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Volumn 12, Issue 3, 2013, Pages 1512-1519

From cells to peptides: "one-stop" integrated proteomic processing using amphipols

Author keywords

amphipols; membrane protein; one stop; proteomics; sample preparation

Indexed keywords

AMPHIPOL A8-35; DETERGENT; MEMBRANE PROTEIN; PROTEOME; TRYPSIN; UNCLASSIFIED DRUG;

EID: 84874617914     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr301064z     Document Type: Article
Times cited : (24)

References (25)
  • 2
    • 33750143252 scopus 로고    scopus 로고
    • Evaluation of the application of sodium deoxycholate to proteomic analysis of rat hippocampal plasma membrane
    • Zhou, J.; Zhou, T.; Cao, R.; Liu, Z.; Shen, J.; Chen, P.; Wang, X.; Liang, S. Evaluation of the application of sodium deoxycholate to proteomic analysis of rat hippocampal plasma membrane J. Proteome Res. 2006, 5 (10) 2547-53
    • (2006) J. Proteome Res. , vol.5 , Issue.10 , pp. 2547-2553
    • Zhou, J.1    Zhou, T.2    Cao, R.3    Liu, Z.4    Shen, J.5    Chen, P.6    Wang, X.7    Liang, S.8
  • 3
    • 0031029477 scopus 로고    scopus 로고
    • Charge density-dependent strength of hydration and biological structure
    • Collins, K. D. Charge density-dependent strength of hydration and biological structure Biophys. J. 1997, 72 (1) 65-76
    • (1997) Biophys. J. , vol.72 , Issue.1 , pp. 65-76
    • Collins, K.D.1
  • 4
    • 0242291099 scopus 로고    scopus 로고
    • Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins
    • Yu, Y. Q.; Gilar, M.; Lee, P. J.; Bouvier, E. S.; Gebler, J. C. Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins Anal. Chem. 2003, 75 (21) 6023-8
    • (2003) Anal. Chem. , vol.75 , Issue.21 , pp. 6023-6028
    • Yu, Y.Q.1    Gilar, M.2    Lee, P.J.3    Bouvier, E.S.4    Gebler, J.C.5
  • 5
    • 1842532945 scopus 로고    scopus 로고
    • A complete peptide mapping of membrane proteins: A novel surfactant aiding the enzymatic digestion of bacteriorhodopsin
    • Yu, Y. Q.; Gilar, M.; Gebler, J. C. A complete peptide mapping of membrane proteins: a novel surfactant aiding the enzymatic digestion of bacteriorhodopsin Rapid Commun. Mass Spectrom. 2004, 18 (6) 711-5
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , Issue.6 , pp. 711-715
    • Yu, Y.Q.1    Gilar, M.2    Gebler, J.C.3
  • 6
    • 78651233674 scopus 로고    scopus 로고
    • Perfluorooctanoic acid for shotgun proteomics
    • Kadiyala, C. S.; Tomechko, S. E.; Miyagi, M. Perfluorooctanoic acid for shotgun proteomics PLoS One 2010, 5 (12) e15332
    • (2010) PLoS One , vol.5 , Issue.12
    • Kadiyala, C.S.1    Tomechko, S.E.2    Miyagi, M.3
  • 7
    • 84856702743 scopus 로고    scopus 로고
    • Perfluorooctanoic acid and ammonium perfluorooctanoate: Volatile surfactants for proteome analysis?
    • Vieira, D. B.; Crowell, A. M.; Doucette, A. A. Perfluorooctanoic acid and ammonium perfluorooctanoate: volatile surfactants for proteome analysis? Rapid Commun. Mass Spectrom. 2012, 26 (5) 523-31
    • (2012) Rapid Commun. Mass Spectrom. , vol.26 , Issue.5 , pp. 523-531
    • Vieira, D.B.1    Crowell, A.M.2    Doucette, A.A.3
  • 8
    • 0030451437 scopus 로고    scopus 로고
    • Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions
    • Tribet, C.; Audebert, R.; Popot, J. L. Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions Proc. Natl. Acad. Sci. U.S.A. 1996, 93 (26) 15047-50
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , Issue.26 , pp. 15047-15050
    • Tribet, C.1    Audebert, R.2    Popot, J.L.3
  • 9
    • 21144446624 scopus 로고    scopus 로고
    • NMR study of a membrane protein in detergent-free aqueous solution
    • Zoonens, M.; Catoire, L. J.; Giusti, F.; Popot, J. L. NMR study of a membrane protein in detergent-free aqueous solution Proc. Natl. Acad. Sci. U.S.A. 2005, 102 (25) 8893-8
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , Issue.25 , pp. 8893-8898
    • Zoonens, M.1    Catoire, L.J.2    Giusti, F.3    Popot, J.L.4
  • 12
    • 57749182936 scopus 로고    scopus 로고
    • Sample prep for proteomics of breast cancer: Proteomics and gene ontology reveal dramatic differences in protein solubilization preferences of radioimmunoprecipitation assay and urea lysis buffers
    • Ngoka, L. C. Sample prep for proteomics of breast cancer: Proteomics and gene ontology reveal dramatic differences in protein solubilization preferences of radioimmunoprecipitation assay and urea lysis buffers Proteome Sci. 2008, 6, 30
