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Volumn 14, Issue , 2013, Pages 159-190

Cellular assays for drug discovery in genetic disorders of intracellular trafficking

Author keywords

Cell based assays; Genetic diseases; High content screening; Membrane trafficking; Pharmacological approach

Indexed keywords

ADAPTOR PROTEIN; ALPHA GALACTOSIDASE; AMBROXOL; ARIMOCLOMOL; CELASTROL; CLATHRIN; COAT PROTEIN; COAT PROTEIN COMPLEX II; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; DYMECLIN; DYSBINDIN; ESCRT PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; HEAT SHOCK PROTEIN 1; HEAT SHOCK PROTEIN 4; LARAZOTIDE; MANNOSE 6 PHOSPHATE; MIGALASTAT; MOLECULAR MOTOR; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL; POLYGLUTAMINE; RAB PROTEIN; SALUBRINAL; SAR1B PROTEIN; SNAP29 PROTEIN; SOMATOMEDIN B RECEPTOR; UBIQUITINATED PROTEIN; UNCLASSIFIED DRUG;

EID: 84884298534     PISSN: 15278204     EISSN: 1545293X     Source Type: Book Series    
DOI: 10.1146/annurev-genom-091212-153415     Document Type: Review
Times cited : (10)

References (180)
  • 1
    • 0029115555 scopus 로고
    • The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset AD families
    • Alzheimer's Dis. Collab. Group
    • Alzheimer's Dis. Collab. Group. 1995. The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset AD families. Nat. Genet. 11:219-22
    • (1995) Nat. Genet , vol.11 , pp. 219-222
  • 2
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): In search of its identity and function
    • Appenzeller-Herzog C, HauriHP. 2006. The ER-Golgi intermediate compartment (ERGIC): In search of its identity and function. J. Cell Sci. 119:2173-83
    • (2006) J. Cell Sci , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 3
    • 0026742127 scopus 로고
    • The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase
    • Attree O, Olivos IM, Okabe I, Bailey LC, Nelson DL, et al. 1992. The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase. Nature 358:239-42
    • (1992) Nature , vol.358 , pp. 239-242
    • Attree, O.1    Olivos, I.M.2    Okabe, I.3    Bailey, L.C.4    Nelson, D.L.5
  • 4
    • 37149056344 scopus 로고    scopus 로고
    • Lack of synapsin I reduces the readily releasable pool of synaptic vesicles at central inhibitory synapses
    • Baldelli P, Fassio A, Valtorta F, Benfenati F. 2007. Lack of synapsin I reduces the readily releasable pool of synaptic vesicles at central inhibitory synapses. J. Neurosci. 27:13520-31
    • (2007) J. Neurosci , vol.27 , pp. 13520-13531
    • Baldelli, P.1    Fassio, A.2    Valtorta, F.3    Benfenati, F.4
  • 5
    • 70349616273 scopus 로고    scopus 로고
    • Screen for chemical modulators of autophagy reveals novel therapeutic inhibitors of mTORC1 signaling
    • Balgi AD, Fonseca BD, Donohue E, Tsang TC, Lajoie P, et al. 2009. Screen for chemical modulators of autophagy reveals novel therapeutic inhibitors of mTORC1 signaling. PLoS ONE 4:e7124
    • (2009) PLoS ONE , vol.4
    • Balgi, A.D.1    Fonseca, B.D.2    Donohue, E.3    Tsang, T.C.4    Lajoie, P.5
  • 6
    • 31844440878 scopus 로고    scopus 로고
    • Functional genomics reveals genes involved in protein secretion and Golgi organization
    • Bard F, Casano L, Mallabiabarrena A, Wallace E, Saito K, et al. 2006. Functional genomics reveals genes involved in protein secretion and Golgi organization. Nature 439:604-7
    • (2006) Nature , vol.439 , pp. 604-607
    • Bard, F.1    Casano, L.2    Mallabiabarrena, A.3    Wallace, E.4    Saito, K.5
  • 7
    • 79951870239 scopus 로고    scopus 로고
    • The CMT4B disease-causing proteins MTMR2 and MTMR13/SBF2 regulate AKT signalling
    • Berger P, Tersar K, Ballmer-Hofer K, Suter U. 2011. The CMT4B disease-causing proteins MTMR2 and MTMR13/SBF2 regulate AKT signalling. J. Cell. Mol. Med. 15:307-15
    • (2011) J. Cell. Mol. Med , vol.15 , pp. 307-315
    • Berger, P.1    Tersar, K.2    Ballmer-Hofer, K.3    Suter, U.4
  • 8
    • 33751159209 scopus 로고    scopus 로고
    • Intracellular signaling by the unfolded protein response
    • Bernales S, Papa FR, Walter P. 2006. Intracellular signaling by the unfolded protein response. Annu. Rev. Cell Dev. Biol. 22:487-508
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , pp. 487-508
    • Bernales, S.1    Papa, F.R.2    Walter, P.3
  • 9
    • 33750344792 scopus 로고    scopus 로고
    • Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins
    • Bethune J, Kol M, Hoffmann J, Reckmann I, Brugger B, Wieland F. 2006. Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins. Mol. Cell. Biol. 26:8011-21
    • (2006) Mol. Cell. Biol , vol.26 , pp. 8011-8021
    • Bethune, J.1    Kol, M.2    Hoffmann, J.3    Reckmann, I.4    Brugger, B.5    Wieland, F.6
  • 10
    • 69349094765 scopus 로고    scopus 로고
    • Mutations in INPP5E, encoding inositol polyphosphate-5-phosphatase E, link phosphatidyl inositol signaling to the ciliopathies
    • Bielas SL, Silhavy JL, Brancati F, Kisseleva MV, Al-Gazali L, et al. 2009. Mutations in INPP5E, encoding inositol polyphosphate-5-phosphatase E, link phosphatidyl inositol signaling to the ciliopathies. Nat. Genet. 41:1032-36
    • (2009) Nat. Genet , vol.41 , pp. 1032-1036
    • Bielas, S.L.1    Silhavy, J.L.2    Brancati, F.3    Kisseleva, M.V.4    Al-Gazali, L.5
  • 11
    • 79960635284 scopus 로고    scopus 로고
    • Fighting neurodegeneration with rapamycin: Mechanistic insights
    • Bové J, Martínez-Vicente M, Vila M. 2011. Fighting neurodegeneration with rapamycin: Mechanistic insights. Nat. Rev. Neurosci. 12:437-52
    • (2011) Nat. Rev. Neurosci , vol.12 , pp. 437-452
    • Bové, J.1    Martínez-Vicente, M.2    Vila, M.3
  • 12
    • 33749128067 scopus 로고    scopus 로고
    • Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-To-Golgi trafficking
    • Boyadjiev SA, Fromme JC, Ben J, Chong SS, Nauta C, et al. 2006. Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-To-Golgi trafficking. Nat. Genet. 38:1192-97
    • (2006) Nat. Genet , vol.38 , pp. 1192-1197
    • Boyadjiev, S.A.1    Fromme, J.C.2    Ben, J.3    Chong, S.S.4    Nauta, C.5
  • 13
    • 79960275945 scopus 로고    scopus 로고
    • Cranio-lenticulo-sutural dysplasia associated with defects in collagen secretion
    • Boyadjiev SA, Kim SD, Hata A, Haldeman-Englert C, Zackai EH, et al. 2011. Cranio-lenticulo-sutural dysplasia associated with defects in collagen secretion. Clin. Genet. 80:169-76
    • (2011) Clin. Genet , vol.80 , pp. 169-176
    • Boyadjiev, S.A.1    Kim, S.D.2    Hata, A.3    Haldeman-Englert, C.4    Zackai, E.H.5
  • 14
    • 53049108504 scopus 로고    scopus 로고
    • Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration, regulates COPI-mediated retrograde traffic
    • Burman JL, Bourbonniere L, Philie J, Stroh T, Dejgaard SY, et al. 2008. Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration, regulates COPI-mediated retrograde traffic. J. Biol. Chem. 283:22774-86
    • (2008) J. Biol. Chem , vol.283 , pp. 22774-22786
    • Burman, J.L.1    Bourbonniere, L.2    Philie, J.3    Stroh, T.4    Dejgaard, S.Y.5
  • 16
    • 84856089134 scopus 로고    scopus 로고
    • Small-molecule proteostasis regulators for protein conformational diseases
    • Calamini B, Silva MC, Madoux F, Hutt DM, Khanna S, et al. 2012. Small-molecule proteostasis regulators for protein conformational diseases. Nat. Chem. Biol. 8:185-96
    • (2012) Nat. Chem. Biol , vol.8 , pp. 185-196
    • Calamini, B.1    Silva, M.C.2    Madoux, F.3    Hutt, D.M.4    Khanna, S.5
  • 17
    • 50549094090 scopus 로고    scopus 로고
    • The potential of intracellular antibodies for therapeutic targeting of proteinmisfolding diseases
    • Cardinale A, Biocca S. 2008. The potential of intracellular antibodies for therapeutic targeting of proteinmisfolding diseases. Trends Mol. Med. 14:373-80
    • (2008) Trends Mol. Med , vol.14 , pp. 373-380
    • Cardinale, A.1    Biocca, S.2
  • 18
    • 0030863352 scopus 로고    scopus 로고
    • Niemann-Pick C1 disease gene: Homology to mediators of cholesterol homeostasis
    • Carstea ED, Morris JA, Coleman KG, Loftus SK, Zhang D, et al. 1997. Niemann-Pick C1 disease gene: Homology to mediators of cholesterol homeostasis. Science 277:228-31
    • (1997) Science , vol.277 , pp. 228-231
    • Carstea, E.D.1    Morris, J.A.2    Coleman, K.G.3    Loftus, S.K.4    Zhang, D.5
  • 19
    • 63449090757 scopus 로고    scopus 로고
