메뉴 건너뛰기




Volumn 81, Issue 2, 2017, Pages 227-239

Proteomics of rimmed vacuoles define new risk allele in inclusion body myositis

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; PROTEIN FYCO1; PROTEIN MAP1LC3; PROTEIN VARIANT; SEQUESTOSOME 1; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; FYCO1 PROTEIN, HUMAN; TRANSCRIPTION FACTOR;

EID: 85011342628     PISSN: 03645134     EISSN: 15318249     Source Type: Journal    
DOI: 10.1002/ana.24847     Document Type: Article
Times cited : (69)

References (53)
  • 1
    • 84925804758 scopus 로고    scopus 로고
    • Sporadic inclusion body myositis: new insights and potential therapy
    • Machado PM, Dimachkie MM, Barohn RJ. Sporadic inclusion body myositis: new insights and potential therapy. Curr Opin Neurol 2014;27:591–598.
    • (2014) Curr Opin Neurol , vol.27 , pp. 591-598
    • Machado, P.M.1    Dimachkie, M.M.2    Barohn, R.J.3
  • 2
    • 79952443273 scopus 로고    scopus 로고
    • Idiopathic inflammatory myopathies
    • Dimachkie MM. Idiopathic inflammatory myopathies. J Neuroimmunol 2011;231:32–42.
    • (2011) J Neuroimmunol , vol.231 , pp. 32-42
    • Dimachkie, M.M.1
  • 3
    • 33645703931 scopus 로고    scopus 로고
    • Mechanisms of disease: signaling pathways and immunobiology of inflammatory myopathies
    • Dalakas MC. Mechanisms of disease: signaling pathways and immunobiology of inflammatory myopathies. Nat Clin Pract Rheumatol 2006;2:219–227.
    • (2006) Nat Clin Pract Rheumatol , vol.2 , pp. 219-227
    • Dalakas, M.C.1
  • 4
    • 84899544973 scopus 로고    scopus 로고
    • A retrospective cohort study identifying the principal pathological features useful in the diagnosis of inclusion body myositis
    • Brady S, Squier W, Sewry C, et al. A retrospective cohort study identifying the principal pathological features useful in the diagnosis of inclusion body myositis. BMJ Open 2014;4:e004552.
    • (2014) BMJ Open , vol.4
    • Brady, S.1    Squier, W.2    Sewry, C.3
  • 5
    • 84888431952 scopus 로고    scopus 로고
    • 188th ENMC International Workshop: Inclusion Body Myositis, 2-4 December 2011, Naarden, the Netherlands
    • Rose MR. 188th ENMC International Workshop: Inclusion Body Myositis, 2-4 December 2011, Naarden, the Netherlands. Neuromuscul Disord 2013;23:1044–1055.
    • (2013) Neuromuscul Disord , vol.23 , pp. 1044-1055
    • Rose, M.R.1
  • 6
    • 84891290012 scopus 로고    scopus 로고
    • Human beta-defensin-3 correlates with muscle fibre degeneration in idiopathic inflammatory myopathies
    • Güttsches A, Jacobsen F, Theiss C, et al. Human beta-defensin-3 correlates with muscle fibre degeneration in idiopathic inflammatory myopathies. Innate Immun 2014;20:49–60.
    • (2014) Innate Immun , vol.20 , pp. 49-60
    • Güttsches, A.1    Jacobsen, F.2    Theiss, C.3
  • 7
    • 84901988674 scopus 로고    scopus 로고
    • Abnormal distribution of heterogeneous nuclear ribonucleoproteins in sporadic inclusion body myositis
    • Pinkus JL, Amato AA, Taylor JP, Greenberg SA. Abnormal distribution of heterogeneous nuclear ribonucleoproteins in sporadic inclusion body myositis. Neuromuscul Disord 2014;24:611–616.
