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Volumn 93, Issue 4, 2017, Pages 737-746

The Complicated Relationship between Gaucher Disease and Parkinsonism: Insights from a Rare Disease

Author keywords

alpha synuclein; autophagy; Gaucher disease; glucocerebrosidase; lysosome; parkinsonism

Indexed keywords

AFEGOSTAT; ALPHA SYNUCLEIN; AMBROXOL; GLUCOSYLCERAMIDASE; GLYCOSIDASE INHIBITOR; VENGLUSTAT;

EID: 85013658130     PISSN: 08966273     EISSN: 10974199     Source Type: Journal    
DOI: 10.1016/j.neuron.2017.01.018     Document Type: Review
Times cited : (122)

References (98)
  • 2
    • 84978826732 scopus 로고    scopus 로고
    • A new Glucocerebrosidase chaperone reduces α-Synuclein and glycolipid levels in iPSC-derived dopaminergic neurons from patients with Gaucher disease and parkinsonism
    • Aflaki, E., Borger, D.K., Moaven, N., Stubblefield, B.K., Rogers, S.A., Patnaik, S., Schoenen, F.J., Westbroek, W., Zheng, W., Sullivan, P., et al. A new Glucocerebrosidase chaperone reduces α-Synuclein and glycolipid levels in iPSC-derived dopaminergic neurons from patients with Gaucher disease and parkinsonism. J. Neurosci. 36 (2016), 7441–7452.
    • (2016) J. Neurosci. , vol.36 , pp. 7441-7452
    • Aflaki, E.1    Borger, D.K.2    Moaven, N.3    Stubblefield, B.K.4    Rogers, S.A.5    Patnaik, S.6    Schoenen, F.J.7    Westbroek, W.8    Zheng, W.9    Sullivan, P.10
  • 3
    • 7444237665 scopus 로고    scopus 로고
    • Mutations in the glucocerebrosidase gene and Parkinson's disease in Ashkenazi Jews
    • Aharon-Peretz, J., Rosenbaum, H., Gershoni-Baruch, R., Mutations in the glucocerebrosidase gene and Parkinson's disease in Ashkenazi Jews. N. Engl. J. Med. 351 (2004), 1972–1977.
    • (2004) N. Engl. J. Med. , vol.351 , pp. 1972-1977
    • Aharon-Peretz, J.1    Rosenbaum, H.2    Gershoni-Baruch, R.3
  • 6
    • 84922971361 scopus 로고    scopus 로고
    • Evolution of prodromal clinical markers of Parkinson disease in a GBA mutation-positive cohort
    • Beavan, M., McNeill, A., Proukakis, C., Hughes, D.A., Mehta, A., Schapira, A.H., Evolution of prodromal clinical markers of Parkinson disease in a GBA mutation-positive cohort. JAMA Neurol. 72 (2015), 201–208.
    • (2015) JAMA Neurol. , vol.72 , pp. 201-208
    • Beavan, M.1    McNeill, A.2    Proukakis, C.3    Hughes, D.A.4    Mehta, A.5    Schapira, A.H.6
  • 7
    • 84968880358 scopus 로고    scopus 로고
    • Gaucher cells are not associated with α-synuclein neuropathology in infants
    • Berger-Sieczkowski, E., Lutz, M.I., Auff, E., Kovacs, G.G., Gaucher cells are not associated with α-synuclein neuropathology in infants. Clin. Neuropathol. 35 (2016), 122–128.
    • (2016) Clin. Neuropathol. , vol.35 , pp. 122-128
    • Berger-Sieczkowski, E.1    Lutz, M.I.2    Auff, E.3    Kovacs, G.G.4
  • 9
    • 84991254228 scopus 로고    scopus 로고
    • Parkinson's disease: acid-glucocerebrosidase activity and alpha-synuclein clearance
    • Blanz, J., Saftig, P., Parkinson's disease: acid-glucocerebrosidase activity and alpha-synuclein clearance. J. Neurochem. 139:Suppl 1 (2016), 198–215.
    • (2016) J. Neurochem. , vol.139 , pp. 198-215
    • Blanz, J.1    Saftig, P.2
  • 10
    • 85012065177 scopus 로고    scopus 로고
    • Alpha-Synuclein as a mediator in the interplay between aging and Parkinson's disease
    • Bobela, W., Aebischer, P., Schneider, B.L., Alpha-Synuclein as a mediator in the interplay between aging and Parkinson's disease. Biomolecules 5 (2015), 2675–2700.