    • Huntingtin as an essential integrator of intracellular vesicular trafficking
    • Caviston JP, Holzbaur EL. 2009. Huntingtin as an essential integrator of intracellular vesicular trafficking. Trends Cell Biol. 19:147-55
    • (2009) Trends Cell Biol , vol.19 , pp. 147-155
    • Caviston, J.P.1    Holzbaur, E.L.2
  • 20
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • Cheng SH, Gregory RJ, Marshall J, Paul S, Souza DW, et al. 1990. Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell 63:827-34
    • (1990) Cell , vol.63 , pp. 827-834
    • Cheng, S.H.1    Gregory, R.J.2    Marshall, J.3    Paul, S.4    Souza, D.W.5
  • 21
    • 33947653114 scopus 로고    scopus 로고
    • Brain slices as models for neurodegenerative disease and screening platforms to identify novel therapeutics
    • Cho S, Wood A, Bowlby MR. 2007. Brain slices as models for neurodegenerative disease and screening platforms to identify novel therapeutics. Curr. Neuropharmacol. 5:19-33
    • (2007) Curr. Neuropharmacol , vol.5 , pp. 19-33
    • Cho, S.1    Wood, A.2    Bowlby, M.R.3
  • 22
    • 79953215473 scopus 로고    scopus 로고
    • Quantitative cell-based protein degradation assays to identify and classify drugs that target the ubiquitin-proteasome system
    • Chou TF, Deshaies RJ. 2011. Quantitative cell-based protein degradation assays to identify and classify drugs that target the ubiquitin-proteasome system. J. Biol. Chem. 286:16546-54
    • (2011) J. Biol. Chem , vol.286 , pp. 16546-16554
    • Chou, T.F.1    Deshaies, R.J.2
  • 23
    • 23044490771 scopus 로고    scopus 로고
    • Lowe syndrome protein OCRL1 interacts with clathrin and regulates protein trafficking between endosomes and the trans-Golgi network
    • Choudhury R, Diao A, Zhang F, Eisenberg E, Saint-Pol A, et al. 2005. Lowe syndrome protein OCRL1 interacts with clathrin and regulates protein trafficking between endosomes and the trans-Golgi network. Mol. Biol. Cell 16:3467-79
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3467-3479
    • Choudhury, R.1    Diao, A.2    Zhang, F.3    Eisenberg, E.4    Saint-Pol, A.5
  • 24
    • 70349567495 scopus 로고    scopus 로고
    • Receptor-mediated endocytosis in renal proximal tubule
    • Christensen EI, Verroust PJ, Nielsen R. 2009. Receptor-mediated endocytosis in renal proximal tubule. Pflugers Arch. 458:1039-48
    • (2009) Pflugers Arch , vol.458 , pp. 1039-1048
    • Christensen, E.I.1    Verroust, P.J.2    Nielsen, R.3
  • 25
    • 67349163727 scopus 로고    scopus 로고
    • Phosphoinositides and the endocytic pathway
    • Clague MJ, Urbe S, De Lartigue J. 2009. Phosphoinositides and the endocytic pathway. Exp. Cell Res. 315:1627-31
    • (2009) Exp. Cell Res , vol.315 , pp. 1627-1631
    • Clague, M.J.1    Urbe, S.2    De Lartigue, J.3
  • 26
    • 84855202429 scopus 로고    scopus 로고
    • Results of a phase IIa study of VX-809, an investigational CFTR corrector compound, in subjects with cystic fibrosis homozygous for the F508del-CFTR mutation
    • Clancy JP, Rowe SM, Accurso FJ, Aitken ML, Amin RS, et al. 2012. Results of a phase IIa study of VX-809, an investigational CFTR corrector compound, in subjects with cystic fibrosis homozygous for the F508del-CFTR mutation. Thorax 67:12-18
    • (2012) Thorax , vol.67 , pp. 12-18
    • Clancy, J.P.1    Rowe, S.M.2    Accurso, F.J.3    Aitken, M.L.4    Amin, R.S.5
  • 27
    • 77949424084 scopus 로고    scopus 로고
    • Systems survey of endocytosis by multiparametric image analysis
    • Collinet C, Stoter M, Bradshaw CR, Samusik N, Rink JC, et al. 2010. Systems survey of endocytosis by multiparametric image analysis. Nature 464:243-49
    • (2010) Nature , vol.464 , pp. 243-249
    • Collinet, C.1    Stoter, M.2    Bradshaw, C.R.3    Samusik, N.4    Rink, J.C.5
  • 28
    • 77149130553 scopus 로고    scopus 로고
    • Automated microscopy for high-content RNAi screening
    • Conrad C, Gerlich DW. 2010. Automated microscopy for high-content RNAi screening. J. Cell Biol. 188:453-61
    • (2010) J. Cell Biol , vol.188 , pp. 453-461
    • Conrad, C.1    Gerlich, D.W.2
  • 29
    • 33746533924 scopus 로고    scopus 로고
    • A-Synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models
    • Cooper AA, Gitler AD, Cashikar A, Haynes CM, Hill KJ, et al. 2006. a-Synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science 313:324-28
    • (2006) Science , vol.313 , pp. 324-328
    • Cooper, A.A.1    Gitler, A.D.2    Cashikar, A.3    Haynes, C.M.4    Hill, K.J.5
  • 30
    • 77956392186 scopus 로고    scopus 로고
    • Mutations in CHMP2B in lower motor neuron predominant amyotrophic lateral sclerosis (ALS)
    • Cox LE, Ferraiuolo L, Goodall EF, Heath PR, Higginbottom A, et al. 2010. Mutations in CHMP2B in lower motor neuron predominant amyotrophic lateral sclerosis (ALS). PLoS ONE 5:e9872
    • (2010) PLoS ONE , vol.5
    • Cox, L.E.1    Ferraiuolo, L.2    Goodall, E.F.3    Heath, P.R.4    Higginbottom, A.5
  • 31
    • 82755181717 scopus 로고    scopus 로고
    • The cellular pathology of lysosomal diseases
    • Cox TM, Cachón-GonzálezMB. 2012. The cellular pathology of lysosomal diseases. J. Pathol. 226:241-54
    • (2012) J. Pathol , vol.226 , pp. 241-254
    • Cox, T.M.1    Cachón-González, M.B.2
  • 35
    • 79551516571 scopus 로고    scopus 로고
    • Dymeclin, the gene underlying dyggve-melchior-clausen syndrome, encodes a protein integral to extracellular matrix and golgi organization and is associated with protein secretion pathways critical in bone development
    • Denais C, Dent CL, Southgate L, Hoyle J, DafouD, et al. 2011. Dymeclin, the gene underlying Dyggve-Melchior-Clausen syndrome, encodes a protein integral to extracellular matrix and Golgi organization and is associated with protein secretion pathways critical in bone development. Hum. Mutat. 32:231-39
    • (2011) Hum. Mutat , vol.32 , pp. 231-239
    • Denais, C.1    Dent, C.L.2    Southgate, L.3    Hoyle, J.4    Dafou, D.5
  • 36
    • 33745239787 scopus 로고    scopus 로고
    • Biologically active molecules that reduce polyglutamine aggregation and toxicity
    • Desai UA, Pallos J, Ma AA, Stockwell BR, Thompson LM, et al. 2006. Biologically active molecules that reduce polyglutamine aggregation and toxicity. Hum. Mol. Genet. 15:2114-24
    • (2006) Hum. Mol. Genet , vol.15 , pp. 2114-2124
    • Desai, U.A.1    Pallos, J.2    Ma, A.A.3    Stockwell, B.R.4    Thompson, L.M.5
  • 38
    • 84865592978 scopus 로고    scopus 로고
    • Amino acids and mTORC1: From lysosomes to disease
    • Efeyan A, Zoncu R, Sabatini DM. 2012. Amino acids and mTORC1: From lysosomes to disease. Trends Mol. Med. 18:524-33
    • (2012) Trends Mol. Med , vol.18 , pp. 524-533
    • Efeyan, A.1    Zoncu, R.2    Sabatini, D.M.3
  • 39
    • 65649085175 scopus 로고    scopus 로고
    • Faciogenital dysplasia protein (FGD1) regulates export of cargo proteins from theGolgi complex via Cdc42 activation
    • Egorov MV, Capestrano M, Vorontsova OA, Di Pentima A, Egorova AV, et al. 2009. Faciogenital dysplasia protein (FGD1) regulates export of cargo proteins from theGolgi complex via Cdc42 activation. Mol. Biol. Cell 20:2413-27
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2413-2427
    • Egorov, M.V.1    Capestrano, M.2    Vorontsova, O.A.3    Di Pentima, A.4    Egorova, A.V.5
  • 41
    • 34548210456 scopus 로고    scopus 로고
    • A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway
    • Erdmann KS, Mao Y, McCrea HJ, Zoncu R, Lee S, et al. 2007. A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway. Dev. Cell 13:377-90
    • (2007) Dev. Cell , vol.13 , pp. 377-390
    • Erdmann, K.S.1    Mao, Y.2    McCrea, H.J.3    Zoncu, R.4    Lee, S.5
  • 42
    • 29244449301 scopus 로고    scopus 로고
    • Distribution and dynamics of Lamp1-containing endocytic organelles in fibroblasts deficient in BLOC-3
    • Falc ón-Pérez JM, Nazarian R, Sabatti C, Dell'Angelica EC. 2005. Distribution and dynamics of Lamp1-containing endocytic organelles in fibroblasts deficient in BLOC-3. J. Cell Sci. 118:5243-55
    • (2005) J. Cell Sci , vol.118 , pp. 5243-5255
    • Falcón-Pérez, J.M.1    Nazarian, R.2    Sabatti, C.3    Dell'Angelica, E.C.4
  • 43
    • 77953593628 scopus 로고    scopus 로고
    • MAPK signaling to the early secretory pathway revealed by kinase/phosphatase functional screening
