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Volumn 44, Issue 9, 2007, Pages 545-555

Cargos and genes: Insights into vesicular transport from inherited human disease

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; RAB PROTEIN;

EID: 34548861233     PISSN: 00222593     EISSN: None     Source Type: Journal    
DOI: 10.1136/jmg.2007.050294     Document Type: Review
Times cited : (34)

References (114)
  • 1
    • 0034330457 scopus 로고    scopus 로고
    • Traffic Jam: A compendium of human diseases that affect intracellular transport processes
    • Aridor M, Hannan L. Traffic Jam: a compendium of human diseases that affect intracellular transport processes. Traffic 2000;1:826-51.
    • (2000) Traffic , vol.1 , pp. 826-851
    • Aridor, M.1    Hannan, L.2
  • 2
    • 0036843129 scopus 로고    scopus 로고
    • Traffic jams II: An update of diseases of intracellular transport
    • Aridor M, Hannan L. Traffic jams II: an update of diseases of intracellular transport. Traffic 2002;3:781-90.
    • (2002) Traffic , vol.3 , pp. 781-790
    • Aridor, M.1    Hannan, L.2
  • 3
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade G. Intracellular aspects of the process of protein synthesis. Science 1975;189:347-58.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 4
    • 0021738607 scopus 로고
    • Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of clathrin coats and of other trafficking components N-acetylglucosamine
    • Balch WE, Dunphy WG, Braell WA, Rothman JE. Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of clathrin coats and of other trafficking components N-acetylglucosamine. Cell 1984;39:405-16.
    • (1984) Cell , vol.39 , pp. 405-416
    • Balch, W.E.1    Dunphy, W.G.2    Braell, W.A.3    Rothman, J.E.4
  • 5
    • 0000756130 scopus 로고
    • Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae
    • Novick P, Schekman R. Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae. Proc Natl Acad Sci USA 1979;76:1858-62.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 1858-1862
    • Novick, P.1    Schekman, R.2
  • 6
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick P, Field C, Schekman R. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 1980;21:205-15.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 7
    • 0015970730 scopus 로고
    • A recognition marker for uptake of a lysosomal enzyme by cultured fibroblasts
    • Hickman S, Shapiro U, Neufield EF. A recognition marker for uptake of a lysosomal enzyme by cultured fibroblasts. Biochem Biophys Res Commun 1974;57:55-61.
    • (1974) Biochem Biophys Res Commun , vol.57 , pp. 55-61
    • Hickman, S.1    Shapiro, U.2    Neufield, E.F.3
  • 8
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin DG, Nelson WJ. Origins of cell polarity. Cell 1996;84:335-44.
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 10
    • 0029100974 scopus 로고
    • Membrane transport in the endocytic pathway
    • Gruenberg J, Maxfield FR. Membrane transport in the endocytic pathway. Curr Opin Cell Biol 1995;7:552-63.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 552-563
    • Gruenberg, J.1    Maxfield, F.R.2
  • 11
    • 0030037845 scopus 로고    scopus 로고
    • Membranes and sorting
    • Mellman I. Membranes and sorting. Curr Opin Cell Biol 1996;8:497-8.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 497-498
    • Mellman, I.1
  • 12
    • 0036191914 scopus 로고    scopus 로고
    • Endosomes: Multipurpose designs for integrating housekeeping and specialized tasks
    • Sachse M, Ramm G, Straus G, Klumperman J. Endosomes: multipurpose designs for integrating housekeeping and specialized tasks. Histochem Cell Biol 2002;117:91-104.
    • (2002) Histochem Cell Biol , vol.117 , pp. 91-104
    • Sachse, M.1    Ramm, G.2    Straus, G.3    Klumperman, J.4
  • 14
    • 0035031562 scopus 로고    scopus 로고
    • Kozyraki R. Cubilin, a multifunctional epithelial receptor: an overview. J Mol Med 2001;79:161-7.
    • Kozyraki R. Cubilin, a multifunctional epithelial receptor: an overview. J Mol Med 2001;79:161-7.
  • 15
    • 0034641833 scopus 로고    scopus 로고
    • Genetic defects of intracellular-membrane transport
    • Olkkonen VM, Ikonen E. Genetic defects of intracellular-membrane transport. N Engl J Med 2000;343:1095-104.