    • (2015) Biomolecules , vol.5 , pp. 2675-2700
    • Bobela, W.1    Aebischer, P.2    Schneider, B.L.3
  • 12
    • 33751118534 scopus 로고    scopus 로고
    • Age-associated increases of alpha-synuclein in monkeys and humans are associated with nigrostriatal dopamine depletion: Is this the target for Parkinson's disease?
    • Chu, Y., Kordower, J.H., Age-associated increases of alpha-synuclein in monkeys and humans are associated with nigrostriatal dopamine depletion: Is this the target for Parkinson's disease?. Neurobiol. Dis. 25 (2007), 134–149.
    • (2007) Neurobiol. Dis. , vol.25 , pp. 134-149
    • Chu, Y.1    Kordower, J.H.2
  • 13
    • 68149123529 scopus 로고    scopus 로고
    • Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions
    • Chu, Y., Dodiya, H., Aebischer, P., Olanow, C.W., Kordower, J.H., Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions. Neurobiol. Dis. 35 (2009), 385–398.
    • (2009) Neurobiol. Dis. , vol.35 , pp. 385-398
    • Chu, Y.1    Dodiya, H.2    Aebischer, P.3    Olanow, C.W.4    Kordower, J.H.5
  • 16
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo, A.M., Stefanis, L., Fredenburg, R., Lansbury, P.T., Sulzer, D., Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305 (2004), 1292–1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 17
    • 79956199921 scopus 로고    scopus 로고
    • Acid β-glucosidase mutants linked to Gaucher disease, Parkinson disease, and Lewy body dementia alter α-synuclein processing
    • Cullen, V., Sardi, S.P., Ng, J., Xu, Y.H., Sun, Y., Tomlinson, J.J., Kolodziej, P., Kahn, I., Saftig, P., Woulfe, J., et al. Acid β-glucosidase mutants linked to Gaucher disease, Parkinson disease, and Lewy body dementia alter α-synuclein processing. Ann. Neurol. 69 (2011), 940–953.
    • (2011) Ann. Neurol. , vol.69 , pp. 940-953
    • Cullen, V.1    Sardi, S.P.2    Ng, J.3    Xu, Y.H.4    Sun, Y.5    Tomlinson, J.J.6    Kolodziej, P.7    Kahn, I.8    Saftig, P.9    Woulfe, J.10
  • 22
    • 84875967929 scopus 로고    scopus 로고
    • Loss of β-glucocerebrosidase activity does not affect alpha-synuclein levels or lysosomal function in neuronal cells
    • Dermentzaki, G., Dimitriou, E., Xilouri, M., Michelakakis, H., Stefanis, L., Loss of β-glucocerebrosidase activity does not affect alpha-synuclein levels or lysosomal function in neuronal cells. PLoS ONE, 8, 2013, e60674.
    • (2013) PLoS ONE , vol.8 , pp. e60674
    • Dermentzaki, G.1    Dimitriou, E.2    Xilouri, M.3    Michelakakis, H.4    Stefanis, L.5
  • 28
    • 54049097933 scopus 로고    scopus 로고
    • The spectrum of parkinsonian manifestations associated with glucocerebrosidase mutations
    • Goker-Alpan, O., Lopez, G., Vithayathil, J., Davis, J., Hallett, M., Sidransky, E., The spectrum of parkinsonian manifestations associated with glucocerebrosidase mutations. Arch. Neurol. 65 (2008), 1353–1357.
    • (2008) Arch. Neurol. , vol.65 , pp. 1353-1357
    • Goker-Alpan, O.1    Lopez, G.2    Vithayathil, J.3    Davis, J.4    Hallett, M.5    Sidransky, E.6
  • 29
    • 84864659715 scopus 로고    scopus 로고
    • The neurobiology of glucocerebrosidase-associated parkinsonism: a positron emission tomography study of dopamine synthesis and regional cerebral blood flow
    • Goker-Alpan, O., Masdeu, J.C., Kohn, P.D., Ianni, A., Lopez, G., Groden, C., Chapman, M.C., Cropp, B., Eisenberg, D.P., Maniwang, E.D., et al. The neurobiology of glucocerebrosidase-associated parkinsonism: a positron emission tomography study of dopamine synthesis and regional cerebral blood flow. Brain 135 (2012), 2440–2448.