    • Farhan H, Wendeler MW, Mitrovic S, Fava E, Silberberg Y, et al. 2010. MAPK signaling to the early secretory pathway revealed by kinase/phosphatase functional screening. J. Cell. Biol. 189:997-1011
    • (2010) J. Cell. Biol , vol.189 , pp. 997-1011
    • Farhan, H.1    Wendeler, M.W.2    Mitrovic, S.3    Fava, E.4    Silberberg, Y.5
  • 44
    • 79957456437 scopus 로고    scopus 로고
    • SYN1 loss-of-function mutations in autism and partial epilepsy cause impaired synaptic function
    • Fassio A, Patry L, Congia S, Onofri F, Piton A, et al. 2011. SYN1 loss-of-function mutations in autism and partial epilepsy cause impaired synaptic function. Hum. Mol. Genet. 20:2297-307
    • (2011) Hum. Mol. Genet , vol.20 , pp. 2297-2307
    • Fassio, A.1    Patry, L.2    Congia, S.3    Onofri, F.4    Piton, A.5
  • 45
    • 80051785915 scopus 로고    scopus 로고
    • Mislocalization of large ARF-GEFs as a potential mechanism for BFA resistance in COG-Deficient cells
    • Flanagan-Steet H, Johnson S, Smith RD, Bangiyeva J, Lupashin V, Steet R. 2011. Mislocalization of large ARF-GEFs as a potential mechanism for BFA resistance in COG-Deficient cells. Exp. Cell Res. 317:2342-52
    • (2011) Exp. Cell Res , vol.317 , pp. 2342-2352
    • Flanagan-Steet, H.1    Johnson, S.2    Smith, R.D.3    Bangiyeva, J.4    Lupashin, V.5    Steet, R.6
  • 46
    • 84868567742 scopus 로고    scopus 로고
    • The hereditary spastic paraplegia protein strumpellin: Characterisation in neurons and of the effect of disease mutations on WASH complex assembly and function
    • Freeman C, Seaman MN, Reid E. 2013. The hereditary spastic paraplegia protein strumpellin: Characterisation in neurons and of the effect of disease mutations on WASH complex assembly and function. Biochim. Biophys. Acta 1832:160-73
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 160-173
    • Freeman, C.1    Seaman, M.N.2    Reid, E.3
  • 47
    • 66449083078 scopus 로고    scopus 로고
    • ULK1áTG13?FIP200 complex mediates mTOR signaling and is essential for autophagy
    • Ganley IG, Lam du H, Wang J, Ding X, Chen S, Jiang X. 2009. ULK1áTG13?FIP200 complex mediates mTOR signaling and is essential for autophagy. J. Biol. Chem. 284:12297-305
    • (2009) J. Biol. Chem , vol.284 , pp. 12297-12305
    • Ganley, I.G.1    Lam Du, H.2    Wang, J.3    Ding, X.4    Chen, S.5    Jiang, X.6
  • 48
    • 0032769695 scopus 로고    scopus 로고
    • Identification of the gene (sedl) causing x-linked spondyloepiphyseal dysplasia tarda
    • Gedeon AK, Colley A, Jamieson R, Thompson EM, Rogers J, et al. 1999. Identification of the gene (SEDL) causing X-linked spondyloepiphyseal dysplasia tarda. Nat. Genet. 22:400-4
    • (1999) Nat. Genet , vol.22 , pp. 400-404
    • Gedeon, A.K.1    Colley, A.2    Jamieson, R.3    Thompson, E.M.4    Rogers, J.5
  • 50
    • 76249116225 scopus 로고    scopus 로고
    • Mutations in the small GTPase gene RAB39B are responsible for X-linked mental retardation associated with autism, epilepsy, and macrocephaly
    • Giannandrea M, Bianchi V, Mignogna ML, Sirri A, Carrabino S, et al. 2010. Mutations in the small GTPase gene RAB39B are responsible for X-linked mental retardation associated with autism, epilepsy, and macrocephaly. Am. J. Hum. Genet. 86:185-95
    • (2010) Am. J. Hum. Genet , vol.86 , pp. 185-195
    • Giannandrea, M.1    Bianchi, V.2    Mignogna, M.L.3    Sirri, A.4    Carrabino, S.5
  • 51
    • 78650146676 scopus 로고    scopus 로고
    • A disease-relevant high-content screening assay to identify antiinflammatory compounds for use in cystic fibrosis
    • Giddings AM, Maitra R. 2010. A disease-relevant high-content screening assay to identify antiinflammatory compounds for use in cystic fibrosis. J. Biomol. Screen. 15:1204-10
    • (2010) J. Biomol. Screen , vol.15 , pp. 1204-1210
    • Giddings, A.M.1    Maitra, R.2
  • 53
    • 33845760114 scopus 로고    scopus 로고
    • Automated subcellular location determination and high-Throughput microscopy
    • Glory E, Murphy RF. 2007. Automated subcellular location determination and high-Throughput microscopy. Dev. Cell 12:7-16
    • (2007) Dev. Cell , vol.12 , pp. 7-16
    • Glory, E.1    Murphy, R.F.2
  • 54
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • Goate A, Chartier-Harlin MC, Mullan M, Brown J, Crawford F, et al. 1991. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 349:704-6
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.C.2    Mullan, M.3    Brown, J.4    Crawford, F.5
  • 55
    • 84855845987 scopus 로고    scopus 로고
    • High throughput screening for small molecule therapy for Gaucher disease using patient tissue as the source of mutant glucocerebrosidase
    • Goldin E, ZhengW, Motabar O, Southall N, Choi JH, et al. 2012. High throughput screening for small molecule therapy for Gaucher disease using patient tissue as the source of mutant glucocerebrosidase. PLoS ONE 7:e29861
    • (2012) PLoS ONE , vol.7
    • Goldin, E.1    Zheng, W.2    Motabar, O.3    Southall, N.4    Choi, J.H.5
  • 56
  • 58
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M. 2011. Molecular chaperones in protein folding and proteostasis. Nature 475:324-32
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 59
    • 58149374223 scopus 로고    scopus 로고
    • High-Throughput functional screening for autophagyrelated genes and identification of TM9SF1 as an autophagosome-inducing gene
    • He P, Peng Z, Luo Y, Wang L, Yu P, et al. 2009. High-Throughput functional screening for autophagyrelated genes and identification of TM9SF1 as an autophagosome-inducing gene. Autophagy 5:52-60
    • (2009) Autophagy , vol.5 , pp. 52-60
    • He, P.1    Peng, Z.2    Luo, Y.3    Wang, L.4    Yu, P.5
  • 61
    • 79955415881 scopus 로고    scopus 로고
    • Suppression of Alzheimer's disease-related phenotypes by expression of heat shock protein 70 in mice
    • Hoshino T, Murao N, Namba T, Takehara M, Adachi H, et al. 2011. Suppression of Alzheimer's disease-related phenotypes by expression of heat shock protein 70 in mice. J. Neurosci. 31:5225-34
    • (2011) J. Neurosci , vol.31 , pp. 5225-5234
    • Hoshino, T.1    Murao, N.2    Namba, T.3    Takehara, M.4    Adachi, H.5
  • 62
    • 57749116036 scopus 로고    scopus 로고
    • FGD2, a CDC42-specific exchange factor expressed by antigen-presenting cells, localizes to early endosomes and active membrane ruffles
    • HuberC, Martensson A, BokochGM, NemazeeD, Gavin AL. 2008. FGD2, a CDC42-specific exchange factor expressed by antigen-presenting cells, localizes to early endosomes and active membrane ruffles. J. Biol. Chem. 283:34002-12
    • (2008) J. Biol. Chem , vol.283 , pp. 34002-34012
    • Huber, C.1    Martensson, A.2    Bokoch, G.M.3    Nemazee, D.4    Gavin, A.L.5
  • 63
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • Huntington's Dis Collab. Group
    • Huntington's Dis. Collab. Group. 1993. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72:971-83
    • (1993) Cell , vol.72 , pp. 971-983
  • 64
    • 33745747824 scopus 로고    scopus 로고
    • Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis
    • Ishida Y, Kubota H, Yamamoto A, Kitamura A, Bächinger HP, Nagata K. 2006. Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis. Mol. Biol. Cell 17:2346-55
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2346-2355
    • Ishida, Y.1    Kubota, H.2    Yamamoto, A.3    Kitamura, A.4    Bächinger, H.P.5    Nagata, K.6
  • 65
    • 35548972537 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: A rapidly expanding disease family
    • Jaeken J, Matthijs G. 2007. Congenital disorders of glycosylation: A rapidly expanding disease family. Annu. Rev. Genomics Hum. Genet. 8:261-78
    • (2007) Annu. Rev. Genomics Hum. Genet , vol.8 , pp. 261-278
    • Jaeken, J.1    Matthijs, G.2
  • 66
    • 73349091579 scopus 로고    scopus 로고
    • Role of dysbindin in dopamine receptor trafficking and cortical GABA function
    • Ji Y, Yang F, Papaleo F, Wang HX, Gao WJ, et al. 2009. Role of dysbindin in dopamine receptor trafficking and cortical GABA function. Proc. Natl. Acad. Sci. USA 106:19593-98
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 19593-19598
    • Ji, Y.1    Yang, F.2    Papaleo, F.3    Wang, H.X.4    Gao, W.J.5
  • 67
    • 84862687793 scopus 로고    scopus 로고
    • Axonal transport deficit in a KIF5A-/-mouse model
