillar amyloid sheets
    • Hurbain, I., Geerts, W.J.C., Boudier, T., Marco, S., Verkleij, A., Marks, M.S., and Raposo, G. (2008). Electron tomography of early melanosomes: implications for melanogenesis and the generation of fibrillar amyloid sheets. Proc. Natl Acad. Sci. USA 105, 19726-19731.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 19726-19731
    • Hurbain, I.1    Geerts, W.J.C.2    Boudier, T.3    Marco, S.4    Verkleij, A.5    Marks, M.S.6    Raposo, G.7
  • 48
    • 0034683126 scopus 로고    scopus 로고
    • Amyloids protect the silkmoth oocyte and embryo
    • Iconomidou, V.A., Vriend, G., and Hamodrakas, S.J. (2000). Amyloids protect the silkmoth oocyte and embryo. FEBS Lett. 479, 141-145.
    • (2000) FEBS Lett. , vol.479 , pp. 141-145
    • Iconomidou, V.A.1    Vriend, G.2    Hamodrakas, S.J.3
  • 49
    • 75149180052 scopus 로고    scopus 로고
    • Competing discrete interfacial effects are critical for amyloidogenesis
    • Jean, L., Lee, C.F., Lee, C., Shaw, M., and Vaux, D.J. (2010). Competing discrete interfacial effects are critical for amyloidogenesis. FASEB J.24, 309-317.
    • (2010) FASEB J. , vol.24 , pp. 309-317
    • Jean, L.1    Lee, C.F.2    Lee, C.3    Shaw, M.4    Vaux, D.J.5
  • 50
    • 44249111681 scopus 로고    scopus 로고
    • Coat-colour dilution and hypotrichosis in Hereford crossbred calves
    • Jolly, R.D., Wills, J.L., Kenny, J.E., Cahill, J.I., and Howe, L. (2008). Coat-colour dilution and hypotrichosis in Hereford crossbred calves. N. Z. Vet. J. 56, 74-77.
    • (2008) N. Z. Vet. J. , vol.56 , pp. 74-77
    • Jolly, R.D.1    Wills, J.L.2    Kenny, J.E.3    Cahill, J.I.4    Howe, L.5
  • 52
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: a case study using the Phyre server
    • Kelley, L.A., and Sternberg, M.J.E. (2009). Protein structure prediction on the web: a case study using the Phyre server. Nat. Protoc. 4, 363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 53
    • 0038612852 scopus 로고    scopus 로고
    • Amyloid as a natural product
    • Kelly, J.W., and Balch, W.E. (2003). Amyloid as a natural product. J. Cell Biol. 161, 461-462.
    • (2003) J. Cell Biol. , vol.161 , pp. 461-462
    • Kelly, J.W.1    Balch, W.E.2
  • 55
    • 19944361828 scopus 로고    scopus 로고
    • The Dominant white, Dun and Smoky color variants in chicken are associated with insertion deletion polymorphisms in the PMEL17 gene
    • Kerje, S., Sharma, P., Gunnarsson, U. et al. (2004). The Dominant white, Dun and Smoky color variants in chicken are associated with insertion deletion polymorphisms in the PMEL17 gene. Genetics 168, 1507-1518.
    • (2004) Genetics , vol.168 , pp. 1507-1518
    • Kerje, S.1    Sharma, P.2    Gunnarsson, U.3
  • 57
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum?
    • Klein, W.L., Krafft, G.A., and Finch, C.E. (2001). Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci. 24, 219-224.
    • (2001) Trends Neurosci. , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 58
    • 34047110250 scopus 로고    scopus 로고
    • An investigation into the genetic background of coat colour dilution in a Charolais × German Holstein F2 resource population
    • Kühn, C., and Weikard, R. (2007). An investigation into the genetic background of coat colour dilution in a Charolais × German Holstein F2 resource population. Anim. Genet. 38, 109-113.
    • (2007) Anim. Genet. , vol.38 , pp. 109-113
    • Kühn, C.1    Weikard, R.2
  • 59
    • 69949099775 scopus 로고    scopus 로고
    • A mutation within the transmembrane domain of melanosomal protein Silver (Pmel17) changes lumenal fragment interactions
    • Kuliawat, R., and Santambrogio, L. (2009). A mutation within the transmembrane domain of melanosomal protein Silver (Pmel17) changes lumenal fragment interactions. Eur. J. Cell Biol. 88, 653-667.