    • (2014) Neuromuscul Disord , vol.24 , pp. 611-616
    • Pinkus, J.L.1    Amato, A.A.2    Taylor, J.P.3    Greenberg, S.A.4
  • 8
    • 77956393778 scopus 로고    scopus 로고
    • Sporadic inclusion body myositis: possible pathogenesis inferred from biomarkers
    • Weihl CC, Pestronk A. Sporadic inclusion body myositis: possible pathogenesis inferred from biomarkers. Curr Opin Neurol 2010;23:482–488.
    • (2010) Curr Opin Neurol , vol.23 , pp. 482-488
    • Weihl, C.C.1    Pestronk, A.2
  • 9
    • 24144484625 scopus 로고    scopus 로고
    • Molecular pathology and pathogenesis of inclusion-body myositis
    • Askanas V, Engel WK. Molecular pathology and pathogenesis of inclusion-body myositis. Microsc Res Tech 2005;67:114–120.
    • (2005) Microsc Res Tech , vol.67 , pp. 114-120
    • Askanas, V.1    Engel, W.K.2
  • 10
    • 84924295587 scopus 로고    scopus 로고
    • Autophagic vacuolar pathology in desminopathies
    • Weihl CC, Iyadurai S, Baloh RH, et al. Autophagic vacuolar pathology in desminopathies. Neuromuscul Disord 2015;25:199–206.
    • (2015) Neuromuscul Disord , vol.25 , pp. 199-206
    • Weihl, C.C.1    Iyadurai, S.2    Baloh, R.H.3
  • 11
    • 84871880606 scopus 로고    scopus 로고
    • A combined laser microdissection and mass spectrometry approach reveals new disease relevant proteins accumulating in aggregates of filaminopathy patients
    • Kley RA, Maerkens A, Leber Y, et al. A combined laser microdissection and mass spectrometry approach reveals new disease relevant proteins accumulating in aggregates of filaminopathy patients. Mol Cell Proteomics 2013;12:215–227.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 215-227
    • Kley, R.A.1    Maerkens, A.2    Leber, Y.3
  • 12
    • 84882686603 scopus 로고    scopus 로고
    • Differential proteomic analysis of abnormal intramyoplasmic aggregates in desminopathy
    • Maerkens A, Kley RA, Olivé M, et al. Differential proteomic analysis of abnormal intramyoplasmic aggregates in desminopathy. J Proteomics 2013;90:14–27.
    • (2013) J Proteomics , vol.90 , pp. 14-27
    • Maerkens, A.1    Kley, R.A.2    Olivé, M.3
  • 13
    • 85013618076 scopus 로고    scopus 로고
    • New insights into the protein aggregation pathology in myotilinopathy by combined proteomic and immunolocalization analyses
    • Maerkens A, Olivé M, Schreiner A, et al. New insights into the protein aggregation pathology in myotilinopathy by combined proteomic and immunolocalization analyses. Acta Neuropathol Commun 2016;4:8.
    • (2016) Acta Neuropathol Commun , vol.4 , pp. 8
    • Maerkens, A.1    Olivé, M.2    Schreiner, A.3
  • 14
    • 84925234233 scopus 로고    scopus 로고
    • Targeted sequencing and identification of genetic variants in sporadic inclusion body myositis
    • Weihl CC, Baloh RH, Lee Y, et al. Targeted sequencing and identification of genetic variants in sporadic inclusion body myositis. Neuromuscul Disord 2015;25:289–296.
    • (2015) Neuromuscul Disord , vol.25 , pp. 289-296
    • Weihl, C.C.1    Baloh, R.H.2    Lee, Y.3
  • 15
    • 84877344130 scopus 로고    scopus 로고
    • Impairment of protein degradation in myofibrillar myopathy caused by FLNC/filamin C mutations
    • Kley RA, van der Ven PF, Olivé M, et al. Impairment of protein degradation in myofibrillar myopathy caused by FLNC/filamin C mutations. Autophagy 2013;9:422–423.
    • (2013) Autophagy , vol.9 , pp. 422-423
    • Kley, R.A.1    van der Ven, P.F.2    Olivé, M.3
  • 16
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999;20:3551–3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 17
    • 84946561820 scopus 로고    scopus 로고
    • PIA: an intuitive protein inference engine with a Web-based user interface
    • Uszkoreit J, Maerkens A, Perez-Riverol Y, et al. PIA: an intuitive protein inference engine with a Web-based user interface. J Proteome Res 2015;14:2988–2997.