    • Karle KN, Mockel D, Reid E, Schols L. 2012. Axonal transport deficit in a KIF5A-/-mouse model. Neurogenetics 13:169-79
    • (2012) Neurogenetics , vol.13 , pp. 169-179
    • Karle, K.N.1    Mockel, D.2    Reid, E.3    Schols, L.4
  • 68
    • 79954471977 scopus 로고    scopus 로고
    • Distinct pathogenic processes between Fig4-Deficient motor and sensory neurons
    • Katona I, Zhang X, Bai Y, Shy ME, Guo J, et al. 2011. Distinct pathogenic processes between Fig4-Deficient motor and sensory neurons. Eur. J. Neurosci. 33:1401-10
    • (2011) Eur. J. Neurosci , vol.33 , pp. 1401-1410
    • Katona, I.1    Zhang, X.2    Bai, Y.3    Shy, M.E.4    Guo, J.5
  • 69
    • 63049113263 scopus 로고    scopus 로고
    • Defining macropinocytosis
    • Kerr MC, Teasdale RD. 2009. Defining macropinocytosis. Traffic 10:364-71
    • (2009) Traffic , vol.10 , pp. 364-371
    • Kerr, M.C.1    Teasdale, R.D.2
  • 70
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran D, Kalmar B, Dick JR, Riddoch-Contreras J, Burnstock G, Greensmith L. 2004. Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat. Med. 10:402-5
    • (2004) Nat. Med , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 71
    • 84863230088 scopus 로고    scopus 로고
    • A Seoul-Fluor-based bioprobe for lipid droplets and its application in image-based high throughput screening
    • Kim E, Lee S, Park SB. 2012. A Seoul-Fluor-based bioprobe for lipid droplets and its application in image-based high throughput screening. Chem. Commun. 48:2331-33
    • (2012) Chem. Commun , vol.48 , pp. 2331-2333
    • Kim, E.1    Lee, S.2    Park, S.B.3
  • 72
    • 34447330452 scopus 로고    scopus 로고
    • COG8 deficiency causes new congenital disorder of glycosylation type IIh
    • Kranz C, Ng BG, Sun L, Sharma V, Eklund EA, et al. 2007. COG8 deficiency causes new congenital disorder of glycosylation type IIh. Hum. Mol. Genet. 16:731-41
    • (2007) Hum. Mol. Genet , vol.16 , pp. 731-741
    • Kranz, C.1    Ng, B.G.2    Sun, L.3    Sharma, V.4    Eklund, E.A.5
  • 73
    • 84863209627 scopus 로고    scopus 로고
    • Antibody-enabled small-molecule drug discovery
    • Lawson AD. 2012. Antibody-enabled small-molecule drug discovery. Nat. Rev. Drug Discov. 11:519-25
    • (2012) Nat. Rev. Drug Discov , vol.11 , pp. 519-525
    • Lawson, A.D.1
  • 75
    • 0242458219 scopus 로고    scopus 로고
    • A microscope-based screening platform for large-scale functional protein analysis in intact cells
    • Liebel U, Starkuviene V, Erfle H, Simpson JC, Poustka A, et al. 2003. A microscope-based screening platform for large-scale functional protein analysis in intact cells. FEBS Lett. 554:394-98
    • (2003) FEBS Lett , vol.554 , pp. 394-398
    • Liebel, U.1    Starkuviene, V.2    Erfle, H.3    Simpson, J.C.4    Poustka, A.5
  • 76
    • 77954898129 scopus 로고    scopus 로고
    • A genome-wide siRNA screen reveals multiple mTORC1 independent signaling pathways regulating autophagy under normal nutritional conditions
    • Lipinski MM, Hoffman G, Ng A, Zhou W, Py BF, et al. 2010. A genome-wide siRNA screen reveals multiple mTORC1 independent signaling pathways regulating autophagy under normal nutritional conditions. Dev. Cell 18:1041-52
    • (2010) Dev. Cell , vol.18 , pp. 1041-1052
    • Lipinski, M.M.1    Hoffman, G.2    Ng, A.3    Zhou, W.4    Py, B.F.5
  • 77
    • 84863881234 scopus 로고    scopus 로고
    • Selective protein degradation in cell signalling
    • Liu H, Urbe S, Clague MJ. 2012. Selective protein degradation in cell signalling. Semin. Cell Dev. Biol. 23:509-14
    • (2012) Semin. Cell Dev. Biol , vol.23 , pp. 509-514
    • Liu, H.1    Urbe, S.2    Clague, M.J.3
  • 78
    • 40649104165 scopus 로고    scopus 로고
    • Restoration of lysosomal pH in RPE cells from cultured human and ABCA4-/-mice: Pharmacologic approaches and functional recovery
    • Liu J, LuW, Reigada D, Nguyen J, Laties AM, Mitchell CH. 2008. Restoration of lysosomal pH in RPE cells from cultured human and ABCA4-/-mice: Pharmacologic approaches and functional recovery. Investig. Ophthalmol. Vis. Sci. 49:772-80
    • (2008) Investig. Ophthalmol. Vis. Sci , vol.49 , pp. 772-780
    • Liu, J.1    Lu, W.2    Reigada, D.3    Nguyen, J.4    Laties, A.M.5    Mitchell, C.H.6
  • 80
    • 0000623605 scopus 로고
    • Organic-Aciduria, decreased renal ammonia production, hydrophthalmos, and mental retardation; a clinical entity
    • Lowe CU, TerreyM, Mac LE. 1952. Organic-Aciduria, decreased renal ammonia production, hydrophthalmos, and mental retardation; a clinical entity. AMA Am. J. Dis. Child. 83:164-84
    • (1952) AMA Am J. Dis. Child , vol.83 , pp. 164-184
    • Lowe, C.U.1    Terrey, M.2    Mac, L.E.3
  • 81
    • 79951558394 scopus 로고    scopus 로고
    • Structural organization of the Golgi apparatus
    • Lowe M. 2011. Structural organization of the Golgi apparatus. Curr. Opin. Cell Biol. 23:85-93
    • (2011) Curr. Opin. Cell Biol , vol.23 , pp. 85-93
    • Lowe, M.1
  • 82
    • 69949119548 scopus 로고    scopus 로고
    • Identification and characterization of ambroxol as an enzyme enhancement agent for gaucher disease
    • Maegawa GH, Tropak MB, Buttner JD, Rigat BA, Fuller M, et al. 2009. Identification and characterization of ambroxol as an enzyme enhancement agent for Gaucher disease. J. Biol. Chem. 284:23502-16
    • (2009) J. Biol. Chem , vol.284 , pp. 23502-23516
    • Maegawa, G.H.1    Tropak, M.B.2    Buttner, J.D.3    Rigat, B.A.4    Fuller, M.5
  • 83
    • 1242274389 scopus 로고    scopus 로고
    • Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed β-Amyloid in neurons
    • Magrane J, Smith RC, Walsh K, Querfurth HW. 2004. Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed β-Amyloid in neurons. J. Neurosci. 24:1700-6
    • (2004) J. Neurosci , vol.24 , pp. 1700-1706
    • Magrane, J.1    Smith, R.C.2    Walsh, K.3    Querfurth, H.W.4
  • 84
    • 55549137036 scopus 로고    scopus 로고
    • Structural basis of cargo membrane protein discrimination by the human COPII coat machinery
    • Mancias JD, Goldberg J. 2008. Structural basis of cargo membrane protein discrimination by the human COPII coat machinery. EMBO J. 27:2918-28
    • (2008) EMBO J. , vol.27 , pp. 2918-2928
    • Mancias, J.D.1    Goldberg, J.2
  • 85
    • 84859901966 scopus 로고    scopus 로고
    • Genome-wide sirna screen reveals amino acid starvation-induced autophagy requires scocandwac
    • McKnight NC, Jefferies HB, Alemu EA, Saunders RE, Howell M, et al 2012 Genome-wide siRNA screen reveals amino acid starvation-induced autophagy requires EMBOJ. 31:1931-46
    • (2012) EMBOJ , vol.31 , pp. 1931-1946
    • McKnight, N.C.1    Jefferies, H.B.2    Alemu, E.A.3    Saunders, R.E.4    Howell, M.5
  • 86
    • 0038107403 scopus 로고    scopus 로고
    • Biochemical and functional characterization of Rab27a mutations occurring in Griscelli syndrome patients
    • MénaschéG, Feldmann J, Houdusse A, Desaymard C, Fischer A, et al. 2003. Biochemical and functional characterization of Rab27a mutations occurring in Griscelli syndrome patients. Blood 101:2736-42
    • (2003) Blood , vol.101 , pp. 2736-2742
    • Ménasché, G.1    Feldmann, J.2    Houdusse, A.3    Desaymard, C.4    Fischer, A.5
  • 87
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
    • Miller EA, Beilharz TH, Malkus PN, Lee MC, Hamamoto S, et al. 2003. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114:497-509
    • (2003) Cell , vol.114 , pp. 497-509
    • Miller, E.A.1    Beilharz, T.H.2    Malkus, P.N.3    Lee, M.C.4    Hamamoto, S.5
  • 88
    • 84862259443 scopus 로고    scopus 로고
    • Re'cog'nition at the golgi
    • Miller VJ, Ungar D. 2012. Re'COG'nition at the Golgi. Traffic 13:891-97
    • (2012) Traffic , vol.13 , pp. 891-897
    • Miller, V.J.1    Ungar, D.2
  • 89
    • 10744221460 scopus 로고    scopus 로고
    • ER-To-Golgi carriers arise through direct en bloc protrusion and multistage maturation of specialized ER exit domains
    • Mironov AA, Mironov AA Jr, Beznoussenko GV, Trucco A, Lupetti P, et al. 2003. ER-To-Golgi carriers arise through direct en bloc protrusion and multistage maturation of specialized ER exit domains. Dev. Cell 5:583-89
    • (2003) Dev. Cell , vol.5 , pp. 583-589
    • Mironov, A.A.1    Mironov Jr., A.A.2    Beznoussenko, G.V.3    Trucco, A.4    Lupetti, P.5
  • 90
    • 50249175120 scopus 로고    scopus 로고
    • Chemical and biological approaches synergize to ameliorate protein-folding diseases