    • (2012) Brain , vol.135 , pp. 2440-2448
    • Goker-Alpan, O.1    Masdeu, J.C.2    Kohn, P.D.3    Ianni, A.4    Lopez, G.5    Groden, C.6    Chapman, M.C.7    Cropp, B.8    Eisenberg, D.P.9    Maniwang, E.D.10
  • 30
    • 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., Zheng, W., Motabar, O., Southall, N., Choi, J.H., Marugan, J., Austin, C.P., Sidransky, E., High throughput screening for small molecule therapy for Gaucher disease using patient tissue as the source of mutant glucocerebrosidase. PLoS ONE, 7, 2012, e29861.
    • (2012) PLoS ONE , vol.7 , pp. e29861
    • Goldin, E.1    Zheng, W.2    Motabar, O.3    Southall, N.4    Choi, J.H.5    Marugan, J.6    Austin, C.P.7    Sidransky, E.8
  • 31
    • 84893669177 scopus 로고    scopus 로고
    • Lysosomal integral membrane protein-2: a new player in lysosome-related pathology
    • Gonzalez, A., Valeiras, M., Sidransky, E., Tayebi, N., Lysosomal integral membrane protein-2: a new player in lysosome-related pathology. Mol. Genet. Metab. 111 (2014), 84–91.
    • (2014) Mol. Genet. Metab. , vol.111 , pp. 84-91
    • Gonzalez, A.1    Valeiras, M.2    Sidransky, E.3    Tayebi, N.4
  • 34
    • 84961655033 scopus 로고    scopus 로고
    • Delivery of therapeutic proteins via extracellular vesicles: review and potential treatments for Parkinson's disease, Glioma, and Schwannoma
    • Hall, J., Prabhakar, S., Balaj, L., Lai, C.P., Cerione, R.A., Breakefield, X.O., Delivery of therapeutic proteins via extracellular vesicles: review and potential treatments for Parkinson's disease, Glioma, and Schwannoma. Cell. Mol. Neurobiol. 36 (2016), 417–427.
    • (2016) Cell. Mol. Neurobiol. , vol.36 , pp. 417-427
    • Hall, J.1    Prabhakar, S.2    Balaj, L.3    Lai, C.P.4    Cerione, R.A.5    Breakefield, X.O.6
  • 36
    • 84964555624 scopus 로고    scopus 로고
    • Progress and potential of non-inhibitory small molecule chaperones for the treatment of Gaucher disease and its implications for Parkinson disease
    • Jung, O., Patnaik, S., Marugan, J., Sidransky, E., Westbroek, W., Progress and potential of non-inhibitory small molecule chaperones for the treatment of Gaucher disease and its implications for Parkinson disease. Expert Rev. Proteomics 13 (2016), 471–479.
    • (2016) Expert Rev. Proteomics , vol.13 , pp. 471-479
    • Jung, O.1    Patnaik, S.2    Marugan, J.3    Sidransky, E.4    Westbroek, W.5
  • 37
    • 77949643182 scopus 로고    scopus 로고
    • The pharmacological chaperone isofagomine increases the activity of the Gaucher disease L444P mutant form of beta-glucosidase
    • Khanna, R., Benjamin, E.R., Pellegrino, L., Schilling, A., Rigat, B.A., Soska, R., Nafar, H., Ranes, B.E., Feng, J., Lun, Y., et al. The pharmacological chaperone isofagomine increases the activity of the Gaucher disease L444P mutant form of beta-glucosidase. FEBS J. 277 (2010), 1618–1638.
    • (2010) FEBS J. , vol.277 , pp. 1618-1638
    • Khanna, R.1    Benjamin, E.R.2    Pellegrino, L.3    Schilling, A.4    Rigat, B.A.5    Soska, R.6    Nafar, H.7    Ranes, B.E.8    Feng, J.9    Lun, Y.10
  • 38
    • 0032742098 scopus 로고    scopus 로고
    • Release of calcium from stores alters the morphology of dendritic spines in cultured hippocampal neurons
    • Korkotian, E., Segal, M., Release of calcium from stores alters the morphology of dendritic spines in cultured hippocampal neurons. Proc. Natl. Acad. Sci. USA 96 (1999), 12068–12072.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12068-12072
    • Korkotian, E.1    Segal, M.2
  • 40
    • 85012094057 scopus 로고    scopus 로고
    • The interplay between Alpha-Synuclein clearance and spreading
    • Lopes da Fonseca, T., Villar-Piqué, A., Outeiro, T.F., The interplay between Alpha-Synuclein clearance and spreading. Biomolecules 5 (2015), 435–471.
