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Volumn 1188, Issue , 2014, Pages 95-106

Stable isotope labeling for proteomic analysis of tissues in mouse

Author keywords

In vivo; Mass spectrometry; Mouse; Proteomics; Quantitative; SILAC; Skeletal muscle; Stable isotope labeling

Indexed keywords

ACTININ; CARBON 13; CONNECTIN; LYSINE; MYOSIN; STABLE ISOTOPE; CARBON; MUSCLE PROTEIN;

EID: 84925883903     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-1142-4_8     Document Type: Article
Times cited : (8)

References (37)
  • 1
    • 0013596620 scopus 로고
    • Deuterium as an indicator in the study of intermediary metabolism
    • Schoenheimer R, Rittenberg D (1935) Deuterium as an indicator in the study of intermediary metabolism. Science 82(2120): 156-157
    • (1935) Science , vol.82 , Issue.2120 , pp. 156-157
    • Schoenheimer, R.1    Rittenberg, D.2
  • 2
    • 77954371891 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture(SILAC) applied to quantitative proteomics of Bacillus subtilis
    • Soufi B, Kumar C, Gnad F et al (2010) Stable isotope labeling by amino acids in cell culture(SILAC) applied to quantitative proteomics of Bacillus subtilis. J Proteome Res 9(7):3638-3646
    • (2010) J Proteome Res , vol.9 , Issue.7 , pp. 3638-3646
    • Soufi, B.1    Kumar, C.2    Gnad, F.3
  • 3
    • 15944377809 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway
    • Gruhler A, Olsen JV, Mohammed S et al (2005) Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway. Mol Cell Proteomics 4(3):310-327
    • (2005) Mol Cell Proteomics , vol.4 , Issue.3 , pp. 310-327
    • Gruhler, A.1    Olsen, J.V.2    Mohammed, S.3
  • 4
    • 79959849574 scopus 로고    scopus 로고
    • Extending SILAC to proteomics of plant cell lines
    • Schutz W, Hausmann N, Krug K et al (2011) Extending SILAC to proteomics of plant cell lines. Plant Cell 23(5):1701-1705
    • (2011) Plant Cell , vol.23 , Issue.5 , pp. 1701-1705
    • Schutz, W.1    Hausmann, N.2    Krug, K.3
  • 5
    • 77958018495 scopus 로고    scopus 로고
    • The SILAC fl y allows for accurate protein quantifi-cation in vivo
    • Sury MD, Chen JX, Selbach M (2010) The SILAC fl y allows for accurate protein quantifi-cation in vivo. Mol Cell Proteomics 9(10): 2173-2183
    • (2010) Mol Cell Proteomics , vol.9 , Issue.10 , pp. 2173-2183
    • Sury, M.D.1    Chen, J.X.2    Selbach, M.3
  • 6
    • 80053363595 scopus 로고    scopus 로고
    • Stable-isotope labeling with amino acids in nematodes
    • Larance M, Bailly AP, Pourkarimi E et al (2011) Stable-isotope labeling with amino acids in nematodes. Nat Methods 8(10):849-851
    • (2011) Nat Methods , vol.8 , Issue.10 , pp. 849-851
    • Larance, M.1    Bailly, A.P.2    Pourkarimi, E.3
  • 7
    • 84866137157 scopus 로고    scopus 로고
    • Spiked-in pulsed in vivo labeling identifi es a new member of the CCN family in regenerating newt hearts
    • Looso M, Michel CS, Konzer A et al (2012) Spiked-in pulsed in vivo labeling identifi es a new member of the CCN family in regenerating newt hearts. J Proteome Res 11(9): 4693-4704
    • (2012) J Proteome Res , vol.11 , Issue.9 , pp. 4693-4704
    • Looso, M.1    Michel, C.S.2    Konzer, A.3
  • 8
    • 47549099572 scopus 로고    scopus 로고
    • SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function
