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Volumn 409, Issue 8, 2017, Pages 2143-2153

Absolute quantification of myosin heavy chain isoforms by selected reaction monitoring can underscore skeletal muscle changes in a mouse model of amyotrophic lateral sclerosis

Author keywords

Absolute quantification; Amyotrophic lateral sclerosis; Myosin heavy chain; Selected reaction monitoring; Skeletal muscle; Targeted proteomics

Indexed keywords

CHAINS; DIAGNOSIS; MAMMALS; MASS SPECTROMETRY; MOLECULAR BIOLOGY; MUSCULOSKELETAL SYSTEM; NEURODEGENERATIVE DISEASES; PROTEINS;

EID: 85009286755     PISSN: 16182642     EISSN: 16182650     Source Type: Journal    
DOI: 10.1007/s00216-016-0160-2     Document Type: Article
Times cited : (27)

References (54)
  • 1
    • 0001257691 scopus 로고
    • Reciprocal relationship of phosphorylase and oxidative enzymes in skeletal muscle
    • COI: 1:CAS:528:DyaF3cXotFOmsg%3D%3D
    • Dubowitz V, Pearse AG. Reciprocal relationship of phosphorylase and oxidative enzymes in skeletal muscle. Nature. 1960;185:701–2.
    • (1960) Nature , vol.185 , pp. 701-702
    • Dubowitz, V.1    Pearse, A.G.2
  • 2
    • 0014341253 scopus 로고
    • Histochemical composition, distribution of fibres and fatiguability of single motor units. Anterior tibial muscle of the rat
    • Edström L, Kugelberg E. Histochemical composition, distribution of fibres and fatiguability of single motor units. Anterior tibial muscle of the rat. J Neurol Neurosurg Psychiatry. 1968;31:424–33.
    • (1968) J Neurol Neurosurg Psychiatry , vol.31 , pp. 424-433
    • Edström, L.1    Kugelberg, E.2
  • 3
    • 0000573855 scopus 로고
    • Histochemical classification of individual skeletal muscle fibers of the rat
    • COI: 1:CAS:528:DyaF3sXhtVChsg%3D%3D
    • Stein JM, Padikula HA. Histochemical classification of individual skeletal muscle fibers of the rat. Am J Anat. 1962;110:103–23.
    • (1962) Am J Anat , vol.110 , pp. 103-123
    • Stein, J.M.1    Padikula, H.A.2
  • 4
    • 0014838245 scopus 로고
    • Three “myosin adenosine triphosphatase” systems: the nature of their pH lability and sulfhydryl dependence
    • COI: 1:CAS:528:DyaE3MXjvVCksQ%3D%3D
    • Brooke MH, Kaiser KK. Three “myosin adenosine triphosphatase” systems: the nature of their pH lability and sulfhydryl dependence. J Histochem Cytochem. 1970;18:670–2.
    • (1970) J Histochem Cytochem , vol.18 , pp. 670-672
    • Brooke, M.H.1    Kaiser, K.K.2
  • 5
    • 0034406390 scopus 로고    scopus 로고
    • Sarcomeric myosin isoforms: fine tuning of a molecular motor
    • COI: 1:CAS:528:DC%2BD3cXhvFeltrg%3D
    • Reggiani C, Bottinelli R, Stienen GJ. Sarcomeric myosin isoforms: fine tuning of a molecular motor. News Physiol Sci. 2000;15:26–33.
    • (2000) News Physiol Sci , vol.15 , pp. 26-33
    • Reggiani, C.1    Bottinelli, R.2    Stienen, G.J.3
  • 6
    • 0025653451 scopus 로고
    • Cellular and molecular diversities of mammalian skeletal muscle fibers
    • COI: 1:STN:280:DyaK3M7ls12isA%3D%3D
    • Pette D, Staron RS. Cellular and molecular diversities of mammalian skeletal muscle fibers. Rev Physiol Biochem Pharmacol. 1990;116:1–76.
