메뉴 건너뛰기




Volumn 16, Issue 13, 2016, Pages 1852-1857

Sensitivity of mass spectrometry analysis depends on the shape of the filtration unit used for filter aided sample preparation (FASP)

Author keywords

FASP; Sample preparation; SDS removal; Sensitivity; Single pancreatic islet; Technology

Indexed keywords

ALCOHOL; DEOXYCHOLATE SODIUM; DETERGENT; DODECYL SULFATE SODIUM;

EID: 84990227024     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201600103     Document Type: Article
Times cited : (43)

References (19)
  • 1
    • 84874805815 scopus 로고    scopus 로고
    • The challenge of the proteome dynamic range and its implications for in-depth proteomics
    • Zubarev, R. A., The challenge of the proteome dynamic range and its implications for in-depth proteomics. Proteomics 2013, 13(5), pp. 723–726.
    • (2013) Proteomics , vol.13 , Issue.5 , pp. 723-726
    • Zubarev, R.A.1
  • 2
    • 4444237731 scopus 로고    scopus 로고
    • A critical evaluation of sample extraction techniques for enhanced proteomic analysis of recalcitrant plant tissues
    • Saravanan, R. S., Rose, J. K., A critical evaluation of sample extraction techniques for enhanced proteomic analysis of recalcitrant plant tissues. Proteomics 2004, 4(9), pp. 2522–2532.
    • (2004) Proteomics , vol.4 , Issue.9 , pp. 2522-2532
    • Saravanan, R.S.1    Rose, J.K.2
  • 3
    • 18844460394 scopus 로고    scopus 로고
    • Sample preparation and digestion for proteomic analyses using spin filters
    • Manza, L. L., Sample preparation and digestion for proteomic analyses using spin filters. Proteomics 2005, 5(7), pp. 1742–1745.
    • (2005) Proteomics , vol.5 , Issue.7 , pp. 1742-1745
    • Manza, L.L.1
  • 4
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski, J. R., Universal sample preparation method for proteome analysis. Nat. Methods 2009, 6(5), pp. 359–362.
    • (2009) Nat. Methods , vol.6 , Issue.5 , pp. 359-362
    • Wisniewski, J.R.1
  • 5
    • 84898731769 scopus 로고    scopus 로고
    • Enhanced FASP (eFASP) to increase proteome coverage and sample recovery for quantitative proteomic experiments
    • Erde, J., Loo, R. R., Loo, J. A., Enhanced FASP (eFASP) to increase proteome coverage and sample recovery for quantitative proteomic experiments. J. Proteome Res. 2014, 13(4), pp. 1885–1895.
    • (2014) J. Proteome Res. , vol.13 , Issue.4 , pp. 1885-1895
    • Erde, J.1    Loo, R.R.2    Loo, J.A.3
  • 6
    • 84902094502 scopus 로고    scopus 로고
    • Comprehensive comparative and semiquantitative proteome of a very low number of native and matched epstein-barr-virus-transformed B lymphocytes infiltrating human melanoma
    • Maurer, M., Comprehensive comparative and semiquantitative proteome of a very low number of native and matched epstein-barr-virus-transformed B lymphocytes infiltrating human melanoma. J. Proteome Res. 2014, 13(6), pp. 2830–2845.
    • (2014) J. Proteome Res. , vol.13 , Issue.6 , pp. 2830-2845
    • Maurer, M.1
  • 7
    • 84883295723 scopus 로고    scopus 로고
    • Comparison of detergent-based sample preparation workflows for LTQ-Orbitrap analysis of the Escherichia coli proteome
    • Tanca, A., Comparison of detergent-based sample preparation workflows for LTQ-Orbitrap analysis of the Escherichia coli proteome. Proteomics 2013, 13(17), pp. 2597–2607.
    • (2013) Proteomics , vol.13 , Issue.17 , pp. 2597-2607
    • Tanca, A.1
  • 8
    • 71549117585 scopus 로고    scopus 로고
    • Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome
    • Wisniewski, J. R., Zougman, A., Mann, M., Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome. J. Proteome Res. 2009, 8(12), pp. 5674–5678.
    • (2009) J. Proteome Res. , vol.8 , Issue.12 , pp. 5674-5678
    • Wisniewski, J.R.1    Zougman, A.2    Mann, M.3
  • 9
    • 77954378942 scopus 로고    scopus 로고
    • Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry
    • Ostasiewicz, P., Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry. J. Proteome Res. 2010, 9(7), pp. 3688–3700.