    • Mu TW, Ong DS, Wang YJ, Balch WE, Yates JR III, et al. 2008. Chemical and biological approaches synergize to ameliorate protein-folding diseases. Cell 134:769-81
    • (2008) Cell , vol.134 , pp. 769-781
    • Mu, T.W.1    Ong, D.S.2    Wang, Y.J.3    Balch, W.E.4    Yates III, J.R.5
  • 91
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski PJ, Wacker JL. 2005. Modulation of neurodegeneration by molecular chaperones. Nat. Rev. Neurosci. 6:11-22
    • (2005) Nat. Rev. Neurosci , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 92
    • 0034704245 scopus 로고    scopus 로고
    • Identification of HE1 as the second gene of Niemann-Pick C disease
    • Naureckiene S, Sleat DE, Lackland H, Fensom A, Vanier MT, et al. 2000. Identification of HE1 as the second gene of Niemann-Pick C disease. Science 290:2298-301
    • (2000) Science , vol.290 , pp. 2298-2301
    • Naureckiene, S.1    Sleat, D.E.2    Lackland, H.3    Fensom, A.4    Vanier, M.T.5
  • 93
    • 73549085595 scopus 로고    scopus 로고
    • Increased expression of a-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis
    • Nemani VM, Lu W, Berge V, Nakamura K, Onoa B, et al. 2010. Increased expression of a-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron 65:66-79
    • (2010) Neuron , vol.65 , pp. 66-79
    • Nemani, V.M.1    Lu, W.2    Berge, V.3    Nakamura, K.4    Onoa, B.5
  • 94
    • 81355149193 scopus 로고    scopus 로고
    • Anderson's disease/chylomicron retention disease in a Japanese patient with uniparental disomy 7 and a normal SAR1B gene protein coding sequence
    • Okada T, Miyashita M, Fukuhara J, Sugitani M, Ueno T, et al. 2011. Anderson's disease/chylomicron retention disease in a Japanese patient with uniparental disomy 7 and a normal SAR1B gene protein coding sequence. Orphanet J. Rare Dis. 6:78
    • (2011) Orphanet J. Rare Dis , vol.6 , pp. 78
    • Okada, T.1    Miyashita, M.2    Fukuhara, J.3    Sugitani, M.4    Ueno, T.5
  • 95
    • 82555187810 scopus 로고    scopus 로고
    • Image-based genome-wide siRNA screen identifies selective autophagy factors
    • Orvedahl A, Sumpter R Jr, Xiao G, Ng A, Zou Z, et al. 2011. Image-based genome-wide siRNA screen identifies selective autophagy factors. Nature 480:113-17
    • (2011) Nature , vol.480 , pp. 113-117
    • Orvedahl, A.1    Sumpter Jr., R.2    Xiao, G.3    Ng, A.4    Zou, Z.5
  • 96
    • 55849115677 scopus 로고    scopus 로고
    • Dyggve-melchior-clausen syndrome: Chondrodysplasia resulting from defects in intracellular vesicle traffic
    • Osipovich AB, Jennings JL, Lin Q, Link AJ, Ruley HE. 2008. Dyggve-Melchior-Clausen syndrome: Chondrodysplasia resulting from defects in intracellular vesicle traffic. Proc. Natl. Acad. Sci. USA 105:16171-76
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16171-16176
    • Osipovich, A.B.1    Jennings, J.L.2    Lin, Q.3    Link, A.J.4    Ruley, H.E.5
  • 97
    • 77449098166 scopus 로고    scopus 로고
    • Treating lysosomal storage diseases with pharmacological chaperones: From concept to clinics
    • Parenti G. 2009. Treating lysosomal storage diseases with pharmacological chaperones: From concept to clinics. EMBO Mol. Med. 1:268-79
    • (2009) EMBO Mol. Med , vol.1 , pp. 268-279
    • Parenti, G.1
  • 98
    • 70350690698 scopus 로고    scopus 로고
    • Deficiency in COG5 causes a moderate form of congenital disorders of glycosylation
    • Paesold-Burda P, Maag C, Troxler H, Foulquier F, Kleinert P, et al. 2009. Deficiency in COG5 causes a moderate form of congenital disorders of glycosylation. Hum. Mol. Genet. 18:4350-56
    • (2009) Hum. Mol. Genet , vol.18 , pp. 4350-4356
    • Paesold-Burda, P.1    Maag, C.2    Troxler, H.3    Foulquier, F.4    Kleinert, P.5
  • 99
    • 27844491492 scopus 로고    scopus 로고
    • Current and emerging therapies for the lysosomal storage disorders
    • Pastores GM, Barnett NL. 2005. Current and emerging therapies for the lysosomal storage disorders. Expert Opin. Emerg. Drugs 10:891-902
    • (2005) Expert Opin. Emerg. Drugs , vol.10 , pp. 891-902
    • Pastores, G.M.1    Barnett, N.L.2
  • 100
    • 34547753513 scopus 로고    scopus 로고
    • Miglustat for treatment ofNiemann-Pick C disease: A randomised controlled study
    • Patterson MC, Vecchio D, PradyH, Abel L, Wraith JE. 2007. Miglustat for treatment ofNiemann-Pick C disease: A randomised controlled study. Lancet Neurol. 6:765-72
    • (2007) Lancet Neurol , vol.6 , pp. 765-772
    • Patterson, M.C.1    Vecchio, D.2    Prady, H.3    Abel, L.4    Wraith, J.E.5
  • 101
    • 24644464284 scopus 로고    scopus 로고
    • Small-molecule correctors of defective-F508-CFTR cellular processing identified by high-Throughput screening
    • Pedemonte N, Lukacs GL, Du K, Caci E, Zegarra-Moran O, et al. 2005. Small-molecule correctors of defective-F508-CFTR cellular processing identified by high-Throughput screening. J. Clin. Investig. 115:2564-71
    • (2005) J. Clin. Investig , vol.115 , pp. 2564-2571
    • Pedemonte, N.1    Lukacs, G.L.2    Du, K.3    Caci, E.4    Zegarra-Moran, O.5
  • 102
    • 21844440569 scopus 로고    scopus 로고
    • Genome-wide analysis of human kinases in clathrin-And caveolae/raft-mediated endocytosis
    • Pelkmans L, Fava E, GrabnerH, HannusM, Habermann B, et al. 2005. Genome-wide analysis of human kinases in clathrin-And caveolae/raft-mediated endocytosis. Nature 436:78-86
    • (2005) Nature , vol.436 , pp. 78-86
    • Pelkmans, L.1    Fava, E.2    Grabner, H.3    Hannus, M.4    Habermann, B.5
  • 103
    • 0031826012 scopus 로고    scopus 로고
    • Three distinct steps in transport of vesicular stomatitis virus glycoprotein from the ER to the cell surface in vivo with differential sensitivities to GTPGTP
    • Pepperkok R, LoweM, Burke B, Kreis TE. 1998. Three distinct steps in transport of vesicular stomatitis virus glycoprotein from the ER to the cell surface in vivo with differential sensitivities to GTPGTP? S. J. Cell Sci. 111:1877-88
    • (1998) S. J. Cell Sci , vol.111 , pp. 1877-1888
    • Pepperkok, R.1    Lowe, M.2    Burke, B.3    Kreis, T.E.4
  • 104
    • 0027220591 scopus 로고
    • Β-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo
    • Pepperkok R, Scheel J, Horstmann H, Hauri HP, Griffiths G, Kreis TE 1993. β-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell 74:71-82
    • (1993) Cell , vol.74 , pp. 71-82
    • Pepperkok, R.1    Scheel, J.2    Horstmann, H.3    Hauri, H.P.4    Griffiths, G.5    Kreis, T.E.6
  • 105
    • 1242353099 scopus 로고    scopus 로고
    • A screen for drugs that protect against the cytotoxicity of polyglutamine-expanded androgen receptor
    • Piccioni F, Roman BR, Fischbeck KH, Taylor JP. 2004. A screen for drugs that protect against the cytotoxicity of polyglutamine-expanded androgen receptor. Hum. Mol. Genet. 13:437-46
    • (2004) Hum. Mol. Genet , vol.13 , pp. 437-446
    • Piccioni, F.1    Roman, B.R.2    Fischbeck, K.H.3    Taylor, J.P.4
  • 106
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • Picollo A, Pusch M. 2005. Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature 436:420-23
    • (2005) Nature , vol.436 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 107
    • 0242657586 scopus 로고    scopus 로고
    • A rapid cellular FRET assay of polyglutamine aggregation identifies a novel inhibitor
    • Pollitt SK, Pallos J, Shao J, Desai UA, Ma AA, et al. 2003. A rapid cellular FRET assay of polyglutamine aggregation identifies a novel inhibitor. Neuron 40:685-94
    • (2003) Neuron , vol.40 , pp. 685-694
    • Pollitt, S.K.1    Pallos, J.2    Shao, J.3    Desai, U.A.4    Ma, A.A.5
  • 108
    • 67349206148 scopus 로고    scopus 로고
    • The pharmacological chaperone N-butyldeoxynojirimycin enhances enzyme replacement therapy in Pompe disease fibroblasts
    • Porto C, Cardone M, Fontana F, Rossi B, Tuzzi MR, et al. 2009. The pharmacological chaperone N-butyldeoxynojirimycin enhances enzyme replacement therapy in Pompe disease fibroblasts. Mol. Ther. 17:964-71
    • (2009) Mol. Ther , vol.17 , pp. 964-971
    • Porto, C.1    Cardone, M.2    Fontana, F.3    Rossi, B.4    Tuzzi, M.R.5
  • 109
    • 48649101763 scopus 로고    scopus 로고
    • A traffic-Activated Golgibased signalling circuit coordinates the secretory pathway