    • (1990) Rev Physiol Biochem Pharmacol , vol.116 , pp. 1-76
    • Pette, D.1    Staron, R.S.2
  • 7
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: gene regulation and functional significance
    • COI: 1:CAS:528:DyaK28XivFWlsLk%3D
    • Schiaffino S, Reggiani C. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol Rev. 1996;76:371–423.
    • (1996) Physiol Rev , vol.76 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 8
    • 74549163611 scopus 로고    scopus 로고
    • Two novel/ancient myosins in mammalian skeletal muscles: MYH14/7b and MYH15 are expressed in extraocular muscles and muscle spindles
    • COI: 1:CAS:528:DC%2BC3cXovVSisA%3D%3D
    • Rossi AC, Mammucari C, Argentini C, Reggiani C, Schiaffino S. Two novel/ancient myosins in mammalian skeletal muscles: MYH14/7b and MYH15 are expressed in extraocular muscles and muscle spindles. J Physiol. 2010;588:353–64.
    • (2010) J Physiol , vol.588 , pp. 353-364
    • Rossi, A.C.1    Mammucari, C.2    Argentini, C.3    Reggiani, C.4    Schiaffino, S.5
  • 9
    • 0022884418 scopus 로고
    • Correlation between myofibrillar ATPase activity and myosin heavy chain composition in rabbit muscle fibres
    • COI: 1:CAS:528:DyaL2sXhs1Chtw%3D%3D
    • Staron RS, Pette D. Correlation between myofibrillar ATPase activity and myosin heavy chain composition in rabbit muscle fibres. Histochemistry. 1986;86:19–23.
    • (1986) Histochemistry , vol.86 , pp. 19-23
    • Staron, R.S.1    Pette, D.2
  • 10
    • 80054690358 scopus 로고    scopus 로고
    • A continuum of myofibers in adult rabbit extraocular muscle: force, shortening velocity, and patterns of myosin heavy chain colocalization
    • COI: 1:CAS:528:DC%2BC3MXhtl2ru7jO
    • McLoon LK, Park HN, Kim JH, Pedrosa-Domellöf F, Thompson LV. A continuum of myofibers in adult rabbit extraocular muscle: force, shortening velocity, and patterns of myosin heavy chain colocalization. J Appl Physiol. 2011;111:1178–89.
    • (2011) J Appl Physiol , vol.111 , pp. 1178-1189
    • McLoon, L.K.1    Park, H.N.2    Kim, J.H.3    Pedrosa-Domellöf, F.4    Thompson, L.V.5
  • 11
    • 0034910559 scopus 로고    scopus 로고
    • Hybrid skeletal muscle fibres: a rare or common phenomenon?
    • COI: 1:CAS:528:DC%2BD3MXlvVSqtb4%3D
    • Stephenson GM. Hybrid skeletal muscle fibres: a rare or common phenomenon? Clin Exp Pharmacol Physiol. 2001;28:692–702.
    • (2001) Clin Exp Pharmacol Physiol , vol.28 , pp. 692-702
    • Stephenson, G.M.1
  • 12
    • 84858440810 scopus 로고    scopus 로고
    • IIb or not IIb? Regulation of myosin heavy chain gene expression in mice and men
    • COI: 1:CAS:528:DC%2BC3MXjsFShurg%3D
    • Harrison BC, Allen DL, Leinwand LA. IIb or not IIb? Regulation of myosin heavy chain gene expression in mice and men. Skelet Muscle. 2011;1:5.
    • (2011) Skelet Muscle , vol.1 , pp. 5
    • Harrison, B.C.1    Allen, D.L.2    Leinwand, L.A.3
  • 13
    • 84893149530 scopus 로고    scopus 로고
    • Mechanisms modulating skeletal muscle phenotype
    • Blaauw B, Schiaffino S, Reggiani C. Mechanisms modulating skeletal muscle phenotype. Compr Physiol. 2013;3:1645–87.
    • (2013) Compr Physiol , vol.3 , pp. 1645-1687
    • Blaauw, B.1    Schiaffino, S.2    Reggiani, C.3
  • 14
    • 0023832469 scopus 로고
    • Fast muscle fibers are preferentially affected in Duchenne muscular dystrophy
    • COI: 1:STN:280:DyaL1c7jsFOltw%3D%3D
    • Webster C, Silberstein L, Hays AP, Blau HM. Fast muscle fibers are preferentially affected in Duchenne muscular dystrophy. Cell. 1988;52:503–13.