    • (2000) N Engl J Med , vol.343 , pp. 1095-1104
    • Olkkonen, V.M.1    Ikonen, E.2
  • 16
    • 33749510461 scopus 로고    scopus 로고
    • Cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex
    • Nyfeler B, Zhang B, Ginsburg D, Kaufman RJ, Hauri HP. Cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex. Traffic 2006;7:1473-81.
    • (2006) Traffic , vol.7 , pp. 1473-1481
    • Nyfeler, B.1    Zhang, B.2    Ginsburg, D.3    Kaufman, R.J.4    Hauri, H.P.5
  • 17
    • 0030814254 scopus 로고    scopus 로고
    • COPII and secretory cargo capture into transport vesicles
    • Kuehn MJ, Schekman R. COPII and secretory cargo capture into transport vesicles. Curr Opin Cell Biol 1997;9:477-83.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 477-483
    • Kuehn, M.J.1    Schekman, R.2
  • 18
    • 0032145879 scopus 로고    scopus 로고
    • Mechanisms of protein sorting and coat assembly: Insights from the clathrin-coated vesicle pathway
    • Le Borgne R, Hoflack B. Mechanisms of protein sorting and coat assembly: insights from the clathrin-coated vesicle pathway. Curr Opin Cell Biol 1998;10:499-503.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 499-503
    • Le Borgne, R.1    Hoflack, B.2
  • 19
    • 0033180320 scopus 로고    scopus 로고
    • Mechanisms of vesicle formation: Insights from the COP system
    • Wieland F, Harter C. Mechanisms of vesicle formation: insights from the COP system. Curr Opin Cell Biol 1999;11:440-6.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 440-446
    • Wieland, F.1    Harter, C.2
  • 21
    • 7044274618 scopus 로고    scopus 로고
    • Protein-lipid interactions in membrane trafficking at the Golgi complex
    • De Matters MA, Godi A. Protein-lipid interactions in membrane trafficking at the Golgi complex. Biochim Biophys Acta 2004;666:264-74.
    • (2004) Biochim Biophys Acta , vol.666 , pp. 264-274
    • De Matters, M.A.1    Godi, A.2
  • 22
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg J, Kozlov M. How proteins produce cellular membrane curvature. Nat Rev Mol Cell Biol 2006;7:9-19.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.2
  • 23
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon HT, Gallop JL. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 2005;438:590-6.
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 25
    • 33749151608 scopus 로고    scopus 로고
    • Secretory COPII coat component Sec23a is essential for craniofacial chondrocyte maturation
    • Lang MR, Lapierre LA, Frotscher M, Goldenring JR, Knapik EW. Secretory COPII coat component Sec23a is essential for craniofacial chondrocyte maturation. Nat Genet 2006;38:1198-203.
    • (2006) Nat Genet , vol.38 , pp. 1198-1203
    • Lang, M.R.1    Lapierre, L.A.2    Frotscher, M.3    Goldenring, J.R.4    Knapik, E.W.5
  • 26
    • 33745022082 scopus 로고    scopus 로고
    • Interaction of Hermansky-Pudlak syndrome genes in the regulation of lysosome-related organelles
    • Gautam R, Novak EK, Tan J, Wakamatsu K, Ito S, Swank RT. Interaction of Hermansky-Pudlak syndrome genes in the regulation of lysosome-related organelles. Traffic 2006;7:779-92.
    • (2006) Traffic , vol.7 , pp. 779-792
    • Gautam, R.1    Novak, E.K.2    Tan, J.3    Wakamatsu, K.4    Ito, S.5    Swank, R.T.6
  • 28
    • 1842509099 scopus 로고    scopus 로고
    • Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins
    • Peden AA, Oorschot V, Hesser BA, Austin CD, Scheller RH, Klumperman J. Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins. J Cell Biol 2004;164:1065-76.
    • (2004) J Cell Biol , vol.164 , pp. 1065-1076
    • Peden, A.A.1    Oorschot, V.2    Hesser, B.A.3    Austin, C.D.4    Scheller, R.H.5    Klumperman, J.6
  • 30
    • 3142516226 scopus 로고    scopus 로고
    • The building BLOC(k)s of lysosomes and related organelles
    • Dell'Angelica EC. The building BLOC(k)s of lysosomes and related organelles. Curr Opin Cell Biol 2004;16:458-64.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 458-464
    • Dell'Angelica, E.C.1
  • 31
    • 8444243363 scopus 로고    scopus 로고
    • Targeting Rab GTPases to distinct membrane compartments
    • Pfeffer S, Aivazian D. Targeting Rab GTPases to distinct membrane compartments. Nat Rev Mol Cell Biol 2004;5:886-96.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 886-896
    • Pfeffer, S.1    Aivazian, D.2
  • 32
    • 0345306636 scopus 로고    scopus 로고
    • Multiple factors contribute to inefficient prenylation of Rab27a in Rab prenylation diseases
    • Larijani B, Hume AN, Tarafder AK, Seabra MC. Multiple factors contribute to inefficient prenylation of Rab27a in Rab prenylation diseases. J Biol Chem 2003;278:46798-804.