    • (2010) J. Proteome Res. , vol.9 , Issue.7 , pp. 3688-3700
    • Ostasiewicz, P.1
  • 10
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D. F., Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 2010, 141(5), pp. 897–907.
    • (2010) Cell , vol.141 , Issue.5 , pp. 897-907
    • Zielinska, D.F.1
  • 11
    • 84924390372 scopus 로고    scopus 로고
    • Comparative reevaluation of FASP and enhanced FASP methods by LC-MS/MS
    • Nel, A. J., Comparative reevaluation of FASP and enhanced FASP methods by LC-MS/MS. J. Proteome Res. 2015, 14(3), pp. 1637–1642.
    • (2015) J. Proteome Res. , vol.14 , Issue.3 , pp. 1637-1642
    • Nel, A.J.1
  • 12
    • 84876299279 scopus 로고    scopus 로고
    • Proteomic analysis of formalin-fixed paraffin-embedded renal tissue samples by label-free MS: assessment of overall technical variability and the impact of block age
    • p
    • Craven, R. A., Proteomic analysis of formalin-fixed paraffin-embedded renal tissue samples by label-free MS: assessment of overall technical variability and the impact of block age. Proteomics Clin. Appl. 2013, 7(3–4), p. 273–282.
    • (2013) Proteomics Clin. Appl. , vol.7 , Issue.3-4 , pp. 273-282
    • Craven, R.A.1
  • 13
    • 84927932541 scopus 로고    scopus 로고
    • Proteomic analysis of the palmitoyl protein thioesterase 1 interactome in SH-SY5Y human neuroblastoma cells
    • Scifo, E., Proteomic analysis of the palmitoyl protein thioesterase 1 interactome in SH-SY5Y human neuroblastoma cells. J. Proteomics 2015, 123, pp. 42–53.
    • (2015) J. Proteomics , vol.123 , pp. 42-53
    • Scifo, E.1
  • 14
    • 57749171580 scopus 로고    scopus 로고
    • Proteomics in diabetes research
    • Sundsten, T., Ortsater, H., Proteomics in diabetes research. Mol. Cell Endocrinol. 2009, 297(1–2), pp. 93–103.
    • (2009) Mol. Cell Endocrinol. , vol.297 , Issue.1-2 , pp. 93-103
    • Sundsten, T.1    Ortsater, H.2
  • 15
    • 73149110595 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of single pancreatic islets
    • Waanders, L. F., Quantitative proteomic analysis of single pancreatic islets. Proc. Natl. Acad. Sci. U S A 2009, 106(45), pp. 18902–18907.
    • (2009) Proc. Natl. Acad. Sci. U S A , vol.106 , Issue.45 , pp. 18902-18907
    • Waanders, L.F.1
  • 16
    • 51149117224 scopus 로고    scopus 로고
    • Cl transport in complemented CF bronchial epithelial cells correlates with CFTR mRNA expression levels
    • Illek, B., Cl transport in complemented CF bronchial epithelial cells correlates with CFTR mRNA expression levels. Cell. Physiol. Biochem. 2008, 22(1–4), pp. 57–68.
    • (2008) Cell. Physiol. Biochem. , vol.22 , Issue.1-4 , pp. 57-68
    • Illek, B.1
  • 17
    • 84942456143 scopus 로고    scopus 로고
    • Catalytic site inhibition of insulin-degrading enzyme by a small molecule induces glucose intolerance in mice
    • Deprez-Poulain, R., Catalytic site inhibition of insulin-degrading enzyme by a small molecule induces glucose intolerance in mice. Nat. Commun. 2015, 6, 8250.
    • (2015) Nat. Commun. , vol.6 , pp. 8250
    • Deprez-Poulain, R.1
  • 18
    • 84920269693 scopus 로고    scopus 로고
    • A new workflow for proteomic analysis of urinary exosomes and assessment in cystinuria patients
    • Bourderioux, M., A new workflow for proteomic analysis of urinary exosomes and assessment in cystinuria patients. J. Proteome Res. 2015, 14(1), pp. 567–777.
    • (2015) J. Proteome Res. , vol.14 , Issue.1 , pp. 567-777
    • Bourderioux, M.1
  • 19
    • 84934874312 scopus 로고    scopus 로고
    • Comparative membrane proteomics: a technical advancement in the search of renal cell carcinoma biomarkers
    • Raimondo, F., Comparative membrane proteomics: a technical advancement in the search of renal cell carcinoma biomarkers. Mol. Biosyst. 2015, 11(6), pp. 1708–1716.
    • (2015) Mol. Biosyst. , vol.11 , Issue.6 , pp. 1708-1716
    • Raimondo, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.