    • (2009) Eur. J. Cell Biol. , vol.88 , pp. 653-667
    • Kuliawat, R.1    Santambrogio, L.2
  • 60
    • 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
  • 62
    • 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., 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.
    • (1987) Mol. Biol. Med. , vol.4 , pp. 339-355
    • Kwon, B.S.1    Halaban, R.2    Kim, G.S.3    Usack, L.4    Pomerantz, S.5    Haq, A.K.6
  • 64
    • 0029876125 scopus 로고    scopus 로고
    • Characterization and subcellular localization of human Pmel 17/silver, a 100-kDa (pre)melanosomal membrane protein associated with 5,6,-dihydroxyindole-2-carboxylic acid (DHICA) converting activity
    • Lee, Z.H., Hou, L., Moellmann, G., Kuklinska, E., Antol, K., Fraser, M., Halaban, R., and Kwon, B.S. (1996). Characterization and subcellular localization of human Pmel 17/silver, a 100-kDa (pre)melanosomal membrane protein associated with 5, 6, -dihydroxyindole-2-carboxylic acid (DHICA) converting activity. J. Invest. Dermatol. 106, 605-610.
    • (1996) J. Invest. Dermatol. , vol.106 , pp. 605-610
    • Lee, Z.H.1    Hou, L.2    Moellmann, G.3    Kuklinska, E.4    Antol, K.5    Fraser, M.6    Halaban, R.7    Kwon, B.S.8
  • 65
    • 77952374811 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER)-export, subcellular distribution and fibril formation by PMEL17 requires an intact N-terminal domain junction J
    • Leonhardt, R.M., Vigneron, N., Rahner, C., Van den Eynde, B.J., and Cresswell, P. (2010). Endoplasmic reticulum (ER)-export, subcellular distribution and fibril formation by PMEL17 requires an intact N-terminal domain junction J. Biol. Chem. 285, 16166-16683.
    • (2010) Biol. Chem. , vol.285 , pp. 16166-16683
    • Leonhardt, R.M.1    Vigneron, N.2    Rahner, C.3    Van den Eynde, B.J.4    Cresswell, P.5
  • 66
    • 79953213297 scopus 로고    scopus 로고
    • Proprotein convertases process Pmel17 during secretion
    • Leonhardt, R.M., Vigneron, N., Rahner, C., and Cresswell, P. (2011). Proprotein convertases process Pmel17 during secretion. J. Biol. Chem. 286, 9321-9337.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9321-9337
    • Leonhardt, R.M.1    Vigneron, N.2    Rahner, C.3    Cresswell, P.4
  • 67
    • 33644551836 scopus 로고    scopus 로고
    • Melanosomal targeting sequences from gp100 are essential for MHC class II-restricted endogenous epitope presentation and mobilization to endosomal compartments
    • Lepage, S., and Lapointe, R. (2006). Melanosomal targeting sequences from gp100 are essential for MHC class II-restricted endogenous epitope presentation and mobilization to endosomal compartments. Cancer Res. 66, 2423-2432.
    • (2006) Cancer Res. , vol.66 , pp. 2423-2432
    • Lepage, S.1    Lapointe, R.2
  • 68
    • 57449109485 scopus 로고    scopus 로고
    • Increased alpha-synuclein aggregation following limited cleavage by certain matrix metalloproteinases
    • Levin, J., Giese, A., Boetzel, K., Israel, L., Högen, T., Nübling, G., Kretzschma, r.H., and Lorenzl, S. (2009). Increased alpha-synuclein aggregation following limited cleavage by certain matrix metalloproteinases. Exp. Neurol. 215, 201-208.