    • (2003) J Biol Chem , vol.278 , pp. 46798-46804
    • Larijani, B.1    Hume, A.N.2    Tarafder, A.K.3    Seabra, M.C.4
  • 33
    • 0036137684 scopus 로고    scopus 로고
    • Rab GTPases, intracellular traffic and disease
    • Seabra MC, Mules EH, Hume AN. Rab GTPases, intracellular traffic and disease. Trends Mol Med 2002;8:23-30.
    • (2002) Trends Mol Med , vol.8 , pp. 23-30
    • Seabra, M.C.1    Mules, E.H.2    Hume, A.N.3
  • 36
    • 0032980145 scopus 로고    scopus 로고
    • Duran-McKinster C, Rodriguez-Jurado R, Ridaura C, de la Luz Orozco-Covarrubias M, Tamayo L, Ruiz-Maldonando R. Elejalde syndrome - a melanolysosomal neurocutaneous syndrome: clinical and morphological findings in 7 patients. Arch Dermatol 1999;135:182-6.
    • Duran-McKinster C, Rodriguez-Jurado R, Ridaura C, de la Luz Orozco-Covarrubias M, Tamayo L, Ruiz-Maldonando R. Elejalde syndrome - a melanolysosomal neurocutaneous syndrome: clinical and morphological findings in 7 patients. Arch Dermatol 1999;135:182-6.
  • 37
    • 0030914460 scopus 로고    scopus 로고
    • Postural E, Barrat FJ, Dufourcq-Lagelouse R, Certain S, Sanal O, Jabado N, Seger R, Griscelli C, Fischer A, de Saint Basile G. Griscelli disease maps to chromosome 15q21 and is associated with mutations in the myosin-Va gene
    • Postural E, Barrat FJ, Dufourcq-Lagelouse R, Certain S, Sanal O, Jabado N, Seger R, Griscelli C, Fischer A, de Saint Basile G. Griscelli disease maps to chromosome 15q21 and is associated with mutations in the myosin-Va gene. Nat Genet 1997;16:289-92.
    • (1997) Nat Genet , vol.16 , pp. 289-292
  • 38
    • 0034949894 scopus 로고    scopus 로고
    • Myosin learns to walk
    • Mehta A. Myosin learns to walk. J Cell Sci 2001;114:1981-98.
    • (2001) J Cell Sci , vol.114 , pp. 1981-1998
    • Mehta, A.1
  • 39
    • 0037044819 scopus 로고    scopus 로고
    • Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin
    • Fukuda M, Kuroda TS. Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin. J Biol Chem 2002;277:43096-103.
    • (2002) J Biol Chem , vol.277 , pp. 43096-43103
    • Fukuda, M.1    Kuroda, T.S.2
  • 40
    • 0036000020 scopus 로고    scopus 로고
    • Wu X, Wang F, Rao K, Sellers JR, Hammer JA 3rd. Rab27a is an essential component of melanosome receptor for myosin Va. Mol Biol Cell 2002;13:1735-49.
    • Wu X, Wang F, Rao K, Sellers JR, Hammer JA 3rd. Rab27a is an essential component of melanosome receptor for myosin Va. Mol Biol Cell 2002;13:1735-49.
  • 41
    • 0037067673 scopus 로고    scopus 로고
    • A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport
    • Strom M, Hume AN, Tarafder AK, Barkagianni E, Seabra MC. A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport. J Biol Chem 2002;277:25423-30.
    • (2002) J Biol Chem , vol.277 , pp. 25423-25430
    • Strom, M.1    Hume, A.N.2    Tarafder, A.K.3    Barkagianni, E.4    Seabra, M.C.5
  • 47
    • 0035849901 scopus 로고    scopus 로고
    • Rab23 is an essential negative regulator of the mouse Sonic hedgehog signalling pathway
    • Eggenschwiler JT, Espinoza E, Anderson KV. Rab23 is an essential negative regulator of the mouse Sonic hedgehog signalling pathway. Nature 2001;412:194-8.