    • Kruger M, Moser M, Ussar S et al (2008) SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function. Cell 134(2):353-364
    • (2008) Cell , vol.134 , Issue.2 , pp. 353-364
    • Kruger, M.1    Moser, M.2    Ussar, S.3
  • 9
    • 34249335982 scopus 로고    scopus 로고
    • 15N metabolic labeling of mammalian tissue with slow protein turnover
    • McClatchy DB, Dong MQ, Wu CC et al (2007) 15N metabolic labeling of mammalian tissue with slow protein turnover. J Proteome Res 6(5):2005-2010
    • (2007) J Proteome Res , vol.6 , Issue.5 , pp. 2005-2010
    • McClatchy, D.B.1    Dong, M.Q.2    Wu, C.C.3
  • 10
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometrybased proteomics turns quantitative
    • Ong SE, Mann M (2005) Mass spectrometrybased proteomics turns quantitative. Nat Chem Biol 1(5):252-262
    • (2005) Nat Chem Biol , vol.1 , Issue.5 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 11
    • 57449099068 scopus 로고    scopus 로고
    • Precision proteomics: The case for high resolution and high mass accuracy
    • Mann M, Kelleher NL (2008) Precision proteomics: the case for high resolution and high mass accuracy. PNAS 105(47):18132-18138
    • (2008) PNAS , vol.105 , Issue.47 , pp. 18132-18138
    • Mann, M.1    Kelleher, N.L.2
  • 12
    • 84868612415 scopus 로고    scopus 로고
    • The role of glycogen synthase in the development of hyperglycemia in type 2 diabetes: To store or not to store glucose, that's the question
    • Beck-Nielsen H (2012) The role of glycogen synthase in the development of hyperglycemia in type 2 diabetes: "To store or not to store glucose, that's the question". Diabetes Metab Res Rev 28(8):635-644
    • (2012) Diabetes Metab Res Rev , vol.28 , Issue.8 , pp. 635-644
    • Beck-Nielsen, H.1
  • 13
    • 67650526816 scopus 로고    scopus 로고
    • Changes in the spinal cord proteome of an amyotrophic lateral sclerosis murine model determined by differential in-gel electrophoresis
    • Bergemalm D, Forsberg K, Jonsson PA et al (2009) Changes in the spinal cord proteome of an amyotrophic lateral sclerosis murine model determined by differential in-gel electrophoresis. Mol Cell Proteomics 8(6):1306-1317
    • (2009) Mol Cell Proteomics , vol.8 , Issue.6 , pp. 1306-1317
    • Bergemalm, D.1    Forsberg, K.2    Jonsson, P.A.3
  • 14
    • 84872686952 scopus 로고    scopus 로고
    • Discovery and initial verifi cation of differentially abundant proteins between multiple sclerosis patients and controls using iTRAQ and SID-SRM
    • Kroksveen AC, Aasebo E, Vethe H et al (2012) Discovery and initial verifi cation of differentially abundant proteins between multiple sclerosis patients and controls using iTRAQ and SID-SRM. J Proteomics 78:312-325
    • (2012) J Proteomics , vol.78 , pp. 312-325
    • Kroksveen, A.C.1    Aasebo, E.2    Vethe, H.3
  • 15
  • 16
    • 80054760368 scopus 로고    scopus 로고
    • Fiber types in mammalian skeletal muscles
    • Schiaffi no S, Reggiani C (2011) Fiber types in mammalian skeletal muscles. Physiological Rev 91(4):1447-1531
    • (2011) Physiological Rev , vol.91 , Issue.4 , pp. 1447-1531
    • Schiaffino, S.1    Reggiani, C.2
  • 17
    • 79953231670 scopus 로고    scopus 로고
    • Accurate quantifi cation of more than 4000 mouse tissue proteins reveals minimal proteome changes during aging
    • M110004523
    • Walther DM, Mann M (2011) Accurate quantifi cation of more than 4000 mouse tissue proteins reveals minimal proteome changes during aging. Mol Cell Proteomics 10(2): M110.004523
