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Volumn 5, Issue 4, 2012, Pages 96-103

Serum peptide profiles of Duchenne Muscular Dystrophy (DMD) patients evaluated by data handling strategies for high resolution content

Author keywords

Data handling; Duchenne Muscular Dystrophy; High resolution; Mass spectrometry; Serum peptide profiles

Indexed keywords

PEPTIDE;

EID: 84860897149     PISSN: None     EISSN: 0974276X     Source Type: Journal    
DOI: 10.4172/jpb.1000219     Document Type: Article
Times cited : (8)

References (32)
  • 1
    • 77957894167 scopus 로고    scopus 로고
    • Accurate peak list extraction from proteomic mass spectra for identification and profiling studies
    • Barbarini N, Magni P (2010) Accurate peak list extraction from proteomic mass spectra for identification and profiling studies. BMC Bioinformatics 11: 518.
    • (2010) BMC Bioinformatics , vol.11 , pp. 518
    • Barbarini, N.1    Magni, P.2
  • 2
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R, Mann M (2003) Mass spectrometry-based proteomics. Nature 422: 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 3
    • 2542640080 scopus 로고    scopus 로고
    • Mass spectrometry as a diagnostic and a cancer biomarker discovery tool: Opportunities and potential limitations
    • Diamandis EP (2004) Mass spectrometry as a diagnostic and a cancer biomarker discovery tool: opportunities and potential limitations. Mol Cell Proteomics 3: 367-378.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 367-378
    • Diamandis, E.P.1
  • 6
    • 1542617944 scopus 로고    scopus 로고
    • Serum peptide profiling by magnetic particle-assisted, automated sample processing and MALDI-TOF mass spectrometry
    • Villanueva J, Philip J, Entenberg D, Chaparro CA, Tanwar MK, et al. (2004) Serum peptide profiling by magnetic particle-assisted, automated sample processing and MALDI-TOF mass spectrometry. Anal Chem 76: 1560-1570.
    • (2004) Anal Chem , vol.76 , pp. 1560-1570
    • Villanueva, J.1    Philip, J.2    Entenberg, D.3    Chaparro, C.A.4    Tanwar, M.K.5
  • 7
    • 63049101911 scopus 로고    scopus 로고
    • Serum protein profiling by solid phase extraction and mass spectrometry: A future diagnostics tool?
    • Callesen AK, Madsen JS, Vach W, Kruse TA, Mogensen O, et al. (2009) Serum protein profiling by solid phase extraction and mass spectrometry: a future diagnostics tool? Proteomics 9: 1428-1441.
    • (2009) Proteomics , vol.9 , pp. 1428-1441
    • Callesen, A.K.1    Madsen, J.S.2    Vach, W.3    Kruse, T.A.4    Mogensen, O.5
  • 8
    • 81555215504 scopus 로고    scopus 로고
    • Precision profiling and identification of human serum peptides using Fourier transform ion cyclotron resonance mass spectrometry
    • Nicolardi S, Palmblad M, Hensbergen PJ, Tollenaar RA, Deelder AM, et al. (2011) Precision profiling and identification of human serum peptides using Fourier transform ion cyclotron resonance mass spectrometry. Rapid Commun Mass Spectrom 25: 3457-3463.
    • (2011) Rapid Commun Mass Spectrom , vol.25 , pp. 3457-3463
    • Nicolardi, S.1    Palmblad, M.2    Hensbergen, P.J.3    Tollenaar, R.A.4    Deelder, A.M.5
  • 9
    • 77955918712 scopus 로고    scopus 로고
    • Quality control based on isotopic distributions for high-throughput MALDI-TOF and MALDI-FTICR serum peptide profiling