    • (2015) Biomolecules , vol.5 , pp. 435-471
    • Lopes da Fonseca, T.1    Villar-Piqué, A.2    Outeiro, T.F.3
  • 42
    • 84875549809 scopus 로고    scopus 로고
    • The chaperone activity and toxicity of ambroxol on Gaucher cells and normal mice
    • Luan, Z., Li, L., Higaki, K., Nanba, E., Suzuki, Y., Ohno, K., The chaperone activity and toxicity of ambroxol on Gaucher cells and normal mice. Brain Dev. 35 (2013), 317–322.
    • (2013) Brain Dev. , vol.35 , pp. 317-322
    • Luan, Z.1    Li, L.2    Higaki, K.3    Nanba, E.4    Suzuki, Y.5    Ohno, K.6
  • 46
    • 84875245748 scopus 로고    scopus 로고
    • Is Parkinson disease associated with lysosomal integral membrane protein type-2?: challenges in interpreting association data
    • Maniwang, E., Tayebi, N., Sidransky, E., Is Parkinson disease associated with lysosomal integral membrane protein type-2?: challenges in interpreting association data. Mol. Genet. Metab. 108 (2013), 269–271.
    • (2013) Mol. Genet. Metab. , vol.108 , pp. 269-271
    • Maniwang, E.1    Tayebi, N.2    Sidransky, E.3
  • 47
    • 71049138581 scopus 로고    scopus 로고
    • Alpha-synuclein-glucocerebrosidase interactions in pharmacological Gaucher models: a biological link between Gaucher disease and parkinsonism
    • Manning-Boğ, A.B., Schüle, B., Langston, J.W., Alpha-synuclein-glucocerebrosidase interactions in pharmacological Gaucher models: a biological link between Gaucher disease and parkinsonism. Neurotoxicology 30 (2009), 1127–1132.
    • (2009) Neurotoxicology , vol.30 , pp. 1127-1132
    • Manning-Boğ, A.B.1    Schüle, B.2    Langston, J.W.3
  • 51
    • 84990246154 scopus 로고    scopus 로고
    • Beyond Krabbe's disease: the potential contribution of galactosylceramidase deficiency to neuronal vulnerability in late-onset synucleinopathies
    • Marshall, M.S., Bongarzone, E.R., Beyond Krabbe's disease: the potential contribution of galactosylceramidase deficiency to neuronal vulnerability in late-onset synucleinopathies. J. Neurosci. Res. 94 (2016), 1328–1332.
    • (2016) J. Neurosci. Res. , vol.94 , pp. 1328-1332
    • Marshall, M.S.1    Bongarzone, E.R.2
  • 55
    • 84958999192 scopus 로고    scopus 로고
    • α-Synuclein-induced lysosomal dysfunction occurs through disruptions in protein trafficking in human midbrain synucleinopathy models
    • Mazzulli, J.R., Zunke, F., Isacson, O., Studer, L., Krainc, D., α-Synuclein-induced lysosomal dysfunction occurs through disruptions in protein trafficking in human midbrain synucleinopathy models. Proc. Natl. Acad. Sci. USA 113 (2016), 1931–1936.
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. 1931-1936
    • Mazzulli, J.R.1    Zunke, F.2    Isacson, O.3    Studer, L.4    Krainc, D.5
  • 57
    • 84938118051 scopus 로고    scopus 로고
    • Cysteine cathepsins are essential in lysosomal degradation of α-synuclein
    • McGlinchey, R.P., Lee, J.C., Cysteine cathepsins are essential in lysosomal degradation of α-synuclein. Proc. Natl. Acad. Sci. USA 112 (2015), 9322–9327.
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 9322-9327
    • McGlinchey, R.P.1    Lee, J.C.2
  • 64
    • 84863083762 scopus 로고    scopus 로고
    • Discovery, structure-activity relationship, and biological evaluation of noninhibitory small molecule chaperones of glucocerebrosidase
    • Patnaik, S., Zheng, W., Choi, J.H., Motabar, O., Southall, N., Westbroek, W., Lea, W.A., Velayati, A., Goldin, E., Sidransky, E., et al. Discovery, structure-activity relationship, and biological evaluation of noninhibitory small molecule chaperones of glucocerebrosidase. J. Med. Chem. 55 (2012), 5734–5748.