    • (2001) Nature , vol.412 , pp. 194-198
    • Eggenschwiler, J.T.1    Espinoza, E.2    Anderson, K.V.3
  • 48
    • 0346752323 scopus 로고    scopus 로고
    • Rab23, a negative regulator of hedgehog signalling, localizes to the plasma membrane and the endocytic pathway
    • Evans TM, Ferguson C, Wainwright BJ, Parton RG, Wicking C. Rab23, a negative regulator of hedgehog signalling, localizes to the plasma membrane and the endocytic pathway. Traffic 2003;4:869-84.
    • (2003) Traffic , vol.4 , pp. 869-884
    • Evans, T.M.1    Ferguson, C.2    Wainwright, B.J.3    Parton, R.G.4    Wicking, C.5
  • 49
    • 0031898897 scopus 로고    scopus 로고
    • RAB3 and Synaptotagmin: The yin and yang of synaptic membrane fusion
    • Geppert M, Sudhof TC. RAB3 and Synaptotagmin: the yin and yang of synaptic membrane fusion. Annu Rev Neurosci 1998;21:75-95.
    • (1998) Annu Rev Neurosci , vol.21 , pp. 75-95
    • Geppert, M.1    Sudhof, T.C.2
  • 50
    • 0028340317 scopus 로고
    • Evidence for the involvement of Rab3A in Ca (2+)-dependent exocytosis from adrenal chromaffin cells
    • Holz RW, Brondyk WH, Senter RA, Kuizon L, Macara IG. Evidence for the involvement of Rab3A in Ca (2+)-dependent exocytosis from adrenal chromaffin cells. J Biol Chem 1994;269:10229-34.
    • (1994) J Biol Chem , vol.269 , pp. 10229-10234
    • Holz, R.W.1    Brondyk, W.H.2    Senter, R.A.3    Kuizon, L.4    Macara, I.G.5
  • 56
  • 57
    • 22544476257 scopus 로고    scopus 로고
    • Microtubule transport defects in neurological and ciliary disease
    • Gerdes JM, Katsanis N. Microtubule transport defects in neurological and ciliary disease. Cell Mol Life Sci 2005;62:1556- 70.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1556-1570
    • Gerdes, J.M.1    Katsanis, N.2
  • 58
  • 60
    • 1042299828 scopus 로고    scopus 로고
    • Further evidence of dementia in SPG4-linked autosomal dominant hereditary spastic paraplegia
    • McMonagle P, Byrne P, Hutchinson M. Further evidence of dementia in SPG4-linked autosomal dominant hereditary spastic paraplegia. Neurology 2004;62:407-10.
    • (2004) Neurology , vol.62 , pp. 407-410
    • McMonagle, P.1    Byrne, P.2    Hutchinson, M.3
  • 62
    • 12344250580 scopus 로고    scopus 로고
    • The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B
    • Reid E, Connell J, Edwards TL, Duley S, Brown SE, Sanderson CM. The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B. Hum Mol Genet 2005;14:19-38.
    • (2005) Hum Mol Genet , vol.14 , pp. 19-38
    • Reid, E.1    Connell, J.2    Edwards, T.L.3    Duley, S.4    Brown, S.E.5    Sanderson, C.M.6
  • 63
    • 5744240094 scopus 로고    scopus 로고
    • Spastin interacts with the centrosomal protein NA14, and is enriched in the spindle pole, the midbody and the distal axon
    • Errico A, Claudiani P, D'Addio M, Rugarli EI. Spastin interacts with the centrosomal protein NA14, and is enriched in the spindle pole, the midbody and the distal axon. Hum Mol Genet 2004;13:2121-32.
    • (2004) Hum Mol Genet , vol.13 , pp. 2121-2132
    • Errico, A.1    Claudiani, P.2    D'Addio, M.3    Rugarli, E.I.4
  • 64
    • 33746094658 scopus 로고    scopus 로고
    • Interaction of two hereditary spastic paraplegia gene products, spastin and atlastin, suggests a common pathway for axonal maintenance
    • Evans K, Keller C, Pavur K, Glasgow K, Conn B, Lauring B. Interaction of two hereditary spastic paraplegia gene products, spastin and atlastin, suggests a common pathway for axonal maintenance. Proc Natl Acad Sci USA 2006;103:10666-71.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10666-10671
    • Evans, K.1    Keller, C.2    Pavur, K.3    Glasgow, K.4    Conn, B.5    Lauring, B.6
  • 65
    • 4644268519 scopus 로고    scopus 로고
    • Troyer syndrome revisited. A clinical and radiological study of a complicated hereditary spastic paraplegia
    • Proukakis C, Cross H, Patel H, Patton MA, Valentine A, Crosby AH. Troyer syndrome revisited. A clinical and radiological study of a complicated hereditary spastic paraplegia. J Neurol 2004;251:1105-10.