    • (2015) J Proteome Res , vol.14 , pp. 2988-2997
    • Uszkoreit, J.1    Maerkens, A.2    Perez-Riverol, Y.3
  • 18
    • 67649884743 scopus 로고    scopus 로고
    • Fast and accurate short read alignment with Burrows-Wheeler transform
    • Li H, Durbin R. Fast and accurate short read alignment with Burrows-Wheeler transform. Bioinformatics 2009;25:1754–1760.
    • (2009) Bioinformatics , vol.25 , pp. 1754-1760
    • Li, H.1    Durbin, R.2
  • 19
    • 68549104404 scopus 로고    scopus 로고
    • The Sequence Alignment/Map format and SAMtools
    • Li H, Handsaker B, Wysoker A, et al. The Sequence Alignment/Map format and SAMtools. Bioinformatics 2009;25:2078–2079.
    • (2009) Bioinformatics , vol.25 , pp. 2078-2079
    • Li, H.1    Handsaker, B.2    Wysoker, A.3
  • 20
    • 77951770756 scopus 로고    scopus 로고
    • BEDTools: a flexible suite of utilities for comparing genomic features
    • Quinlan AR, Hall IM. BEDTools: a flexible suite of utilities for comparing genomic features. Bioinformatics 2010;26:841–842.
    • (2010) Bioinformatics , vol.26 , pp. 841-842
    • Quinlan, A.R.1    Hall, I.M.2
  • 21
    • 84949057575 scopus 로고    scopus 로고
    • FYCO1 contains a C-terminally extended, LC3A/B-preferring LC3-interacting region (LIR) motif required for efficient maturation of autophagosomes during basal autophagy
    • Olsvik HL, Lamark T, Takagi K, et al. FYCO1 contains a C-terminally extended, LC3A/B-preferring LC3-interacting region (LIR) motif required for efficient maturation of autophagosomes during basal autophagy. J Biol Chem 2015;290:29361–29374.
    • (2015) J Biol Chem , vol.290 , pp. 29361-29374
    • Olsvik, H.L.1    Lamark, T.2    Takagi, K.3
  • 22
    • 79958786419 scopus 로고    scopus 로고
    • Mutations in FYCO1 cause autosomal-recessive congenital cataracts
    • Chen J, Ma Z, Jiao X, et al. Mutations in FYCO1 cause autosomal-recessive congenital cataracts. Am J Hum Genet 2011;88:827–838.
    • (2011) Am J Hum Genet , vol.88 , pp. 827-838
    • Chen, J.1    Ma, Z.2    Jiao, X.3
  • 23
    • 0038758988 scopus 로고    scopus 로고
    • Expression of the intermediate filament protein synemin in myofibrillar myopathies and other muscle diseases
    • Olivé M, Goldfarb L, Dagvadorj A, et al. Expression of the intermediate filament protein synemin in myofibrillar myopathies and other muscle diseases. Acta Neuropathol 2003;106:1–7.
    • (2003) Acta Neuropathol , vol.106 , pp. 1-7
    • Olivé, M.1    Goldfarb, L.2    Dagvadorj, A.3
  • 24
    • 67049165108 scopus 로고    scopus 로고
    • Fast-twitch sarcomeric and glycolytic enzyme protein loss in inclusion body myositis
    • Parker KC, Kong SW, Walsh RJ, et al. Fast-twitch sarcomeric and glycolytic enzyme protein loss in inclusion body myositis. Muscle Nerve 2009;39:739–753.
    • (2009) Muscle Nerve , vol.39 , pp. 739-753
    • Parker, K.C.1    Kong, S.W.2    Walsh, R.J.3
  • 25
    • 84872397240 scopus 로고    scopus 로고
    • Expression of myogenic regulatory factors and myo-endothelial remodeling in sporadic inclusion body myositis
    • Wanschitz JV, Dubourg O, Lacene E, et al. Expression of myogenic regulatory factors and myo-endothelial remodeling in sporadic inclusion body myositis. Neuromuscul Disord 2013;23:75–83.