    • Nicolardi S, Palmblad M, Dalebout H, Bladergroen M, Tollenaar RA, et al. (2010) Quality control based on isotopic distributions for high-throughput MALDI-TOF and MALDI-FTICR serum peptide profiling. J Am Soc Mass Spectrom 21: 1515-1525.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 1515-1525
    • Nicolardi, S.1    Palmblad, M.2    Dalebout, H.3    Bladergroen, M.4    Tollenaar, R.A.5
  • 11
    • 18744411077 scopus 로고    scopus 로고
    • Improved peak detection and quantification of mass spectrometry data acquired from surface-enhanced laser desorption and ionization by denoising spectra with the undecimated discrete wavelet transform
    • Coombes KR, Tsavachidis S, Morris JS, Baggerly KA, Hung MC, et al. (2005) Improved peak detection and quantification of mass spectrometry data acquired from surface-enhanced laser desorption and ionization by denoising spectra with the undecimated discrete wavelet transform. Proteomics 5: 4107-4117.
    • (2005) Proteomics , vol.5 , pp. 4107-4117
    • Coombes, K.R.1    Tsavachidis, S.2    Morris, J.S.3    Baggerly, K.A.4    Hung, M.C.5
  • 12
    • 18744384734 scopus 로고    scopus 로고
    • Feature extraction and quantification for mass spectrometry in biomedical applications using the mean spectrum
    • Morris JS, Coombes KR, Koomen J, Baggerly KA, Kobayashi R (2005) Feature extraction and quantification for mass spectrometry in biomedical applications using the mean spectrum. Bioinformatics 21: 1764-1775.
    • (2005) Bioinformatics , vol.21 , pp. 1764-1775
    • Morris, J.S.1    Coombes, K.R.2    Koomen, J.3    Baggerly, K.A.4    Kobayashi, R.5
  • 13
    • 33748659203 scopus 로고    scopus 로고
    • Improved peak detection in mass spectrum by incorporating continuous wavelet transform-based pattern matching
    • Du P, Kibbe WA, Lin SM (2006) Improved peak detection in mass spectrum by incorporating continuous wavelet transform-based pattern matching. Bioinformatics 22: 2059-2065.
    • (2006) Bioinformatics , vol.22 , pp. 2059-2065
    • Du, P.1    Kibbe, W.A.2    Lin, S.M.3
  • 14
    • 69949096828 scopus 로고    scopus 로고
    • Profiling MS proteomics data using smoothed non-linear energy operator and Bayesian additive regression trees
    • He S, Li X, Viant MR, Yao X (2009) Profiling MS proteomics data using smoothed non-linear energy operator and Bayesian additive regression trees. Proteomics 9: 4176-4191.
    • (2009) Proteomics , vol.9 , pp. 4176-4191
    • He, S.1    Li, X.2    Viant, M.R.3    Yao, X.4
  • 15
    • 79955127408 scopus 로고    scopus 로고
    • On the use of double cross-validation for the combination of proteomic mass spectral data for enhanced diagnosis and prediction
    • Mertens BJA, van der Burgt YEM, Velstra B, Mesker WE, Tollenaar RAEM, et al. (2011) On the use of double cross-validation for the combination of proteomic mass spectral data for enhanced diagnosis and prediction. Stat Probab Lett 81: 759-766.
    • (2011) Stat Probab Lett , vol.81 , pp. 759-766
    • Mertens, B.J.A.1    van der Burgt, Y.E.M.2    Velstra, B.3    Mesker, W.E.4    Tollenaar, R.A.E.M.5
  • 16
    • 35748977591 scopus 로고    scopus 로고
    • Improved model-based, platform-independent feature extraction for mass spectrometry
    • Noy K, Fasulo D (2007) Improved model-based, platform-independent feature extraction for mass spectrometry. Bioinformatics 23: 2528-2535.