    • (2004) J Neurol , vol.251 , pp. 1105-1110
    • Proukakis, C.1    Cross, H.2    Patel, H.3    Patton, M.A.4    Valentine, A.5    Crosby, A.H.6
  • 68
    • 14844331501 scopus 로고    scopus 로고
    • Molecular motors and mechanisms of directional transport in neurons
    • Hirokawa N, Takemura R. Molecular motors and mechanisms of directional transport in neurons. Nat Rev Neurosci 2005;6:201-14.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 201-214
    • Hirokawa, N.1    Takemura, R.2
  • 71
    • 0036890143 scopus 로고    scopus 로고
    • Mouse models of Charcot-Marie-Tooth disease
    • Tanaka M, Hirokawa M. Mouse models of Charcot-Marie-Tooth disease. Trends Genet 2002;18:S39-44.
    • (2002) Trends Genet , vol.18
    • Tanaka, M.1    Hirokawa, M.2
  • 72
    • 0037884961 scopus 로고    scopus 로고
    • Kidney-specific inactivation of the KIF3A subunit of kinesin-II inhibits renal ciliogenesis and produces polycystic kidney disease
    • Lin F, Hiesberger T, Cordes K, Sinclair AM, Goldstein LS, Somlo S, Igarashi P. Kidney-specific inactivation of the KIF3A subunit of kinesin-II inhibits renal ciliogenesis and produces polycystic kidney disease. Proc Natl Acad Sci USA 2003;100:5286-91.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5286-5291
    • Lin, F.1    Hiesberger, T.2    Cordes, K.3    Sinclair, A.M.4    Goldstein, L.S.5    Somlo, S.6    Igarashi, P.7
  • 73
    • 0032005206 scopus 로고    scopus 로고
    • Cytoskeletal proteins and Golgi dynamics
    • Lippincott-Schwartz J. Cytoskeletal proteins and Golgi dynamics. Curr Opin Cell Biol 1998;10:52-9.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 52-59
    • Lippincott-Schwartz, J.1
  • 77
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall V, Post PL, Mooseker MS. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science 1998;279:527-33.
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 78
    • 33646856845 scopus 로고    scopus 로고
    • Molecular basis of human Usher syndrome: Deciphering the meshes of the Usher protein network provides insights into the pathomechanisms of the Usher disease
    • Reiners J, Nagel-Wolfrum K, Jurgens K, Marker T, Wolfrum U. Molecular basis of human Usher syndrome: deciphering the meshes of the Usher protein network provides insights into the pathomechanisms of the Usher disease. Exp Eye Res 2006;83:97-119.
    • (2006) Exp Eye Res , vol.83 , pp. 97-119
    • Reiners, J.1    Nagel-Wolfrum, K.2    Jurgens, K.3    Marker, T.4    Wolfrum, U.5
  • 80
    • 0345133276 scopus 로고    scopus 로고
    • Myosin XVa localizes to the tips of inner ear sensory cell stereocilia and is essential for staircase formation of the hair bundle
    • Belyantseva IA, Boger ET, Friedman TB. Myosin XVa localizes to the tips of inner ear sensory cell stereocilia and is essential for staircase formation of the hair bundle. Proc Natl Acad Sci U S A 2003;100:13958-63.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 13958-13963
    • Belyantseva, I.A.1    Boger, E.T.2    Friedman, T.B.3
  • 81
    • 0035890255 scopus 로고    scopus 로고
    • SNARE complex structure and function
    • Hey JC. SNARE complex structure and function. Exp Cell Res 2001;271:10-21.
    • (2001) Exp Cell Res , vol.271 , pp. 10-21
    • Hey, J.C.1
  • 82
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino JS, Glick ES. The mechanisms of vesicle budding and fusion. Cell 2004;16:153-66.