    • (2009) Exp. Neurol. , vol.215 , pp. 201-208
    • Levin, J.1    Giese, A.2    Boetzel, K.3    Israel, L.4    Högen, T.5    Nübling, G.6    Kretzschma, rH.7    Lorenzl, S.8
  • 69
    • 34948876842 scopus 로고    scopus 로고
    • Melanosome maturation defect in Rab38-deficient retinal pigment epithelium results in instability of immature melanosomes during transient melanogenesis
    • Lopes, V.S., Wasmeier, C., Seabra, M.C., and Futter, C.E. (2007). Melanosome maturation defect in Rab38-deficient retinal pigment epithelium results in instability of immature melanosomes during transient melanogenesis. Mol. Biol. Cell 18, 3914-3927.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3914-3927
    • Lopes, V.S.1    Wasmeier, C.2    Seabra, M.C.3    Futter, C.E.4
  • 70
    • 67650809307 scopus 로고    scopus 로고
    • Functional amyloids as natural storage of peptide hormones in pituitary secretory granules
    • Maji, S.K., Perrin, M.H., Sawaya, M.R. et al. (2009). Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325, 328-332.
    • (2009) Science , vol.325 , pp. 328-332
    • Maji, S.K.1    Perrin, M.H.2    Sawaya, M.R.3
  • 71
    • 84862776939 scopus 로고    scopus 로고
    • Critical role of amyloid-like oligomers of Drosophila Orb2 in the persistence of memory
    • Majumdar, A., Cesario, W.C., White-Grindley, E. et al. (2012). Critical role of amyloid-like oligomers of Drosophila Orb2 in the persistence of memory. Cell 148, 515-529.
    • (2012) Cell , vol.148 , pp. 515-529
    • Majumdar, A.1    Cesario, W.C.2    White-Grindley, E.3
  • 75
    • 69549088661 scopus 로고    scopus 로고
    • The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis
    • McGlinchey, R.P., Shewmaker, F., McPhie, P., Monterroso, B., Thurber, K., and Wickner, R.B. (2009). The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. Proc. Natl Acad. Sci. USA 106, 13731-13736.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 13731-13736
    • McGlinchey, R.P.1    Shewmaker, F.2    McPhie, P.3    Monterroso, B.4    Thurber, K.5    Wickner, R.B.6
  • 76
    • 79953136045 scopus 로고    scopus 로고
    • The repeat domains of melanosome matrix protein Pmel17 orthologs form amyloid fibrils at the acidic melanosomal pH
    • McGlinchey, R.P., Shewmaker, F., Hu, K.N., McPhie, P., Tycko, R., and Wickner, R.B. (2011). The repeat domains of melanosome matrix protein Pmel17 orthologs form amyloid fibrils at the acidic melanosomal pH. J. Biol. Chem. 286, 8385-8393.
    • (2011) J. Biol. Chem. , vol.286 , pp. 8385-8393
    • McGlinchey, R.P.1    Shewmaker, F.2    Hu, K.N.3    McPhie, P.4    Tycko, R.5    Wickner, R.B.6
  • 77
    • 0013882116 scopus 로고
    • Genetic variations in the fine structure and ontogeny of mouse melanin granules
    • Moyer, F.H. (1966). Genetic variations in the fine structure and ontogeny of mouse melanin granules. Am. Zool. 6, 43-66.
    • (1966) Am. Zool. , vol.6 , pp. 43-66
    • Moyer, F.H.1
  • 79
    • 0014288538 scopus 로고
    • Ultrastructural and cytochemical observations on B-16 and Harding-Passey mouse melanomas. The origin of premelanosomes and compound melanosomes
    • Novikoff, A.B., Albala, A., and Biempica, L. (1968). Ultrastructural and cytochemical observations on B-16 and Harding-Passey mouse melanomas. The origin of premelanosomes and compound melanosomes. J. Histochem. Cytochem. 16, 299-319.
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 299-319
    • Novikoff, A.B.1    Albala, A.2    Biempica, L.3
  • 82
    • 78650749876 scopus 로고    scopus 로고
    • Effects of pH on aggregation kinetics of the repeat domain of a functional amyloid, Pmel17
    • Pfefferkorn, C.M., McGlinchey, R.P., and Lee, J.C. (2010). Effects of pH on aggregation kinetics of the repeat domain of a functional amyloid, Pmel17. Proc. Natl Acad. Sci. USA 107, 21447-21452.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 21447-21452
    • Pfefferkorn, C.M.1    McGlinchey, R.P.2    Lee, J.C.3
  • 83
    • 84862889144 scopus 로고    scopus 로고
    • Physiological functions of the amyloid secretases ADAM10, BACE1, and presenlilin
    • Prox, J., Rittger, A., and Saftig, P. (2012). Physiological functions of the amyloid secretases ADAM10, BACE1, and presenlilin. Exp. Brain Res. 217, 331-341.