    • (2013) Neuromuscul Disord , vol.23 , pp. 75-83
    • Wanschitz, J.V.1    Dubourg, O.2    Lacene, E.3
  • 27
    • 84930956908 scopus 로고    scopus 로고
    • Vimentin filament organization and stress sensing depend on its single cysteine residue and zinc binding
    • Pérez-Sala D, Oeste CL, Martinez AE, et al. Vimentin filament organization and stress sensing depend on its single cysteine residue and zinc binding. Nat Commun 2015;6:7287.
    • (2015) Nat Commun , vol.6 , pp. 7287
    • Pérez-Sala, D.1    Oeste, C.L.2    Martinez, A.E.3
  • 28
    • 79955526987 scopus 로고    scopus 로고
    • Protein kinase CK2 regulates the formation and clearance of aggresomes in response to stress
    • Watabe M, Nakaki T. Protein kinase CK2 regulates the formation and clearance of aggresomes in response to stress. J Cell Sci 2011;124:1519–1532.
    • (2011) J Cell Sci , vol.124 , pp. 1519-1532
    • Watabe, M.1    Nakaki, T.2
  • 29
    • 48249084875 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of aggresomes is not a universal phenomenon
    • Wong ESP, Tan JMM, Soong W, et al. Autophagy-mediated clearance of aggresomes is not a universal phenomenon. Hum Mol Genet 2008;17:2570–2582.
    • (2008) Hum Mol Genet , vol.17 , pp. 2570-2582
    • Wong, E.S.P.1    Tan, J.M.M.2    Soong, W.3
  • 30
    • 84961773841 scopus 로고    scopus 로고
    • Targeting protein homeostasis in sporadic inclusion body myositis
    • Ahmed M, Machado PM, Miller A, et al. Targeting protein homeostasis in sporadic inclusion body myositis. Sci Transl Med 2016;8:331ra41.
    • (2016) Sci Transl Med , vol.8 , pp. 331ra41
    • Ahmed, M.1    Machado, P.M.2    Miller, A.3
  • 31
    • 33645107853 scopus 로고    scopus 로고
    • Homocysteine-induced endoplasmic reticulum protein (Herp) is up-regulated in sporadic inclusion-body myositis and in endoplasmic reticulum stress-induced cultured human muscle fibers
    • Nogalska A, Engel WK, McFerrin J, et al. Homocysteine-induced endoplasmic reticulum protein (Herp) is up-regulated in sporadic inclusion-body myositis and in endoplasmic reticulum stress-induced cultured human muscle fibers. J Neurochem 2006;96:1491–1499.
    • (2006) J Neurochem , vol.96 , pp. 1491-1499
    • Nogalska, A.1    Engel, W.K.2    McFerrin, J.3
  • 32
    • 1542784578 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle
    • Vattemi G, Engel WK, McFerrin J, Askanas V. Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am J Pathol 2004;164:1–7.
    • (2004) Am J Pathol , vol.164 , pp. 1-7
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 33
    • 84908109103 scopus 로고    scopus 로고
    • Proteomic study of sporadic inclusion body myositis
    • Li K, Pu C, Huang X, et al. Proteomic study of sporadic inclusion body myositis. Proteome Sci 2014;12:45.
    • (2014) Proteome Sci , vol.12 , pp. 45
    • Li, K.1    Pu, C.2    Huang, X.3
  • 34
    • 72449199088 scopus 로고    scopus 로고
    • Proinflammatory cell stress in sporadic inclusion body myositis muscle: overexpression of alphaB-crystallin is associated with amyloid precursor protein and accumulation of beta-amyloid
    • Muth IE, Barthel K, Bahr M, et al. Proinflammatory cell stress in sporadic inclusion body myositis muscle: overexpression of alphaB-crystallin is associated with amyloid precursor protein and accumulation of beta-amyloid. J Neurol Neurosurg Psychiatry 2009;80:1344–1349.