    • Pulvirenti T, Giannotta M, Capestrano M, Capitani M, Pisanu A, et al. 2008. A traffic-Activated Golgibased signalling circuit coordinates the secretory pathway. Nat. Cell Biol. 10:912-22
    • (2008) Nat. Cell Biol , vol.10 , pp. 912-922
    • Pulvirenti, T.1    Giannotta, M.2    Capestrano, M.3    Capitani, M.4    Pisanu, A.5
  • 111
    • 78649704325 scopus 로고    scopus 로고
    • Autophagy and metabolism
    • Rabinowitz JD, White E. 2010. Autophagy and metabolism. Science 330:1344-48
    • (2010) Science , vol.330 , pp. 1344-1348
    • Rabinowitz, J.D.1    White, E.2
  • 112
    • 80455162465 scopus 로고    scopus 로고
    • A CFTR potentiator in patients with cystic fibrosis and the G551D mutation
    • Ramsey BW, Davies J, McElvaney NG, Tullis E, Bell SC, et al. 2011. A CFTR potentiator in patients with cystic fibrosis and the G551D mutation. N. Engl. J. Med. 365:1663-72
    • (2011) N. Engl. J. Med , vol.365 , pp. 1663-1672
    • Ramsey, B.W.1    Davies, J.2    McElvaney, N.G.3    Tullis, E.4    Bell, S.C.5
  • 113
    • 79952117266 scopus 로고    scopus 로고
    • Loss of SNAP29 impairs endocytic recycling and cell motility
    • Rapaport D, Lugassy Y, Sprecher E, Horowitz M. 2010. Loss of SNAP29 impairs endocytic recycling and cell motility. PLoS ONE 5:e9759
    • (2010) PLoS ONE , vol.5
    • Rapaport, D.1    Lugassy, Y.2    Sprecher, E.3    Horowitz, M.4
  • 115
    • 77951234323 scopus 로고    scopus 로고
    • Chemical inducers of autophagy that enhance the clearance of mutant proteins in neurodegenerative diseases
    • Renna M, Jimenez-Sanchez M, Sarkar S, Rubinsztein DC. 2010. Chemical inducers of autophagy that enhance the clearance of mutant proteins in neurodegenerative diseases. J. Biol. Chem. 285:11061-67
    • (2010) J. Biol. Chem , vol.285 , pp. 11061-11067
    • Renna, M.1    Jimenez-Sanchez, M.2    Sarkar, S.3    Rubinsztein, D.C.4
  • 116
    • 84865082850 scopus 로고    scopus 로고
    • Spg20-/-mice reveal multimodal functions for Troyer syndrome protein spartin in lipid droplet maintenance, cytokinesis and BMP signaling
    • Renvoise B, Stadler J, Singh R, Bakowska JC, Blackstone C. 2012. Spg20-/-mice reveal multimodal functions for Troyer syndrome protein spartin in lipid droplet maintenance, cytokinesis and BMP signaling. Hum. Mol. Genet. 21:3604-18
    • (2012) Hum. Mol. Genet , vol.21 , pp. 3604-3618
    • Renvoise, B.1    Stadler, J.2    Singh, R.3    Bakowska, J.C.4    Blackstone, C.5
  • 117
    • 68749117665 scopus 로고    scopus 로고
    • Golgi function and dysfunction in the first COG4-Deficient CDG type II patient
    • Reynders E, Foulquier F, Leão Teles E, Quelhas D, Morelle W, et al. 2009. Golgi function and dysfunction in the first COG4-Deficient CDG type II patient. Hum. Mol. Genet. 18:3244-56
    • (2009) Hum. Mol. Genet , vol.18 , pp. 3244-3256
    • Reynders, E.1    Foulquier, F.2    Leão Teles, E.3    Quelhas, D.4    Morelle, W.5
  • 118
    • 12944284535 scopus 로고    scopus 로고
    • Melanocytes derived from patients with Hermansky-Pudlak Syndrome types 1 2, and 3 have distinct defects in cargo trafficking
    • Richmond B, HuizingM, Knapp J, Koshoffer A, Zhao Y, et al. 2005. Melanocytes derived from patients with Hermansky-Pudlak Syndrome types 1, 2, and 3 have distinct defects in cargo trafficking. J. Investig. Dermatol. 124:420-27
    • (2005) J. Investig. Dermatol , vol.124 , pp. 420-427
    • Richmond, B.1    HuizingM Knapp, J.2    Koshoffer, A.3    Zhao, Y.4
  • 119
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink J, Ghigo E, Kalaidzidis Y, Zerial M. 2005. Rab conversion as a mechanism of progression from early to late endosomes. Cell 122:735-49
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 120
    • 77950620209 scopus 로고    scopus 로고
    • Mistargeting of SH3TC2 away from the recycling endosome causes Charcot-Marie-Tooth disease type 4C
    • Roberts RC, Peden AA, Buss F, Bright NA, Latouche M, et al. 2010. Mistargeting of SH3TC2 away from the recycling endosome causes Charcot-Marie-Tooth disease type 4C. Hum. Mol. Genet. 19:1009-18
    • (2010) Hum. Mol. Genet , vol.19 , pp. 1009-1018
    • Roberts, R.C.1    Peden, A.A.2    Buss, F.3    Bright, N.A.4    Latouche, M.5
  • 121
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of theHsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe SM, Prodromou C, O'BrienR, Ladbury JE, PiperPW, PearlLH. 1999. Structural basis for inhibition of theHsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem. 42:260-66
    • (1999) J. Med. Chem , vol.42 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 122
    • 73949107514 scopus 로고    scopus 로고
    • Chemical screen to reduce sterol accumulation in Niemann-Pick C disease cells identifies novel lysosomal acid lipase inhibitors
    • Rosenbaum AI, Rujoi M, Huang AY, Du H, Grabowski GA, Maxfield FR. 2009. Chemical screen to reduce sterol accumulation in Niemann-Pick C disease cells identifies novel lysosomal acid lipase inhibitors. Biochim. Biophys. Acta 1791:1155-65
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 1155-1165
    • Rosenbaum, A.I.1    Rujoi, M.2    Huang, A.Y.3    Du, H.4    Grabowski, G.A.5    Maxfield, F.R.6
  • 123
    • 77958494831 scopus 로고    scopus 로고
    • Cholesterol pathways affected by small molecules that decrease sterol levels in niemann-pick type c mutant cells
    • RujoiM, Pipalia NH, Maxfield FR. 2010. Cholesterol pathways affected by small molecules that decrease sterol levels in Niemann-Pick type C mutant cells. PLoS ONE 5:e12788
    • (2010) PLoS ONE , vol.5
    • RujoiM Pipalia, N.H.1    Maxfield, F.R.2
  • 124
    • 0037214462 scopus 로고    scopus 로고
    • Mouse hippocampal organotypic tissue cultures exposed to in vitro ischemia show selective and delayed ca1 damage that is aggravated by glucose
    • Rytter A, Cronberg T, Asztely F, Nemali S, Wieloch T. 2003. Mouse hippocampal organotypic tissue cultures exposed to in vitro ischemia show selective and delayed CA1 damage that is aggravated by glucose. J. Cereb. Blood Flow Metab. 23:23-33
    • (2003) J. Cereb. Blood Flow Metab , vol.23 , pp. 23-33
    • Rytter, A.1    Cronberg, T.2    Asztely, F.3    Nemali, S.4    Wieloch, T.5
  • 125
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomalmembrane proteins: Trafficking meets function
    • Saftig P, Klumperman J. 2009. Lysosome biogenesis and lysosomalmembrane proteins: Trafficking meets function. Nat. Rev. Mol. Cell Biol. 10:623-35
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 126
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mtorindependent autophagy enhancer, accelerates the clearance of mutant huntingtin and a-synuclein
    • Sarkar S, Davies JE, Huang Z, Tunnacliffe A, Rubinsztein DC. 2007. Trehalose, a novel mTORindependent autophagy enhancer, accelerates the clearance of mutant huntingtin and a-synuclein. J. Biol. Chem. 282:5641-52
    • (2007) J. Biol. Chem , vol.282 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 128
    • 34248994604 scopus 로고    scopus 로고
    • Small molecules enhance autophagy and reduce toxicity in Huntington's disease models
    • Sarkar S, PerlsteinEO, Imarisio S, Pineau S, Cordenier A, et al. 2007. Small molecules enhance autophagy and reduce toxicity in Huntington's disease models. Nat. Chem. Biol. 3:331-38
    • (2007) Nat. Chem. Biol , vol.3 , pp. 331-338
    • Sarkar, S.1    Perlstein, E.O.2    Imarisio, S.3    Pineau, S.4    Cordenier, A.5
  • 129
    • 49749096430 scopus 로고    scopus 로고
    • Small molecule enhancers of autophagy for neurodegenerative diseases
    • Sarkar S, RubinszteinDC. 2008. Small molecule enhancers of autophagy for neurodegenerative diseases. Mol. Biosyst. 4:895-901
    • (2008) Mol. Biosyst , vol.4 , pp. 895-901
    • Sarkar, S.1    Rubinsztein, D.C.2
  • 130
    • 65649136884 scopus 로고    scopus 로고
    • The structure of Atg4B-LC3 complex reveals themechanism ofLC3processing and delipidation during autophagy
    • Satoo K, Noda NN, Kumeta H, Fujioka Y, Mizushima N, et al 2009. The structure of Atg4B-LC3 complex reveals themechanism ofLC3processing and delipidation during autophagy.EMBOJ. 28:1341-50
    • (2009) EMBOJ , vol.28 , pp. 1341-1350
    • Satoo, K.1    Noda, N.N.2    Kumeta, H.3    Fujioka, Y.4    Mizushima, N.5
  • 131
    • 28044444522 scopus 로고    scopus 로고
    • The small gtpase rab7 controls the endosomal trafficking and neuritogenic signaling of the nerve growth factor receptor trka