    • (2012) Exp. Brain Res. , vol.217 , pp. 331-341
    • Prox, J.1    Rittger, A.2    Saftig, P.3
  • 84
    • 0033778117 scopus 로고    scopus 로고
    • Aberrant pH of melanosomes in pink-eyed dilution (p) mutant melanocytes
    • Puri, N., Gardner, J.M., and Brilliant, M.H. (2000). Aberrant pH of melanosomes in pink-eyed dilution (p) mutant melanocytes. J. Invest. Dermatol. 115, 607-613.
    • (2000) J. Invest. Dermatol. , vol.115 , pp. 607-613
    • Puri, N.1    Gardner, J.M.2    Brilliant, M.H.3
  • 86
    • 0035911146 scopus 로고    scopus 로고
    • Distinct protein sorting and localization to premelanosomes, 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 premelanosomes, 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
  • 87
    • 71849085568 scopus 로고    scopus 로고
    • MHC class II presentation of gp100 epitopes in melanoma cells requires the function of conventional endosomes and is influenced by melanosomes
    • Robila, V., Ostankovitch, M., Altrich-Vanlith, M.L., Theos, A.C., Drover, S., Marks, M.S., Restifo, N., and Engelhard, V.H. (2008). MHC class II presentation of gp100 epitopes in melanoma cells requires the function of conventional endosomes and is influenced by melanosomes. J. Immunol. 181, 7843-7852.
    • (2008) J. Immunol. , vol.181 , pp. 7843-7852
    • Robila, V.1    Ostankovitch, M.2    Altrich-Vanlith, M.L.3    Theos, A.C.4    Drover, S.5    Marks, M.S.6    Restifo, N.7    Engelhard, V.H.8
  • 88
    • 84872065456 scopus 로고    scopus 로고
    • Interaction of MC1R and PMEL alleles on solid coat colors in Highland cattle
    • Schmutz, S.M., and Dreger, D.L. (2013). Interaction of MC1R and PMEL alleles on solid coat colors in Highland cattle. Anim. Genet., 44, 9-13.
    • (2013) Anim. Genet., , vol.44 , pp. 9-13
    • Schmutz, S.M.1    Dreger, D.L.2
  • 89
    • 22544475390 scopus 로고    scopus 로고
    • A mutation in the silver gene leads to defects in melanosome biogenesis and alterations in the visual system in the zebrafish mutant fading vision
    • Schonthaler, H.B., Lampert, J.M., von Lintig, J., Schwarz, H., Geisler, R., and Neuhauss, S.C. (2005). A mutation in the silver gene leads to defects in melanosome biogenesis and alterations in the visual system in the zebrafish mutant fading vision. Dev. Biol. 284, 421-436.
    • (2005) Dev. Biol. , vol.284 , pp. 421-436
    • Schonthaler, H.B.1    Lampert, J.M.2    von Lintig, J.3    Schwarz, H.4    Geisler, R.5    Neuhauss, S.C.6
  • 90
    • 0029348980 scopus 로고
    • Transport of endocytosed material into melanin granules in cultured choroidal melanocytes of cattle-new insights into the relationship of melanosomes with lysosomes
    • Schraermeyer, U. (1995). Transport of endocytosed material into melanin granules in cultured choroidal melanocytes of cattle-new insights into the relationship of melanosomes with lysosomes. Pigment Cell Res. 8, 209-214.
    • (1995) Pigment Cell Res. , vol.8 , pp. 209-214
    • Schraermeyer, U.1
  • 91
    • 0030255017 scopus 로고    scopus 로고
    • Detection of a fine lamellar gridwork after degradation of ocular melanin granules by cultured peritoneal macrophages
    • Schraermeyer, U., and Dohms, M. (1996). Detection of a fine lamellar gridwork after degradation of ocular melanin granules by cultured peritoneal macrophages. Pigment Cell Res. 9, 248-254.