    • (2009) J Neurol Neurosurg Psychiatry , vol.80 , pp. 1344-1349
    • Muth, I.E.1    Barthel, K.2    Bahr, M.3
  • 35
    • 57149098022 scopus 로고    scopus 로고
    • Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
    • Yam AY, Xia Y, Lin HJ, et al. Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nat Struct Mol Biol 2008;15:1255–1262.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1255-1262
    • Yam, A.Y.1    Xia, Y.2    Lin, H.J.3
  • 36
    • 33749176269 scopus 로고    scopus 로고
    • Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state
    • Kitamura A, Kubota H, Pack C, et al. Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state. Nature Cell Biol 2006;8:1163–1170.
    • (2006) Nature Cell Biol , vol.8 , pp. 1163-1170
    • Kitamura, A.1    Kubota, H.2    Pack, C.3
  • 37
    • 33749177252 scopus 로고    scopus 로고
    • The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
    • Tam S, Geller R, Spiess C, Frydman J. The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 2006;8:1155–1162.
    • (2006) Nat Cell Biol , vol.8 , pp. 1155-1162
    • Tam, S.1    Geller, R.2    Spiess, C.3    Frydman, J.4
  • 38
    • 84919761983 scopus 로고    scopus 로고
    • A direct regulatory interaction between chaperonin TRiC and stress-responsive transcription factor HSF1
    • Neef DW, Jaeger AM, Gomez-Pastor R, et al. A direct regulatory interaction between chaperonin TRiC and stress-responsive transcription factor HSF1. Cell Rep 2014;9:955–966.
    • (2014) Cell Rep , vol.9 , pp. 955-966
    • Neef, D.W.1    Jaeger, A.M.2    Gomez-Pastor, R.3
  • 39
    • 84876869300 scopus 로고    scopus 로고
    • Identification of a tissue-selective heat shock response regulatory network
    • Guisbert E, Czyz DM, Richter K, et al. Identification of a tissue-selective heat shock response regulatory network. PLoS Genet 2013;9:e1003466.
    • (2013) PLoS Genet , vol.9
    • Guisbert, E.1    Czyz, D.M.2    Richter, K.3
  • 40
    • 84856147995 scopus 로고    scopus 로고
    • Etiology of limb girdle muscular dystrophy 1D/1E determined by laser capture microdissection proteomics
    • Greenberg SA, Salajegheh M, Judge DP, et al. Etiology of limb girdle muscular dystrophy 1D/1E determined by laser capture microdissection proteomics. Ann Neurol 2012;71:141–145.
    • (2012) Ann Neurol , vol.71 , pp. 141-145
    • Greenberg, S.A.1    Salajegheh, M.2    Judge, D.P.3
  • 41
    • 40549108276 scopus 로고    scopus 로고
    • Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy
    • Schessl J, Zou Y, McGrath MJ, et al. Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy. J Clin Invest 2008;118:904–912.
    • (2008) J Clin Invest , vol.118 , pp. 904-912
    • Schessl, J.1    Zou, Y.2    McGrath, M.J.3
  • 42
    • 70350211088 scopus 로고    scopus 로고
    • Sporadic inclusion body myositis: HLA-DRB1 allele interactions influence disease risk and clinical phenotype
    • Mastaglia FL, Needham M, Scott A, et al. Sporadic inclusion body myositis: HLA-DRB1 allele interactions influence disease risk and clinical phenotype. Neuromuscul Disord 2009;19:763–765.
    • (2009) Neuromuscul Disord , vol.19 , pp. 763-765
    • Mastaglia, F.L.1    Needham, M.2    Scott, A.3
  • 43
    • 84945749129 scopus 로고    scopus 로고
    • Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways
    • Cirulli ET, Lasseigne BN, Petrovski S, et al. Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways. Science 2015;347:1436–1441.