    • (1988) Cell , vol.52 , pp. 503-513
    • Webster, C.1    Silberstein, L.2    Hays, A.P.3    Blau, H.M.4
  • 15
    • 48949120504 scopus 로고    scopus 로고
    • Preferential motor unit loss in the SOD1 G93A transgenic mouse model of amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BD1cXptlantb8%3D
    • Hegedus J, Putman CT, Tyreman N, Gordon T. Preferential motor unit loss in the SOD1 G93A transgenic mouse model of amyotrophic lateral sclerosis. J Physiol. 2008;586:3337–51.
    • (2008) J Physiol , vol.586 , pp. 3337-3351
    • Hegedus, J.1    Putman, C.T.2    Tyreman, N.3    Gordon, T.4
  • 16
    • 84861226652 scopus 로고    scopus 로고
    • Muscle atrophy induced by SOD1G93A expression does not involve the activation of caspase in the absence of denervation
    • COI: 1:CAS:528:DC%2BC3MXjsFShurY%3D
    • Dobrowolny G, Aucello M, Musarò A. Muscle atrophy induced by SOD1G93A expression does not involve the activation of caspase in the absence of denervation. Skelet Muscle. 2011;1:3.
    • (2011) Skelet Muscle , vol.1 , pp. 3
    • Dobrowolny, G.1    Aucello, M.2    Musarò, A.3
  • 17
    • 83455171580 scopus 로고    scopus 로고
    • Congenital fiber-type disproportion
    • Clarke NF. Congenital fiber-type disproportion. Semin Pediatr Neurol. 2011;18:264–71.
    • (2011) Semin Pediatr Neurol , vol.18 , pp. 264-271
    • Clarke, N.F.1
  • 18
    • 84872316386 scopus 로고    scopus 로고
    • Myosinopathies: pathology and mechanisms
    • COI: 1:CAS:528:DC%2BC3sXktVyqtg%3D%3D
    • Tajsharghi H, Oldfors A. Myosinopathies: pathology and mechanisms. Acta Neuropathol. 2013;125:3–18.
    • (2013) Acta Neuropathol , vol.125 , pp. 3-18
    • Tajsharghi, H.1    Oldfors, A.2
  • 19
    • 0014838245 scopus 로고
    • Three “myosin ATPase” systems. The nature of their pH liability and sulphydryl dependence
    • COI: 1:CAS:528:DyaE3MXjvVCksQ%3D%3D
    • Brooke MH, Kaiser KK. Three “myosin ATPase” systems. The nature of their pH liability and sulphydryl dependence. J Histochem Cytochem. 1970;18:670–2.
    • (1970) J Histochem Cytochem , vol.18 , pp. 670-672
    • Brooke, M.H.1    Kaiser, K.K.2
  • 20
    • 0017366067 scopus 로고
    • Histochemical sub-types of three fibre-types of avian skeletal muscle
    • COI: 1:STN:280:DyaE2s%2FntFWisQ%3D%3D
    • Khan MA. Histochemical sub-types of three fibre-types of avian skeletal muscle. Histochemistry. 1976;50:9–16.
    • (1976) Histochemistry , vol.50 , pp. 9-16
    • Khan, M.A.1
  • 21
    • 0026589152 scopus 로고
    • Histochemical, biochemical, and ultrastructural analyses of single human muscle fibers, with special reference to the C-fiber population
    • Staron RS, Hikida RS. Histochemical, biochemical, and ultrastructural analyses of single human muscle fibers, with special reference to the C-fiber population. J Histochem Cytochem. 1982;40:563–8.
    • (1982) J Histochem Cytochem , vol.40 , pp. 563-568
    • Staron, R.S.1    Hikida, R.S.2
  • 23
    • 0027452352 scopus 로고
    • Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms
    • COI: 1:CAS:528:DyaK2cXivFegtLo%3D
    • Talmadge RJ, Roy RR. Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms. J Appl Physiol. 1993;75:2337–40.