    • (1996) Pigment Cell Res. , vol.9 , pp. 248-254
    • Schraermeyer, U.1    Dohms, M.2
  • 92
    • 0033083518 scopus 로고    scopus 로고
    • Melanin granules of retinal pigment epithelium are connected with the lysosomal degradation pathway
    • Schraermeyer, U., Peters, S., Thumann, G., Kociok, N., and Heimann, K. (1999). Melanin granules of retinal pigment epithelium are connected with the lysosomal degradation pathway. Exp. Eye Res. 68, 237-245.
    • (1999) Exp. Eye Res. , vol.68 , pp. 237-245
    • Schraermeyer, U.1    Peters, S.2    Thumann, G.3    Kociok, N.4    Heimann, K.5
  • 93
    • 0001259952 scopus 로고
    • Chemical composition and terminology of specialized organelles (melanosomes and melanin granules) in mammalian melanocytes
    • Seiji, M., Fitzpatrick, T.M., 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.M.2    Simpson, R.T.3    Birbeck, M.S.C.4
  • 94
    • 50649121059 scopus 로고    scopus 로고
    • Cell-specific ATP7A transport sustains copper-dependent tyrosinase activity in melanosomes
    • Setty, S.R.G., Tenza, D., Sviderskaya, E.V., Bennett, D.C., Raposo, G., and Marks, M.S. (2008). Cell-specific ATP7A transport sustains copper-dependent tyrosinase activity in melanosomes. Nature 454, 1142-1146.
    • (2008) Nature , vol.454 , pp. 1142-1146
    • Setty, S.R.G.1    Tenza, D.2    Sviderskaya, E.V.3    Bennett, D.C.4    Raposo, G.5    Marks, M.S.6
  • 95
    • 69449104505 scopus 로고    scopus 로고
    • Current challenges in understanding melanogenesis: bridging chemistry, biological control, morphology and function
    • Simon, J.D., Peles, D., Wakamatsu, K., and Ito, S. (2009). Current challenges in understanding melanogenesis: bridging chemistry, biological control, morphology and function. Pigment Cell Melanoma Res. 22, 563-579.
    • (2009) Pigment Cell Melanoma Res. , vol.22 , pp. 563-579
    • Simon, J.D.1    Peles, D.2    Wakamatsu, K.3    Ito, S.4
  • 96
    • 84859738620 scopus 로고    scopus 로고
    • Mechanisms of protein delivery to melanosomes in pigment cells
    • Sitaram, A., and Marks, M.S. (2012). Mechanisms of protein delivery to melanosomes in pigment cells. Physiology 27, 85-99.
    • (2012) Physiology , vol.27 , pp. 85-99
    • Sitaram, A.1    Marks, M.S.2
  • 98
    • 0026519258 scopus 로고
    • Effects of the developmental colour mutations silver and recessive spotting on proliferation of diploid and immortal mouse melanocytes in culture
    • Spanakis, E., Lamina, P., and Bennett, D.C. (1992). Effects of the developmental colour mutations silver and recessive spotting on proliferation of diploid and immortal mouse melanocytes in culture. Development 114, 675-680.
    • (1992) Development , vol.114 , pp. 675-680
    • Spanakis, E.1    Lamina, P.2    Bennett, D.C.3
  • 100
    • 27644555189 scopus 로고    scopus 로고
    • Functions of AP-3 and AP-1 in tyrosinase sorting from endosomes to melanosomes
    • Theos, A.C., Tenza, D., Martina, J.A. et al. (2005a). Functions of AP-3 and AP-1 in tyrosinase sorting from endosomes to melanosomes. Mol. Biol. Cell 16, 5356-5372.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5356-5372
    • Theos, A.C.1    Tenza, D.2    Martina, J.A.3
  • 101
    • 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. (2005b). 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
  • 102
    • 33746617878 scopus 로고    scopus 로고
    • Dual loss of ER export and endocytic signals with altered melanosome morphology in the silver mutation of Pmel17
    • Theos, A.C., Berson, J.F., Theos, S.C. et al. (2006a). Dual loss of ER export and endocytic signals with altered melanosome morphology in the silver mutation of Pmel17. Mol. Biol. Cell 17, 3598-3612.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3598-3612
    • Theos, A.C.1    Berson, J.F.2    Theos, S.C.3
  • 103
    • 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. (2006b). 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
  • 104
    • 68549136802 scopus 로고    scopus 로고
    • ESCRT-1 function is required for Tyrp1 transport from early endosomes to the melanosome limiting membrane
    • Truschel, S.T., SImoes, S., Setty, S.R.G. et al. (2009). ESCRT-1 function is required for Tyrp1 transport from early endosomes to the melanosome limiting membrane. Traffic 10, 1318-1336.