    • (2004) Cell , vol.16 , pp. 153-166
    • Bonifacino, J.S.1    Glick, E.S.2
  • 85
    • 29944442846 scopus 로고    scopus 로고
    • Mutation spectrum in children with primary hemophagocytic lymphohistiocytosis: Molecular and functional analyses of PRF1, UNC13D, STX11, and RAB27A
    • Zur Stadt U, Beutel K, Kolberg S, Schneppenheim R, Kabisch H, Janka G, Hennies HC. Mutation spectrum in children with primary hemophagocytic lymphohistiocytosis: molecular and functional analyses of PRF1, UNC13D, STX11, and RAB27A. Hum Mutat 2006;27:62-8.
    • (2006) Hum Mutat , vol.27 , pp. 62-68
    • Zur Stadt, U.1    Beutel, K.2    Kolberg, S.3    Schneppenheim, R.4    Kabisch, H.5    Janka, G.6    Hennies, H.C.7
  • 86
    • 0032925888 scopus 로고    scopus 로고
    • Syntaxin 11 is associated with SNAP-23 on late endosomes and the trans-Golgi network
    • Valdez AC, Cabaniols JP, Brown MJ, Roche PA. Syntaxin 11 is associated with SNAP-23 on late endosomes and the trans-Golgi network. J Cell Sci 1999;112:845-54.
    • (1999) J Cell Sci , vol.112 , pp. 845-854
    • Valdez, A.C.1    Cabaniols, J.P.2    Brown, M.J.3    Roche, P.A.4
  • 88
    • 0033784541 scopus 로고    scopus 로고
    • Interactions within the yeast t-SNARE Sso1p that control SNARE complex assembly
    • Munson M, Chen X, Cocina AE, Schultz SM, Hughson FM. Interactions within the yeast t-SNARE Sso1p that control SNARE complex assembly. Nat Struct Biol 2000;7:894-902.
    • (2000) Nat Struct Biol , vol.7 , pp. 894-902
    • Munson, M.1    Chen, X.2    Cocina, A.E.3    Schultz, S.M.4    Hughson, F.M.5
  • 95
    • 17344365600 scopus 로고    scopus 로고
    • Liu J, Aoki M, Illa I, Wu C, Fardeau M, Angelini C, Serrano C, Urtizberea JA, Hentati F, Hamida MB, Bohlega S, Culper FJ, Amato AA, Bossie K, Oeltjen J, Bejaoui K, McKenna-Yasek D, Hosler BA, Schurr E, Arahata K, de Jong PJ, Brown RH Jr. Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy. Nat Genet 1998;20:31-6.
    • Liu J, Aoki M, Illa I, Wu C, Fardeau M, Angelini C, Serrano C, Urtizberea JA, Hentati F, Hamida MB, Bohlega S, Culper FJ, Amato AA, Bossie K, Oeltjen J, Bejaoui K, McKenna-Yasek D, Hosler BA, Schurr E, Arahata K, de Jong PJ, Brown RH Jr. Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy. Nat Genet 1998;20:31-6.
  • 96
    • 1842556210 scopus 로고    scopus 로고
    • Dysferlin and the plasma membrane repair in muscular dystrophy
    • Bansal D, Campbell KP. Dysferlin and the plasma membrane repair in muscular dystrophy. Trends Cell Biol 2004;14:206-13.
    • (2004) Trends Cell Biol , vol.14 , pp. 206-213
    • Bansal, D.1    Campbell, K.P.2
  • 102
    • 0032104120 scopus 로고    scopus 로고
    • Evidence for defects in the trafficking and translocation of GLUT4 glucose transporters in skeletal muscle as a cause of human insulin resistance
    • Garvey WT, Maianu L, Zhu JH, Brechtel-Hook G, Wallace P, Baron AD. Evidence for defects in the trafficking and translocation of GLUT4 glucose transporters in skeletal muscle as a cause of human insulin resistance. J Clin Invest 1998;101:2377-86.
    • (1998) J Clin Invest , vol.101 , pp. 2377-2386
    • Garvey, W.T.1    Maianu, L.2    Zhu, J.H.3    Brechtel-Hook, G.4    Wallace, P.5    Baron, A.D.6
  • 103
    • 0035191192 scopus 로고    scopus 로고
    • Adipocytes exhibit abnormal subcellular distribution and translocation of vesicles containing glucose transporter 4 and insulin-regulated aminopeptidase in type 2 diabetes mellitus: Implications regarding defects in vesicle trafficking
    • Maianu L, Keller SR, Garvey WT. Adipocytes exhibit abnormal subcellular distribution and translocation of vesicles containing glucose transporter 4 and insulin-regulated aminopeptidase in type 2 diabetes mellitus: implications regarding defects in vesicle trafficking. J Clin Endocrinol Metab 2001;86:5450-6.