    • (1993) J Appl Physiol , vol.75 , pp. 2337-2340
    • Talmadge, R.J.1    Roy, R.R.2
  • 24
    • 0032915685 scopus 로고    scopus 로고
    • Enhanced protein electrophoresis technique for separating human skeletal muscle myosin heavy chain isoforms
    • COI: 1:CAS:528:DyaK1MXis1Wjt7g%3D
    • Bamman MM, Clarke MS, Talmadge RJ, Feeback DL. Enhanced protein electrophoresis technique for separating human skeletal muscle myosin heavy chain isoforms. Electrophoresis. 1999;20:466–8.
    • (1999) Electrophoresis , vol.20 , pp. 466-468
    • Bamman, M.M.1    Clarke, M.S.2    Talmadge, R.J.3    Feeback, D.L.4
  • 25
    • 0030068816 scopus 로고    scopus 로고
    • Enhanced electrophoretic separation and resolution of myosin heavy chains in mammalian and avian skeletal muscles
    • COI: 1:CAS:528:DyaK28XmtVKmtg%3D%3D
    • Blough ER, Rennie ER, Zhang F, Reiser PJ. Enhanced electrophoretic separation and resolution of myosin heavy chains in mammalian and avian skeletal muscles. Anal Biochem. 1996;233:31–5.
    • (1996) Anal Biochem , vol.233 , pp. 31-35
    • Blough, E.R.1    Rennie, E.R.2    Zhang, F.3    Reiser, P.J.4
  • 26
    • 0035871229 scopus 로고    scopus 로고
    • Pulse electrophoresis of muscle myosin heavy chains in sodium dodecyl sulfate-polyacrylamide gels
    • Sant’Ana Pereira JA, Greaser M, Moss RL. Pulse electrophoresis of muscle myosin heavy chains in sodium dodecyl sulfate-polyacrylamide gels. Anal Biochem. 2001;291:229–36.
    • (2001) Anal Biochem , vol.291 , pp. 229-236
    • Sant’Ana Pereira, J.A.1    Greaser, M.2    Moss, R.L.3
  • 27
    • 79960401692 scopus 로고    scopus 로고
    • Protocol for high-resolution electrophoresis separation of myosin heavy chain isoforms in bovine skeletal muscle
    • COI: 1:CAS:528:DC%2BC3MXns1Oht74%3D
    • Picard B, Barboiron C, Chadeyron D, Jurie C. Protocol for high-resolution electrophoresis separation of myosin heavy chain isoforms in bovine skeletal muscle. Electrophoresis. 2011;32:1804–6.
    • (2011) Electrophoresis , vol.32 , pp. 1804-1806
    • Picard, B.1    Barboiron, C.2    Chadeyron, D.3    Jurie, C.4
  • 28
    • 42649145391 scopus 로고    scopus 로고
    • Protocol for high-resolution separation of rodent myosin heavy chain isoforms in a mini-gel electrophoresis system
    • COI: 1:CAS:528:DC%2BD1cXlsFCmtrs%3D
    • Mizunoya W, Wakamatsu J, Tatsumi R, Ikeuchi Y. Protocol for high-resolution separation of rodent myosin heavy chain isoforms in a mini-gel electrophoresis system. Anal Biochem. 2008;377:111–3.
    • (2008) Anal Biochem , vol.377 , pp. 111-113
    • Mizunoya, W.1    Wakamatsu, J.2    Tatsumi, R.3    Ikeuchi, Y.4
  • 29
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS
    • COI: 1:CAS:528:DC%2BD38Xmt1WitLs%3D
    • Cleveland DW, Rothstein JD. From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat Rev Neurosci. 2001;2:806–19.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 30
    • 0035978743 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BD3MXkslWjtbo%3D
    • Rowland LP, Shneider NA. Amyotrophic lateral sclerosis. N Engl J Med. 2001;344:1688–700.