    • (2009) Traffic , vol.10 , pp. 1318-1336
    • Truschel, S.T.1    Imoes, S.S.2    Setty, S.R.G.3
  • 105
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • Uptain, S.M., and Lindquist, S. (2002). Prions as protein-based genetic elements. Annu. Rev. Microbiol. 56, 703-741.
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.2
  • 106
    • 33645748895 scopus 로고    scopus 로고
    • Sorting of Pmel17 to melanosomes through the plasma membrane by AP1 and AP2: evidence for the polarized nature of melanocytes
    • Valencia, J.C., Watabe, H., Chi, A. et al. (2006). Sorting of Pmel17 to melanosomes through the plasma membrane by AP1 and AP2: evidence for the polarized nature of melanocytes. J. Cell Sci. 119, 1080-1091.
    • (2006) J. Cell Sci. , vol.119 , pp. 1080-1091
    • Valencia, J.C.1    Watabe, H.2    Chi, A.3
  • 107
    • 34249654014 scopus 로고    scopus 로고
    • Sialylated core 1 O-glycans influence the sorting of Pmel17/gp100 and determine its capacity to form fibrils
    • Valencia, J.C., Rouzaud, F., Julien, S. et al. (2007). Sialylated core 1 O-glycans influence the sorting of Pmel17/gp100 and determine its capacity to form fibrils. J. Biol. Chem. 282, 11266-11280.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11266-11280
    • Valencia, J.C.1    Rouzaud, F.2    Julien, S.3
  • 108
    • 33745017140 scopus 로고    scopus 로고
    • The quest for the mechanism of melanin transfer
    • Van Den Bossche, K., Naeyaert, J.-M., and Lambert, J. (2006). The quest for the mechanism of melanin transfer. Traffic 7, 769-778.
    • (2006) Traffic , vol.7 , pp. 769-778
    • Van Den Bossche, K.1    Naeyaert, J.-M.2    Lambert, J.3
  • 110
    • 0026051621 scopus 로고
    • Biosynthesis and intracellular movement of the melanosomal membrane glycoprotein gp75, the human b (brown) locus product
    • Vijayasaradhi, S., Doskoch, P.M., and Houghton, A.N. (1991). Biosynthesis and intracellular movement of the melanosomal membrane glycoprotein gp75, the human b (brown) locus product. Exp. Cell Res. 196, 233-240.
    • (1991) Exp. Cell Res. , vol.196 , pp. 233-240
    • Vijayasaradhi, S.1    Doskoch, P.M.2    Houghton, A.N.3
  • 111
    • 0029126743 scopus 로고
    • Intracellular sorting and targeting of melanosomal membrane proteins: identification of signals for sorting of the human brown locus protein, gp75
    • Vijayasaradhi, S., Xu, Y.Q., Bouchard, B., and Houghton, A.N. (1995). Intracellular sorting and targeting of melanosomal membrane proteins: identification of signals for sorting of the human brown locus protein, gp75. J. Cell Biol. 130, 807-820.
    • (1995) J. Cell Biol. , vol.130 , pp. 807-820
    • Vijayasaradhi, S.1    Xu, Y.Q.2    Bouchard, B.3    Houghton, A.N.4
  • 112
    • 0035851151 scopus 로고    scopus 로고
    • The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein
    • Vincent, B., Paitel, E., Saftig, P., Frobert, Y., Hartmann, D., De Strooper, B., Grassi, J., Lopez-Perez, E., and Checler, F. (2001). The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J. Biol. Chem. 276, 37743-37746.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37743-37746
    • Vincent, B.1    Paitel, E.2    Saftig, P.3    Frobert, Y.4    Hartmann, D.5    De Strooper, B.6    Grassi, J.7    Lopez-Perez, E.8    Checler, F.9
  • 113
    • 33645065115 scopus 로고    scopus 로고
    • Tyrosinase maturation through the mammalian secretory pathway: bringing color to life
    • Wang, N., and Hebert, D.N. (2006). Tyrosinase maturation through the mammalian secretory pathway: bringing color to life. Pigment Cell Res. 19, 3-18.