    • Saxena S, Bucci C, Weis J, Kruttgen A. 2005. The small GTPase Rab7 controls the endosomal trafficking and neuritogenic signaling of the nerve growth factor receptor TrkA. J. Neurosci. 25:10930-40
    • (2005) J. Neurosci , vol.25 , pp. 10930-10940
    • Saxena, S.1    Bucci, C.2    Weis, J.3    Kruttgen, A.4
  • 134
    • 70249145840 scopus 로고    scopus 로고
    • Neurodegeneration in niemann-pick type c disease and huntington's disease: Impact of defects in membrane trafficking
    • Schweitzer JK, Krivda JP, D'souza-Schorey C. 2009. Neurodegeneration in Niemann-Pick Type C disease and Huntington's disease: Impact of defects in membrane trafficking. Curr. Drug Targets 10:653-65
    • (2009) Curr. Drug Targets , vol.10 , pp. 653-665
    • Schweitzer, J.K.1    Krivda, J.P.2    D'souza-Schorey, C.3
  • 136
    • 34047171306 scopus 로고    scopus 로고
    • An RNAi screening platform to identify secretion machinery in mammalian cells
    • Simpson JC, Cetin C, ErfleH, Joggerst B, LiebelU, et al. 2007. An RNAi screening platform to identify secretion machinery in mammalian cells. J. Biotechnol. 129:352-65
    • (2007) J. Biotechnol , vol.129 , pp. 352-365
    • Simpson, J.C.1    Cetin, C.2    Erfle, H.3    Joggerst, B.4    Liebel, U.5
  • 137
    • 84863205689 scopus 로고    scopus 로고
    • Genome-wide RNAi screening identifies human proteins with a regulatory function in the early secretory pathway
    • Simpson JC, Joggerst B, Laketa V, Verissimo F, Cetin C, et al. 2012. Genome-wide RNAi screening identifies human proteins with a regulatory function in the early secretory pathway. Nat. Cell Biol. 14:764-74
    • (2012) Nat. Cell Biol , vol.14 , pp. 764-774
    • Simpson, J.C.1    Joggerst, B.2    Laketa, V.3    Verissimo, F.4    Cetin, C.5
  • 138
    • 23044471011 scopus 로고    scopus 로고
    • Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia
    • SkibinskiG, Parkinson NJ, Brown JM, Chakrabarti L, Lloyd SL, et al. 2005. Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia. Nat. Genet. 37:806-8
    • (2005) Nat. Genet , vol.37 , pp. 806-808
    • Skibinski, G.1    Parkinson, N.J.2    Brown, J.M.3    Chakrabarti, L.4    Lloyd, S.L.5
  • 139
    • 74849098404 scopus 로고    scopus 로고
    • Lethal skeletal dysplasia in mice and humans lacking the golgin GMAP-210
    • Smits P, Bolton AD, Funari V, Hong M, Boyden ED, et al. 2010. Lethal skeletal dysplasia in mice and humans lacking the golgin GMAP-210. N. Engl. J. Med. 362:206-16
    • (2010) N. Engl. J. Med , vol.362 , pp. 206-216
    • Smits, P.1    Bolton, A.D.2    Funari, V.3    Hong, M.4    Boyden, E.D.5
  • 140
    • 78650056095 scopus 로고    scopus 로고
    • Targeted disruption of the Mast syndrome gene SPG21 in mice impairs hind limb function and alters axon branching in cultured cortical neurons
    • Soderblom C, Stadler J, Jupille H, Blackstone C, Shupliakov O, Hanna MC. 2010. Targeted disruption of the Mast syndrome gene SPG21 in mice impairs hind limb function and alters axon branching in cultured cortical neurons. Neurogenetics 11:369-78
    • (2010) Neurogenetics , vol.11 , pp. 369-378
    • Soderblom, C.1    Stadler, J.2    Jupille, H.3    Blackstone, C.4    Shupliakov, O.5    Hanna, M.C.6
  • 141
    • 67949093139 scopus 로고    scopus 로고
    • On the fate of early endosomes
    • Spang A. 2009. On the fate of early endosomes. Biol. Chem. 390:753-59
    • (2009) Biol. Chem , vol.390 , pp. 753-759
    • Spang, A.1
  • 142
    • 40949159198 scopus 로고    scopus 로고
    • Building ?-secretase: The bits and pieces
    • Spasic D, AnnaertW. 2008. Building ?-secretase: The bits and pieces. J. Cell Sci. 121:413-20
    • (2008) J. Cell Sci , vol.121 , pp. 413-420
    • Spasic, D.1    Annaert, W.2
  • 143
    • 6344222240 scopus 로고    scopus 로고
    • High-content screeningmicroscopy identifies novel proteins with a putative role in secretory membrane traffic
    • StarkuvieneV, LiebelU, Simpson JC, ErfleH, PoustkaA, et al. 2004. High-content screeningmicroscopy identifies novel proteins with a putative role in secretory membrane traffic. Genome Res. 14:1948-56
    • (2004) Genome Res , vol.14 , pp. 1948-1956
    • Starkuviene, V.1    Liebel, U.2    Simpson, J.C.3    Erfle, H.4    Poustka, A.5
  • 144
    • 67349135343 scopus 로고    scopus 로고
    • ESCRT proteins in physiology and disease
    • Stuffers S, Brech A, Stenmark H. 2009. ESCRT proteins in physiology and disease. Exp. Cell Res. 315:1619-26
    • (2009) Exp. Cell Res , vol.315 , pp. 1619-1626
    • Stuffers, S.1    Brech, A.2    Stenmark, H.3
  • 146
    • 78650463149 scopus 로고    scopus 로고
    • Optimization of a yellow fluorescent proteinbased iodide influx high-Throughput screening assay for cystic fibrosis transmembrane conductance regulator (cftr) modulators
    • Sui J, Cotard S, Andersen J, Zhu P, Staunton J, et al. 2010. Optimization of a yellow fluorescent proteinbased iodide influx high-Throughput screening assay for cystic fibrosis transmembrane conductance regulator (CFTR) modulators. Assay Drug Dev. Technol. 8:656-68
    • (2010) Assay Drug Dev. Technol , vol.8 , pp. 656-668
    • Sui, J.1    Cotard, S.2    Andersen, J.3    Zhu, P.4    Staunton, J.5
  • 149
    • 54249158324 scopus 로고    scopus 로고
    • Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
    • Tai HC, Schuman EM. 2008. Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nat. Rev. Neurosci. 9:826-38
    • (2008) Nat. Rev. Neurosci , vol.9 , pp. 826-838
    • Tai, H.C.1    Schuman, E.M.2
  • 150
    • 1642633757 scopus 로고    scopus 로고
    • Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease
    • Tanaka M, MachidaY, Niu S, IkedaT, JanaNR, et al. 2004. Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease. Nat. Med. 10:148-54
    • (2004) Nat. Med , vol.10 , pp. 148-154
    • Tanaka, M.1    Machida, Y.2    Niu, S.3    Ikeda, T.4    Jana, N.R.5
  • 151
    • 57649221135 scopus 로고    scopus 로고
    • Amyloid precursor protein trafficking, processing, and function
    • Thinakaran G, Koo EH. 2008. Amyloid precursor protein trafficking, processing, and function. J. Biol. Chem. 283:29615-19
    • (2008) J. Biol. Chem , vol.283 , pp. 29615-29619
    • Thinakaran, G.1    Koo, E.H.2
  • 152
    • 84856112882 scopus 로고    scopus 로고
    • Diseases in a dish: Modeling human genetic disorders using induced pluripotent cells
    • TiscorniaG, Vivas EL, Izpisua Belmonte JC. 2011. Diseases in a dish: Modeling human genetic disorders using induced pluripotent cells. Nat. Med. 17:1570-76
    • (2011) Nat. Med , vol.17 , pp. 1570-1576
    • Tiscornia, G.1    Vivas, E.L.2    Izpisua Belmonte, J.C.3
  • 153
  • 154
    • 0031945551 scopus 로고    scopus 로고
    • A novel gene encoding an integral membrane protein is mutated in nephropathic cystinosis
    • Town M, Jean G, Cherqui S, Attard M, Forestier L, et al. 1998. A novel gene encoding an integral membrane protein is mutated in nephropathic cystinosis. Nat. Genet. 18:319-24
    • (1998) Nat. Genet , vol.18 , pp. 319-324
    • Town, M.1    Jean, G.2    Cherqui, S.3    Attard, M.4    Forestier, L.5
  • 155
    • 70349579493 scopus 로고    scopus 로고
    • The hereditary spastic paraplegia proteins NIPA1, spastin and spartin are inhibitors of mammalian BMP signalling
    • TsangHT, Edwards TL, Wang X, Connell JW, Davies RJ, et al. 2009. The hereditary spastic paraplegia proteins NIPA1, spastin and spartin are inhibitors of mammalian BMP signalling. Hum. Mol. Genet. 18:3805-21
    • (2009) Hum. Mol. Genet , vol.18 , pp. 3805-3821
    • Tsang, H.T.1    Edwards, T.L.2    Wang, X.3    Connell, J.W.4    Davies, R.J.5
  • 156
    • 43449099127 scopus 로고    scopus 로고
    • The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors
    • Tsuda H, Han SM, Yang Y, Tong C, Lin YQ, et al. 2008. The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors. Cell 133:963-77
    • (2008) Cell , vol.133 , pp. 963-977
    • Tsuda, H.1    Han, S.M.2    Yang, Y.3    Tong, C.4    Lin, Y.Q.5
  • 157
    • 77953583994 scopus 로고    scopus 로고
    • Disruption of endocytic trafficking in frontotemporal dementia with CHMP2B mutations
    • Urwin H, Authier A, Nielsen JE, Metcalf D, Powell C, et al. 2010. Disruption of endocytic trafficking in frontotemporal dementia with CHMP2B mutations. Hum. Mol. Genet. 19:2228-38
    • (2010) Hum. Mol. Genet , vol.19 , pp. 2228-2238