    • (2012) J. Med. Chem. , vol.55 , pp. 5734-5748
    • Patnaik, S.1    Zheng, W.2    Choi, J.H.3    Motabar, O.4    Southall, N.5    Westbroek, W.6    Lea, W.A.7    Velayati, A.8    Goldin, E.9    Sidransky, E.10
  • 66
    • 84855444970 scopus 로고    scopus 로고
    • Biophysics of α-synuclein membrane interactions
    • Pfefferkorn, C.M., Jiang, Z., Lee, J.C., Biophysics of α-synuclein membrane interactions. Biochim. Biophys. Acta 1818 (2012), 162–171.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 162-171
    • Pfefferkorn, C.M.1    Jiang, Z.2    Lee, J.C.3
  • 68
    • 85012093582 scopus 로고    scopus 로고
    • Seeking a mechanism for the toxicity of oligomeric α-synuclein
    • Roberts, H.L., Brown, D.R., Seeking a mechanism for the toxicity of oligomeric α-synuclein. Biomolecules 5 (2015), 282–305.
    • (2015) Biomolecules , vol.5 , pp. 282-305
    • Roberts, H.L.1    Brown, D.R.2
  • 74
    • 84922216790 scopus 로고    scopus 로고
    • Gaucher-related synucleinopathies: the examination of sporadic neurodegeneration from a rare (disease) angle
    • Sardi, S.P., Cheng, S.H., Shihabuddin, L.S., Gaucher-related synucleinopathies: the examination of sporadic neurodegeneration from a rare (disease) angle. Prog. Neurobiol. 125 (2015), 47–62.
    • (2015) Prog. Neurobiol. , vol.125 , pp. 47-62
    • Sardi, S.P.1    Cheng, S.H.2    Shihabuddin, L.S.3
  • 76
    • 84929703186 scopus 로고    scopus 로고
    • Glucocerebrosidase and Parkinson disease: recent advances
    • Schapira, A.H., Glucocerebrosidase and Parkinson disease: recent advances. Mol. Cell. Neurosci. 66:Pt A (2015), 37–42.
    • (2015) Mol. Cell. Neurosci. , vol.66 , pp. 37-42
    • Schapira, A.H.1
  • 78
    • 80655134725 scopus 로고    scopus 로고
    • TFEB regulates autophagy: an integrated coordination of cellular degradation and recycling processes
    • Settembre, C., Ballabio, A., TFEB regulates autophagy: an integrated coordination of cellular degradation and recycling processes. Autophagy 7 (2011), 1379–1381.
    • (2011) Autophagy , vol.7 , pp. 1379-1381
    • Settembre, C.1    Ballabio, A.2
  • 83
    • 84899818136 scopus 로고    scopus 로고
    • Glucocerebrosidase is shaking up the synucleinopathies
    • Siebert, M., Sidransky, E., Westbroek, W., Glucocerebrosidase is shaking up the synucleinopathies. Brain 137 (2014), 1304–1322.
    • (2014) Brain , vol.137 , pp. 1304-1322
    • Siebert, M.1    Sidransky, E.2    Westbroek, W.3
  • 84
    • 84973915581 scopus 로고    scopus 로고
    • The evolution of genetics: Alzheimer's and Parkinson's diseases
    • Singleton, A., Hardy, J., The evolution of genetics: Alzheimer's and Parkinson's diseases. Neuron 90 (2016), 1154–1163.
    • (2016) Neuron , vol.90 , pp. 1154-1163
    • Singleton, A.1    Hardy, J.2
  • 85
    • 84937730909 scopus 로고    scopus 로고
    • Alpha-synuclein function and dysfunction on cellular membranes
    • Snead, D., Eliezer, D., Alpha-synuclein function and dysfunction on cellular membranes. Exp. Neurobiol. 23 (2014), 292–313.
    • (2014) Exp. Neurobiol. , vol.23 , pp. 292-313
    • Snead, D.1    Eliezer, D.2
  • 87
    • 84863076106 scopus 로고    scopus 로고
    • Ex vivo and in vivo effects of isofagomine on acid β-glucosidase variants and substrate levels in Gaucher disease
    • Sun, Y., Liou, B., Xu, Y.H., Quinn, B., Zhang, W., Hamler, R., Setchell, K.D., Grabowski, G.A., Ex vivo and in vivo effects of isofagomine on acid β-glucosidase variants and substrate levels in Gaucher disease. J. Biol. Chem. 287 (2012), 4275–4287.