    • (2001) N Engl J Med , vol.344 , pp. 1688-1700
    • Rowland, L.P.1    Shneider, N.A.2
  • 31
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DyaK3sXhvV2hs74%3D
    • Rosen DR, Siddique T, Patterson D, Figlewicz DA, Sapp P, Hentati A, et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 1993;362:59–62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3    Figlewicz, D.A.4    Sapp, P.5    Hentati, A.6
  • 32
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation
    • COI: 1:CAS:528:DyaK2cXksFGisbk%3D
    • Gurney ME, Pu H, Chiu AY, Dal Canto MC, Polchow CY, Alexander DD, et al. Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Science. 1994;264:1772–5.
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurney, M.E.1    Pu, H.2    Chiu, A.Y.3    Dal Canto, M.C.4    Polchow, C.Y.5    Alexander, D.D.6
  • 33
    • 4043124885 scopus 로고    scopus 로고
    • Cell death in amyotrophic lateral sclerosis: interplay between neuronal and glial cells
    • COI: 1:CAS:528:DC%2BD2cXmsVSltr8%3D
    • Ferri A, Nencini M, Casciati A, Cozzolino M, Angelini DF, Longone P, et al. Cell death in amyotrophic lateral sclerosis: interplay between neuronal and glial cells. FASEB J. 2004;18:1261–3.
    • (2004) FASEB J , vol.18 , pp. 1261-1263
    • Ferri, A.1    Nencini, M.2    Casciati, A.3    Cozzolino, M.4    Angelini, D.F.5    Longone, P.6
  • 34
    • 77953530958 scopus 로고    scopus 로고
    • Skeletal muscle-restricted expression of human SOD1 causes motor neuron degeneration in transgenic mice
    • COI: 1:CAS:528:DC%2BC3cXlvVWkt74%3D
    • Wong M, Martin LJ. Skeletal muscle-restricted expression of human SOD1 causes motor neuron degeneration in transgenic mice. Hum Mol Genet. 2010;19:2284–302.
    • (2010) Hum Mol Genet , vol.19 , pp. 2284-2302
    • Wong, M.1    Martin, L.J.2
  • 36
    • 84896543905 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis and skeletal muscle: an update
    • COI: 1:CAS:528:DC%2BC3sXhsleks7vO
    • Pansarasa O, Rossi D, Berardinelli A, Cereda C. Amyotrophic lateral sclerosis and skeletal muscle: an update. Mol Neurobiol. 2014;49:984–90.
    • (2014) Mol Neurobiol , vol.49 , pp. 984-990
    • Pansarasa, O.1    Rossi, D.2    Berardinelli, A.3    Cereda, C.4
  • 37
    • 78049403334 scopus 로고    scopus 로고
    • Cellular prion protein promotes regeneration of adult muscle tissue
    • COI: 1:CAS:528:DC%2BC3cXhtlyqtL3P
    • Stella R, Massimino ML, Sandri M, Sorgato MC, Bertoli A. Cellular prion protein promotes regeneration of adult muscle tissue. Mol Cell Biol. 2010;30:4864–76.
    • (2010) Mol Cell Biol , vol.30 , pp. 4864-4876
    • Stella, R.1    Massimino, M.L.2    Sandri, M.3    Sorgato, M.C.4    Bertoli, A.5
  • 38
    • 84969377141 scopus 로고    scopus 로고
    • Age-dependent neuromuscular impairment in prion protein knock-out mice
    • COI: 1:CAS:528:DC%2BC28XivFOmsLs%3D
    • Massimino ML, Peggion C, Loro F, Stella R, Megighian A, Scorzeto M, et al. Age-dependent neuromuscular impairment in prion protein knock-out mice. Muscle Nerve. 2016;53:269–79.
    • (2016) Muscle Nerve , vol.53 , pp. 269-279
    • Massimino, M.L.1    Peggion, C.2    Loro, F.3    Stella, R.4    Megighian, A.5    Scorzeto, M.6
  • 39
    • 0018720271 scopus 로고
    • A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels
    • COI: 1:CAS:528:DyaE1MXmtVKlt7c%3D
    • Switzer RC, Merril CR, Shifrin S. A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels. Anal Biochem. 1979;98:231–7.