    • (2006) Pigment Cell Res. , vol.19 , pp. 3-18
    • Wang, N.1    Hebert, D.N.2
  • 114
    • 31044438340 scopus 로고    scopus 로고
    • Regulation of tyrosinase trafficking and processing by presenilins: partial loss of function by familial Alzheimer's disease mutation
    • Wang, R., Tang, P., Wang, P., Boissy, R.E., and Zheng, H. (2006). Regulation of tyrosinase trafficking and processing by presenilins: partial loss of function by familial Alzheimer's disease mutation. Proc. Natl Acad. Sci. USA 103, 353-358.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 353-358
    • Wang, R.1    Tang, P.2    Wang, P.3    Boissy, R.E.4    Zheng, H.5
  • 115
    • 34250158426 scopus 로고    scopus 로고
    • Lipid interaction converts prion protein to a PrPSc-like proteinase K-resistant conformation under physiological conditions
    • Wang, F., Yang, F., Hu, Y., Wang, X., Wang, X., Jin, C., and Ma, J. (2007). Lipid interaction converts prion protein to a PrPSc-like proteinase K-resistant conformation under physiological conditions. Biochemistry 46, 7045-7053.
    • (2007) Biochemistry , vol.46 , pp. 7045-7053
    • Wang, F.1    Yang, F.2    Hu, Y.3    Wang, X.4    Wang, X.5    Jin, C.6    Ma, J.7
  • 116
    • 72149111129 scopus 로고    scopus 로고
    • N-terminal domains elicit formation of functional Pmel17 amyloid fibrils
    • Watt, B., van Niel, G., Fowler, D.M. et al. (2009). N-terminal domains elicit formation of functional Pmel17 amyloid fibrils. J. Biol. Chem. 284, 35543-35555.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35543-35555
    • Watt, B.1    van Niel, G.2    Fowler, D.M.3
  • 117
    • 80053436733 scopus 로고    scopus 로고
    • Pmel17: an amyloid determinant of organelle structure
    • S., Rigacci, and M., Bucciantini, eds. (Trivandrum, Kerala, India: Research Signpost) -.
    • Watt, B., Raposo, G., and Marks, M.S. (2010). Pmel17: an amyloid determinant of organelle structure. In Functional Amyloid Aggregation, S., Rigacci, and M., Bucciantini, eds. (Trivandrum, Kerala, India: Research Signpost), pp. 89-113.
    • (2010) Functional Amyloid Aggregation , pp. 89-113
    • Watt, B.1    Raposo, G.2    Marks, M.S.3
  • 118
    • 80053457547 scopus 로고    scopus 로고
    • Mutations in or near the transmembrane domain alter PMEL amyloid formation from functional to pathogenic
    • Watt, B., Tenza, D., Lemmon, M.A., Kerje, S., Raposo, G., Andersson, L., and Marks, M.S. (2011). Mutations in or near the transmembrane domain alter PMEL amyloid formation from functional to pathogenic. PLoS Genet. 7, e1002286.
    • (2011) PLoS Genet. , vol.7
    • Watt, B.1    Tenza, D.2    Lemmon, M.A.3    Kerje, S.4    Raposo, G.5    Andersson, L.6    Marks, M.S.7
  • 120
    • 0028235783 scopus 로고
    • Identification of a melanosomal matrix protein encoded by the murine si (silver) locus using "organelle scanning"
    • Zhou, B.K., Kobayashi, T., Donatien, P.D., Bennett, D.C., Hearing, V.J., and Orlow, S.J. (1994). Identification of a melanosomal matrix protein encoded by the murine si (silver) locus using "organelle scanning". Proc. Natl Acad. Sci. USA 91, 7076-7080.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7076-7080
    • Zhou, B.K.1    Kobayashi, T.2    Donatien, P.D.3    Bennett, D.C.4    Hearing, V.J.5    Orlow, S.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.