    • (2012) J. Biol. Chem. , vol.287 , pp. 4275-4287
    • Sun, Y.1    Liou, B.2    Xu, Y.H.3    Quinn, B.4    Zhang, W.5    Hamler, R.6    Setchell, K.D.7    Grabowski, G.A.8
  • 89
    • 84986628114 scopus 로고    scopus 로고
    • Enzyme replacement or substrate reduction? A review of Gaucher disease treatment options
    • Van Rossum, A., Holsopple, M., Enzyme replacement or substrate reduction? A review of Gaucher disease treatment options. Hosp. Pharm. 51 (2016), 553–563.
    • (2016) Hosp. Pharm. , vol.51 , pp. 553-563
    • Van Rossum, A.1    Holsopple, M.2
  • 92
    • 84992535791 scopus 로고    scopus 로고
    • Lysosomal trafficking defects link Parkinson's disease with Gaucher's disease
    • Wong, Y.C., Krainc, D., Lysosomal trafficking defects link Parkinson's disease with Gaucher's disease. Mov. Disord. 31 (2016), 1610–1618.
    • (2016) Mov. Disord. , vol.31 , pp. 1610-1618
    • Wong, Y.C.1    Krainc, D.2
  • 94
    • 84969439344 scopus 로고    scopus 로고
    • Toxic oligomeric Alpha-Synuclein variants present in human Parkinson's disease brains are differentially generated in mammalian cell models
    • Xin, W., Emadi, S., Williams, S., Liu, Q., Schulz, P., He, P., Alam, N.B., Wu, J., Sierks, M.R., Toxic oligomeric Alpha-Synuclein variants present in human Parkinson's disease brains are differentially generated in mammalian cell models. Biomolecules 5 (2015), 1634–1651.
    • (2015) Biomolecules , vol.5 , pp. 1634-1651
    • Xin, W.1    Emadi, S.2    Williams, S.3    Liu, Q.4    Schulz, P.5    He, P.6    Alam, N.B.7    Wu, J.8    Sierks, M.R.9
  • 95
    • 79959925894 scopus 로고    scopus 로고
    • Alpha-synuclein interacts with Glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases
    • Yap, T.L., Gruschus, J.M., Velayati, A., Westbroek, W., Goldin, E., Moaven, N., Sidransky, E., Lee, J.C., Alpha-synuclein interacts with Glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases. J. Biol. Chem. 286 (2011), 28080–28088.
    • (2011) J. Biol. Chem. , vol.286 , pp. 28080-28088
    • Yap, T.L.1    Gruschus, J.M.2    Velayati, A.3    Westbroek, W.4    Goldin, E.5    Moaven, N.6    Sidransky, E.7    Lee, J.C.8
  • 96
    • 84886020944 scopus 로고    scopus 로고
    • Saposin C protects glucocerebrosidase against α-synuclein inhibition
    • Yap, T.L., Gruschus, J.M., Velayati, A., Sidransky, E., Lee, J.C., Saposin C protects glucocerebrosidase against α-synuclein inhibition. Biochemistry 52 (2013), 7161–7163.
    • (2013) Biochemistry , vol.52 , pp. 7161-7163
    • Yap, T.L.1    Gruschus, J.M.2    Velayati, A.3    Sidransky, E.4    Lee, J.C.5
  • 97
    • 84920913800 scopus 로고    scopus 로고
    • Structural features of membrane-bound glucocerebrosidase and α-synuclein probed by neutron reflectometry and fluorescence spectroscopy
    • Yap, T.L., Jiang, Z., Heinrich, F., Gruschus, J.M., Pfefferkorn, C.M., Barros, M., Curtis, J.E., Sidransky, E., Lee, J.C., Structural features of membrane-bound glucocerebrosidase and α-synuclein probed by neutron reflectometry and fluorescence spectroscopy. J. Biol. Chem. 290 (2015), 744–754.
    • (2015) J. Biol. Chem. , vol.290 , pp. 744-754
    • Yap, T.L.1    Jiang, Z.2    Heinrich, F.3    Gruschus, J.M.4    Pfefferkorn, C.M.5    Barros, M.6    Curtis, J.E.7    Sidransky, E.8    Lee, J.C.9
  • 98
    • 84871994423 scopus 로고    scopus 로고
    • Pilot study using ambroxol as a pharmacological chaperone in type 1 Gaucher disease
    • Zimran, A., Altarescu, G., Elstein, D., Pilot study using ambroxol as a pharmacological chaperone in type 1 Gaucher disease. Blood Cells Mol. Dis. 50 (2013), 134–137.
    • (2013) Blood Cells Mol. Dis. , vol.50 , pp. 134-137
    • Zimran, A.1    Altarescu, G.2    Elstein, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.