    • (1979) Anal Biochem , vol.98 , pp. 231-237
    • Switzer, R.C.1    Merril, C.R.2    Shifrin, S.3
  • 40
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wiśniewski JR, Zougman A, Nagaraj N, Mann M. Universal sample preparation method for proteome analysis. Nat Methods. 2009;6:359–62.
    • (2009) Nat Methods , vol.6 , pp. 359-362
    • Wiśniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 41
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications
    • COI: 1:CAS:528:DC%2BD2MXhslWlsr8%3D
    • Kirkpatrick DS, Gerber SA, Gygi SP. The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods. 2005;35:265–73.
    • (2005) Methods , vol.35 , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 42
    • 77951965920 scopus 로고    scopus 로고
    • Skyline: an open source document editor for creating and analyzing targeted proteomics experiments
    • COI: 1:CAS:528:DC%2BC3cXjvFykurk%3D
    • MacLean B, Tomazela DM, Shulman N, Chambers M, Finney GL, Frewen B, et al. Skyline: an open source document editor for creating and analyzing targeted proteomics experiments. Bioinformatics. 2010;26:966–8.
    • (2010) Bioinformatics , vol.26 , pp. 966-968
    • MacLean, B.1    Tomazela, D.M.2    Shulman, N.3    Chambers, M.4    Finney, G.L.5    Frewen, B.6
  • 43
    • 84871791617 scopus 로고    scopus 로고
    • Proteome-wide selected reaction monitoring assays for the human pathogen Streptococcus pyogenes
    • Karlsson C, Malmström L, Aebersold R, Malmström J. Proteome-wide selected reaction monitoring assays for the human pathogen Streptococcus pyogenes. Nat Commun. 2012;3:1301.
    • (2012) Nat Commun , vol.3 , pp. 1301
    • Karlsson, C.1    Malmström, L.2    Aebersold, R.3    Malmström, J.4
  • 44
    • 74049131716 scopus 로고    scopus 로고
    • High-throughput generation of selected reaction-monitoring assays for proteins and proteomes
    • COI: 1:CAS:528:DC%2BD1MXhsFWksb7K
    • Picotti P, Rinner O, Stallmach R, Dautel F, Farrah T, Domon B, et al. High-throughput generation of selected reaction-monitoring assays for proteins and proteomes. Nat Methods. 2010;7:43–6.
    • (2010) Nat Methods , vol.7 , pp. 43-46
    • Picotti, P.1    Rinner, O.2    Stallmach, R.3    Dautel, F.4    Farrah, T.5    Domon, B.6
  • 45
    • 34250722602 scopus 로고    scopus 로고
    • Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signalling networks
    • COI: 1:CAS:528:DC%2BD2sXkt1Kgt7w%3D
    • Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM. Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signalling networks. Proc Natl Acad Sci U S A. 2007;104:5860–5.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 5860-5865
    • Wolf-Yadlin, A.1    Hautaniemi, S.2    Lauffenburger, D.A.3    White, F.M.4
  • 46
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: a tutorial
    • Lange V, Picotti P, Domon B, Aebersold R. Selected reaction monitoring for quantitative proteomics: a tutorial. Mol Syst Biol. 2008;4:222.
    • (2008) Mol Syst Biol , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 47
    • 33846133955 scopus 로고    scopus 로고
    • Computational prediction of proteotypic peptides for quantitative proteomics
    • COI: 1:CAS:528:DC%2BD2sXis1GrtA%3D%3D
    • Mallick P, Schirle M, Chen SS, Flory MR, Lee H, Martin D, et al. Computational prediction of proteotypic peptides for quantitative proteomics. Nat Biotechnol. 2007;25:125–31.
    • (2007) Nat Biotechnol , vol.25 , pp. 125-131
    • Mallick, P.1    Schirle, M.2    Chen, S.S.3    Flory, M.R.4    Lee, H.5    Martin, D.6
  • 48
    • 84864987862 scopus 로고    scopus 로고
    • The use of selected reaction monitoring in quantitative proteomics
    • COI: 1:CAS:528:DC%2BC38XhtFOht7nK
    • Holman SW, Sims PF, Eyers CE. The use of selected reaction monitoring in quantitative proteomics. Bioanalysis. 2012;4:1763–8.