    • (2008) Proteome Sci. , vol.6 , pp. 30
    • Ngoka, L.C.1
  • 13
    • 84865830479 scopus 로고    scopus 로고
    • Protein solubilization: Attend to the choice of lysis buffer
    • Peach, M.; Marsh, N.; Macphee, D. J. Protein solubilization: Attend to the choice of lysis buffer Methods Mol. Biol. 2012, 869, 37-47
    • (2012) Methods Mol. Biol. , vol.869 , pp. 37-47
    • Peach, M.1    Marsh, N.2    MacPhee, D.J.3
  • 14
    • 1542652441 scopus 로고
    • A spectrophotometric determination of trypsin and chymotrypsin
    • Schwert, G. W.; Takenaka, Y. A spectrophotometric determination of trypsin and chymotrypsin Biochim. Biophys. Acta 1955, 16 (4) 570-5
    • (1955) Biochim. Biophys. Acta , vol.16 , Issue.4 , pp. 570-575
    • Schwert, G.W.1    Takenaka, Y.2
  • 15
    • 0028225554 scopus 로고
    • Isolation of integral membrane proteins by phase partitioning with Triton X-114
    • Brusca, J. S.; Radolf, J. D. Isolation of integral membrane proteins by phase partitioning with Triton X-114 Methods Enzymol. 1994, 228, 182-93
    • (1994) Methods Enzymol. , vol.228 , pp. 182-193
    • Brusca, J.S.1    Radolf, J.D.2
  • 16
    • 33645774852 scopus 로고    scopus 로고
    • Modular stop and go extraction tips with stacked disks for parallel and multidimensional peptide fractionation in proteomics
    • Ishihama, Y.; Rappsilber, J.; Mann, M. Modular stop and go extraction tips with stacked disks for parallel and multidimensional peptide fractionation in proteomics J. Proteome Res. 2006, 5 (4) 988-94
    • (2006) J. Proteome Res. , vol.5 , Issue.4 , pp. 988-994
    • Ishihama, Y.1    Rappsilber, J.2    Mann, M.3
  • 17
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski, J. R.; Zougman, A.; Nagaraj, N.; Mann, M. Universal sample preparation method for proteome analysis Nat. Methods 2009, 6 (5) 359-62
    • (2009) Nat. Methods , vol.6 , Issue.5 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 19
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J.; Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification Nat. Biotechnol. 2008, 26 (12) 1367-72
    • (2008) Nat. Biotechnol. , vol.26 , Issue.12 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 20
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N.; Pappin, D. J.; Creasy, D. M.; Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 1999, 20 (18) 3551-67
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 21
    • 84863239359 scopus 로고    scopus 로고
    • BuildSummary: Using a group-based approach to improve the sensitivity of peptide/protein identification in shotgun proteomics
    • Sheng, Q.; Dai, J.; Wu, Y.; Tang, H.; Zeng, R. BuildSummary: Using a group-based approach to improve the sensitivity of peptide/protein identification in shotgun proteomics J. Proteome Res. 2012, 11 (3) 1494-502
    • (2012) J. Proteome Res. , vol.11 , Issue.3 , pp. 1494-1502
    • Sheng, Q.1    Dai, J.2    Wu, Y.3    Tang, H.4    Zeng, R.5
  • 22
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J.; Doolittle, R. F. A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 1982, 157 (1) 105-32
    • (1982) J. Mol. Biol. , vol.157 , Issue.1 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 23
    • 0034705564 scopus 로고    scopus 로고
    • Interaction of amphipols with sarcoplasmic reticulum Ca2+-ATPase
    • Champeil, P.; Menguy, T.; Tribet, C.; Popot, J. L.; le Maire, M. Interaction of amphipols with sarcoplasmic reticulum Ca2+-ATPase J. Biol. Chem. 2000, 275 (25) 18623-37
    • (2000) J. Biol. Chem. , vol.275 , Issue.25 , pp. 18623-18637
    • Champeil, P.1    Menguy, T.2    Tribet, C.3    Popot, J.L.4    Le Maire, M.5
  • 24
    • 84863935182 scopus 로고    scopus 로고
    • Well-defined critical association concentration and rapid adsorption at the air/water interface of a short amphiphilic polymer, amphipol a8-35: A study by forster resonance energy transfer and dynamic surface tension measurements
    • Giusti, F.; Popot, J. L.; Tribet, C. Well-defined critical association concentration and rapid adsorption at the air/water interface of a short amphiphilic polymer, amphipol a8-35: a study by forster resonance energy transfer and dynamic surface tension measurements Langmuir 2012, 28 (28) 10372-80
    • (2012) Langmuir , vol.28 , Issue.28 , pp. 10372-10380
    • Giusti, F.1    Popot, J.L.2    Tribet, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.