    • Urwin, H.1    Authier, A.2    Nielsen, J.E.3    Metcalf, D.4    Powell, C.5
  • 158
    • 51749094612 scopus 로고    scopus 로고
    • Knockdown of myosin Va isoforms by RNAi as a tool to block melanosome transport in primary human melanocytes
    • Van Gele M, Geusens B, Schmitt AM, Aguilar L, Lambert J. 2008. Knockdown of myosin Va isoforms by RNAi as a tool to block melanosome transport in primary human melanocytes. J. Investig. Dermatol. 128:2474-84
    • (2008) J. Investig. Dermatol , vol.128 , pp. 2474-2484
    • Van Gele, M.1    Geusens, B.2    Schmitt, A.M.3    Aguilar, L.4    Lambert, J.5
  • 159
  • 161
    • 84866759304 scopus 로고    scopus 로고
    • Sedlin controls the ER export of procollagen by regulating the Sar1 cycle
    • Venditti R, Scanu T, Santoro M, Di Tullio G, Spaar A, et al. 2012. Sedlin controls the ER export of procollagen by regulating the Sar1 cycle. Science 337:1668-72
    • (2012) Science , vol.337 , pp. 1668-1672
    • Venditti, R.1    Scanu, T.2    Santoro, M.3    Di Tullio, G.4    Spaar, A.5
  • 162
    • 53549122990 scopus 로고    scopus 로고
    • Function and dysfunction of the PI system in membrane trafficking
    • Vicinanza M, D'Angelo G, Di Campli A, De Matteis MA. 2008. Function and dysfunction of the PI system in membrane trafficking. EMBO J. 27:2457-70
    • (2008) EMBO J. , vol.27 , pp. 2457-2470
    • Vicinanza, M.1    D'Angelo, G.2    Di Campli, A.3    De Matteis, M.A.4
  • 163
    • 83555163852 scopus 로고    scopus 로고
    • 2011.OCRLcontrols trafficking through early endosomes via PtdIns4,5P2-Dependent regulation of endosomal actin
    • Vicinanza M, Di Campli A, Polishchuk E, Santoro M, Di Tullio G, et al. 2011.OCRLcontrols trafficking through early endosomes via PtdIns4,5P2-Dependent regulation of endosomal actin. EMBO J. 30:4970-85
    • EMBO J. , vol.30 , pp. 4970-4985
    • Vicinanza, M.1    Di Campli, A.2    Polishchuk, E.3    Santoro, M.4    Di Tullio, G.5
  • 164
    • 54549123514 scopus 로고    scopus 로고
    • Myosin Vb mobilizes recycling endosomes and AMPA receptors for postsynaptic plasticity
    • Wang Z, Edwards JG, Riley N, Provance DWJr, Karcher R, et al. 2008. Myosin Vb mobilizes recycling endosomes and AMPA receptors for postsynaptic plasticity. Cell 135:535-48
    • (2008) Cell , vol.135 , pp. 535-548
    • Wang, Z.1    Edwards, J.G.2    Riley, N.3    Provance Jr., D.W.4    Karcher, R.5
  • 165
    • 20544471158 scopus 로고    scopus 로고
    • ER-To-Golgi transport: Form and formation of vesicular and tubular carriers
    • Watson P, Stephens DJ. 2005. ER-To-Golgi transport: Form and formation of vesicular and tubular carriers. Biochim. Biophys. Acta 1744:304-15
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 304-315
    • Watson, P.1    Stephens, D.J.2
  • 166
    • 75049083932 scopus 로고    scopus 로고
    • A genome-wideRNAinterference screen identifies two novel components of themetazoan secretory pathway
    • Wendler F, Gillingham AK, Sinka R, Rosa-FerreiraC, Gordon DE, et al. 2010. A genome-wideRNAinterference screen identifies two novel components of themetazoan secretory pathway. EMBO J. 29:304-14
    • (2010) EMBO J. , vol.29 , pp. 304-314
    • Wendler, F.1    Gillingham, A.K.2    Sinka, R.3    Rosa-Ferreira, C.4    Gordon, D.E.5
  • 167
    • 42249106042 scopus 로고    scopus 로고
    • Novel targets for Huntington's disease in an mTOR-independent autophagy pathway
    • Williams A, Sarkar S, Cuddon P, Ttofi EK, Saiki S, et al. 2008. Novel targets for Huntington's disease in an mTOR-independent autophagy pathway. Nat. Chem. Biol. 4:295-305
    • (2008) Nat. Chem. Biol , vol.4 , pp. 295-305
    • Williams, A.1    Sarkar, S.2    Cuddon, P.3    Ttofi, E.K.4    Saiki, S.5
  • 169
    • 79960844736 scopus 로고    scopus 로고
    • A pharmacogenetic approach to identify mutant forms of a-galactosidase A that respond to a pharmacological chaperone for Fabry disease
    • Wu X, Katz E, Della Valle MC, Mascioli K, Flanagan JJ, et al. 2011. A pharmacogenetic approach to identify mutant forms of a-galactosidase A that respond to a pharmacological chaperone for Fabry disease. Hum. Mutat. 32:965-77
    • (2011) Hum. Mutat , vol.32 , pp. 965-977
    • Wu, X.1    Katz, E.2    Della Valle, M.C.3    Mascioli, K.4    Flanagan, J.J.5
  • 170
    • 84863519526 scopus 로고    scopus 로고
    • Structural insights into Atg10-mediated formation of the autophagy-essential Atg12-Atg5 conjugate
    • Yamaguchi M, Noda NN, Yamamoto H, Shima T, Kumeta H, et al. 2012. Structural insights into Atg10-mediated formation of the autophagy-essential Atg12-Atg5 conjugate. Structure 20:1244-54
    • (2012) Structure , vol.20 , pp. 1244-1254
    • Yamaguchi, M.1    Noda, N.N.2    Yamamoto, H.3    Shima, T.4    Kumeta, H.5
  • 171
    • 0034471359 scopus 로고    scopus 로고
    • Defective organellar membrane protein trafficking in Ap3b1-Deficient cells
    • Yang W, Li C, Ward DM, Kaplan J, Mansour SL. 2000. Defective organellar membrane protein trafficking in Ap3b1-Deficient cells. J. Cell Sci. 113:4077-86
    • (2000) J. Cell Sci , vol.113 , pp. 4077-4086
    • Yang, W.1    Li, C.2    Ward, D.M.3    Kaplan, J.4    Mansour, S.L.5
  • 173
    • 77951975169 scopus 로고    scopus 로고
    • High content screening: Seeing is believing
    • Zanella F, Lorens JB, Link W. 2010. High content screening: Seeing is believing. Trends Biotechnol. 28:237-45
    • (2010) Trends Biotechnol , vol.28 , pp. 237-245
    • Zanella, F.1    Lorens, J.B.2    Link, W.3
  • 174
    • 32244442749 scopus 로고    scopus 로고
    • Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking
    • Zeng X, Overmeyer JH, Maltese WA. 2006. Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking. J. Cell Sci. 119:259-70
    • (2006) J. Cell Sci , vol.119 , pp. 259-270
    • Zeng, X.1    Overmeyer, J.H.2    Maltese, W.A.3
  • 175
    • 84865763232 scopus 로고    scopus 로고
    • Brefeldin A-inhibited guanine exchange factor 2 regulates filamin A phosphorylation and neuronal migration
    • Zhang J, Neal J, Lian G, Shi B, Ferland RJ, Sheen V. 2012. Brefeldin A-inhibited guanine exchange factor 2 regulates filamin A phosphorylation and neuronal migration. J. Neurosci. 32:12619-29
    • (2012) J. Neurosci , vol.32 , pp. 12619-12629
    • Zhang, J.1    Neal, J.2    Lian, G.3    Shi, B.4    Ferland, R.J.5    Sheen, V.6
  • 176
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang JH, Chung TDY, Oldenburg KR. 1999. A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J. Biomol. Screen. 4:67-73
    • (1999) J. Biomol. Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.Y.2    Oldenburg, K.R.3
  • 177
    • 37649024076 scopus 로고    scopus 로고
    • Small molecule regulators of autophagy identified by an image-based high-Throughput screen
    • Zhang L, Yu J, Pan H, Hu P, Hao Y, et al. 2007. Small molecule regulators of autophagy identified by an image-based high-Throughput screen. Proc. Natl. Acad. Sci. USA 104:19023-28
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19023-19028
    • Zhang, L.1    Yu, J.2    Pan, H.3    Hu, P.4    Hao, Y.5
  • 178
    • 0018942213 scopus 로고
    • Mutants of vesicular stomatitis virus blocked at different stages in maturation of the viral glycoprotein
    • Zilberstein A, Snider MD, Porter M, Lodish HF. 1980. Mutants of vesicular stomatitis virus blocked at different stages in maturation of the viral glycoprotein. Cell 21:417-27
    • (1980) Cell , vol.21 , pp. 417-427
    • Zilberstein, A.1    Snider, M.D.2    Porter, M.3    Lodish, H.F.4
  • 179
    • 84871994423 scopus 로고    scopus 로고
    • Pilot study using ambroxol as a pharmacological chaperone in type 1 Gaucher disease
    • Zimran A, Altarescu G, Elstein D. 2013. Pilot study using ambroxol as a pharmacological chaperone in type 1 Gaucher disease. Blood Cells Mol. Dis. 50:134-37
    • (2013) Blood Cells Mol. Dis , vol.50 , pp. 134-137
    • Zimran, A.1    Altarescu, G.2    Elstein, D.3
  • 180
    • 0035919701 scopus 로고    scopus 로고
    • Loss of huntingtin-mediated bdnf gene transcription in huntington's disease
    • ZuccatoC, Ciammola A, RigamontiD, Leavitt BR, GoffredoD, et al. 2001. Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease. Science 293:493-98
    • (2001) Science , vol.293 , pp. 493-498
    • Zuccato, C.1    Ciammola, A.2    Rigamonti, D.3    Leavitt, B.R.4    Goffredo, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.