    • (2012) Bioanalysis , vol.4 , pp. 1763-1768
    • Holman, S.W.1    Sims, P.F.2    Eyers, C.E.3
  • 49
    • 84924052631 scopus 로고    scopus 로고
    • Single muscle fiber proteomics reveals unexpected mitochondrial specialization
    • COI: 1:CAS:528:DC%2BC2MXjs1Gntbc%3D
    • Murgia M, Nagaraj N, Deshmukh AS, Zeiler M, Cancellara P, Moretti I, et al. Single muscle fiber proteomics reveals unexpected mitochondrial specialization. EMBO Rep. 2015;16:387–95.
    • (2015) EMBO Rep , vol.16 , pp. 387-395
    • Murgia, M.1    Nagaraj, N.2    Deshmukh, A.S.3    Zeiler, M.4    Cancellara, P.5    Moretti, I.6
  • 50
    • 0027327708 scopus 로고
    • Selective accumulation of MyoD and myogenin mRNAs in fast and slow adult skeletal muscle is controlled by innervation and hormones
    • COI: 1:CAS:528:DyaK2cXhtlSrsrc%3D
    • Hughes SM, Taylor JM, Tapscott SJ, Gurley CM, Carter WJ, Peterson CA. Selective accumulation of MyoD and myogenin mRNAs in fast and slow adult skeletal muscle is controlled by innervation and hormones. Development. 1993;118:1137–47.
    • (1993) Development , vol.118 , pp. 1137-1147
    • Hughes, S.M.1    Taylor, J.M.2    Tapscott, S.J.3    Gurley, C.M.4    Carter, W.J.5    Peterson, C.A.6
  • 51
    • 84861990380 scopus 로고    scopus 로고
    • Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions
    • COI: 1:CAS:528:DC%2BC38XotVSrurg%3D
    • Picotti P, Aebersold R. Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions. Nat Methods. 2012;9:555–66.
    • (2012) Nat Methods , vol.9 , pp. 555-566
    • Picotti, P.1    Aebersold, R.2
  • 52
    • 35349025311 scopus 로고    scopus 로고
    • Time course of preferential motor unit loss in the SOD1 G93A mouse model of amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BD2sXht1aktr7E
    • Hegedus J, Putman CT, Gordon T. Time course of preferential motor unit loss in the SOD1 G93A mouse model of amyotrophic lateral sclerosis. Neurobiol Dis. 2007;28:154–64.
    • (2007) Neurobiol Dis , vol.28 , pp. 154-164
    • Hegedus, J.1    Putman, C.T.2    Gordon, T.3
  • 53
    • 33344462702 scopus 로고    scopus 로고
    • Selective vulnerability and pruning of phasic motoneuron axons in motoneuron disease alleviated by CNTF
    • COI: 1:CAS:528:DC%2BD28Xhsleltr8%3D
    • Pun S, Santos AF, Saxena S, Xu L, Caroni P. Selective vulnerability and pruning of phasic motoneuron axons in motoneuron disease alleviated by CNTF. Nat Neurosci. 2006;9:408–19.
    • (2006) Nat Neurosci , vol.9 , pp. 408-419
    • Pun, S.1    Santos, A.F.2    Saxena, S.3    Xu, L.4    Caroni, P.5
  • 54
    • 84884765656 scopus 로고    scopus 로고
    • Neuroprotection through excitability and mTOR required in ALS motoneurons to delay disease and extend survival
    • COI: 1:CAS:528:DC%2BC3sXhsFGru7nK
    • Saxena S, Roselli F, Singh K, Leptien K, Julien JP, Gros-Louis F, et al. Neuroprotection through excitability and mTOR required in ALS motoneurons to delay disease and extend survival. Neuron. 2013;80:80–96.
    • (2013) Neuron , vol.80 , pp. 80-96
    • Saxena, S.1    Roselli, F.2    Singh, K.3    Leptien, K.4    Julien, J.P.5    Gros-Louis, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.