    • (2015) Science , vol.347 , pp. 1436-1441
    • Cirulli, E.T.1    Lasseigne, B.N.2    Petrovski, S.3
  • 44
    • 84897398469 scopus 로고    scopus 로고
    • TREM2 variant p.R47H as a risk factor for sporadic amyotrophic lateral sclerosis
    • Cady J, Koval ED, Benitez BA, et al. TREM2 variant p.R47H as a risk factor for sporadic amyotrophic lateral sclerosis. JAMA Neurol 2014;71:449–453.
    • (2014) JAMA Neurol , vol.71 , pp. 449-453
    • Cady, J.1    Koval, E.D.2    Benitez, B.A.3
  • 45
    • 84891461247 scopus 로고    scopus 로고
    • The LC3 interactome at a glance
    • Wild P, McEwan DG, Dikic I. The LC3 interactome at a glance. J Cell Sci 2014;127:3–9.
    • (2014) J Cell Sci , vol.127 , pp. 3-9
    • Wild, P.1    McEwan, D.G.2    Dikic, I.3
  • 46
    • 76149086512 scopus 로고    scopus 로고
    • FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport
    • Pankiv S, Alemu EA, Brech A, et al. FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport. J Cell Biol 2010;188:253–269.
    • (2010) J Cell Biol , vol.188 , pp. 253-269
    • Pankiv, S.1    Alemu, E.A.2    Brech, A.3
  • 47
    • 77953708505 scopus 로고    scopus 로고
    • FYCO1: linking autophagosomes to microtubule plus end-directing molecular motors
    • Pankiv S, Johansen T. FYCO1: linking autophagosomes to microtubule plus end-directing molecular motors. Autophagy 2010;6:550–552.
    • (2010) Autophagy , vol.6 , pp. 550-552
    • Pankiv, S.1    Johansen, T.2
  • 48
    • 84890814455 scopus 로고    scopus 로고
    • Increased autophagy accelerates colchicine-induced muscle toxicity
    • Ching JK, Ju JS, Pittman SK, et al. Increased autophagy accelerates colchicine-induced muscle toxicity. Autophagy 2013;9:2115–2125.
    • (2013) Autophagy , vol.9 , pp. 2115-2125
    • Ching, J.K.1    Ju, J.S.2    Pittman, S.K.3
  • 49
    • 74049124412 scopus 로고    scopus 로고
    • Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease
    • Ju JS, Fuentealba RA, Miller SE, et al. Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease. J Cell Biol 2009;187:875–888.
    • (2009) J Cell Biol , vol.187 , pp. 875-888
    • Ju, J.S.1    Fuentealba, R.A.2    Miller, S.E.3
  • 50
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • Watts GD, Wymer J, Kovach MJ, et al. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat Genet 2004;36:377–381.
    • (2004) Nat Genet , vol.36 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3
  • 51
    • 84940039149 scopus 로고    scopus 로고
    • SQSTM1 splice site mutation in distal myopathy with rimmed vacuoles
    • Bucelli RC, Arhzaouy K, Pestronk A, et al. SQSTM1 splice site mutation in distal myopathy with rimmed vacuoles. Neurology 2015;85:665–674.
    • (2015) Neurology , vol.85 , pp. 665-674
    • Bucelli, R.C.1    Arhzaouy, K.2    Pestronk, A.3
  • 52
    • 34548259958 scopus 로고    scopus 로고
    • p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • Pankiv S, Clausen TH, Lamark T, et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem 2007;282:24131–24145.
    • (2007) J Biol Chem , vol.282 , pp. 24131-24145
    • Pankiv, S.1    Clausen, T.H.2    Lamark, T.3
  • 53
    • 84994512347 scopus 로고    scopus 로고
    • Rare variants in SQSTM1 and VCP genes and risk of sporadic inclusion body myositis
    • Gang Q, Bettencourt C, Machado PM, et al. Rare variants in SQSTM1 and VCP genes and risk of sporadic inclusion body myositis. Neurobiol Aging 2016;47:218.e1–218.e9.
    • (2016) Neurobiol Aging , vol.47 , pp. 218.e1-218.e9.
    • Gang, Q.1    Bettencourt, C.2    Machado, P.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.