    • (2007) Bioinformatics , vol.23 , pp. 2528-2535
    • Noy, K.1    Fasulo, D.2
  • 17
    • 33847114732 scopus 로고    scopus 로고
    • Identification of leptomeningeal metastasis-related proteins in cerebrospinal fluid of patients with breast cancer by a combination of MALDI-TOF, MALDI-FTICR and nanoLC-FTICR MS
    • Rompp A, Dekker L, Taban I, Jenster G, Boogerd W, et al. (2007) Identification of leptomeningeal metastasis-related proteins in cerebrospinal fluid of patients with breast cancer by a combination of MALDI-TOF, MALDI-FTICR and nanoLC-FTICR MS. Proteomics 7: 474-481.
    • (2007) Proteomics , vol.7 , pp. 474-481
    • Rompp, A.1    Dekker, L.2    Taban, I.3    Jenster, G.4    Boogerd, W.5
  • 19
    • 71549172816 scopus 로고    scopus 로고
    • Interventions for muscular dystrophy: Molecular medicines entering the clinic
    • Bushby K, Lochmuller H, Lynn S, Straub V (2009) Interventions for muscular dystrophy: molecular medicines entering the clinic. Lancet 374: 1849-1856.
    • (2009) Lancet , vol.374 , pp. 1849-1856
    • Bushby, K.1    Lochmuller, H.2    Lynn, S.3    Straub, V.4
  • 20
    • 79960898220 scopus 로고    scopus 로고
    • Serum matrix metalloproteinase-9 (MMP-9) as a biomarker for monitoring disease progression in Duchenne muscular dystrophy (DMD)
    • Nadarajah VD, van Putten M, Chaouch A, Garrood P, Straub V, et al. (2011) Serum matrix metalloproteinase-9 (MMP-9) as a biomarker for monitoring disease progression in Duchenne muscular dystrophy (DMD). Neuromuscul Disord 21: 569-578.
    • (2011) Neuromuscul Disord , vol.21 , pp. 569-578
    • Nadarajah, V.D.1    van Putten, M.2    Chaouch, A.3    Garrood, P.4    Straub, V.5
  • 21
    • 68949215206 scopus 로고    scopus 로고
    • Mass spectrometry-based serum proteome pattern analysis in molecular diagnostics of early stage breast cancer
    • Pietrowska M, Marczak L, Polanska J, Behrendt K, Nowicka E, et al. (2009) Mass spectrometry-based serum proteome pattern analysis in molecular diagnostics of early stage breast cancer. J Transl Med 7: 60.
    • (2009) J Transl Med , vol.7 , pp. 60
    • Pietrowska, M.1    Marczak, L.2    Polanska, J.3    Behrendt, K.4    Nowicka, E.5
  • 22
    • 70350469122 scopus 로고    scopus 로고
    • MR imaging in Duchenne muscular dystrophy: Quantification of T1-weighted signal, contrast uptake, and the effects of exercise
    • Garrood P, Hollingsworth KG, Eagle M, Aribisala BS, Birchall D, et al. (2009) MR imaging in Duchenne muscular dystrophy: quantification of T1-weighted signal, contrast uptake, and the effects of exercise. J Magn Reson Imaging 30: 1130-1138.
    • (2009) J Magn Reson Imaging , vol.30 , pp. 1130-1138
    • Garrood, P.1    Hollingsworth, K.G.2    Eagle, M.3    Aribisala, B.S.4    Birchall, D.5
  • 23
    • 42549137898 scopus 로고    scopus 로고
    • Serum protein profiling in mice: Identification of Factor XIIIa as a potential biomarker for muscular dystrophy
    • Alagaratnam S, Mertens BJ, Dalebout JC, Deelder AM, van Ommen GJ, et al. (2008) Serum protein profiling in mice: identification of Factor XIIIa as a potential biomarker for muscular dystrophy. Proteomics 8: 1552-1563.
    • (2008) Proteomics , vol.8 , pp. 1552-1563
    • Alagaratnam, S.1    Mertens, B.J.2    Dalebout, J.C.3    Deelder, A.M.4    van Ommen, G.J.5
  • 24
    • 72149117126 scopus 로고    scopus 로고