    • (2011) Mol Cell Proteomics , vol.10 , Issue.2
    • Walther, D.M.1    Mann, M.2
  • 18
    • 84862321368 scopus 로고    scopus 로고
    • On marathons and sprints: An integrated quantitative proteomics and transcriptomics analysis of differences between slow and fast muscle fi bers
    • Drexler HC, Ruhs A, Konzer A et al (2012) On marathons and sprints: an integrated quantitative proteomics and transcriptomics analysis of differences between slow and fast muscle fi bers. Mol Cell Proteomics 11(6): M111.010801
    • (2012) Mol Cell Proteomics , vol.11 , Issue.6
    • Drexler, H.C.1    Ruhs, A.2    Konzer, A.3
  • 20
    • 78751672587 scopus 로고    scopus 로고
    • Proteome-wide quantitation by SILAC
    • Rigbolt KT, Blagoev B (2010) Proteome-wide quantitation by SILAC. Methods Mol Biol 658:187-204
    • (2010) Methods Mol Biol , vol.658 , pp. 187-204
    • Rigbolt, K.T.1    Blagoev, B.2
  • 21
    • 70349213385 scopus 로고    scopus 로고
    • Acquisition of the contractile phenotype by murine arterial smooth muscle cells depends on the Mir143/145 gene cluster
    • Boettger T, Beetz N, Kostin S et al (2009) Acquisition of the contractile phenotype by murine arterial smooth muscle cells depends on the Mir143/145 gene cluster. J Clinic Invest 119(9):2634-2647
    • (2009) J Clinic Invest , vol.119 , Issue.9 , pp. 2634-2647
    • Boettger, T.1    Beetz, N.2    Kostin, S.3
  • 22
    • 84866467141 scopus 로고    scopus 로고
    • Loss of the tumor suppressor BAP1 causes myeloid transformation
    • Dey A, Seshasayee D, Noubade R et al (2012) Loss of the tumor suppressor BAP1 causes myeloid transformation. Science 337(6101): 1541-1546
    • (2012) Science , vol.337 , Issue.6101 , pp. 1541-1546
    • Dey, A.1    Seshasayee, D.2    Noubade, R.3
  • 23
    • 84859562759 scopus 로고    scopus 로고
    • Regulation of lipid metabolism by Dicer revealed through SILAC mice
    • Huang TC, Sahasrabuddhe NA, Kim MS et al (2012) Regulation of lipid metabolism by Dicer revealed through SILAC mice. J Proteome Res 11(4):2193-2205
    • (2012) J Proteome Res , vol.11 , Issue.4 , pp. 2193-2205
    • Huang, T.C.1    Sahasrabuddhe, N.A.2    Kim, M.S.3
  • 24
    • 79953317808 scopus 로고    scopus 로고
    • Obesity-induced overexpression of miRNA-143 inhibits insulin-stimulated AKT activation and impairs glucose metabolism
    • Jordan SD, Kruger M, Willmes DM et al (2011) Obesity-induced overexpression of miRNA-143 inhibits insulin-stimulated AKT activation and impairs glucose metabolism. Nat Cell Biol 13(4):434-446
    • (2011) Nat Cell Biol , vol.13 , Issue.4 , pp. 434-446
    • Jordan, S.D.1    Kruger, M.2    Willmes, D.M.3
  • 25
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber J, Ishihama Y, Mann M (2003) Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal Chem 75(3):663-670
    • (2003) Anal Chem , vol.75 , Issue.3 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 26
    • 1542609969 scopus 로고    scopus 로고
    • Liquid chromatography-mass spectrometry and tandem mass spectrometry of peptides and proteins
    • Shen TL, Noon KR (2004) Liquid chromatography-mass spectrometry and tandem mass spectrometry of peptides and proteins. Methods Mol Biol 251:111-140
    • (2004) Methods Mol Biol , vol.251 , pp. 111-140
    • Shen, T.L.1    Noon, K.R.2
  • 27