    • (2001) J Clin Endocrinol Metab , vol.86 , pp. 5450-5456
    • Maianu, L.1    Keller, S.R.2    Garvey, W.T.3
  • 105
    • 0034518216 scopus 로고    scopus 로고
    • The genetics and molecular pathology of Alzheimer's disease: Roles of amyloid and the presenilis
    • Selkoe DJ. The genetics and molecular pathology of Alzheimer's disease: roles of amyloid and the presenilis. Neurol Clin 2000;18:903-22.
    • (2000) Neurol Clin , vol.18 , pp. 903-922
    • Selkoe, D.J.1
  • 106
    • 0035949487 scopus 로고    scopus 로고
    • Presenilin, Notch, and the genesis and treatment of Alzheimer's disease
    • Selkoe DJ. Presenilin, Notch, and the genesis and treatment of Alzheimer's disease. Proc Natl Acad Sci U S A 2001;98:11039-41.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11039-11041
    • Selkoe, D.J.1
  • 107
    • 33746930858 scopus 로고    scopus 로고
    • Trafficking of Alzheimer's disease-related membrane proteins and its participation in disease pathogenesis
    • Suzuki T, Araki Y, Yamamoto T, Nokaya T. Trafficking of Alzheimer's disease-related membrane proteins and its participation in disease pathogenesis. J Bioehem (Tokyo) 2006;139:949-55.
    • (2006) J Bioehem (Tokyo) , vol.139 , pp. 949-955
    • Suzuki, T.1    Araki, Y.2    Yamamoto, T.3    Nokaya, T.4
  • 108
    • 32544435097 scopus 로고    scopus 로고
    • The lipoprotein receptor LR11 regulates amyloid beta production and amyloid precursor protein traffic in endosomal compartments
    • Offe K, Dodson SE, Shoemaker JT, Fritz JJ, Gearing M, Levey AI, Lah JJ. The lipoprotein receptor LR11 regulates amyloid beta production and amyloid precursor protein traffic in endosomal compartments. J Neurosci 2006;26:1596-603.
    • (2006) J Neurosci , vol.26 , pp. 1596-1603
    • Offe, K.1    Dodson, S.E.2    Shoemaker, J.T.3    Fritz, J.J.4    Gearing, M.5    Levey, A.I.6    Lah, J.J.7
  • 109
    • 0038603918 scopus 로고    scopus 로고
    • A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1
    • Inomata H, Nakamura Y, Hayakawa A, Takata H, Suzuki T, Miyazawa K, Kitamura N. A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1. J Biol Chem 2003;278:22946-55.
    • (2003) J Biol Chem , vol.278 , pp. 22946-22955
    • Inomata, H.1    Nakamura, Y.2    Hayakawa, A.3    Takata, H.4    Suzuki, T.5    Miyazawa, K.6    Kitamura, N.7
  • 112
    • 33845757628 scopus 로고    scopus 로고
    • Phosphorylation inhibits turnover of the tau protein by the proteasome: Influence of RCAN1 and oxidative stress
    • Poppek D, Keck S, Ermak G, Jung T, Stolzing A, Ullrich O, Davies KJ, Grune T. Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress. Biochem J 2006;400:511-20.
    • (2006) Biochem J , vol.400 , pp. 511-520
    • Poppek, D.1    Keck, S.2    Ermak, G.3    Jung, T.4    Stolzing, A.5    Ullrich, O.6    Davies, K.J.7    Grune, T.8
  • 114
    • 33847122608 scopus 로고    scopus 로고
    • Modulating the folding of P-glycoprotein and cystic fibrosis transmembrane conductance regulator truncation mutants with pharmacological chaperones
    • Wang Y, Loo TW, Bartlett MC, Clarke DM. Modulating the folding of P-glycoprotein and cystic fibrosis transmembrane conductance regulator truncation mutants with pharmacological chaperones. Mol Pharmacol 2007;71:751-8.
    • (2007) Mol Pharmacol , vol.71 , pp. 751-758
    • Wang, Y.1    Loo, T.W.2    Bartlett, M.C.3    Clarke, D.M.4


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