    • Different expression of fibrinopeptide A and related fragments in serum of type 1 diabetic patients with nephropathy
    • Gianazza E, Mainini V, Castoldi G, Chinello C, Zerbini G, et al. (2010) Different expression of fibrinopeptide A and related fragments in serum of type 1 diabetic patients with nephropathy. J Proteomics 73: 593-601.
    • (2010) J Proteomics , vol.73 , pp. 593-601
    • Gianazza, E.1    Mainini, V.2    Castoldi, G.3    Chinello, C.4    Zerbini, G.5
  • 25
    • 33745442821 scopus 로고    scopus 로고
    • The MALDI-TOF mass spectrometric view of the plasma proteome and peptidome
    • Hortin GL (2006) The MALDI-TOF mass spectrometric view of the plasma proteome and peptidome. Clin Chem 52: 1223-1237.
    • (2006) Clin Chem , vol.52 , pp. 1223-1237
    • Hortin, G.L.1
  • 26
    • 77956548344 scopus 로고    scopus 로고
    • A well-characterised peak identification list of MALDI MS profile peaks for human blood serum
    • Tiss A, Smith C, Menon U, Jacobs I, Timms JF, et al. (2010) A well-characterised peak identification list of MALDI MS profile peaks for human blood serum. Proteomics 10: 3388-3392.
    • (2010) Proteomics , vol.10 , pp. 3388-3392
    • Tiss, A.1    Smith, C.2    Menon, U.3    Jacobs, I.4    Timms, J.F.5
  • 29
    • 67651213696 scopus 로고    scopus 로고
    • Serum levels of vascular endothelial growth factor elevated in patients with muscular dystrophy
    • Saito T, Yamamoto Y, Matsumura T, Fujimura H, Shinno S (2009) Serum levels of vascular endothelial growth factor elevated in patients with muscular dystrophy. Brain Dev 31: 612-617.
    • (2009) Brain Dev , vol.31 , pp. 612-617
    • Saito, T.1    Yamamoto, Y.2    Matsumura, T.3    Fujimura, H.4    Shinno, S.5
  • 30
    • 46249086678 scopus 로고    scopus 로고
    • Fibrinogen drives dystrophic muscle fibrosis via a TGFbeta/alternative macrophage activation pathway
    • Vidal B, Serrano AL, Tjwa M, Suelves M, Ardite E, et al. (2008) Fibrinogen drives dystrophic muscle fibrosis via a TGFbeta/alternative macrophage activation pathway. Genes Dev 22: 1747-1752.
    • (2008) Genes Dev , vol.22 , pp. 1747-1752
    • Vidal, B.1    Serrano, A.L.2    Tjwa, M.3    Suelves, M.4    Ardite, E.5
  • 31
    • 50349095252 scopus 로고    scopus 로고
    • Common genetic polymorphisms and haplotypes of fibrinogen alpha, beta, and gamma chains affect fibrinogen levels and the response to proinflammatory stimulation in myocardial infarction survivors: The AIRGENE study
    • Jacquemin B, Antoniades C, Nyberg F, Plana E, Mueller M, et al. (2008) Common genetic polymorphisms and haplotypes of fibrinogen alpha, beta, and gamma chains affect fibrinogen levels and the response to proinflammatory stimulation in myocardial infarction survivors: the AIRGENE study. J Am Coll Cardiol 52: 941-952.
    • (2008) J Am Coll Cardiol , vol.52 , pp. 941-952
    • Jacquemin, B.1    Antoniades, C.2    Nyberg, F.3    Plana, E.4    Mueller, M.5
  • 32
    • 48849086000 scopus 로고    scopus 로고
    • The Proteo Miner and the Forty Niners: Searching for gold nuggets in the proteomic arena
    • Righetti PG, Boschetti E (2008) The Proteo Miner and the Forty Niners: searching for gold nuggets in the proteomic arena. Mass Spectrom Rev 27: 596-608.
    • (2008) Mass Spectrom Rev , vol.27 , pp. 596-608
    • Righetti, P.G.1    Boschetti, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.