    • 80052769923 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics using Q Exactive, a high-performance benchtop quadrupole Orbitrap mass spectrometer
    • Michalski A, Damoc E, Hauschild JP et al (2011) Mass spectrometry-based proteomics using Q Exactive, a high-performance benchtop quadrupole Orbitrap mass spectrometer. Mol Cell Proteomics 10(9):M111.011015
    • (2011) Mol Cell Proteomics , vol.10 , Issue.9
    • Michalski, A.1    Damoc, E.2    Hauschild, J.P.3
  • 28
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics
    • Cox J, Matic I, Hilger M et al (2009) A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat Protoc 4(5):698-705
    • (2009) Nat Protoc , vol.4 , Issue.5 , pp. 698-705
    • Cox, J.1    Matic, I.2    Hilger, M.3
  • 29
    • 84873845648 scopus 로고    scopus 로고
    • ResA3: A web tool for resampling analysis of arbitrary annotations
    • Ruhs A, Cemic F, Braun T et al (2013) ResA3: a web tool for resampling analysis of arbitrary annotations. PLoS One 8(1):e53743
    • (2013) PLoS One , vol.8 , Issue.1
    • Ruhs, A.1    Cemic, F.2    Braun, T.3
  • 30
    • 80054723147 scopus 로고    scopus 로고
    • In vivo quantitative proteomics: The SILAC mouse
    • Zanivan S, Krueger M, Mann M (2012) In vivo quantitative proteomics: the SILAC mouse. Methods Mol Biol 757:435-450
    • (2012) Methods Mol Biol , vol.757 , pp. 435-450
    • Zanivan, S.1    Krueger, M.2    Mann, M.3
  • 31
    • 0019427325 scopus 로고
    • Amino acid requirements of growing mice: Arginine, lysine, tryptophan and phenylalanine
    • Bell JM, John AM (1981) Amino acid requirements of growing mice: arginine, lysine, tryptophan and phenylalanine. J Nutrition 111(3): 525-530
    • (1981) J Nutrition , vol.111 , Issue.3 , pp. 525-530
    • Bell, J.M.1    John, A.M.2
  • 34
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski JR, Zougman A, Nagaraj N et al (2009) Universal sample preparation method for proteome analysis. Nat Methods 6(5):359-362
    • (2009) Nat Methods , vol.6 , Issue.5 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3
  • 35
    • 79959691201 scopus 로고    scopus 로고
    • Comparison between procedures using SDS for shotgun proteomic analyses of complex samples
    • Bereman MS, Egertson JD, MacCoss MJ (2011) Comparison between procedures using SDS for shotgun proteomic analyses of complex samples. Proteomics 11(14):2931-2935
    • (2011) Proteomics , vol.11 , Issue.14 , pp. 2931-2935
    • Bereman, M.S.1    Egertson, J.D.2    MacCoss, M.J.3
  • 36
    • 84863633005 scopus 로고    scopus 로고
    • Tissue proteomics by one-dimensional gel electrophoresis combined with label-free protein quantifi cation
    • Vasilj A, Gentzel M, Ueberham E et al (2012) Tissue proteomics by one-dimensional gel electrophoresis combined with label-free protein quantifi cation. Proteome Res 11(7): 3680-3689
    • (2012) Proteome Res , vol.11 , Issue.7 , pp. 3680-3689
    • Vasilj, A.1    Gentzel, M.2    Ueberham, E.3
  • 37
    • 71549117585 scopus 로고    scopus 로고
    • Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome
    • Wisniewski JR, Zougman A, Mann M (2009) Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome. J Proteome Res 8(12):5674-5678
    • (2009) J Proteome Res , vol.8 , Issue.12 , pp. 5674-5678
    • Wisniewski, J.R.1    Zougman, A.2    Mann, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.